Author: "van Raaij MJ" - Searchworks@Jio Institute Digital Library Search Results

132 results on '"van Raaij MJ"'

1. Large expert-curated database for benchmarking document similarity detection in biomedical literature search

Author: Brown, P, Zhou, Y, Tan, AC, El-Esawi, MA, Liehr, T, Blanck, O, Gladue, DP, Almeida, GMF, Cernava, T, Sorzano, CO, Yeung, AWK, Engel, MS, Chandrasekaran, AR, Muth, T, Staege, MS, Daulatabad, SV, Widera, D, Zhang, J, Meule, A, Honjo, K, Pourret, O, Yin, CC, Zhang, Z, Cascella, M, Flegel, WA, Goodyear, CS, van Raaij, MJ, Bukowy-Bieryllo, Z, Campana, LG, Kurniawan, NA, Lalaouna, D, Hüttner, FJ, Ammerman, BA, Ehret, F, Cobine, PA, Tan, EC, Han, H, Xia, W, McCrum, C, Dings, RPM, Marinello, F, Nilsson, H, Nixon, B, Voskarides, K, Yang, L, Costa, VD, Bengtsson-Palme, J, Bradshaw, W, Grimm, DG, Kumar, N, Martis, E, Prieto, D, Sabnis, SC, Amer, SEDR, Liew, AWC, Perco, P, Rahimi, F, Riva, G, Zhang, C, Devkota, HP, Ogami, K, Basharat, Z, Fierz, W, Siebers, R, Tan, KH, Boehme, KA, Brenneisen, P, Brown, JAL, Dalrymple, BP, Harvey, DJ, Ng, G, Werten, S, Bleackley, M, Dai, Z, Dhariwal, R, Gelfer, Y, Hartmann, MD, Miotla, P, Tamaian, R, Govender, P, Gurney-Champion, OJ, Kauppila, JH, Zhang, X, Echeverría, N, Subhash, S, Sallmon, H, Tofani, M, Bae, T, Bosch, O, Cuív, PO, Danchin, A, Diouf, B, Eerola, T, Evangelou, E, Filipp, F, Klump, H, Kurgan, L, Smith, SS, Terrier, O, Tuttle, N, Brown, P, Zhou, Y, Tan, AC, El-Esawi, MA, Liehr, T, Blanck, O, Gladue, DP, Almeida, GMF, Cernava, T, Sorzano, CO, Yeung, AWK, Engel, MS, Chandrasekaran, AR, Muth, T, Staege, MS, Daulatabad, SV, Widera, D, Zhang, J, Meule, A, Honjo, K, Pourret, O, Yin, CC, Zhang, Z, Cascella, M, Flegel, WA, Goodyear, CS, van Raaij, MJ, Bukowy-Bieryllo, Z, Campana, LG, Kurniawan, NA, Lalaouna, D, Hüttner, FJ, Ammerman, BA, Ehret, F, Cobine, PA, Tan, EC, Han, H, Xia, W, McCrum, C, Dings, RPM, Marinello, F, Nilsson, H, Nixon, B, Voskarides, K, Yang, L, Costa, VD, Bengtsson-Palme, J, Bradshaw, W, Grimm, DG, Kumar, N, Martis, E, Prieto, D, Sabnis, SC, Amer, SEDR, Liew, AWC, Perco, P, Rahimi, F, Riva, G, Zhang, C, Devkota, HP, Ogami, K, Basharat, Z, Fierz, W, Siebers, R, Tan, KH, Boehme, KA, Brenneisen, P, Brown, JAL, Dalrymple, BP, Harvey, DJ, Ng, G, Werten, S, Bleackley, M, Dai, Z, Dhariwal, R, Gelfer, Y, Hartmann, MD, Miotla, P, Tamaian, R, Govender, P, Gurney-Champion, OJ, Kauppila, JH, Zhang, X, Echeverría, N, Subhash, S, Sallmon, H, Tofani, M, Bae, T, Bosch, O, Cuív, PO, Danchin, A, Diouf, B, Eerola, T, Evangelou, E, Filipp, F, Klump, H, Kurgan, L, Smith, SS, Terrier, O, and Tuttle, N
Abstract: Document recommendation systems for locating relevant literature have mostly relied on methods developed a decade ago. This is largely due to the lack of a large offline gold-standard benchmark of relevant documents that cover a variety of research fields such that newly developed literature search techniques can be compared, improved and translated into practice. To overcome this bottleneck, we have established the RElevant LIterature SearcH consortium consisting of more than 1500 scientists from 84 countries, who have collectively annotated the relevance of over 180 000 PubMed-listed articles with regard to their respective seed (input) article/s. The majority of annotations were contributed by highly experienced, original authors of the seed articles. The collected data cover 76% of all unique PubMed Medical Subject Headings descriptors. No systematic biases were observed across different experience levels, research fields or time spent on annotations. More importantly, annotations of the same document pairs contributed by different scientists were highly concordant. We further show that the three representative baseline methods used to generate recommended articles for evaluation (Okapi Best Matching 25, Term Frequency-Inverse Document Frequency and PubMed Related Articles) had similar overall performances. Additionally, we found that these methods each tend to produce distinct collections of recommended articles, suggesting that a hybrid method may be required to completely capture all relevant articles. The established database server located at https://relishdb.ict.griffith.edu.au is freely available for the downloading of annotation data and the blind testing of new methods. We expect that this benchmark will be useful for stimulating the development of new powerful techniques for title and title/abstract-based search engines for relevant articles in biomedical science.
Published: 2019

2. Chemical Modification of a Dehydratase Enzyme Involved in Bacterial Virulence by an Ammonium Derivative: Evidence of its Active Site Covalent Adduct

Author: Alejandro Beceiro, Marta Martínez-Guitián, Emilio Lence, van Raaij Mj, Paul Thompson, Concepción González-Bello, Alastair R. Hawkins, José M. Otero, L. Tizon, Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares, and Universidade de Santiago de Compostela. Departamento de Bioquímica e Bioloxía Molecular
Subjects: Staphylococcus aureus, Stereochemistry, Reaction intermediate, Molecular Dynamics Simulation, Biochemistry, Catalysis, Cell Line, Adduct, chemistry.chemical_compound, Colloid and Surface Chemistry, Catalytic Domain, Ammonium Compounds, Humans, Enzyme Inhibitors, Hydro-Lyases, Virulence, biology, Chemical modification, Active site, General Chemistry, Salmonella typhi, Ligand (biochemistry), Lyase, chemistry, Dehydratase, biology.protein, Derivative (chemistry)
Abstract: The first example of an ammonium derivative that causes a specific modification of the active site of type I dehydroquinase (DHQ1), a dehydratase enzyme that is a promising target for antivirulence drug discovery, is described. The resolution at 1.35 Å of the crystal structure of DHQ1 from Salmonella typhi chemically modified by this ammonium derivative revealed that the ligand is covalently attached to the essential Lys170 through the formation of an amine. The detection by mass spectroscopy of the reaction intermediates, in conjunction with the results of molecular dynamics simulations, allowed us to explain the inhibition mechanism and the experimentally observed differences between S. typhi and Staphylococcus aureus enzymes. The results presented here reveal that the replacement of Phe225 in St-DHQ1 by Tyr214 in Sa-DHQ1 and its hydrogen bonding interaction with the conserved water molecule observed in several crystal structures protects the amino adduct against further dehydration/aromatization reactions. In contrast, for the St-DHQ1 enzyme, the carboxylate group of Asp114, with the assistance of this water molecule, would trigger the formation of a Schiff base that can undergo further dehydration reactions until full aromatization of the cyclohexane ring is achieved. Moreover, in vitro antivirulence studies showed that the reported compound is able to reduce the ability of Salmonella Enteritidis to kill A459 respiratory cells. These studies have identified a good scaffold for the design of irreversible inhibitors that can be used as drugs and has opened up new opportunities for the development of novel antivirulence agents by targeting the DHQ1 enzyme Financial support from the Spanish Ministry of Science and Innovation (SAF2013-42899-R), Xunta de Galicia (GRC2013-041), and the European Regional Development Fund (ERDF) is gratefully acknowledged. E.L. thanks the Xunta de Galicia for his postdoctoral fellowship. A.B. thanks the Miguel Servet Programme ISCIII-FEDER (CP13/00226) and the ISCIIIGeneral Subdirection of Assesment and Promotion of the Research (PI14/00059) for financial support SI
Published: 2015

3. Exploring the Water-Binding Pocket of the Type II Dehydroquinase Enzyme in the Structure-Based Design of Inhibitors

Author: B. Blanco, José M. Otero, Concepción González-Bello, A. Peon, Paul Thompson, Alastair R. Hawkins, A. Sedes, van Raaij Mj, Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares, and Universidade de Santiago de Compostela. Departamento de Bioquímica e Bioloxía Molecular
Subjects: chemistry.chemical_classification, biology, Arginine, Stereochemistry, Active site, Water, Crystal structure, Molecular Dynamics Simulation, Lyase, Residue (chemistry), chemistry.chemical_compound, Structure-Activity Relationship, Enzyme, chemistry, Drug Design, Drug Discovery, biology.protein, Molecular Medicine, Carboxylate, Enzyme Inhibitors, Water binding, Crystallization, Hydro-Lyases
Abstract: Structural and computational studies to explore the WAT1 binding pocket in the structure-based design of inhibitors against the type II dehydroquinase (DHQ2) enzyme are reported. The crystal structures of DHQ2 from M. tuberculosis in complex with four of the reported compounds are described. The electrostatic interaction observed between the guanidinium group of the essential arginine and the carboxylate group of one of the inhibitors in the reported crystal structures supports the recently suggested role of this arginine as the residue that triggers the release of the product from the active site. The results of the structural and molecular dynamics simulation studies revealed that the inhibitory potency is favored by promoting interactions with WAT1 and the residues located within this pocket and, more importantly, by avoiding situations where the ligands occupy the WAT1 binding pocket. The new insights can be used to advantage in the structure-based design of inhibitors Financial support from the Spanish Ministry of Science and Innovation (Grant SAF2010-15076) and the Xunta de Galicia (Grant GRC2013/041) is gratefully acknowledged. B.B. and A.P. thank the Spanish Ministry of Education for their respective FPU fellowships. A.S. thanks the Spanish Ministry of Economy and Competitiveness for her FPI fellowship. J.M.O. thanks the Xunta de Galicia for a Plan I2C postdoctoral fellowship SI
Published: 2014

4. Mycobacterium tuberculosis Shikimate Kinase Inhibitors: Design and Simulation Studies of the Catalytic Turnover

Author: van Raaij Mj, Antonio L. Llamas-Saiz, Carmela Garcia-Doval, Emilio Lence, Heather K. Lamb, José M. Otero, Alastair R. Hawkins, Concepción González-Bello, Prado, B. Blanco, Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares, and Universidade de Santiago de Compostela. Departamento de Bioquímica e Bioloxía Molecular
Subjects: Stereochemistry, Shikimic Acid, medicine.disease_cause, Biochemistry, Shikimate kinase, Catalysis, Mycobacterium tuberculosis, chemistry.chemical_compound, Colloid and Surface Chemistry, Catalytic Domain, medicine, Transferase, Enzyme Inhibitors, chemistry.chemical_classification, biology, Chemistry, Substrate (chemistry), Pathogenic bacteria, General Chemistry, Shikimic acid, biology.organism_classification, Adenosine Diphosphate, Phosphotransferases (Alcohol Group Acceptor), Enzyme, Drug Design, Biocatalysis
Abstract: Shikimate kinase (SK) is an essential enzyme in several pathogenic bacteria and does not have any counterpart in human cells, thus making it an attractive target for the development of new antibiotics. The key interactions of the substrate and product binding and the enzyme movements that are essential for catalytic turnover of the Mycobacterium tuberculosis shikimate kinase enzyme (Mt-SK) have been investigated by structural and computational studies. Based on these studies several substrate analogs were designed and assayed. The crystal structure of Mt-SK in complex with ADP and one of the most potent inhibitors has been solved at 2.15 Å. These studies reveal that the fixation of the diaxial conformation of the C4 and C5 hydroxyl groups recognized by the enzyme or the replacement of the C3 hydroxyl group in the natural substrate by an amino group is a promising strategy for inhibition because it causes a dramatic reduction of the flexibility of the LID and shikimic acid binding domains. Molecular dynamics simulation studies showed that the product is expelled from the active site by three arginines (Arg117, Arg136, and Arg58). This finding represents a previously unknown key role of these conserved residues. These studies highlight the key role of the shikimic acid binding domain in the catalysis and provide guidance for future inhibitor designs Financial support from ́ the Spanish Ministry of Economy and Competitiveness (SAF2010-15076 to CGB and BFU2011-24843 to M.J.vR.) and the Xunta de Galicia (10PXIB2200122PR and GRC2010/ 12) is gratefully acknowledged. B.B. thanks the Spanish Ministry of Education for her FPU fellowship. V.P. and C.G.D. thank the Spanish Ministry of Economy and Competitiveness for their respective FPI fellowships. J.M.O. thanks the Xunta de Galicia for a Plan I2C postdoctoral fellowship SI
Published: 2013

5. F0 Membrane Domain of ATP Synthase from Bovine Heart Mitochondria: Purification, Subunit Composition, and Reconstitution with F1-ATPase

Author: van Raaij Mj, Griffiths De, Ian Collinson, J M Skehel, Michael J. Runswick, Ian M. Fearnley, John E. Walker, and Susan K. Buchanan
Subjects: Biochemistry, biology, ATP synthase, Membrane protein, ATP synthase gamma subunit, Mitochondrial Membrane Protein, Chemistry, Protein subunit, Peripheral membrane protein, biology.protein, Submitochondrial particle, Venturicidin
Abstract: The Fo membrane domain of the F1Fo-ATP synthase complex has been purified from bovine heart mitochondria. The purification procedure involves the removal of peripheral membrane proteins, including F1-ATPase, from submitochondrial particles with guanidine hydrochloride, followed by extraction of Fo and other membrane proteins from the stripped membranes in the presence of the detergent n-dodecyl beta-D-maltoside. Fo was then purified by ion-exchange and dye ligand chromatography in the presence of the same detergent. Approximately 15 mg of pure Fo was recovered from 1.8 g of mitochondrial membrane protein. The purified Fo is a complex of nine different polypeptides. They are subunits a, b, c, d, e, F6, and A6L characterized before in F1Fo-ATPase preparations, and two new hitherto undetected subunits, named f and g. The sequences of subunits f and g have been determined. They are not related significantly to any known protein, but subunit f appears to contain a membrane-spanning alpha-helix. Proteins f and g are also present in approximately stoichiometric amounts in a highly purified preparation of intact F1Fo-ATPase, and so it is concluded that they are authentic subunits of the bovine enzyme with unknown functions. Dibutyltin 3-hydroxyflavone, an inhibitor of F1Fo-ATPase, also binds to the purified Fo in detergent and competes for binding with venturicidin. In the presence of F1 and OSCP, the purified Fo was reassembled into the intact F1Fo-ATPase complex. Therefore, this procedure provides a relatively abundant source of pure and functional Fo that is suitable for structural analysis.
Published: 1994

6. High Yield Production of a Soluble Human Interleukin-3 Variant from E. coli with Wild-Type Bioactivity and Improved Radiolabeling Properties

Author: van Raaij, MJ, Hercus, TR, Barry, EF, Dottore, M, McClure, BJ, Webb, AI, Lopez, AF, Young, IG, Murphy, JM, van Raaij, MJ, Hercus, TR, Barry, EF, Dottore, M, McClure, BJ, Webb, AI, Lopez, AF, Young, IG, and Murphy, JM
Abstract: Human interleukin-3 (hIL-3) is a polypeptide growth factor that regulates the proliferation, differentiation, survival and function of hematopoietic progenitors and many mature blood cell lineages. Although recombinant hIL-3 is a widely used laboratory reagent in hematology, standard methods for its preparation, including those employed by commercial suppliers, remain arduous owing to a reliance on refolding insoluble protein expressed in E. coli. In addition, wild-type hIL-3 is a poor substrate for radio-iodination, which has been a long-standing hindrance to its use in receptor binding assays. To overcome these problems, we developed a method for expression of hIL-3 in E. coli as a soluble protein, with typical yields of >3mg of purified hIL-3 per litre of shaking microbial culture. Additionally, we introduced a non-native tyrosine residue into our hIL-3 analog, which allowed radio-iodination to high specific activities for receptor binding studies whilst not compromising bioactivity. The method presented herein provides a cost-effective and convenient route to milligram quantities of a hIL-3 analog with wild-type bioactivity that, unlike wild-type hIL‑3, can be efficiently radio-iodinated for receptor binding studies.
Published: 2013

7. [11] Structural analysis of ATP synthase from bovine heart mitochondria

Author: Ian Collinson, John E. Walker, van Raaij Mj, and Michael J. Runswick
Subjects: chemistry.chemical_compound, Protein structure, Biochemistry, chemistry, biology, ATP synthase, ATP synthase gamma subunit, ATPase, biology.protein, Submitochondrial particle, Mitochondrion, Cell fractionation, Adenosine triphosphate
Abstract: Publisher Summary This chapter discusses the structural analysis of Adenosine triphosphate (ATP) synthase from bovine heart mitochondria and the purification and crystallization of bovine F 1 -ATPase, the purification and characterization of monodisperse bovine F 1 F 0 -ATPase and F 0 , the bacterial expression and purification of the bovine ATPase inhibitor protein, and bovine ATPase and the reconstitution of the stalk and the F 1 stalk complexes. The membrane association and the complexity of ATP synthase remain as obstacles that impede progress toward this objective. Pure monodisperse bovine F 1 F 0 -ATPase can be prepared from heart mitochondria as a product of a multi-enzyme preparation based on chromatography for the isolation of respiratory enzymes from mitochondria. Alternatively, it can be prepared from mitochondrial membranes by extraction with dodecyl-β-d-maltoside and chromatography on Diethylaminoethyl (DEAE) cellulose. The chapter concludes with the discussion on the interactions between F 1 -ATPase and various subunits of F 1 F 0 -ATPase.
Published: 1995

8. Large expert-curated database for benchmarking document similarity detection in biomedical literature search

Author: Zeineb, Zian, Brown, Peter, Tan, Aik-Choon, El-Esawi, Mohamed A., Liehr, Thomas, Blanck, Oliver, Gladue, Douglas P., Almeida, Gabriel M. F., Cernava, Tomislav, Sorzano, Carlos O., Yeung, Andy W. K., Engel, Michael S., Chandrasekaran, Arun Richard, Muth, Thilo, Staege, Martin S., Daulatabad, Swapna V., Widera, Darius, Zhang, Junpeng, Meule, Adrian, Honjo, Ken, Pourret, Olivier, Yin, Cong-Cong, Zhang, Zhongheng, Cascella, Marco, Flegel, Willy A., Goodyear, Carl S., Raaij, Mark J. van, Bukowy-Bieryllo, Zuzanna, Campana, Luca G., Kurniawan, Nicholas A., Lalaouna, David, Hüttner, Felix J., Ammerman, Brooke A., Ehret, Felix, Cobine, Paul A., Tan, Ene-Choo, Han, Hyemin, Xia, Wenfeng, McCrum, Christopher, Dings, Ruud P. M., Marinello, Francesco, Nilsson, Henrik, Nixon, Brett, Voskarides, Konstantinos, Yang, Long, Costa, Vincent D., Bengtsson-Palme, Johan, Bradshaw, William, Grimm, Dominik G., Kumar, Nitin, Martis, Elvis, Prieto, Daniel, Sabnis, Sandeep C., Amer, Said E. D. R., Liew, Alan W. C., Perco, Paul, Rahimi, Farid, Riva, Giuseppe, Zhang, Chongxing, Devkota, Hari P., Ogami, Koichi, Basharat, Zarrin, Fierz, Walter, Siebers, Robert, Tan, Kok-Hian, Boehme, Karen A., Brenneisen, Peter, Brown, James A. L., Dalrymple, Brian P., Harvey, David J., Ng, Grace, Werten, Sebastiaan, Bleackley, Mark, Dai, Zhanwu, Dhariwal, Raman, Gelfer, Yael, Hartmann, Marcus D., Miotla, Pawel, Tamaian, Radu, Govender, Pragashnie, Gurney-Champion, Oliver J., Kauppila, Joonas H., Zhang, Xiaolei, Echeverría, Natalia, Subhash, Santhilal, Sallmon, Hannes, Tofani, Marco, Bae, Taeok, Bosch, Oliver, Cuív, Páraic O., Danchin, Antoine, Diouf, Barthelemy, Eerola, Tuomas, Evangelou, Evangelos, Filipp, Fabian V., Klump, Hannes, Kurgan, Lukasz, Smith, Simon S., Terrier, Olivier, Tuttle, Neil, Ascher, David B., Janga, Sarath C., Schulte, Leon N., Becker, Daniel, Browngardt, Christopher, Bush, Stephen J., Gaullier, Guillaume, Ide, Kazuki, Meseko, Clement, Werner, Gijsbert D. A., Zaucha, Jan, Al-Farha, Abd A., Greenwald, Noah F., Popoola, Segun I., Rahman, Md Shaifur, Xu, Jialin, Yang, Sunny Y., Hiroi, Noboru, Alper, Ozgul M., Baker, Chris I., Bitzer, Michael, Chacko, George, Debrabant, Birgit, Dixon, Ray, Forano, Evelyne, Gilliham, Matthew, Kelly, Sarah, Klempnauer, Karl-Heinz, Lidbury, Brett A., Lin, Michael Z., Lynch, Iseult, Ma, Wujun, Maibach, Edward W., Mather, Diane E., Nandakumar, Kutty S., Ohgami, Robert S., Parchi, Piero, Tressoldi, Patrizio, Xue, Yu, Armitage, Charles, Barraud, Pierre, Chatzitheochari, Stella, Coelho, Luis P., Diao, Jiajie, Doxey, Andrew C., Hu, Pingzhao, Kaiser, Stefan, Mitchell, Kate M., Salama, Mohamed F., Shabalin, Ivan G., Song, Haijun, Stevanovic, Dejan, Yadollahpour, Ali, Zeng, Erliang, Zinke, Katharina, Alimba, C. G., Beyene, Tariku J., Cao, Zehong, Chan, Sherwin S., Gatchell, Michael, Kleppe, Andreas, Piotrowski, Marcin, Torga, Gonzalo, Woldesemayat, Adugna A., Cosacak, Mehmet I., Haston, Scott, Ross, Stephanie A., Williams, Richard, Wong, Alvin, Abramowitz, Matthew K., Effiong, Andem, Lee, Senhong, Abid, Muhammad Bilal, Agarabi, Cyrus, Alaux, Cedric, Albrecht, Dirk R., Atkins, Gerald J., Beck, Charles R., Bonvin, A. M. J. J., Bourke, Emer, Brand, Thomas, Braun, Ralf J., Bull, James A., Cardoso, Pedro, Carter, Dee, Delahay, Robin M., Ducommun, Bernard, Duijf, Pascal H. G., Epp, Trevor, Eskelinen, Eeva-Liisa, Fallah, Mazyar, Farber, Debora B., Fernandez-Triana, Jose, Feyerabend, Frank, Florio, Tullio, Friebe, Michael, Furuta, Saori, Gabrielsen, Mads, Gruber, Jens, Grybos, Malgorzata, Han, Qian, Heinrich, Michael, Helanterä, Heikki, Huber, Michael, Jeltsch, Albert, Jiang, Fan, Josse, Claire, Jurman, Giuseppe, Kamiya, Haruyuki, Keersmaecker, Kim de, Kristiansson, Erik, Leeuw, Frank-Erik de, Li, Jiuyong, Liang, Shide, Lopez-Escamez, Jose A., Lopez-Ruiz, Francisco J., Marchbank, Kevin J., Marschalek, Rolf, Martín, Carmen S., Miele, Adriana E., Montagutelli, Xavier, Morcillo, Esteban, Nicoletti, Rosario, Niehof, Monika, O’Toole, Ronan, Ohtomo, Toshihiko, Oster, Henrik, Palma, Jose-Alberto, Paterson, Russell, Peifer, Mark, Portilla, Maribel, Portillo, M. C., Pritchard, Antonia L., Pusch, Stefan, Raghava, Gajendra P. S., Roberts, Nicola J., Ross, Kehinde, Schuele, Birgitt, Sergeant, Kjell, Shen, Jun, Stella, Alessandro, Sukocheva, Olga, Uversky, Vladimir N., Vanneste, Sven, Villet, Martin H., Viveiros, Miguel, Vorholt, Julia A., Weinstock, Christof, Yamato, Masayuki, Zabetakis, Ioannis, Zhao, Xin, Ziegler, Andreas, Aizat, Wan M., Atlas, Lauren, Bridges, Kristina M., Chakraborty, Sayan, Deschodt, Mieke, Domingues, Helena S., Esfahlani, Shabnam S., Falk, Sebastian, Guisado, J. L., Kane, Nolan C., Kueberuwa, Gray, Lau, Colleen L., Liang, Dai, Liu, Enwu, Luu, Andreas M., Ma, Chuang, Ma, Lisong, Moyer, Robert, Norris, Adam D., Panthee, Suresh, Parsons, Jerod R., Peng, Yousong, Pinto, Inês Mendes, Reschke, Cristina R., Sillanpää, Elina, Stewart, Christopher J., Uhle, Florian, Yang, Hui, Zhou, Kai, Zhu, Shu, Ashry, Mohamed, Bergsland, Niels, Berthold, Maximilian, Chen, Chang-Er, Colella, Vito, Cuypers, Maarten, Eskew, Evan A., Fan, Xiao, Gajda, Maksymilian, Gonzálezlez-Prendes, Rayner, Goodin, Amie, Graham, Emily B., Groen, Ewout J. N., Gutiérrez-Sacristán, Alba, Habes, Mohamad, Heffler, Enrico, Higginbottom, Daniel B., Janzen, Thijs, Jayaraman, Jayakumar, Jibb, Lindsay A., Jongen, Stefan, Kinyanjui, Timothy, Koleva-Kolarova, Rositsa G., Li, Zhixiu, Liu, Yu-Peng, Lund, Bjarte A., Lussier, Alexandre A., Ma, Liping, Mier, Pablo, Moore, Matthew D., Nagler, Katja, Orme, Mark W., Pearson, James A., Prajapati, Anilkumar S., Saito, Yu, Tröder, Simon E., Uchendu, Florence, Verloh, Niklas, Voutchkova, Denitza D., Abu-Zaid, Ahmed, Bakkach, Joaira, Baumert, Philipp, Dono, Marcos, Hanson, Jack, Herbelet, Sandrine, Hobbs, Emma, Kulkarni, Ameya, Kumar, Narendra, Liu, Siqi, Loft, Nikolai D., Reddan, Tristan, Senghore, Thomas, Vindin, Howard, Xu, Haotian, Bannon, Ross, Chen, Branson, Cheung, Johnny T. K., Cooper, Jeffrey, Esnakula, Ashwini K., Feghali, Karine A., Ghelardi, Emilia, Gnasso, Agostino, Horbar, Jeffrey, Lai, Hei M., Li, Jian, Ma, Lan, Ma, Ruiyan, Pan, Zihang, Peres, Marco A., Pranata, Raymond, Seow, Esmond, Sydes, Matthew, Testoni, Ines, Westermair, Anna L., Yang, Yongliang, Afnan, Masoud, Albiol, Joan, Albuquerque, Lucia G., Amiya, Eisuke, Amorim, Rogerio M., An, Qianli, Andersen, Stig U., Aplin, John D., Argyropoulos, Christos, Asmann, Yan W., Assaeed, Abdulaziz M., Atanasov, Atanas G., Atchison, David A., Avery, Simon V., Avillach, Paul, Baade, Peter D., Backman, Lars, Badie, Christophe, Baldi, Alfonso, Ball, Elizabeth, Bardot, Olivier, Barnett, Adrian G., Basner, Mathias, Batra, Jyotsna, Bazanova, O. M., Beale, Andrew, Beddoe, Travis, Bell, Melanie L., Berezikov, Eugene, Berners-Price, Sue, Bernhardt, Peter, Berry, Edward, Bessa, Theolis B., Billington, Craig, Birch, John, Blakely, Randy D., Blaskovich, Mark A. T., Blum, Robert, Boelaert, Marleen, Bogdanos, Dimitrios, Bosch, Carles, Bourgoin, Thierry, Bouvard, Daniel, Boykin, Laura M., Bradley, Graeme, Braun, Daniel, Brownlie, Jeremy, Brühl, Albert, Burt, Austin, Butler, Lisa M., Byrareddy, Siddappa N., Byrne, Hugh J., Cabantous, Stephanie, Calatayud, Sara, Candal, Eva, Carlson, Kimberly, Casillas, Sònia, Castelvetro, Valter, Caswell, Patrick T., Cavalli, Giacomo, Cerovsky, Vaclav, Chagoyen, Monica, Chen, Chang-Shi, Chen, Dong F., Chen, Hao, Chen, Hui, Chen, Jui-Tung, Chen, Yinglong, Cheng, Changxiu, Cheng, Jianlin, Chinapaw, Mai, Chinopoulos, Christos, Cho, William C. S., Chong, Lillian, Chowdhury, Debashish, Chwalibog, Andre, Ciresi, A., Cockcroft, Shamshad, Conesa, Ana, Cook, Penny A., Cooper, David N., Coqueret, Olivier, Corea, Enoka M., Costa, Elisio, Coupland, Carol, Crawford, Stephanie Y., Cruz, Aparecido D., Cui, Huijuan, Cui, Qiang, Culver, David C., D’Angiulli, Amedeo, Dahms, Tanya E. S., Daigle, France, Dalgleish, Raymond, Danielsen, Håvard E., Darras, Sébastien, Davidson, Sean M., Day, David A., Degirmenci, Volkan, Demaison, Luc, Devriendt, Koenraad, Ding, Jiandong, Dogan, Yunus, Dong, X. C., Donner, Claudio F., Dressick, Walter, Drevon, Christian A., Duan, Huiling, Ducho, Christian, Dumaz, Nicolas, Dwarakanath, Bilikere S., Ebell, Mark H., Eisenhardt, Steffen, Elkum, Naser, Engel, Nadja, Erickson, Timothy B., Fairhead, Michael, Faville, Marty J., Fejzo, Marlena S., Festa, Fernanda, Feteira, Antonio, Flood-Page, Patrick, Forsayeth, John, Fox, Simon A., Franks, Steven J., Frentiu, Francesca D., Frilander, Mikko J., Fu, Xinmiao, Fujita, Satoshi, Galea, Ian, Galluzzi, Luca, Gani, Federica, Ganpule, Arvind P., García-Alix, Antonio, Gedye, Kristene, Giordano, Maurizio, Giunta, Cecilia, Gleeson, Paul A., Goarant, Cyrille, Gong, Haipeng, Gora, Diop, Gough, Michael J., Goyal, Ravinder, Graham, Kathryn E., Grande-Pérez, Ana, Graves, Patricia M., Greidanus, Harm, Grice, Darren, Grunau, Christoph, Gumulya, Yosephine, Guo, Yabin, Gurevich, Vsevolod V., Gusev, Oleg, Hacker, Elke, Hage, Steffen R., Hagen, Guy, Hahn, Steven, Haller, Dagmar M., Hammerschmidt, Sven, Han, Jianwei, Han, Renzhi, Handfield, Martin, Hapuarachchi, Hapuarachchige C., Harder, Timm, Hardingham, Jennifer E., Heck, Michelle, Heers, Marcel, Hew, Khe F., Higuchi, Yohei, Hilaire, Cynthia St, Hilton, Rachel, Hodzic, Enisa, Hone, Andrew, Hongoh, Yuichi, Hu, Guoku, Huber, Heinz P., Hueso, Luis E., Huirne, Judith, Hurt, Lisa, Idborg, Helena, Ikeo, Kazuho, Ingley, Evan, Jakeman, Philip M., Jensen, Arne, Jia, Hong, Jia, Husen, Jia, Shuqin, Jiang, Jianping, Jiang, Xingyu, Jin, Yi, Jo, Daehyun, Johnson, Andrew M., Johnston, Marie, Jonscher, Karen R., Jorens, Philippe G., Jorgensen, Jens O. L., Joubert, Johan W., Jung, Sin-Ho, Junior, Antonio M., Kahan, Thomas, Kamboj, Sunjeev K., Kang, Yong-Kook, Karamanos, Yannis, Karp, Natasha A., Kelly, Ryan, Kenna, Ralph, Kennedy, Jonathan, Kersten, Birgit, Khalaf, Roy A., Khalid, Javaria M., Khatlani, T., Khider, Tarig, Kijanka, Gregor S., King, Sarah R. B., Kluz, Tomasz, Knox, Paul, Kobayashi, Tatsuya, Koch, Karl-Wilhelm, Kohonen-Corish, Maija R. J., Kong, Xiangpeng, Konkle-Parker, Deborah, Korpela, Kalevi M., Kostrikis, Leondios G., Kraiczy, Peter, Kratz, Harald, Krause, Günter, Krebsbach, Paul H., Kristensen, Søren R., Kumari, Prerna, Kunimatsu, Akira, Kurdak, Hatice, Kwon, Young D., Lachat, Carl, Lagisz, Malgorzata, Laky, Brenda, Lammerding, Jan, Lange, Matthias, Larrosa, Mar, Laslett, Andrew L., LeClair, Elizabeth E., Lee, Kyung-Woo, Lee, Ming-Yih, Lee, Moon-Soo, Li, Genyuan, Li, Jiansheng, Lieb, Klaus, Lim, Yau Y., Lindsey, Merry L., Line, Paul-Dag, Liu, Dengcai, Liu, Fengbin, Liu, Haiyan, Liu, Hongde, Lloyd, Vett K., Lo, Te-Wen, Locci, Emanuela, Loidl, Josef, Lorenzen, Johan, Lorkowski, Stefan, Lovell, Nigel H., Lu, Hua, Lu, Wei, Lu, Zhiyong, Luengo, Gustavo S., Lundh, Lars-Gunnar, Lysy, Philippe A., Mabb, Angela, Mack, Heather G., Mackey, David A., Mahdavi, S. R., Maher, Pamela, Maher, Toby, Maity, Sankar N., Malgrange, Brigitte, Mamoulakis, Charalampos, Mangoni, Arduino A., Manke, Thomas, Manstead, Antony S. R., Mantalaris, Athanasios, Marsal, Jan, Marschall, Hanns-Ulrich, Martin, Francis L., Martinez-Raga, Jose, Martinez-Salas, Encarnacion, Mathieu, Daniel, Matsui, Yoichi, Maza, Elie, McCutcheon, James E., McKay, Gareth J., McMillan, Brian, McMillan, Nigel, Meads, Catherine, Medina, Loreta, Merrick, B. Alex, Metzger, Dennis W., Meunier, Frederic A., Michaelis, Martin, Micheau, Olivier, Mihara, Hisaaki, Mintz, Eric M., Mizukami, Takuo, Moalic, Yann, Mohapatra, D. P., Monteiro, Antonia, Montes, Matthieu, Moran, John V., Morozov, Sergey Y., Mort, Matthew, Murai, Noriyuki, Murphy, Denis J., Murphy, Susan K., Murray, Shauna A., Naganawa, Shinji, Nammi, Srinivas, Nasios, Grigorios, Natoli, Roman M., Nguyen, Frederique, Nicol, Christine, Nieuwerburgh, Filip van, Nilsen, Erlend B., Nobile, Clarissa J., O’Mahony, Margaret, Ohlsson, Sophie, Olatunbosun, Oluremi, Olofsson, Per, Ortiz, Alberto, Ostrikov, Kostya, Otto, Siegmar, Outeiro, Tiago F., Ouyang, Songying, Paganoni, Sabrina, Page, Andrew, Palm, Christoph, Paradies, Yin, Parsons, Michael H., Parsons, Nick, Pascal, Pigny, Paul, Elisabeth, Peckham, Michelle, Pedemonte, Nicoletta, Pellizzon, Michael A., Petrelli, M., Pichugin, Alexander, Pinto, Carlos J. C., Plevris, John N., Pollesello, Piero, Polz, Martin, Ponti, Giovanna, Porcelli, Piero, Prince, Martin, Quinn, Gwendolyn P., Quinn, Terence J., Ramula, Satu, Rappsilber, Juri, Rehfeldt, Florian, Reiling, Jan H., Remacle, Claire, Rezaei, Mohsen, Riddick, Eric W., Ritter, Uwe, Roach, Neil W., Roberts, David D., Robles, Guillermo, Rodrigues, Tiago, Rodriguez, Cesar, Roislien, Jo, Roobol, Monique J., Rowe, J. Alexandra, Ruepp, Andreas, Ruitenbeek, Jan van, Rust, Petra, Saad, Sonia, Sack, George H., Santos, Manuela, Saudemont, Aurore, Sava, Gianni, Schrading, Simone, Schramm, Alexander, Schreiber, Martin, Schuler, Sidney, Schymkowitz, Joost, Sczyrba, Alexander, Seib, Kate L., Shi, Han-Ping, Shimada, Tomohiro, Shin, Jeon-Soo, Shortt, Colette, Silveyra, Patricia, Skinner, Debra, Small, Ian, Smeets, Paul A. M., So, Po-Wah, Solano, Francisco, Sonenshine, Daniel E., Song, Jiangning, Southall, Tony, Speakman, John R., Srinivasan, Mandyam V., Stabile, Laura P., Stasiak, Andrzej, Steadman, Kathryn J., Stein, Nils, Stephens, Andrew W., Stewart, Douglas I., Stine, Keith, Storlazzi, Curt, Stoynova, Nataliya V., Strzalka, Wojciech, Suarez, Oscar M., Sultana, Taranum, Sumant, Anirudha V., Summers, Mathew J., Sun, Gang, Tacon, Paul, Tanaka, Kozo, Tang, Haixu, Tanino, Yoshinori, Targett-Adams, Paul, Tayebi, Mourad, Tayyem, Reema, Tebbe, Christoph C., Telfer, Evelyn E., Tempel, Wolfram, Teodorczyk-Injeyan, Julita A., Thijs, Gert, Thorne, Sally, Thrift, Amanda G., Tiffon, Celine, Tinnefeld, Philip, Tjahjono, Daryono H., Tolle, Fabrice, Toth, Ervin, Tredici, Andria L. del, Tsapas, Apostolos, Tsirigotis, Konstantinos, Turak, Ayse, Tzotzos, George, Udo, Edet E., Utsumi, Toshiaki, Vaidyanathan, Subramanian, Vaillant, Michel, Valsesia, Armand, Vandenbroucke, Roosmarijn E., Veiga, Feliciano H., Vendrell, Marc, Vesk, Peter A., Vickers, Paul, Victor, Victor M., Villemur, Richard, Vohl, Marie-Claude, Voolstra, Christian R., Vuillemin, Anne, Wakelin, Steven, Waldron, Levi, Walsh, Laurence J., Wang, Amanda Y., Wang, Fuan, Wang, Yun, Watanabe, Yoichi, Weigert, Andreas, Wen, Jet-Chau, Wham, Carol, White, Ethan P., Wiener, Jan, Wilharm, Gottfried, Wilkinson, Simon, Willmann, Raffaella, Wilson, Coralie, Wirth, Brunhilde, Wojan, Timothy R., Wolff, Mathieu, Wong, Bryan M., Wu, Tzu-Wei, Wuerbel, Hanno, Xiao, Xiangshu, Xu, Dong, Xu, J. W., Xu, Jianping, Xue, Bin, Yalcin, Suayib, Yan, Hong, Yang, En-Cheng, Yang, Shiqi, Yang, Wei, Ye, Yuzhen, Ye, Zhi-Qiang, Yli-Kauhaluoma, Jari, Yoneyama, Hiroshi, Yu, Ying, Yuan, Guo-Cheng, Yuh, Chiou-Hwa, Zaccolo, Manuela, Zeng, Chen, Zevnik, Branko, Zhang, Chi, Zhang, Li, Zhang, Yingkai, Zhang, Yusen, Zhang, Zhiyong, Zhang, Zhong-Yin, Zhao, Yuan, Zhou, Min, Zuberbier, Torsten, Aanei, Carmen M., Ahmad, Rafi, Al-Lawama, Manar, Alanio, Alexandre, Allardyce, Judith, Alonso-Caneiro, David, Atack, John M., Baier, Dirk, Bansal, Abhisheka, Benezeth, Yannick, Berbesque, Colette, Berrevoet, Frederik, Biedermann, Peter H. W., Bijleveld, Erik, Bittner, Florian, Blombach, Fabian, Bos, Wouter van den, Boudreau, Shellie A., Bramoweth, Adam D., Braubach, Oliver, Cai, Yufeng, Campbell, Matthew, Cao, Zanxia, Catry, Thibault, Chen, Xin, Cheng, Shuiqin, Chung, Hee-Jung, Chávez-Fumagalli, Miguel A., Conway, Aaron, Costa, Bruno M., Cyr, Normand, Dean, Lorraine T., Denzel, Martin S., Dlamini, S. V., Dudley, Kevin J., Dufies, Maeva, Ecke, Thorsten, Eckweiler, Denitsa, Eixarch, Elisenda, El-Adawy, Hosny, Emmrich, Julius V., Eustace, Alex J., Falter-Wagner, Christine M., Fuss, Johannes, Gao, Jianzhao, Gill, Martin R., Gloyn, Liz, Goggs, Robert, Govinden, Usha, Greene, Garrett, Greiff, Victor, Grundle, D. S., Grüneberg, Patrick, Gumede, Nicksy, Haore, Gbaguidi, Harrison, Pille, Hoenner, Xavier, Hojsgaard, Diego, Hori, Hikaru, Ikonomopoulou, Maria P., Jeurissen, Patrick, Johnson, Daniel M., Kabra, Dhiraj, Kamagata, Koji, Karmakar, Chandan, Kasian, Olga, Kaye, Linda K., Khan, Murad M., Kim, Yong-Min, Kish, J. K., Kobold, Sebastian, Kohanbash, Gary, Kohls, Gregor, Kugler, Jan-Michael, Kumar, Gyanendra, Lacy-Colson, Jon, Latif, Asam, Lauschke, Volker M., Li, Bingling, Lim, Chinten J., Liu, Fang, Liu, Xiaodong, Lu, Jin-Jian, Lu, Qiang, Mahavadi, Poornima, Marzocchi, Ugo, McGarrigle, Christine A., Meerten, Tom van, Min, Rogier, Moal, Iain, Molari, Massimiliano, Molleman, Lucas, Mondal, Saiful R., Mortel, Thea van de, Moss, W. N., Moultos, Othonas A., Mukherjee, Maheswari, Nakayama, Kazuhiko, Narayan, Edward, Navaratnarajah, Neumann, Philipp-Alexander, Nie, Jiyun, Nie, Yingjiu, Niemeyer, Frank, Nolan, Fiona, Nwaiwu, Ogueri, Oldenmenger, Wendy H., Olumayede, Emmanuel, Ou, Jianhong, Pallebage-Gamarallage, Menuka, Pearce, Simon P., Pelkonen, Tuula, Pelleri, Maria C., Pereira, Joana L., Pheko, Mpho, Pinto, Karina A., Piovesan, Allison, Pluess, Michael, Podolsky, Illya M., Prescott, Julie, Qi, Dongchen, Qi, Xingshun, Raikou, Vaia D., Ranft, Andreas, Rhodes, Johanna, Rotge, Jean-Yves, Rowe, Anna D., Saggar, Manish, Schuon, Robert A., Shahid, Shaouli, Shalchyan, Vahid, Shirvalkar, Prasad, Shiryayev, Oleg, Singh, Jugpreet, Smout, Michael J., Soares, António, Song, Chunjiao, Srivastava, Kshitij, Srivastava, Rupesh K., Sun, Jim, Szabo, Attila, Szymanski, Wiktor, Tai, Chan N. P., Takeuchi, Hisashi, Tanadini-Lang, S., Tang, Fei, Tao, Wanyin, Theron, G., Tian, Chang F., Tian, Yu-Shi, Tuttle, Lisa M., Valenti, Anna, Verlot, Pierre, Walker, Mirella, Wang, Jun, Welter, Danielle, Winslade, Matthew, Wu, Dalei, Wu, Yi-Rui, Xiao, Han, Xu, Beisi, Xu, Juan, Xu, Ziyue, Yang, Dongdong, Yang, Mingjun, Yankilevich, Patricio, You, Yuyi, Yu, Chenglong, Zhan, Jian, Zhang, Gong, Zhang, Kai, Zhang, Tuo, Zhang, Yi, Zhao, Guoyan, Zhao, Jing, Zhou, Xiaofan, Zhu, Zhenxing, Ajani, Penelope A., Anazodo, Udunna C., Bagloee, Saeed A., Bail, Kasia, Bar, Ido, Bathelt, Joe, Benkeser, David, Bernier, Meghan L., Blanchard, Adam M., Boakye, Dominic W., Bonatsos, Vasileios, Boon, Michele H., Bouboulis, George, Bromfield, Elizabeth, Brown, Joshua, Bul, Kim C. M., Burton, Kathryn J., Butkowski, Eugene G., Carroll, Grace, Chao, Fengqing, Charrier, Elisabeth E., Chen, Xiaoyin, Chen, Yu-Chih, Chenguang, Choi, Jane R., Christoffersen, Tore, Comel, João C., Cosse, Cyril, Cui, Yanru, Dessel, Pieter van, Dhaval, Diodato, Daria, Duffey, Maelle, Dutt, Avik, Egea, Luis G., El-Said, Mohammed, Faye, Martin, Fernandez-Fernandez, Beatriz, Foley, Kieran G., Founou, Luria L., Fu, Fan, Gadelkareem, Rabea A., Galimov, Evgeny, Garip, Gulcan, Gemmill, Alison, Gouil, Quentin, Grey, James, Gridneva, Zoya, Grothe, Michel J., Grébert, Théophile, Guerrero, Fabricio, Guignard, Léo, Haenssgen, Marco J., Hasler, David, Holgate, Joan Y., Huang, Ancheng, Hulse-Kemp, Amanda M., Jean-Quartier, Claire, Jeon, Sang-Min, Jia, Yangyang, Jutzeler, Catherine, Kalatzis, Panagiotis, Karim, Masud, Karsay, Kathrin, Keitel, Anne, Kempe, Andreas, Keown, Jeremy R., Khoo, Chin M., Khwaja, Nyil, Kievit, Rogier A., Kosanic, Aleksandra, Koutoukidis, Dimitrios A., Kramer, Paul, Kumar, Dilip, Kırağ, Nükhet, Lanza, Giuseppe, Le, Thuc D., Leem, Jung W., Leightley, Daniel, Leite, Andreia, Lercher, Lukas, Li, Ying, Lim, Renly, Lima, Luiz R. A., Lin, Li, Ling, Tong, Liu, Yuchen, Liu, Zhonghua, Lu, Yao, Lum, Fok M., Luo, Hang, Machhi, Jatin, Macleod, Angus, Macwan, Isaac, Madala, Hanumantha R., Madani, Nima, Maio, Nicola de, Makowiecki, Kalina, Mallinson, Daniel J., Margelyte, Ruta, Maria, Caracausi, Markonis, Y., Marsili, Luca, Mavoa, Suzanne, McWilliams, Lorna, Megersa, Moa, Mendes, Caetano S. M., Menichetti, Julia, Mercieca-Bebber, Rebecca, Miller, Jack J., Minde, David-Paul M., Minges, Alexander, Mishra, Eleanor, Mishra, Virendra R., Moores, Carly, Morrice, Nicola, Moskalensky, Alexander E., Navarin, Nicolò, Negera, Edessa, Nolet, Philippe, Nordberg, Ana, Nordén, Rickard, Nowicki, Jessica P., Olova, Nelly, Olszewski, Paweł, Onzima, Robert, Pan, Chih-Long, Park, Charny, Park, Dong Ik, Park, Seyoung, Patil, Chandrashekhar D., Pedro, Sansoa A., Perry, Samuel R., Peter, Jessica, Peterson, Brent M., Pezzuolo, Andrea, Pozdnyakov, Ilya, Qian, Siyu, Qin, Lei, Rafe, Ali, Raote, Ishier, Raza, Ali, Rebl, Henrike, Refai, Osama, Regan, Tim, Richa, Tambi, Richardson, Mark F., Robinson, K. R., Rossoni, Luca, Rouet, Romain, Safaei, Soroush, Schneeberger, Pierre H. H., Schwotzer, Daniela, Sebastian, Agata, Selinski, Jennifer, Seltmann, Stefanie, Sha, Feng, Shalev, Nir, Shang, Jin-Long, Singer, Josef, Singh, Mandeep, Smith, Taylor, Solomon-Moore, Emma, Song, Lijuan, Soraggi, Samuele, Stanley, Ryan, Steckhan, Nico, Strobl, Frederic, Subissi, Lorenzo, Supriyanto, Irwan, Surve, Chinmay R., Suzuki, Tomo, Syme, Caitlin, Sörelius, Karl, Tang, Young, Tantawy, Marwa, Tennakoon, Sumudu, Teseo, Serafino, Toelzer, Christine, Tomov, Nikola, Tovar, Miguel, Tran, Linh, Tripathi, Sushil, Tuladhar, Anil M., Ukubuiwe, Azubuike C., Ung, Carolina O. L., Valgepea, Kaspar, Vatanparast, Hamid, Vidal, Arnau, Wang, Fang, Wang, Qing, Watari, Ricky, Webster, Rebecca, Webster, Ruth, Wei, Junnian, Wibowo, David, Wingenbach, Tanja S. H., Xavier, Rose M., Xiao, Shumin, Xiong, Peng, Xu, Shicai, Xu, Shilin, Yao, Ruifeng, Yao, Wen, Yin, Qinan, Yu, Yongbo, Zaitsu, Masayoshi, Zhan, Xiao-Yong, Zhang, Jilei, Zhang, Rongqiang, Zhang, Wei, Zhang, Xianglilan, Zheng, Shan, Zhou, Bailing, Zhou, Xiaoyan, Ahmad, Haroon, Akinwumi, Sayo A., Albery, Gregory F., Alhowimel, Ahmed, Ali, Junaid, Alshehri, Mansour, Alsuhaibani, Mohammed, Anikin, Andrey, Azubuike, Samuel O., Bach-Mortensen, Anders, Baltiansky, Lior, Bartas, Martin, Belachew, Kiflemariam Y., Bhardwaj, Vivek, Binder, Karin, Bland, Nicholas S., Boah, Michael, Bullen, Benjamin, Calabrò, Giovanna E., Callahan, Tiffany J., Cao, Bing, Chalmers, Kelsey, Chang, Wei, Che, Zhengping, Chen, Andrew T. Y., Chen, Haimin, Chen, Huaming, Chen, Youning, Chen, Zhao, Choi, YoungRok, Chowdhury, Mohiuddin A. K., Christensen, Martin R., Cooke, Robert S. C., Cottini, Marzia, Covington, Natalie V., Cunningham, Catriona, Delarocque, Julien, Devos, Lucie, Dhar, Aurup R., Ding, Ke-Feng, Dong, Kexian, Dong, Zheng, Dreyer, Niklas, Ekstrand, Chelsea, Fardet, Tanguy, Feleke, Berhanu E., Feurer, Thomas, Freitas, Angela, Gao, Tian, Asefa, N. G., Giganti, Francesco, Grabowski, Piotr, Guerra-Mora, José R., Guo, Chengying, Guo, Xinyi, Gupta, Himanshu, He, Shuonan, Heijne, Marloes, Heinemann, Stephanie, Hogrebe, Alexander, Huang, Zhengping, Iskander-Rizk, Sophinese, Iyer, Lavanya M., Jahan, Yasmin, James, Ameh S., Joel, Emmanuel, Joffroy, Bastian, Jégousse, Clara, Kambondo, George, Karnati, Priyanka, Kaya, Cihan, Ke, An, Kelly, Daniel, Kickert, Rob, Kidibule, Peter E., Kieselmann, Jennifer P., Kim, Hyeon J., Kitazawa, Takeshi, Lamberts, Aniek, Li, You, Liang, Huakang, Linn, Sabrina N., Litfin, Thomas, Liusuo, Wang, Lygirou, Vasiliki, Mahato, Ajay K., Mai, Zhi-Ming, Major, Rupert W., Mali, Samira, Mallis, Panagiotis, Mao, Wenzhi, Marvin-Dowle, Katie, Mason, Leanda D., Merideth, Ben, Merino-Plaza, Maria J., Merlaen, Britt, Messina, Rossella, Mishra, Anand K., Muhammad, Junaid, Musinguzi, Conrad, Nanou, Afroditi, Naqash, Amreen, Nguyen, Joe T., Nguyen, Thi T. H., Ni, Duan, Nida, Notcovich, Shirli, Ohst, Barnabas, Ollivier, Quinn R., Osses, Daniël F., Peng, Xiangda, Plantinga, Arnoud, Pulia, Michael, Rafiq, Muhammad, Raman, Ayush, Raucher-Chéné, Delphine, Rawski, Rafał, Ray, Asit, Razak, Lubna A., Rudolf, Kevin, Rusch, Peter, Schmidt, Axel, Schurr, Roey, Searles, Stephen, Sharma, Saurab, Sheehan, Barry, Shi, Chunhu, Shohayeb, Belal, Sommerlad, Andrew, Strehlow, Jan, Sun, Xianbao, Sundar, Raghav, Taherzadeh, Ghazaleh, Tahir, Nur D. M., Tang, Jun, Testa, Jean, Tian, Zhiqi, Tingting, Qian, Verheijen, Geert P., Vickstrom, Casey, Wang, Teng, Wang, Xiaomin, Wang, Zhenxing, Wei, Pan, Wilson, Alex, Wyart, Yassine, Abdul-Amir, Yousefzadeh, Abbas, Zare, Asma, Zeng, Zhen, Zhang, Chengrong, Zhang, Haowen, Zhang, Linxing, Zhang, Tongchuan, Zhang, Weijia, Zhang, Zhe, Zhou, Jianyu, Zhu, Dongjie, Adamo, Vincenzo, Adeyemo, Adebolajo A., Aggelidou, Maria, Al-Owaifeer, Adi M., Al-Riyami, Arwa Z., Alzghari, Saeed K., Andersen, Vibeke, Angus, Kathryn, Asaduzzaman, Muhammad, Asady, Hadi, Ato, Dai, Bai, Xiaoyong, Baines, Rebecca L., Ballantyne, Maghan, Ban, Bo, Beck, Jill, Ben-Nafa, Walid, Black, Emma, Blancher, Antoine, Blankstein, Ron, Bodagh, Neil, Borges, Paulo A. V., Brooks, Anastasia, Brox-Ponce, Josue, Brunetti, Arturo, Canham, Colin D., Carninci, Piero, Carvajal, Richard, Chang, Shun C., Chao, Jie, Chatterjee, Pranab, Chen, He, Chen, Yi-Chun, Chhatriwalla, Adnan K., Chikowe, Ibrahim, Chuang, Trees-Juen, Collevatti, Rosane G., Valera-Cornejo, Diego A., Cuenda, Ana, Dao, Myriam, Dauga, Delphine, Deng, Zaian, Devkota, Kiran, Doan, Lisa V., Elewa, Yaser H. A., Fan, Dongsheng, Faruk, Mohammed, Feifei, Shi, Ferguson, Trevor S., Fleres, Francesco, Foster, Emma J., Foster, C. Stephen, Furer, Tzvi, Gao, Yibo, Garcia-Rivera, Enid J., Gazdar, Adi, George, Ronald B., Ghosh, Sayantan, Gianchecchi, Elena, Gleason, Joshua M., Hackshaw, Allan, Hall, Adam, Hall, Richard, Harper, Paul, Hogg, William E., Huang, Guangqun, Hunter, Kylie E., IJzerman, Adriaan P., Jesus, Carlos, Jian, Gao, Jr, James S. Lewis, Kanj, Souha S., Kaur, Harsheen, Kelly, Shona, Kheir, Fayez, Kichatova, V. S., Kiyani, Musa, Klein, Reinhild, Kovesi, Tom, Kraschnewski, Jennifer L., Kumar, Addanki P., Labutin, Dmitry, Lazo-Langner, Alejandro, Leclercq, Guy, Li, Maoteng, Li, Qingchun, Li, Tangliang, Li, Yongzhe, Liao, Wei-Ting, Liao, Zheng-yin, Lin, Jessica, Lizer, J., Lobreglio, Giambattista, Lowies, Cher, Lu, Cheng, Majeed, Haroon, Martin, Adam, Martinez-Sobrido, Luis, Meresh, Edwin, Middelveen, Marianne, Mohebbi, Alireza, Mota, Jorge, Mozaheb, Zahra, Muyaya, Ley, Nandhakumar, Amar, Ng, Sheryl H. X., Obeidat, Monther, Oh, Deog-Hwan, Owais, Mohammed, Pace-Asciak, Pia, Panwar, Ajay, Park, Caroline, Patterson, Chris, Penagos-Tabaree, Felipe, Pianosi, Paolo T., Pinzi, Valentina, Pridans, Clare, Psaroulaki, Anna, Pujala, Ravi Kumar, Pulido-Arjona, Leonardo, Qi, Peng-Fei, Rahman, Proton, Rai, Nayanjot K., Rassaf, Tienush, Refardt, Julie, Ricciardi, Walter, Riess, Olaf, Rovas, Alexandros, Sacks, Frank M., Saleh, Sherif, Sampson, Christopher, Schmutz, Axel, Sepanski, Robert, Sharma, Neeraj, Singh, Manisha, Spearman, Paul, Subramaniapillai, Mehala, Swali, Ritu, Tan, Cher M., Tellechea, Juan I., Thomas, Lisa-Marie, Tong, Xin, Vavvas, Demetrios G., Veys, Ralf, Vitriol, Veronica, Wang, Horng-Dar, Wang, Jinhui, Wang, Jiucun, Waugh, Jason, Webb, S. A., Williams, Brendan A., Workman, Alan D., Xiang, Tingxiu, Xie, Li-Xin, Xu, Jun, Xu, Taosheng, Yang, Chongjun, Yoon, Jihoon G., Yuan, Christina M., Zaritsky, Arno, Zhang, Yao, Zhao, Haochen, Zuckerman, Hannah, Lyu, Ran, Pullan, Wayne, Zhou, Yaoqi, Gobet, Angélique, Sadoine, Margaux L., Ontwikkelingspsychologie (Psychologie, FMG), British Lung Foundation, Brown, P, Zhou, Y, Tan, A, El-Esawi, M, Liehr, T, Blanck, O, Gladue, D, Almeida, G, Cernava, T, Sorzano, C, Yeung, A, Engel, M, Chandrasekaran, A, Muth, T, Staege, M, Daulatabad, S, Widera, D, Zhang, J, Meule, A, Honjo, K, Pourret, O, Yin, C, Zhang, Z, Cascella, M, Flegel, W, Goodyear, C, van Raaij, M, Bukowy-Bieryllo, Z, Campana, L, Kurniawan, N, Lalaouna, D, Huttner, F, Ammerman, B, Ehret, F, Cobine, P, Tan, E, Han, H, Xia, W, Mccrum, C, Dings, R, Marinello, F, Nilsson, H, Nixon, B, Voskarides, K, Yang, L, Costa, V, Bengtsson-Palme, J, Bradshaw, W, Grimm, D, Kumar, N, Martis, E, Prieto, D, Sabnis, S, Amer, S, Liew, A, Perco, P, Rahimi, F, Riva, G, Zhang, C, Devkota, H, Ogami, K, Basharat, Z, Fierz, W, Siebers, R, Tan, K, Boehme, K, Brenneisen, P, Brown, J, Dalrymple, B, Harvey, D, Ng, G, Werten, S, Bleackley, M, Dai, Z, Dhariwal, R, Gelfer, Y, Hartmann, M, Miotla, P, Tamaian, R, Govender, P, Gurney-Champion, O, Kauppila, J, Zhang, X, Echeverria, N, Subhash, S, Sallmon, H, Tofani, M, Bae, T, Bosch, O, Cuiv, P, Danchin, A, Diouf, B, Eerola, T, Evangelou, E, Filipp, F, Klump, H, Kurgan, L, Smith, S, Terrier, O, Tuttle, N, Ascher, D, Janga, S, Schulte, L, Becker, D, Browngardt, C, Bush, S, Gaullier, G, Ide, K, Meseko, C, Werner, G, Zaucha, J, Al-Farha, A, Greenwald, N, Popoola, S, Rahman, S, Xu, J, Yang, S, Hiroi, N, Alper, O, Baker, C, Bitzer, M, Chacko, G, Debrabant, B, Dixon, R, Forano, E, Gilliham, M, Kelly, S, Klempnauer, K, Lidbury, B, Lin, M, Lynch, I, Ma, W, Maibach, E, Mather, D, Nandakumar, K, Ohgami, R, Parchi, P, Tressoldi, P, Xue, Y, Armitage, C, Barraud, P, Chatzitheochari, S, Coelho, L, Diao, J, Doxey, A, Gobet, A, Hu, P, Kaiser, S, Mitchell, K, Salama, M, Shabalin, I, Song, H, Stevanovic, D, Yadollahpour, A, Zeng, E, Zinke, K, Alimba, C, Beyene, T, Cao, Z, Chan, S, Gatchell, M, Kleppe, A, Piotrowski, M, Torga, G, Woldesemayat, A, Cosacak, M, Haston, S, Ross, S, Williams, R, Wong, A, Abramowitz, M, Effiong, A, Lee, S, Abid, M, Agarabi, C, Alaux, C, Albrecht, D, Atkins, G, Beck, C, Bonvin, A, Bourke, E, Brand, T, Braun, R, Bull, J, Cardoso, P, Carter, D, Delahay, R, Ducommun, B, Duijf, P, Epp, T, Eskelinen, E, Fallah, M, Farber, D, Fernandez-Triana, J, Feyerabend, F, Florio, T, Friebe, M, Furuta, S, Gabrielsen, M, Gruber, J, Grybos, M, Han, Q, Heinrich, M, Helantera, H, Huber, M, Jeltsch, A, Jiang, F, Josse, C, Jurman, G, Kamiya, H, de Keersmaecker, K, Kristiansson, E, de Leeuw, F, Li, J, Liang, S, Lopez-Escamez, J, Lopez-Ruiz, F, Marchbank, K, Marschalek, R, Martin, C, Miele, A, Montagutelli, X, Morcillo, E, Nicoletti, R, Niehof, M, O'Toole, R, Ohtomo, T, Oster, H, Palma, J, Paterson, R, Peifer, M, Portilla, M, Portillo, M, Pritchard, A, Pusch, S, Raghava, G, Roberts, N, Ross, K, Schuele, B, Sergeant, K, Shen, J, Stella, A, Sukocheva, O, Uversky, V, Vanneste, S, Villet, M, Viveiros, M, Vorholt, J, Weinstock, C, Yamato, M, Zabetakis, I, Zhao, X, Ziegler, A, Aizat, W, Atlas, L, Bridges, K, Chakraborty, S, Deschodt, M, Domingues, H, Esfahlani, S, Falk, S, Guisado, J, Kane, N, Kueberuwa, G, Lau, C, Liang, D, Liu, E, Luu, A, Ma, C, Ma, L, Moyer, R, Norris, A, Panthee, S, Parsons, J, Peng, Y, Pinto, I, Reschke, C, Sillanpaa, E, Stewart, C, Uhle, F, Yang, H, Zhou, K, Zhu, S, Ashry, M, Bergsland, N, Berthold, M, Chen, C, Colella, V, Cuypers, M, Eskew, E, Fan, X, Gajda, M, Gonzalezlez-Prendes, R, Goodin, A, Graham, E, Groen, E, Gutierrez-Sacristan, A, Habes, M, Heffler, E, Higginbottom, D, Janzen, T, Jayaraman, J, Jibb, L, Jongen, S, Kinyanjui, T, Koleva-Kolarova, R, Li, Z, Liu, Y, Lund, B, Lussier, A, Mier, P, Moore, M, Nagler, K, Orme, M, Pearson, J, Prajapati, A, Saito, Y, Troder, S, Uchendu, F, Verloh, N, Voutchkova, D, Abu-Zaid, A, Bakkach, J, Baumert, P, Dono, M, Hanson, J, Herbelet, S, Hobbs, E, Kulkarni, A, Liu, S, Loft, N, Reddan, T, Senghore, T, Vindin, H, Xu, H, Bannon, R, Chen, B, Cheung, J, Cooper, J, Esnakula, A, Feghali, K, Ghelardi, E, Gnasso, A, Horbar, J, Lai, H, Ma, R, Pan, Z, Peres, M, Pranata, R, Seow, E, Sydes, M, Testoni, I, Westermair, A, Yang, Y, Afnan, M, Albiol, J, Albuquerque, L, Amir, S, Amiya, E, Amorim, R, An, Q, Andersen, S, Aplin, J, Argyropoulos, C, Asmann, Y, Assaeed, A, Atanasov, A, Atchison, D, Avery, S, Avillach, P, Baade, P, Backman, L, Badie, C, Baldi, A, Ball, E, Bardot, O, Barnett, A, Basner, M, Batra, J, Bazanova, O, Beale, A, Beddoe, T, Bell, M, Berezikov, E, Berners-Price, S, Bernhardt, P, Berry, E, Bessa, T, Billington, C, Birch, J, Blakely, R, Blaskovich, M, Blum, R, Boelaert, M, Bogdanos, D, Bosch, C, Bourgoin, T, Bouvard, D, Boykin, L, Bradley, G, Braun, D, Brownlie, J, Bruhl, A, Burt, A, Butler, L, Byrareddy, S, Byrne, H, Cabantous, S, Calatayud, S, Candal, E, Carlson, K, Casillas, S, Castelvetro, V, Caswell, P, Cavalli, G, Cerovsky, V, Chagoyen, M, Chen, D, Chen, H, Chen, J, Chen, Y, Cheng, C, Cheng, J, Chinapaw, M, Chinopoulos, C, Cho, W, Chong, L, Chowdhury, D, Chwalibog, A, Ciresi, A, Cockcroft, S, Conesa, A, Cook, P, Cooper, D, Coqueret, O, Corea, E, Costa, A, Costa, E, Coupland, C, Crawford, S, Cruz, A, Cui, H, Cui, Q, Culver, D, D'Angiulli, A, Dahms, T, Daigle, F, Dalgleish, R, Danielsen, H, Darras, S, Davidson, S, Day, D, Degirmenci, V, Demaison, L, Devriendt, K, Ding, J, Dogan, Y, Dong, X, Donner, C, Dressick, W, Drevon, C, Duan, H, Ducho, C, Dumaz, N, Dwarakanath, B, Ebell, M, Eisenhardt, S, Elkum, N, Engel, N, Erickson, T, Fairhead, M, Faville, M, Fejzo, M, Festa, F, Feteira, A, Flood-Page, P, Forsayeth, J, Fox, S, Franks, S, Frentiu, F, Frilander, M, Fu, X, Fujita, S, Galea, I, Galluzzi, L, Gani, F, Ganpule, A, Garcia-Alix, A, Gedye, K, Giordano, M, Giunta, C, Gleeson, P, Goarant, C, Gong, H, Gora, D, Gough, M, Goyal, R, Graham, K, Grande-Perez, A, Graves, P, Greidanus, H, Grice, D, Grunau, C, Gumulya, Y, Guo, Y, Gurevich, V, Gusev, O, Hacker, E, Hage, S, Hagen, G, Hahn, S, Haller, D, Hammerschmidt, S, Han, J, Han, R, Handfield, M, Hapuarachchi, H, Harder, T, Hardingham, J, Heck, M, Heers, M, Hew, K, Higuchi, Y, Hilaire, C, Hilton, R, Hodzic, E, Hone, A, Hongoh, Y, Hu, G, Huber, H, Hueso, L, Huirne, J, Hurt, L, Idborg, H, Ikeo, K, Ingley, E, Jakeman, P, Jensen, A, Jia, H, Jia, S, Jiang, J, Jiang, X, Jin, Y, Jo, D, Johnson, A, Johnston, M, Jonscher, K, Jorens, P, Jorgensen, J, Joubert, J, Jung, S, Junior, A, Kahan, T, Kamboj, S, Kang, Y, Karamanos, Y, Karp, N, Kelly, R, Kenna, R, Kennedy, J, Kersten, B, Khalaf, R, Khalid, J, Khatlani, T, Khider, T, Kijanka, G, King, S, Kluz, T, Knox, P, Kobayashi, T, Koch, K, Kohonen-Corish, M, Kong, X, Konkle-Parker, D, Korpela, K, Kostrikis, L, Kraiczy, P, Kratz, H, Krause, G, Krebsbach, P, Kristensen, S, Kumari, P, Kunimatsu, A, Kurdak, H, Kwon, Y, Lachat, C, Lagisz, M, Laky, B, Lammerding, J, Lange, M, Larrosa, M, Laslett, A, Laverman, G, Leclair, E, Lee, K, Lee, M, Li, G, Lieb, K, Lim, Y, Lindsey, M, Line, P, Liu, D, Liu, F, Liu, H, Lloyd, V, Lo, T, Locci, E, Loidl, J, Lorenzen, J, Lorkowski, S, Lovell, N, Lu, H, Lu, W, Lu, Z, Luengo, G, Lundh, L, Lysy, P, Mabb, A, Mack, H, Mackey, D, Mahdavi, S, Maher, P, Maher, T, Maity, S, Malgrange, B, Mamoulakis, C, Mangoni, A, Manke, T, Manstead, A, Mantalaris, A, Marsal, J, Marschall, H, Martin, F, Martinez-Raga, J, Martinez-Salas, E, Mathieu, D, Matsui, Y, Maza, E, Mccutcheon, J, Mckay, G, Mcmillan, B, Mcmillan, N, Meads, C, Medina, L, Merrick, B, Metzger, D, Meunier, F, Michaelis, M, Micheau, O, Mihara, H, Mintz, E, Mizukami, T, Moalic, Y, Mohapatra, D, Monteiro, A, Montes, M, Moran, J, Morozov, S, Mort, M, Murai, N, Murphy, D, Murphy, S, Murray, S, Naganawa, S, Nammi, S, Nasios, G, Natoli, R, Nguyen, F, Nicol, C, van Nieuwerburgh, F, Nilsen, E, Nobile, C, O'Mahony, M, Ohlsson, S, Olatunbosun, O, Olofsson, P, Ortiz, A, Ostrikov, K, Otto, S, Outeiro, T, Ouyang, S, Paganoni, S, Page, A, Palm, C, Paradies, Y, Parsons, M, Parsons, N, Pascal, P, Paul, E, Peckham, M, Pedemonte, N, Pellizzon, M, Petrelli, M, Pichugin, A, Pinto, C, Plevris, J, Pollesello, P, Polz, M, Ponti, G, Porcelli, P, Prince, M, Quinn, G, Quinn, T, Ramula, S, Rappsilber, J, Rehfeldt, F, Reiling, J, Remacle, C, Rezaei, M, Riddick, E, Ritter, U, Roach, N, Roberts, D, Robles, G, Rodrigues, T, Rodriguez, C, Roislien, J, Roobol, M, Rowe, A, Ruepp, A, van Ruitenbeek, J, Rust, P, Saad, S, Sack, G, Santos, M, Saudemont, A, Sava, G, Schrading, S, Schramm, A, Schreiber, M, Schuler, S, Schymkowitz, J, Sczyrba, A, Seib, K, Shi, H, Shimada, T, Shin, J, Shortt, C, Silveyra, P, Skinner, D, Small, I, Smeets, P, So, P, Solano, F, Sonenshine, D, Song, J, Southall, T, Speakman, J, Srinivasan, M, Stabile, L, Stasiak, A, Steadman, K, Stein, N, Stephens, A, Stewart, D, Stine, K, Storlazzi, C, Stoynova, N, Strzalka, W, Suarez, O, Sultana, T, Sumant, A, Summers, M, Sun, G, Tacon, P, Tanaka, K, Tang, H, Tanino, Y, Targett-Adams, P, Tayebi, M, Tayyem, R, Tebbe, C, Telfer, E, Tempel, W, Teodorczyk-Injeyan, J, Thijs, G, Thorne, S, Thrift, A, Tiffon, C, Tinnefeld, P, Tjahjono, D, Tolle, F, Toth, E, Del Tredici, A, Tsapas, A, Tsirigotis, K, Turak, A, Tzotzos, G, Udo, E, Utsumi, T, Vaidyanathan, S, Vaillant, M, Valsesia, A, Vandenbroucke, R, Veiga, F, Vendrell, M, Vesk, P, Vickers, P, Victor, V, Villemur, R, Vohl, M, Voolstra, C, Vuillemin, A, Wakelin, S, Waldron, L, Walsh, L, Wang, A, Wang, F, Wang, Y, Watanabe, Y, Weigert, A, Wen, J, Wham, C, White, E, Wiener, J, Wilharm, G, Wilkinson, S, Willmann, R, Wilson, C, Wirth, B, Wojan, T, Wolff, M, Wong, B, Wu, T, Wuerbel, H, Xiao, X, Xu, D, Xue, B, Yalcin, S, Yan, H, Yang, E, Yang, W, Ye, Y, Ye, Z, Yli-Kauhaluoma, J, Yoneyama, H, Yu, Y, Yuan, G, Yuh, C, Zaccolo, M, Zeng, C, Zevnik, B, Zhang, L, Zhang, Y, Zhao, Y, Zhou, M, Zuberbier, T, Aanei, C, Ahmad, R, Al-Lawama, M, Alanio, A, Allardyce, J, Alonso-Caneiro, D, Atack, J, Baier, D, Bansal, A, Benezeth, Y, Berbesque, C, Berrevoet, F, Biedermann, P, Bijleveld, E, Bittner, F, Blombach, F, van den Bos, W, Boudreau, S, Bramoweth, A, Braubach, O, Cai, Y, Campbell, M, Catry, T, Chen, X, Cheng, S, Chung, H, Chavez-Fumagalli, M, Conway, A, Costa, B, Cyr, N, Dean, L, Denzel, M, Dlamini, S, Dudley, K, Dufies, M, Ecke, T, Eckweiler, D, Eixarch, E, El-Adawy, H, Emmrich, J, Eustace, A, Falter-Wagner, C, Farhoudi, R, Fuss, J, Gao, J, Gill, M, Gloyn, L, Goggs, R, Govinden, U, Greene, G, Greiff, V, Grundle, D, Gruneberg, P, Gumede, N, Haore, G, Harrison, P, Hoenner, X, Hojsgaard, D, Hori, H, Ikonomopoulou, M, Jeurissen, P, Johnson, D, Kabra, D, Kamagata, K, Karmakar, C, Kasian, O, Kaye, L, Khan, M, Kim, Y, Kish, J, Kobold, S, Kohanbash, G, Kohls, G, Kugler, J, Kumar, G, Lacy-Colson, J, Latif, A, Lauschke, V, Li, B, Lim, C, Liu, X, Lu, J, Lu, Q, Mahavadi, P, Marzocchi, U, Mcgarrigle, C, van Meerten, T, Min, R, Moal, I, Molari, M, Molleman, L, Mondal, S, van de Mortel, T, Moss, W, Moultos, O, Mukherjee, M, Nakayama, K, Narayan, E, Navaratnarajah, Neumann, P, Nie, J, Nie, Y, Niemeyer, F, Nolan, F, Nwaiwu, O, Oldenmenger, W, Olumayede, E, Ou, J, Pallebage-Gamarallage, M, Pearce, S, Pelkonen, T, Pelleri, M, Pereira, J, Pheko, M, Pinto, K, Piovesan, A, Pluess, M, Podolsky, I, Prescott, J, Qi, D, Qi, X, Raikou, V, Ranft, A, Rhodes, J, Rotge, J, Saggar, M, Schuon, R, Shahid, S, Shalchyan, V, Shirvalkar, P, Shiryayev, O, Singh, J, Smout, M, Soares, A, Song, C, Srivastava, K, Srivastava, R, Sun, J, Szabo, A, Szymanski, W, Tai, C, Takeuchi, H, Tanadini-Lang, S, Tang, F, Tao, W, Theron, G, Tian, C, Tian, Y, Tuttle, L, Valenti, A, Verlot, P, Walker, M, Wang, J, Welter, D, Winslade, M, Wu, D, Wu, Y, Xiao, H, Xu, B, Xu, Z, Yang, D, Yang, M, Yankilevich, P, You, Y, Yu, C, Zhan, J, Zhang, G, Zhang, K, Zhang, T, Zhao, G, Zhao, J, Zhou, X, Zhu, Z, Ajani, P, Anazodo, U, Bagloee, S, Bail, K, Bar, I, Bathelt, J, Benkeser, D, Bernier, M, Blanchard, A, Boakye, D, Bonatsos, V, Boon, M, Bouboulis, G, Bromfield, E, Bul, K, Burton, K, Butkowski, E, Carroll, G, Chao, F, Charrier, E, Chenguang, Choi, J, Christoffersen, T, Comel, J, Cosse, C, Cui, Y, van Dessel, P, Dhaval, Diodato, D, Duffey, M, Dutt, A, Egea, L, El-Said, M, Faye, M, Fernandez-Fernandez, B, Foley, K, Founou, L, Fu, F, Gadelkareem, R, Galimov, E, Garip, G, Gemmill, A, Gouil, Q, Grey, J, Gridneva, Z, Grothe, M, Grebert, T, Guerrero, F, Guignard, L, Haenssgen, M, Hasler, D, Holgate, J, Huang, A, Hulse-Kemp, A, Jean-Quartier, C, Jeon, S, Jia, Y, Jutzeler, C, Kalatzis, P, Karim, M, Karsay, K, Keitel, A, Kempe, A, Keown, J, Khoo, C, Khwaja, N, Kievit, R, Kosanic, S, Koutoukidis, D, Kramer, P, Kumar, D, Kirag, N, Lanza, G, Le, T, Leem, J, Leightley, D, Leite, A, Lercher, L, Li, Y, Lim, R, Lima, L, Lin, L, Ling, T, Liu, Z, Lu, Y, Lum, F, Luo, H, Machhi, J, Macleod, A, Macwan, I, Madala, H, Madani, N, de Maio, N, Makowiecki, K, Mallinson, D, Margelyte, R, Maria, C, Markonis, Y, Marsili, L, Mavoa, S, Mcwilliams, L, Megersa, M, Souto-Maior, C, Menichetti, J, Mercieca-Bebber, R, Miller, J, Minde, D, Minges, A, Mishra, E, Mishra, V, Moores, C, Morrice, N, Moskalensky, A, Navarin, N, Negera, E, Nolet, P, Nordberg, A, Norden, R, Nowicki, J, Olova, N, Olszewski, P, Onzima, R, Pan, C, Park, C, Park, D, Park, S, Patil, C, Pedro, S, Perry, S, Peter, J, Peterson, B, Pezzuolo, A, Pozdnyakov, I, Qian, S, Qin, L, Rafe, A, Raote, I, Raza, A, Rebl, H, Refai, O, Regan, T, Richa, T, Richardson, M, Robinson, K, Rossoni, L, Rouet, R, Safaei, S, Schneeberger, P, Schwotzer, D, Sebastian, A, Selinski, J, Seltmann, S, Sha, F, Shalev, N, Shang, J, Singer, J, Singh, M, Smith, T, Solomon-Moore, E, Song, L, Soraggi, S, Stanley, R, Steckhan, N, Strobl, F, Subissi, L, Supriyanto, I, Surve, C, Suzuki, T, Syme, C, Sorelius, K, Tang, Y, Tantawy, M, Tennakoon, S, Teseo, S, Toelzer, C, Tomov, N, Tovar, M, Tran, L, Tripathi, S, Tuladhar, A, Ukubuiwe, A, Ung, C, Valgepea, K, Vatanparast, H, Vidal, A, Wang, Q, Watari, R, Webster, R, Wei, J, Wibowo, D, Wingenbach, T, Xavier, R, Xiao, S, Xiong, P, Xu, S, Yao, R, Yao, W, Yin, Q, Zaitsu, M, Zeineb, Z, Zhan, X, Zhang, R, Zhang, W, Zheng, S, Zhou, B, Ahmad, H, Akinwumi, S, Albery, G, Alhowimel, A, Ali, J, Alshehri, M, Alsuhaibani, M, Anikin, A, Azubuike, S, Bach-Mortensen, A, Baltiansky, L, Bartas, M, Belachew, K, Bhardwaj, V, Binder, K, Bland, N, Boah, M, Bullen, B, Calabro, G, Callahan, T, Cao, B, Chalmers, K, Chang, W, Che, Z, Chen, A, Chen, Z, Choi, Y, Chowdhury, M, Christensen, M, Cooke, R, Cottini, M, Covington, N, Cunningham, C, Delarocque, J, Devos, L, Dhar, A, Ding, K, Dong, K, Dong, Z, Dreyer, N, Ekstrand, C, Fardet, T, Feleke, B, Feurer, T, Freitas, A, Gao, T, Gebremedhin, Giganti, F, Grabowski, P, Guerra-Mora, J, Guo, C, Guo, X, Gupta, H, He, S, Heijne, M, Heinemann, S, Hogrebe, A, Huang, Z, Iskander-Rizk, S, Iyer, L, Jahan, Y, James, A, Joel, E, Joffroy, B, Jegousse, C, Kambondo, G, Karnati, P, Kaya, C, Ke, A, Kelly, D, Kickert, R, Kidibule, P, Kieselmann, J, Kim, H, Kitazawa, T, Lamberts, A, Liang, H, Linn, S, Litfin, T, Liusuo, W, Lygirou, V, Mahato, A, Mai, Z, Major, R, Mali, S, Mallis, P, Mao, W, Marvin-Dowle, K, Mason, L, Merideth, B, Merino-Plaza, M, Merlaen, B, Messina, R, Mishra, A, Muhammad, J, Musinguzi, C, Nanou, A, Naqash, A, Nguyen, J, Nguyen, T, Ni, D, Nida, Notcovich, S, Ohst, B, Ollivier, Q, Osses, D, Peng, X, Plantinga, A, Pulia, M, Rafiq, M, Raman, A, Raucher-Chene, Rawski, R, Ray, A, Razak, L, Rudolf, K, Rusch, P, Sadoine, M, Schmidt, A, Schurr, R, Searles, S, Sharma, S, Sheehan, B, Shi, C, Shohayeb, B, Sommerlad, A, Strehlow, J, Sun, X, Sundar, R, Taherzadeh, G, Tahir, N, Tang, J, Testa, J, Tian, Z, Tingting, Q, Verheijen, G, Vickstrom, C, Wang, T, Wang, X, Wang, Z, Wei, P, Wilson, A, Wyart, Yassine, A, Yousefzadeh, A, Zare, A, Zeng, Z, Zhang, H, Zhou, J, Zhu, D, Adamo, V, Adeyemo, A, Aggelidou, M, Al-Owaifeer, A, Al-Riyami, A, Alzghari, S, Andersen, V, Angus, K, Asaduzzaman, M, Asady, H, Ato, D, Bai, X, Baines, R, Ballantyne, M, Ban, B, Beck, J, Ben-Nafa, W, Black, E, Blancher, A, Blankstein, R, Bodagh, N, Borges, P, Brooks, A, Brox-Ponce, J, Brunetti, A, Canham, C, Carninci, P, Carvajal, R, Chang, S, Chao, J, Chatterjee, P, Chen, L, Chhatriwalla, A, Chikowe, I, Chuang, T, Collevatti, R, Cornejo, D, Cuenda, A, Dao, M, Dauga, D, Deng, Z, Devkota, K, Doan, L, Elewa, Y, Fan, D, Faruk, M, Feifei, S, Ferguson, T, Fleres, F, Foster, E, Foster, S, Furer, T, Gao, Y, Garcia-Rivera, E, Gazdar, A, George, R, Ghosh, S, Gianchecchi, E, Gleason, J, Hackshaw, A, Hall, A, Hall, R, Harper, P, Hogg, W, Huang, G, Hunter, K, Ijzerman, A, Jesus, C, Jian, G, Lewis, J, Kanj, S, Kaur, H, Kheir, F, Kichatova, V, Kiyani, M, Klein, R, Kovesi, T, Kraschnewski, J, Kumar, A, Labutin, D, Lazo-Langner, A, Leclercq, G, Li, M, Li, Q, Li, T, Liao, W, Liao, Z, Lin, J, Lizer, J, Lobreglio, G, Lowies, C, Lu, C, Majeed, H, Martin, A, Martinez-Sobrido, L, Meresh, E, Middelveen, M, Mohebbi, A, Mota, J, Mozaheb, Z, Muyaya, L, Nandhakumar, A, Ng, S, Obeidat, M, Oh, D, Owais, M, Pace-Asciak, P, Panwar, A, Patterson, C, Penagos-Tabaree, F, Pianosi, P, Pinzi, V, Pridans, C, Psaroulaki, A, Pujala, R, Pulido-Arjona, L, Qi, P, Rahman, P, Rai, N, Rassaf, T, Refardt, J, Ricciardi, W, Riess, O, Rovas, A, Sacks, F, Saleh, S, Sampson, C, Schmutz, A, Sepanski, R, Sharma, N, Spearman, P, Subramaniapillai, M, Swali, R, Tan, C, Tellechea, J, Thomas, L, Tong, X, Vavvas, D, Veys, R, Vitriol, V, Wang, H, Waugh, J, Webb, S, Williams, B, Workman, A, Xiang, T, Xie, L, Xu, T, Yang, C, Yoon, J, Yuan, C, Zaritsky, A, Zhao, H, Zuckerman, H, Lyu, R, Pullan, W, Public and occupational health, APH - Health Behaviors & Chronic Diseases, APH - Societal Participation & Health, APH - Quality of Care, Amsterdam Reproduction & Development (AR&D), Obstetrics and gynaecology, Amsterdam Neuroscience - Cellular & Molecular Mechanisms, Pediatric surgery, APH - Methodology, ACS - Atherosclerosis & ischemic syndromes, RELISH Consortium [Member of the MPIB: Lucas Molleman], Kostrikis, Leondios G. [0000-0002-5340-7109], Tan, AC, El-Esawi, MA, Gladue, DP, Almeida, GMF, Sorzano, CO, Yeung, AWK, Engel, MS, Chandrasekaran, AR, Staege, MS, Daulatabad, SV, Yin, CC, Flegel, WA, Goodyear, CS, van Raaij, MJ, Campana, LG, Kurniawan, NA, Huttner, FJ, Ammerman, BA, Cobine, PA, Tan, EC, Han, HM, Xia, WF, McCrum, C, Dings, RPM, Costa, VD, Grimm, DG, Sabnis, SC, Amer, SEDR, Liew, AWC, Zhang, CX, Devkota, HP, Tan, KH, Boehme, KA, Brown, JAL, Dalrymple, BP, Harvey, DJ, Dai, ZW, Hartmann, MD, Gurney-Champion, OJ, Kauppila, JH, Zhang, XL, Cuiv, PO, Filipp, FV, Smith, SS, Ascher, DB, Janga, SC, Schulte, LN, Bush, SJ, Werner, GDA, Al-Farha, AA, Greenwald, NF, Popoola, SI, Rahman, MS, Xu, JL, Yang, SY, Alper, OM, Baker, CI, Klempnauer, KH, Lidbury, BA, Lin, MZ, Ma, WJ, Maibach, EW, Mather, DE, Nandakumar, KS, Ohgami, RS, Coelho, LP, Doxey, AC, Hu, PZ, Mitchell, KM, Salama, MF, Shabalin, IG, Song, HJ, Zeng, EL, Alimba, CG, Beyene, TJ, Cao, ZH, Chan, SS, Woldesemayat, AA, Cosacak, MI, Ross, SA, Abramowitz, MK, Lee, SH, Abid, MB, Albrecht, DR, Atkins, GJ, Beck, CR, Bonvin, AMJJ, Braun, RJ, Bull, JA, Delahay, RM, Duijf, PHG, Eskelinen, EL, Farber, DB, Leeuw, FE, Lopez-Escamez, JA, Lopez-Ruiz, FJ, Marchbank, KJ, Martin, CS, Miele, AE, Palma, JA, Portillo, MC, Pritchard, AL, Raghava, GPS, Roberts, NJ, Uversky, VN, Villet, MH, Vorholt, JA, Aizat, WM, Bridges, KM, Domingues, HS, Esfahlani, SS, Guisado, JL, Kane, NC, Lau, CL, Luu, AM, Ma, LS, Norris, AD, Parsons, JR, Pinto, IM, Reschke, CR, Stewart, CJ, Chen, CE, Eskew, EA, Graham, EB, Groen, EJN, Higginbottom, DB, Jibb, LA, Koleva-Kolarova, RG, Liu, YP, Lund, BA, Lussier, AA, Moore, MD, Orme, MW, Pearson, JA, Prajapati, AS, Troder, SE, Voutchkova, DD, Liu, SQ, Loft, ND, Xu, HT, Cheung, JTK, Esnakula, AK, Feghali, KA, Lai, HM, Ma, RY, Pan, ZH, Peres, MA, Westermair, AL, Albuquerque, LG, Amorim, RM, Andersen, SU, Aplin, JD, Asmann, YW, Assaeed, AM, Atanasov, AG, Atchison, DA, Avery, SV, Baade, PD, Barnett, AG, Bazanova, OM, Bell, ML, Bessa, TB, Blakely, RD, Blaskovich, MAT, Boykin, LM, Butler, LM, Byrareddy, SN, Byrne, HJ, Caswell, PT, Chen, CS, Chen, DF, Chen, JT, Chen, YL, Cheng, CX, Cheng, JL, Cho, WCS, Cook, PA, Cooper, DN, Corea, EM, Crawford, SY, Cruz, AD, Cui, HJ, Culver, DC, Dahms, TES, Danielsen, HE, Davidson, SM, Day, DA, Dong, XC, Donner, CF, Drevon, CA, Duan, HL, Dwarakanath, BS, Ebell, MH, Erickson, TB, Faville, MJ, Fejzo, MS, Fox, SA, Franks, SJ, Frentiu, FD, Frilander, MJ, Fu, XM, Ganpule, AP, Gleeson, PA, Gong, HP, Gough, MJ, Graham, KE, Graves, PM, Guo, YB, Gurevich, VV, Hage, SR, Haller, DM, Han, JW, Hapuarachchi, HC, Hardingham, JE, Hew, KF, St Hilaire, C, Hu, GK, Huber, HP, Hueso, LE, Jakeman, PM, Jia, HS, Jia, SQ, Jiang, JP, Jiang, XY, Johnson, AM, Jonscher, KR, Jorens, PG, Jorgensen, JOL, Joubert, JW, Jung, SH, Junior, AM, Kamboj, SK, Kang, YK, Karp, NA, Khalaf, RA, Khalid, JM, Kijanka, GS, King, SRB, Koch, KW, Kohonen-Corish, MRJ, Korpela, KM, Kostrikis, LG, Krebsbach, PH, Kristensen, SR, Kwon, YD, Laslett, AL, LeClair, EE, Lee, KW, Lee, MY, Lee, MS, Li, GY, Li, JS, Lim, YY, Lindsey, ML, Line, PD, Liu, DC, Liu, FB, Liu, HY, Liu, HD, Lloyd, VK, Lo, TW, Lovell, NH, Lu, ZY, Luengo, GS, Lundh, LG, Lysy, PA, Mack, HG, Mackey, DA, Mahdavi, SR, Maity, SN, Mangoni, AA, Manstead, ASR, Marschall, HU, Martin, FL, McCutcheon, JE, Mckay, GJ, McMillan, B, McMillan, N, Merrick, BA, Metzger, DW, Meunier, FA, Mintz, EM, Mohapatra, DP, Moran, JV, Morozov, SY, Murphy, DJ, Murphy, SK, Murray, SA, Natoli, RM, Nilsen, EB, Nobile, CJ, Outeiro, TF, Parsons, MH, Pellizzon, MA, Pinto, CJC, Plevris, JN, Quinn, GP, Quinn, TJ, Reiling, JH, Riddick, EW, Roach, NW, Roberts, DD, Roobol, MJ, Rowe, JA, Sack, GH, Seib, KL, Shi, HP, Shin, JS, Smeets, PAM, So, PW, Sonenshine, DE, Song, JN, Speakman, JR, Srinivasan, MV, Stabile, LP, Steadman, KJ, Stephens, AW, Stewart, DI, Stoynova, NV, Suarez, OM, Sumant, AV, Summers, MJ, Tang, HX, Tebbe, CC, Telfer, EE, Teodorczyk-Injeyan, JA, Thrift, AG, Tjahjono, DH, del Tredici, AL, Udo, EE, Vandenbroucke, RE, Veiga, FH, Vesk, PA, Victor, VM, Vohl, MC, Voolstra, CR, Walsh, LJ, Wang, AY, Wen, JC, White, EP, Wojan, TR, Wong, BM, Wu, TW, Xiao, XS, Xu, JW, Xu, JP, Yang, EC, Yang, SQ, Ye, YZ, Ye, ZQ, Yuan, GC, Yuh, CH, Zhang, YK, Zhang, YS, Zhang, ZY, Aanei, CM, Atack, JM, Biedermann, PHW, den Bos, W, Boudreau, SA, Bramoweth, AD, Cao, ZX, Cheng, SQ, Chung, HJ, Chavez-Fumagalli, MA, Costa, BM, Dean, LT, Denzel, MS, Dlamini, SV, Dudley, KJ, Emmrich, JV, Eustace, AJ, Falter-Wagner, CM, Gao, JZ, Gill, MR, Grundle, DS, Ikonomopoulou, MP, Johnson, DM, Kaye, LK, Khan, MM, Kim, YM, Kish, JK, Kugler, JM, Lauschke, VM, Li, BL, Lim, CJ, Liu, XD, Lu, JJ, McGarrigle, CA, Mondal, SR, Van de Mortel, T, Moss, WN, Moultos, OA, Neumann, PA, Nie, JY, Nie, YJ, Oldenmenger, WH, Ou, JH, Pearce, SP, Pelleri, MC, Pereira, JL, Pinto, KA, Podolsky, IM, Qi, DC, Qi, XS, Raikou, VD, Rotge, JY, Rowe, AD, Schuon, RA, Smout, MJ, Song, CJ, Srivastava, RK, Tai, CNP, Tao, WY, Tian, CF, Tian, YS, Tuttle, LM, Wu, DL, Wu, YR, Xu, BS, Xu, ZY, Yang, DD, Yang, MJ, You, YY, Yu, CL, Zhao, GY, Zhou, XF, Zhu, ZX, Ajani, PA, Anazodo, UC, Bagloee, SA, Bernier, ML, Blanchard, AM, Boakye, DW, Boon, MH, Bul, KCM, Burton, KJ, Butkowski, EG, Chao, FQ, Charrier, EE, Chen, XY, Chen, YC, Choi, JR, Comel, JC, Cui, YR, Egea, LG, Foley, KG, Founou, LL, Gadelkareem, RA, Grothe, MJ, Haenssgen, MJ, Holgate, JY, Huang, AC, Hulse-Kemp, AM, Jeon, SM, Jia, YY, Keown, JR, Khoo, CM, Kievit, RA, Kosanic, A, Koutoukidis, DA, Le, TD, Leem, JW, Lim, RL, Lima, LRA, Liu, YC, Liu, ZH, Lum, FM, Madala, HR, Mallinson, DJ, Caracausi, M, McWilliams, L, Mendes, CSM, Miller, JJ, Minde, DPM, Mishra, VR, Moskalensky, AE, Nowicki, JP, Pan, CL, Park, DI, Patil, CD, Pedro, SA, Perry, SR, Peterson, BM, Qian, SY, Richardson, MF, Robinson, KR, Schneeberger, PHH, Shang, JL, Song, LJ, Surve, CR, Tuladhar, AM, Ukubuiwe, AC, Ung, COL, Wei, JN, Wingenbach, TSH, Xavier, RM, Xiao, SM, Xu, SC, Xu, SL, Yao, RF, Yu, YB, Zhan, XY, Zhang, JL, Zhang, RQ, Zhou, BL, Zhou, XY, Akinwumi, SA, Albery, GF, Azubuike, SO, Belachew, KY, Bland, NS, Calabro, GE, Callahan, TJ, Che, ZP, Chen, ATY, Chen, HM, Chen, YN, Chowdhury, MAK, Christensen, MR, Cooke, RSC, Covington, NV, Dhar, AR, Ding, KF, Dong, KX, Feleke, BE, Asefa, NG, Guerra-Mora, JR, Guo, CY, Guo, XY, He, SN, Huang, ZP, Iyer, LM, James, AS, Kidibule, PE, Kieselmann, JP, Kim, HJ, Liang, HK, Linn, SN, Mahato, AK, Mai, ZM, Major, RW, Mao, WZ, Mason, LD, Merino-Plaza, MJ, Mishra, AK, Nguyen, JT, Nguyen, TTH, Ollivier, QR, Osses, DF, Peng, XD, Raucher-Chene, D, Razak, LA, Sadoine, ML, Shi, CH, Sun, XB, Tahir, NDM, Tian, ZQ, Verheijen, GP, Wang, XM, Wang, ZX, Yassine, AA, Zhang, CR, Zhang, HW, Zhang, LX, Zhang, TC, Zhang, WJ, Zhou, JY, Zhu, DJ, Adeyemo, AA, Al-Owaifeer, AM, Al-Riyami, AZ, Alzghari, SK, Bai, XY, Baines, RL, Borges, PAV, Canham, CD, Chang, SC, Chhatriwalla, AK, Chuang, TJ, Collevatti, RG, Valera-Cornejo, DA, Doan, LV, Elewa, YHA, Fan, DS, Ferguson, TS, Foster, EJ, Foster, CS, Gao, YB, Garcia-Rivera, EJ, George, RB, Gleason, JM, Hogg, WE, Huang, GQ, Hunter, KE, IJzerman, AP, Lewis, JS, Kanj, SS, Kichatova, VS, Kraschnewski, JL, Kumar, AP, Li, MT, Li, QC, Li, TL, Li, YZ, Liao, WT, Liao, ZY, Ng, SHX, Oh, DH, Pianosi, PT, Pujala, RK, Qi, PF, Rai, NK, Sacks, FM, Tan, CM, Tellechea, JI, Thomas, LM, Wang, HD, Wang, JH, Wang, JC, Webb, SA, Williams, BA, Workman, AD, Xiang, TX, Xie, LX, Xu, TS, Yang, CJ, Yoon, JG, Yuan, CM, Zhao, HC, Zuckerman, HN, Zhou, YQ, RELISH Consortium, Yhteiskuntatieteiden tiedekunta - Faculty of Social Sciences, Tampere University, Griffith Univ, Univ Colorado, Tanta Univ, Friedrich Schiller Univ, Univ Med Ctr Schleswig Holstein, ARS, Univ Jyvaskyla, Graz Univ Technol, CSIC, Univ Hong Kong, Univ Kansas, SUNY Albany, Robert Koch Inst, Martin Luther Univ Halle Wittenberg, Indiana Univ Purdue Univ, Univ Reading, Dali Univ, Univ Hosp Munich LMU, Univ Tsukuba, UniLaSalle, Henry Ford Hlth Syst, Zhejiang Univ, Ist Nazl Tumori Fdn Pascale IRCCS, NIH, Univ Glasgow, Polish Acad Sci, Univ Padua, Eindhoven Univ Technol, Univ Strasbourg, Heidelberg Univ, Univ Notre Dame, Harvard Med Sch, Auburn Univ, KK Womens & Childrens Hosp, Univ Alabama, UCL, Maastricht Univ, Univ Arkansas Med Sci, Univ Gothenburg, Univ Newcastle, Univ Cyprus, Shandong Agr Univ, NIMH, Univ Wisconsin, Univ Oxford, Weihenstephan Triesdorf Univ Appl Sci, Univ Michigan, Bombay Coll Pharm, Inst Invest Biol Clemente Estable, Gem Hosp & Res Ctr, Kafr El Sheikh Univ, Med Univ Innsbruck, Australian Natl Univ, Univ Cattolica Sacro Cuore, Shandong Inst Parasit Dis, Kumamoto Univ, Nagoya City Univ, Univ Karachi, Labormed Zentrum Dr Risch, Univ Otago, Albert Ludwigs Univ Freiburg, Heinrich Heine Univ, Natl Univ Ireland Galway, Univ Western Australia, SingHlth Polyclin, La Trobe Univ, Univ Bordeaux, Agr & Agri Food Canada, St George Hosp, Max Planck Inst Dev Biol, Med Univ Lublin, ICIT, Univ KwaZulu Natal, Inst Canc Res, Karolinska Inst, Wenzhou Med Univ, Univ Republica, Charite Med Univ Berlin, Bambino Gesu Pediat Hosp, Indiana Univ Sch Med Northwest, Univ Regensburg, Univ Queensland, Translat Res Inst, St Jude Childrens Res Hosp, Univ Durham, Univ Ioannina, Tech Univ Munich, Univ Hosp Essen, Virginia Commonwealth Univ, Univ Lyon, Univ Melbourne, Philipps Univ Marburg, Indiana Univ, Univ Florida, Kyoto Univ, Friedrich Loeffler Inst, Univ Adelaide, Stanford Univ, Covenant Univ, Univ British Columbia, Albert Einstein Coll Med, Akdeniz Univ, Med Univ Hosp, NET ESolut, Univ Southern Denmark, John Innes Ctr, Univ Cambridge, Univ Munster, Univ Birmingham, Murdoch Univ, George Mason Univ, Southern Med Univ, Univ Bologna, Huazhong Univ Sci & Technol, Queensland Univ Technol, French Natl Ctr Sci Res, Univ Warwick, European Mol Biol Lab, Univ Cincinnati, Univ Waterloo, Sorbonne Univ, Univ Manitoba, Max Planck Inst Solid State Res, Imperial Coll London, Mansoura Univ, Univ Virginia, China Univ Geosci, Clin Neurol & Psychiat Children & Youth, Ahvaz Jundishapur Univ Med Sci, Univ Iowa City, Univ Tubingen, Univ Ibadan, Kansas State Univ, Univ Tasmania, Childrens Mercy Hosp, Stockholm Univ, Oslo Univ Hosp, CSIRO, Johns Hopkins Sch Med, Univ South Africa, German Ctr Neurodegenerat Dis, Simon Fraser Univ, Univ Manchester, Georgetown Univ, Dermatol Skin & Canc Fdn, Med Coll Wisconsin, US FDA, Worcester Polytech Inst, Publ Hlth England, Univ Utrecht, Danube Private Univ, Univ Helsinki, Univ Sydney, Univ Nottingham, Univ Toulouse, ASCR, Univ Turku, York Univ, Univ Calif Los Angeles, Helmholtz Zentrum Geesthacht, Unvers Genova, Otto von Guericke Univ, Univ Toledo, CRUK Beatson Inst, Leibniz Inst Primate Res, Univ Limoges, Hainan Univ, Univ Oulu, Rhein Westfal TH Aachen, Univ Stuttgart, Peking Univ, GIGA Res Inst, CHULiege, Fdn Bruno Kessler, Hokkaido Univ, Univ Leuven, Chalmers Univ Technol, Radboud Univ Nijmegen, Univ South Australia, Bio Thera Solut Ltd, Inst Invest Biosanitario Granada IBS, Curtin Univ, Newcastle Univ, Goethe Univ, Inst Pasteur, Univ Valencia, Council Agr Res & Econ, Fraunhofer Inst Toxicol & Expt Med ITEM, Chugai Pharmaceut Co Ltd, Univ Lubeck, NYU, Univ Putra Malaysia, Univ N Carolina, Univ Southampton, Univ Highlands & Islands, Indraprastha Inst Informat Technol, Glasgow Caledonian Univ, Liverpool John Moores Univ, Parkinsons Inst & Clin Ctr, Luxembourg Inst Sci & Technol, Univ Wollongong, Univ Bari Aldo Moro, Flinders Univ S Australia, Univ S Florida, Univ Texas Dallas, Rhodes Univ, Univ Nova Lisboa, Swiss Fed Inst Technol, Inst Ulm, Tokyo Womens Med Univ, Univ Limerick, McGill Univ, StatSol, Univ Kebangsaan Malaysia, ASTAR, Int Iberian Nanotechnol Lab INL, Anglia Ruskin, Max Planck Inst Biochem, Univ Seville, Singapore MIT Alliance Res & Technol, Australian Catholic Univ, Ruhr Univ Bochum, Northwest A&F Univ, Battelle Mem Inst, Southern Methodist Univ, Teikyo Univ, Tempus Labs, Hunan Univ, Inst Cochin, Royal Coll Surgeons Ireland, Penn State Univ, Chinese Acad Sci, Univ Sci & Technol China, Michigan State Univ, SUNY Buffalo, Univ Rostock, South China Normal Univ, Univ Bari, EcoHlth Alliance, Mayo Clin, Med Univ Silesia, Univ Lleida, Pacific Northwest Natl Lab, Univ Edinburgh, Univ Penn, Humanitas Univ & Res Hosp, Carl von Ossietzky Univ Oldenburg, Int Med Univ, Univ Ottawa, Kings Coll London, Harbin Med Univ, UiT Arctic Univ Norway, Cornell Univ, East China Normal Univ, Johannes Gutenberg Univ Mainz, Univ Massachusetts, Max Planck Inst Terr Microbiol, NIHR Biomed Res Ctr Resp, Yale Univ, Sardar Patel Univ, Univ Tokyo, Univ Cologne, Natl Open Univ Nigeria, Univ Hosp Regensburg, Natl Univ Singapore, Alfaisal Univ, Abdelmalek Essaadi Univ, Univ Santiago de Compostela, Univ Ghent, Ghent Univ Hosp, Anglia Ruskin Univ, Herlev & Gentofte Hosp, Lady Cilento Childrens Hosp, Univ Gambia, Wayne State Univ, Aberdeen Royal Infirm, Univ Toronto, Chinese Univ Hong Kong, Univ Nebraska Med Ctr, Univ Texas MD Anderson Canc Ctr, Univ Pisa, Magna Grecia Univ, Univ Vermont, Sun Yat Sen Univ, Fudan Univ, Shanxi Agr Univ, Pelita Harapan Univ, Inst Mental Hlth, Dalian Univ Technol, Tianjin United Family Healthcare, Univ Autonoma Barcelona, Universidade Estadual Paulista (Unesp), Helmholtz Zentrum Munchen, Aarhus Univ, Univ New Mexico, King Saud Univ, Canc Council Queensland, Umea Univ, Univ Campania L Vanvitelli, Bartshealth, Univ Clermont Auvergne, INRA Abeilles & Environm, Novosibirsk State Univ, Univ Arizona, Univ Groningen, SUNY Upstate Med Univ, Fundacao Oswaldo Cruz, Inst Environm Sci & Res ESR, Florida Atlantic Univ, Univ Hosp Wurzburg, Inst Trop Med, Univ Thessaly, Univ Basel, CNRS, Univ Ft Hare, Philosoph Theol Hsch Vallendar, Technol Univ Dublin, INSERM, Univ Nebraska, Univ Montpellier, Czech Acad Sci, Natl Cheng Kung Univ, Lanzhou Univ, Univ Technol Sydney, JT Chen Clin, Beijing Normal Univ, Univ Missouri, Vrije Univ Amsterdam Med Ctr, Semmelweis Univ, Queen Elizabeth Hosp, Univ Pittsburgh, GB Pant Inst Post Grad Med Educ & Res, Univ Copenhagen, Univ Palermo, Univ Salford, Cardiff Univ, Univ Colombo, Beijing Univ Chinese Med, Univ Porto, Univ Illinois, Pontificia Univ Catolica Goias, China Japan Friendship Hosp, Boston Univ, Amer Univ, Carleton Univ, Univ Regina, Univ Montreal, Univ Leicester, Katholieke Univ Leuven, Dokuz Eylul Univ, Indiana Univ Sch Med, Mondo Med, US Naval, Univ Oslo, Saarland Univ, Shanghai Proton & Heavy Ion Ctr, Univ Georgia, Univ Freiburg, Sidra Med, Rostock Univ, AgResearch, Arizona State Univ, Sheffield Hallam Univ, Aneurin Bevan Univ Healthboard, Univ Calif San Francisco, Fordham Univ, Fujian Normal Univ, Univ Fukui, Univ Urbino, Osped San Luigi, Muljibhai Patel Urol Hosp, Univ Granada, Massey Univ, CNR, Univ Childrens Hosp Zurich, Tsinghua Univ, Cheikh Anta Diop Univ UCAD, Providence Portland Med Ctr, Alberta Innovates, Univ Malaga, James Cook Univ, European Commiss, Vanderbilt Univ, RIKEN, Fred Hutchinson Canc Ctr, Univ Geneva, Ernst Moritz Arndt Univ Greifswald, East China Univ Sci & Technol, Ohio State Univ, Oragenics, Natl Environm Agcy, USDA, Guys & St Thomas NHS Fdn Trust, Univ Sarajevo, Univ Kent, Tokyo Inst Technol, Univ Appl Sci Munich, CIC NanoGUNE, Natl Inst Genet, Southwest Med Univ, Beijing Canc Hosp, Key Lab Nano Biol Effects & Safety, NIBR, Daejeon St Marys Hosp, Univ Western Ontario, Univ Aberdeen, Univ Antwerp, Aarhus Univ Hosp, Univ Pretoria, Duke Univ, KRIBB, Univ dArtois, AstraZeneca, Coventry Univ, Wilton Ctr, Thunen Inst Forest Genet, Lebanese Amer Univ, Takeda, King Abdullah Int Med Res Ctr, Univ Bahri, Colorado State Univ, Rzeszow Univ Hosp, Univ Leeds, Massachusetts Gen Hosp, UNSW, Univ Mississippi, Tampere Univ, Aalborg Univ Hosp, Manipal Acad Higher Educ, Cukurova Univ, Catholic Univ Korea, UNSW Sydney, St Vincent Shoulder & Sports Clin, Leibniz Inst Plant Genet & Crop Plant Res IPK, Univ Europea Madrid, CSIRO Mfg, Depaul Univ, Konkuk Univ, Chang Gung Univ, Korea Univ, Princeton Univ, Henan Univ Chinese Med, Univ Med Ctr Mainz, Monash Univ Malaysia, Sichuan Agr Univ, Guangzhou Univ Chinese Med, Southeast Univ, Mt Allison Univ, Ithaca Coll, Univ Cagliari, Univ Vienna, Univ Zurich, Tulane Univ, NINDS, LOreal Res & Innovat, Lund Univ, Catholic Univ Louvain, Georgia State Univ, Iran Univ Med Sci, Salk Inst Biol Studies, Univ Liege, Univ Crete, Max Planck Inst Immunobiol & Epigenet, Sahlgrens Acad, Univ Cent Lancashire, Hosp Univ Doctor Peset, Ctr Biol Mol Severo Ochoa, Unvivers Hosp Lille, Kansai Med Univ, Queens Univ, NIEHS, Albany Med Coll, Univ Bourgogne Franche Comte, Ritsumeikan Univ, Kent State Univ, Natl Inst Infect Dis, Universidade Estadual de Maringá (UEM), Univ Iowa, Conservatoire Natl Arts & Metiers, Lomonosov Moscow State Univ, Jikei Univ, Univ South Wales, Nagoya Univ, Western Sydney Univ, TEI Epirus, Oniris, Royal Vet Coll, Norwegian Inst Nat Res, Univ Calif Merced, Univ Dublin, Fdn Jimenez Diaz Hosp, Univ Med Ctr Gottingen, Quadram Inst Biosci, Ostbayer Tech Hsch Regensburg OTH Regensburg, Deakin Univ, IRCCS Ist Giannina Gaslini, Res Diets Inc, Univ Perugia, Walter Reed Natl Mil Med Ctr, Universidade Federal de Santa Catarina (UFSC), Orion Pharma, MIT, Univ Turin, Univ G dAnnunzio, Tech Univ Berlin, Univ Goettingen, Tarbiat Modares Univ, Univ Carlos III Madrid, Inst Med Mol, Univ Costa Rica, Univ Stavanger, Erasmus MC, German Res Ctr Environm Hlth GmbH, Leiden Univ, Kolling Inst Med Res, GlaxoSmithKline, Univ Trieste, Univ Duisburg Essen, Med Univ Vienna, FHI 360, KU Leuven VIB, Bielefeld Univ, Capital Med Univ, Meiji Univ, Yonsei Univ, Johnson & Johnson EAME, Penn State Coll Med, Wageningen Univ, Univ Murcia, Old Dominion Univ, Monash Univ, Univ Lausanne, Leibniz Inst Plant Genet & Crop Plant Res IPK Gat, Piramal Imaging, US Geol Survey, Ajinomoto Genet Res Inst, Jagiellonian Univ, Univ Puerto Rico, Argonne Natl Lab, Univ Sunshine Coast, Chinese Peoples Liberat Army Gen Hosp, Tohoku Univ, Fukushima Med Univ, MEDIVIR AB, Univ Jordan, Canadian Mem Chiropract Coll, Agilent Technol, French Natl Canc Inst, Ludwig Maximilians Univ Munchen, Bandung Inst Technol, Univ Luxembourg, Millennium Hlth, Aristotle Univ Thessaloniki, Jan Kochanowski Univ Humanities & Sci, McMaster Univ, Marche Polytech Univ, Kuwait Univ, Fujita Hlth Univ, North West Reg Spinal Injuries Ctr, Luxembourg Inst Hlth, Nestle Inst Hlth Sci SA, Ctr Inflammat Res VIB, Univ Lisbon, Northumbria Univ, INRS, Univ Laval, Univ Konstanz, Univ Cote dAzur, Scion, CUNY, George Inst Global Hlth, Wuhan Univ, Univ Minnesota, Natl Yunlin Univ Sci & Technol, Bournemouth Univ, Rural Econ Branch, Uivers Bordeaux, Univ Calif Riverside, Mackay Med Coll, Univ Bern, Oregon Hlth & Sci Univ, Shanghai Univ Tradit Chinese Med, Hacettepe Univ, City Univ Hong Kong, Natl Taiwan Univ, Chinese Acad Agr Sci, Florida State Univ, Tianjin Med Univ, Dana Farber Canc Inst, Natl Hlth Res Inst, George Washington Univ, Toronto Gen Hosp, Shandong Univ, Purdue Univ, NIBSC, Shanghai Jiao Tong Univ, Univ Hosp St Etienne, Inland Norway Univ Appl Sci, Zurich Univ Appl Sci, Jawaharlal Nehru Univ, Univ Burgundy Franche Comte, Univ Roehampton, Univ Wurzburg, Fraunhofer WKI, Univ Amsterdam, Aalborg Univ, VA Pittsburgh Healthcare Syst, Cedars Sinai Med Ctr, Dezhou Univ, Maison Teledetection, Xiamen Univ, Nanjing Univ, Universidade Federal de Minas Gerais (UFMG), Univ Minho, Johns Hopkins Bloomberg Sch Publ Hlth, Max Planck Inst Biol Ageing, Univ Swaziland, Ctr Sci Monaco, HELIOS Hosp, Tech Univ Carolo Wilhelmina Braunschweig, Univ Barcelona, Dublin City Univ, Schoen Clin Roseneck, Univ Med Ctr Hamburg Eppendorf, Nankai Univ, Royal Holloway Univ London, Bermuda Inst Ocean Sci, Kanazawa Univ, World Hlth Org Reg Off Africa, Univ Hosp BesanCon, Galapagos NV, Georg August Univ Gottingen, Univ Occupat & Environm Hlth, IMDEA Food, German Diabet Ctr, Juntendo Univ, Max Planck Inst Eusenforschung, Edge Hill Univ, Aga Khan Univ, Cardinal Hlth Specialty Solut, Klinikum Univ Munchen, Royal Shrewsbury Hosp, Univ Macau, North China Elect Power Univ, Justus Liegbig Univ, EBI, Max Planck Inst Marine Microbiol, Max Planck Inst Human Dev, King Faisal Univ, Iowa State Univ, Delft Univ Technol, Shinko Mem Hosp, James Madison Univ, Univ Hosp Ulm, Univ Essex, Alpha Altis, Fed Univ Oye, Helsinki Univ Hosp, Univ Aveiro, Univ Botswana, Universidade Federal da Bahia (UFBA), Queen Mary Univ London, Natl Univ Pharm, Univ Bolton, Gen Hosp Northern Theater Command, Doctors Hosp, Hannover Med Sch, Iran Univ Sci & Technol, Khalifa Univ Sci & Technol, Shaoxing Peoples Hosp, AIIMS, Tokyo Med Univ, Univ Hosp Zurich, Univ Maryland, Stellenbosch Univ, China Agr Univ, Osaka Univ, Univ Washington, Natl Res Council Italy, Charles Sturt Univ, Shantou Univ, Shanxi Univ, Georgia Inst Technol, XtalPi Inc, Consejo Nacl Invest Cient & Tecn, Jinan Univ, Univ Texas Hlth Sci Ctr Houston, Weill Cornell Med, Guangdong Inst Appl Biol Resources, Shandong Normal Univ, South China Agr Univ, Liaoning Acad Agr Sci, Lawson Hlth Res Inst, Univ Canberra, Emory Univ, Nottingham Trent Univ, Univ Exeter, Hillingdon Hosp NHS Fdn Trust, Natl & Kapodistrian Univ Athens, Lausanne Univ Hosp, Queens Univ Belfast, Cold Spring Harbor Lab, Hosp Clin Porto Alegre, Univ Paris 05, Indian Inst Adv Res, Bambino Ges Childrens Res Hosp, Univ Cadiz, Mansoura Univ Hosp, Ctr Expertise & Biol Diagnost Cameroon, Swiss Fed Labs Mat Sci & Technol, Assiut Univ, Univ Derby, SUNY Stony Brook, Walter & Eliza Hall Inst Med Res, Janelia Res Campus, USDA ARS, Med Univ Graz, Ajou Univ, Univ Dundee, Tech Univ Dresden, Natl Univ Hlth Syst, Univ Canterbury, Univ Hosp Southern Denmark, Baylor Coll Med, Adnan Menderes Univ Aydin, Oasi Res Inst IRCCS, LSHTM, Leibniz Univ Hannover, Xi An Jiao Tong Univ, Shenzhen Univ, Cent South Univ, Univ Bridgeport, Texas Tech Univ, Univ Montana, NHLBI, Cleveland Clin, NARO, Eduardo Mondlane Univ, RAS, Beijing Inst Technol, Univ Hlth Network, Univ Bath, Fisheries & Oceans Canada, Queensland Govt, Uppsala Univ, Childrens Canc Hosp, Leibniz Inst Nat Prod Res & Infect Biol, Duy Tan Univ, Henan Agr Univ, Beijing Inst Microbiol & Epidemiol, Minist Hlth, Prince Sattam Bin Abdulaziz Univ, Univ Auckland, Osped Niguarda Ca Granda, Univ Vet Med, Univ Saskatchewan, Univ Coimbra, South Cent High Specialty Hosp, Wageningen Bioveterinary Res, Guangdong Second Prov Gen Hosp, Hiroshima Univ, Univ Iceland, Kathmandu Univ, Fraunhofer MEVIS, Univ Tehran Med Sci, Univ Messina, AO Papardo Hosp Messina, Univ Stirling, Saveh Univ Med Sci, Gakujutsu Shien Co Ltd, Univ Plymouth, CHU Toulouse, Azorean Biodivers Grp, Univ Acores, Univ Malawi, Bioself Commun, Ahmadu Bello Univ, Dalhousie Univ, VisMederi Srl, Amer Univ Beirut, Mechnikov Res Inst Vaccines & Sera, Vreden Russian Res Inst Traumatol & Orthopaed, Hangzhou Ctr Dis Control & Prevent, Kaohsiung Med Univ, Zoetis, Aintree Univ Hosp NHS Fdn Trust, Wrightington Hosp, Loyola Univ, Atkins Vet Serv, Kangwon Natl Univ, Kakatiya Med Coll, Univ Antioquia, IISER, Univ Rosario, Univ Hosp Basel, Univ Hosp Munster, Univ Kentucky, Univ Calif Irvine, Univ Hosp Leuven, Chongqing Med Univ, Childrens Hosp Kings Daughters, China Three Gorges Univ, and Xiangtan Univ
Subjects: Technology and Engineering, SCIENTIFIC SEARCH, Expert-curated database, Biokemia, solu- ja molekyylibiologia - Biochemistry, cell and molecular biology, Databases, RElevant LIterature SearcH consortium, Medicine and Health Sciences, Biomedical research, benchmarking, Biology, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries), Settore MED/42 - IGIENE GENERALE E APPLICATA, database, Computer. Automation, Science & Technology, 0804 Data Format, relisch, Scientific research in health sciences, Mathematics and Statistics, litearture search, relisch , database, biomedical research, Biomedical literature, Original Article, RELISH, Mathematical & Computational Biology, RECOMMENDER-SYSTEMS, Life Sciences & Biomedicine, Mathematics, 0807 Library and Information Studies
Abstract: Made available in DSpace on 2020-12-11T01:57:28Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-10-29 Griffith University Gowonda HPC Cluster Queensland Cyber Infrastructure Foundation Document recommendation systems for locating relevant literature have mostly relied on methods developed a decade ago. This is largely due to the lack of a large offline gold-standard benchmark of relevant documents that cover a variety of research fields such that newly developed literature search techniques can be compared, improved and translated into practice. To overcome this bottleneck, we have established the RElevant LIterature SearcH consortium consisting of more than 1500 scientists from 84 countries, who have collectively annotated the relevance of over 180 000 PubMed-listed articles with regard to their respective seed (input) article/s. The majority of annotations were contributed by highly experienced, original authors of the seed articles. The collected data cover 76% of all unique PubMed Medical Subject Headings descriptors. No systematic biases were observed across different experience levels, research fields or time spent on annotations. More importantly, annotations of the same document pairs contributed by different scientists were highly concordant. We further show that the three representative baseline methods used to generate recommended articles for evaluation (Okapi Best Matching 25, Term Frequency-Inverse Document Frequency and PubMed Related Articles) had similar overall performances. Additionally, we found that these methods each tend to produce distinct collections of recommended articles, suggesting that a hybrid method may be required to completely capture all relevant articles. The established database server located at https://relishdb.ict.griffith.edu.au is freely available for the downloading of annotation data and the blind testing of new methods. We expect that this benchmark will be useful for stimulating the development of new powerful techniques for title and title/abstract-based search engines for relevant articles in biomedical research. Griffith Univ, Sch Informat & Commun Technol, Gold Coast, Qld 4222, Australia Griffith Univ, Inst Glyc, Gold Coast, Qld 4222, Australia Univ Colorado, Dept Med Med Oncol, Anschutz Med Campus, Denver, CO USA Tanta Univ, Fac Sci, Bot Dept, Tanta, Egypt Friedrich Schiller Univ, Jena Univ Hosp, Inst Human Genet, Jena, Germany Univ Med Ctr Schleswig Holstein, Dept Radiat Oncol, Campus Kiel, Kiel, Germany ARS, USDA, Plum Isl Anim Dis Ctr, Greenport, NY 11944 USA Univ Jyvaskyla, Dept Biol & Environm Sci, Jyvaskyla, Finland Graz Univ Technol, Inst Environm Biotechnol, Graz, Austria CSIC, CNB, Natl Biotechnol Ctr, Dept Macromol Struct, Madrid, Spain Univ Hong Kong, Fac Dent, Oral & Maxillofacial Radiol Appl Oral Sci & Commu, Hong Kong, Peoples R China Univ Kansas, Div Entomol, Biodivers Inst, Lawrence, KS 66045 USA SUNY Albany, RNA Inst, Albany, NY 12222 USA Robert Koch Inst, Dept Methods Dev & Res Infrastruct, Berlin, Germany Martin Luther Univ Halle Wittenberg, Dept Surg & Conservat Pediat & Adolescent Med, Halle, Germany Indiana Univ Purdue Univ, IU Sch Informat & Comp, Dept BioHlth Informat, Indianapolis, IN 46202 USA Univ Reading, Sch Pharm Stem Cell Biol & Regenerat Med, Reading, Berks, England Dali Univ, Sch Engn, Dali City, Yunnan, Peoples R China Univ Hosp Munich LMU, Dept Psychiat & Psychotherapy, Munich, Germany Univ Tsukuba, Fac Life & Environm Sci, Ibaraki, Japan UniLaSalle, Aghyle, Beauvais, France Henry Ford Hlth Syst, Dept Immunol, Detroit, MI USA Zhejiang Univ, Sch Med, Sir Run Run Shaw Hosp, Dept Emergency, Hangzhou 310016, Zhejiang, Peoples R China Ist Nazl Tumori Fdn Pascale IRCCS, Anesthesia & Pain Med, Naples, Italy NIH, Dept Transfus Med, Bethesda, MD USA Univ Glasgow, Inst Infect Immun & Inflammat, Glasgow, Lanark, Scotland Polish Acad Sci, Inst Human Genet, Poznan, Poland Univ Padua, Dept Surg Oncol & Gastroenterol DISCOG, Padua, Italy Eindhoven Univ Technol, Biomed Engn, Eindhoven, Netherlands Univ Strasbourg, IBMC, Strasbourg, France Heidelberg Univ, Dept Gen Visceral & Transplantat Surg, Heidelberg, Germany Univ Notre Dame, Psychol, Notre Dame, IN 46556 USA Harvard Med Sch, Massachusetts Gen Hosp, Radiol & Pathol, Boston, MA 02115 USA Auburn Univ, Dept Biol Sci, Auburn, AL 36849 USA KK Womens & Childrens Hosp, KK Res Ctr, Singapore, Singapore Univ Alabama, Educ Psychol, Tuscaloosa, AL USA UCL, Wellcome EPSRC Ctr Intervent & Surg Sci, London, England Maastricht Univ, Dept Nutr & Movement Sci, Maastricht, Netherlands Univ Arkansas Med Sci, Dept Radiat Oncol, Little Rock, AR 72205 USA Univ Padua, Dept Land Environm Agr & Forestry, Padua, Italy Univ Gothenburg, Dept Biol & Environm Sci, Gothenburg, Sweden Univ Newcastle, Prior Res Ctr Reprod Sci, Callaghan, NSW, Australia Univ Cyprus, Med Sch, Nicosia, Cyprus Shandong Agr Univ, Coll Plant Protect, Agr Big Data Res Ctr, Tai An, Shandong, Peoples R China NIMH, Neuropsychol Lab, Bldg 9, Bethesda, MD 20892 USA Univ Wisconsin, Wisconsin Inst Discovery, Madison, WI USA Univ Oxford, Struct Genom Consortium, Oxford, England Weihenstephan Triesdorf Univ Appl Sci, TUM Campus Straubing Biotechnol & Sustainabil, Bioinformat, Straubing, Germany Univ Michigan, Cardiovasc Res, Ann Arbor, MI 48109 USA Bombay Coll Pharm, Pharmaceut Chem, Mumbai, Maharashtra, India Inst Invest Biol Clemente Estable, Dev Neurobiol, Montevideo, Uruguay Gem Hosp & Res Ctr, Surg Gastroenterol & HPB Surg, Coimbatore, Tamil Nadu, India Kafr El Sheikh Univ, Fac Sci, Dept Zool, Kafr Al Sheikh, Egypt Med Univ Innsbruck, Dept Internal Med 4, Innsbruck, Austria Australian Natl Univ, Div Biomed Sci & Biochem, Canberra, ACT, Australia Univ Cattolica Sacro Cuore, Appl Technol Neuropsychol Lab, Milan, Italy Shandong Inst Parasit Dis, Med Entomol, Jinan, Shandong, Peoples R China Kumamoto Univ, Sch Pharm, Kumamoto, Japan Nagoya City Univ, Grad Sch Pharmaceut Sci, Dept Biol Chem, Nagoya, Aichi, Japan Univ Karachi, ICCBS, PCMD, Jamil ur Rahman Ctr Genome Res, Karachi 75270, Pakistan Labormed Zentrum Dr Risch, Vaduz, Liechtenstein Univ Otago, Med, Dunedin, New Zealand KK Womens & Childrens Hosp, Maternal Fetal Med, Singapore, Singapore Albert Ludwigs Univ Freiburg, GERN Tissue Replacement Regenerat & Neogenesis, Dept Orthoped & Trauma Surg, Med Ctr,Fac Med, Freiburg, Germany Heinrich Heine Univ, Inst Biochem & Mol Biol, Dusseldorf, Germany Natl Univ Ireland Galway, Surg, Galway, Ireland Univ Western Australia, Inst Agr, Perth, WA, Australia Univ Oxford, Nuffield Dept Med, Oxford, England SingHlth Polyclin, Punggol Polyclin, Singapore, Singapore Med Univ Innsbruck, Bioctr, Div Biol Chem, Innsbruck, Austria La Trobe Univ, La Trobe Inst Mol Sci, Biochem & Genet, Melbourne, Vic, Australia Univ Bordeaux, INRA, Bordeaux, France Agr & Agri Food Canada, Lethbridge Res & Dev Ctr, Lethbridge, AB, Canada St George Hosp, Trauma & Orthopaed, London, England Max Planck Inst Dev Biol, Dept Prot Evolut, Tubingen, Germany Med Univ Lublin, Dept Gynaecol 2, Lublin, Poland ICIT, ICSI Analyt Natl Res & Dev, Ramnicu Valcea, VL, Romania Univ KwaZulu Natal, Occupat Therapy, Westville Campus, Durban, South Africa Inst Canc Res, Joint Dept Phys, London, England Karolinska Inst, Dept Mol Med & Surg, Solna, Sweden Wenzhou Med Univ, Affiliated Hosp 2, Orthopaed, Wenzhou, Zhejiang, Peoples R China Univ Republica, Fac Ciencias, Ctr Invest Nucl, Lab Virol Mol, Montevideo, Uruguay Univ Gothenburg, Dept Med Biochem & Cell Biol, Gothenburg, Sweden Charite Med Univ Berlin, Pediat Cardiol, Berlin, Germany Bambino Gesu Pediat Hosp, Dept Neurosci & Neurorehabil, Neurorehabil Unit, Rome, Italy Indiana Univ Sch Med Northwest, Microbiol & Immunol, Gary, IN USA Univ Regensburg, Dept Behav & Mol Neurobiol, Regensburg, Germany Univ Queensland, Diamantina Inst, Brisbane, Qld, Australia Translat Res Inst, Brisbane, Qld, Australia Univ Hong Kong, Sch Biomed Sci, Hong Kong, Peoples R China St Jude Childrens Res Hosp, Pharmaceut Sci Dept, 332 N Lauderdale St, Memphis, TN 38105 USA Univ Durham, Mus, Durham, England Univ Ioannina, Med Sch, Dept Hyg & Epidemiol, Ioannina, Greece Tech Univ Munich, Sch Life Sci Weihenstephan, Maximus von Imhof Forum 3, D-85354 Freising Weihenstephan, Germany Univ Hosp Essen, Inst Transfus Med, Essen, Germany Virginia Commonwealth Univ, Comp Sci, Richmond, VA USA Univ Queensland, Inst Social Sci Res, Brisbane, Qld, Australia Univ Lyon, Ctr Int Rech Infectiol, Lyon, France Griffith Univ, Sch Allied Hlth Sci, Gold Coast, Qld, Australia Univ Melbourne, Dept Biochem & Mol Biol, Parkville, Vic, Australia Indiana Univ Purdue Univ, Dept Biohlth Informat, Sch Informat & Comp, Indianapolis, IN 46202 USA Philipps Univ Marburg, Inst Lung Res, Marburg, Germany Indiana Univ, Dept Biol, Bloomington, IN USA Univ Florida, Oral Biol, Gainesville, FL USA Univ Colorado, Dept Biochem, Boulder, CO 80309 USA Kyoto Univ, Ctr Promot Interdisciplinary Educ & Res, Kyoto, Japan Friedrich Loeffler Inst, Inst Virus Diagnost, Greifswald, Germany Univ Oxford, Dept Zool, Oxford, England Tech Univ Munich, Dept Bioinformat, Munich, Germany Univ Adelaide, Sch Anim & Vet Sci, Adelaide, SA, Australia Stanford Univ, Canc Biol, Palo Alto, CA 94304 USA Covenant Univ, Dept Elect & Informat Engn, Ota, Nigeria Heinrich Heine Univ, Inst Stem Cell Res & Regenerat Med, Dusseldorf, Germany Univ British Columbia, Fac Pharmaceut Sci, Vancouver, BC, Canada Albert Einstein Coll Med, Psychiat, New York, NY USA Akdeniz Univ, Med Biol & Genet, Antalya, Turkey NIMH, NIH, Bethesda, MD 20892 USA Med Univ Hosp, Internal Med 1, Tubingen, Germany NET ESolut, Netelabs, Mclean, VA USA Univ Southern Denmark, Inst Publ Hlth, Odense, Denmark John Innes Ctr, Mol Microbiol, Norwich, Norfolk, England Univ Adelaide, Waite Res Precinct, Australian Res Council, Ctr Excellence Plant Energy Biol, Adelaide, SA, Australia Univ Cambridge, Cambridge Inst Publ Hlth, Cambridge, England Univ Munster, Inst Biochem, Munster, Germany Australian Natl Univ, Natl Ctr Epidemiol & Populat Hlth RSPH, Canberra, ACT, Australia Stanford Univ, Neurobiol & Bioengn, Palo Alto, CA 94304 USA Univ Birmingham, Geog Earth & Environm Sci, Birmingham, W Midlands, England Murdoch Univ, Sch Vet & Life Sci, Perth, WA, Australia George Mason Univ, Ctr Climate Change Commun, Fairfax, VA 22030 USA Univ Adelaide, Sch Agr Food & Wine, Adelaide, SA, Australia Southern Med Univ, Sch Pharmaceut Sci, Guangzhou, Guangdong, Peoples R China Stanford Univ, Pathol, Palo Alto, CA 94304 USA Univ Bologna, Dept Expt Diagnost & Specialty Med, Bologna, Italy Univ Padua, Dept Gen Psychol, Padua, Italy Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Bioinformat & Syst Biol, Key Lab Mol Biophys,Minist Educ, Wuhan, Hubei, Peoples R China Huazhong Univ Sci & Technol, Collaborat Innovat Ctr Biomed Engn, Wuhan, Hubei, Peoples R China Queensland Univ Technol, Sch Biomed Sci, Brisbane, Qld, Australia French Natl Ctr Sci Res, CNRS, Inst Biol Physicochim, Paris, France Univ Warwick, Dept Sociol, Coventry, W Midlands, England European Mol Biol Lab, Struct & Computat Biol, Heidelberg, Germany Univ Cincinnati, Coll Med, Canc Biol, Cincinnati, OH USA Univ Waterloo, Biol, Waterloo, ON, Canada Sorbonne Univ, CNRS, Integrat Biol Marine Models LBI2M, SBR, Roscoff, France Univ Manitoba, Biochem & Med Genet, Winnipeg, MB, Canada Max Planck Inst Solid State Res, Ultrafast Solid State Spect, Stuttgart, Germany Imperial Coll London, Sch Publ Hlth, Dept Infect Dis Epidemiol, London, England Mansoura Univ, Fac Vet Med, Biochem, Mansoura, Egypt Univ Virginia, Mol Physiol & Biol Phys, Charlottesville, VA USA China Univ Geosci, State Key Lab Biogeol & Environm Geol, Wuhan, Hubei, Peoples R China Clin Neurol & Psychiat Children & Youth, Child Psychiat, Belgrade, Serbia Ahvaz Jundishapur Univ Med Sci, Med Phys, Ahwaz, Iran Univ Iowa City, Coll Dent, Div Biostat & Computat Biol, Dept Prevent & Community Dent, Iowa City, IA USA Univ Iowa City, Coll Dent, Div Biostat & Computat Biol, Dept Biomed Engn, Iowa City, IA USA Univ Iowa City, Coll Dent, Div Biostat & Computat Biol, Dept Biostat, Iowa City, IA USA Univ Tubingen, Inst Med Psychol & Behav Neurobiol, Tubingen, Germany Univ Ibadan, Dept Zool, Ibadan, Nigeria Kansas State Univ, Coll Vet Med, Manhattan, KS 66506 USA Univ Tasmania, Sch Technol Environm & Design, Discipline ICT, Hobart, Tas, Australia Childrens Mercy Hosp, Radiol, Kansas City, MO 64108 USA Stockholm Univ, Dept Phys, Stockholm, Sweden Oslo Univ Hosp, Inst Canc Genet & Informat, Oslo, Norway CSIRO, CSIRO Mfg, Pullenvale, Qld, Australia Johns Hopkins Sch Med, Urol, Baltimore, MD USA Univ South Africa, Life & Consumer Sci, Johannesburg, South Africa German Ctr Neurodegenerat Dis, Mech Induced Plast Brain, Bonn, Germany UCL, Inst Child Hlth, Dev Biol & Canc, London, England Simon Fraser Univ, Biomed Physiol & Kinesiol, Burnaby, BC, Canada Univ Manchester, Ctr Hlth Informat, Manchester, Lancs, England Univ Queensland, Sch Human Movement & Nutr Sci, Brisbane, Qld, Australia Albert Einstein Coll Med, Dept Med, New York, NY USA Georgetown Univ, Kennedy Inst Eth, Washington, DC 20057 USA Dermatol Skin & Canc Fdn, Carlton, Vic, Australia Med Coll Wisconsin, Div Hematol, Milwaukee, WI 53226 USA Med Coll Wisconsin, Div Oncol, Milwaukee, WI 53226 USA Med Coll Wisconsin, Div Infect Dis, Milwaukee, WI 53226 USA US FDA, Off Biotechnol Prod, Washington, DC 20204 USA Worcester Polytech Inst, Biomed Engn, Worcester, MA 01609 USA Univ Adelaide, Ctr Orthopaed & Trauma Res, Adelaide, SA, Australia Publ Hlth England, Natl Infect Serv, Bristol, Avon, England Univ Utrecht, Fac Sci Chem, Utrecht, Netherlands Natl Univ Ireland Galway, Pathol, Galway, Ireland Imperial Coll London, NHLI, London, England Danube Private Univ, Neurodegenerat, Krems Donau, Austria Imperial Coll London, Dept Chem, London, England Univ Helsinki, Finnish Museum Nat Hist, Helsinki, Finland Univ Sydney, Sch Life & Environm Sci, Sydney, NSW, Australia Univ Nottingham, Nottingham Digest Dis Ctr, Nottingham, England Univ Toulouse, CNRS, ITAV, USR3505, Toulouse, France ASCR, Inst Mol Genet, CZ Openscreen, Prague, Czech Republic Univ Turku, Inst Biomed, Turku, Finland York Univ, Sch Kinesiol & Hlth Sci, Toronto, ON, Canada Univ Calif Los Angeles, Stein Eye Inst, Ophthalmol, Los Angeles, CA USA Agr & Agri Food Canada, Ottawa Res & Dev Ctr, Ottawa, ON, Canada Helmholtz Zentrum Geesthacht, Mat Design & Characterizat, Geesthacht, Germany Unvers Genova, Internal Med, Genoa, Italy Otto von Guericke Univ, Intelligent Catheter INKS, Magdeburg, Germany Univ Toledo, Canc Biol, 2801 W Bancroft St,Hlth Sci Campus, Toledo, OH 43606 USA CRUK Beatson Inst, Struct Biol, Glasgow, Lanark, Scotland Leibniz Inst Primate Res, Med RNA Biol, Gottingen, Germany Univ Limoges, PEIRENE, EA 7500, Limoges, France Hainan Univ, Vet Med, Haikou, Hainan, Peoples R China UCL, Sch Pharam, Pharmacognosy & Phytotherapy, London, England Univ Oulu, Ecol & Genet Res Unit, Oulu, Finland Rhein Westfal TH Aachen, Inst Biochem & Mol Immunol, Aachen, Germany Univ Stuttgart, Inst Biochem & Tech Biochem, Stuttgart, Germany Peking Univ, Shenzhen Grad Sch, Sch Chem Biol & Biotechnol, Shenzhen, Peoples R China GIGA Res Inst, Med Oncol, Liege, Belgium CHULiege, Liege, Belgium Fdn Bruno Kessler, MPBA, Trento, Italy Hokkaido Univ, Grad Sch Med, Dept Neurobiol, Sapporo, Hokkaido, Japan Univ Leuven, Oncol, Leuven, Belgium Chalmers Univ Technol, Dept Math Sci, Gothenburg, Sweden Radboud Univ Nijmegen, Med Ctr, Dept Neurol, Nijmegen, Netherlands Univ South Australia, Sch Informat Technol & Math Sci, Adelaide, SA, Australia Bio Thera Solut Ltd, Dept Computat Biol, Guangzhou, Guangdong, Peoples R China Inst Invest Biosanitario Granada IBS, Otolaryngol, Granada, Spain Curtin Univ, Sch Mol & Life Sci, Perth, WA, Australia Newcastle Univ, Inst Cellular Med, Newcastle Upon Tyne, Tyne & Wear, England Goethe Univ, Biol DCAL, Inst Pharm, Frankfurt, Germany Univ Lyon, ICBMS, UMR 5246, Lyon, France Inst Pasteur, Dept Genomes & Genet, Paris, France Univ Valencia, Pharmacol, Valencia, Spain Council Agr Res & Econ, Res Ctr Olive Citrus & Tree Fruit, Caserta, Italy Fraunhofer Inst Toxicol & Expt Med ITEM, Preclin Pharmacol & Vitro Toxicol, Hannover, Germany Univ Tasmania, Sch Med, Hobart, Tas, Australia Chugai Pharmaceut Co Ltd, Oncol Lifecycle Management Dept, Tokyo, Japan Univ Lubeck, Inst Neurobiol, Lubeck, Germany NYU, Sch Med, Neurol, New York, NY USA Univ Putra Malaysia, Dept Plant Pathol, Seri Kembangan, Malaysia Univ N Carolina, Biol, Chapel Hill, NC 27515 USA Univ Southampton, Fac Hlth Sci, Southampton, Hants, England Univ Highlands & Islands, Genet & Immunol Res Grp, Inverness, Scotland Heidelberg Univ, Inst Pathol, Heidelberg, Germany Indraprastha Inst Informat Technol, Dept Computat Biol, New Delhi, India Glasgow Caledonian Univ, Sch Hlth & Life Sci, Glasgow, Lanark, Scotland Liverpool John Moores Univ, Pharm & Biomol Sci, Liverpool, Merseyside, England Parkinsons Inst & Clin Ctr, Basic Res, Sunnyvale, CA USA Luxembourg Inst Sci & Technol, Environm Res & Innovat, Luxembourg, Luxembourg Univ Wollongong, Sch Comp & Informat Technol, Wollongong, NSW, Australia Univ Bari Aldo Moro, Dept Biomed Sci & Human Oncol, Bari, Italy Flinders Univ S Australia, Coll Nursing & Hlth Sci, Adelaide, SA, Australia Univ S Florida, Mol Med, Tampa, FL USA Univ Texas Dallas, Behav & Brain Sci, Richardson, TX 75083 USA Rhodes Univ, Zool & Entomol, Grahamstown, South Africa Univ Nova Lisboa, Inst Higiene & Med Trop, Lisbon, Portugal Swiss Fed Inst Technol, Inst Microbiol, Zurich, Switzerland Inst Ulm, German Red Cross Blood Serv, Immunohaematol, Ulm, Germany Tokyo Womens Med Univ, Inst Adv Biomed Engn & Sci, Tokyo, Japan Univ Limerick, Biol Sci, Limerick, Ireland McGill Univ, Dept Anim Sci, Montreal, PQ, Canada StatSol, Lubeck, Germany Univ KwaZulu Natal, Sch Math Stat & Comp Sci, Pietermaritzburg, South Africa Univ Kebangsaan Malaysia, Inst Syst Biol INBIOSIS, Bangi, Malaysia NIH, Natl Ctr Complementary & Integrat Hlth, Bldg 10, Bethesda, MD 20892 USA Univ Kansas, Med Ctr, Family Med Res Div, Kansas City, KS 66103 USA ASTAR, Inst Mol & Cell Biol, Multimodal Mol Biol, Singapore, Singapore Univ Leuven, Dept Chron Dis Metab & Ageing, Leuven, Belgium Int Iberian Nanotechnol Lab INL, Braga, Portugal Anglia Ruskin, Comp & Technol, Cambridge, England Max Planck Inst Biochem, Struct Cell Biol, Planegg, Germany Univ Seville, Dept Comp Architecture & Technol, Seville, Spain Univ Colorado, EBIO, Boulder, CO 80309 USA Univ Manchester, Canc Sci, Manchester, Lancs, England Australian Natl Univ, Res Sch Populat Hlth, Canberra, ACT, Australia Singapore MIT Alliance Res & Technol, Biosyst, Singapore, Singapore Australian Catholic Univ, Mary MacKillop Inst Hlth Res, Musculoskeletal Hlth & Ageing Res Program, Melbourne, Vic, Australia Ruhr Univ Bochum, Gen Surg, St Josef Hosp, Bochum, Germany Northwest A&F Univ, Coll Life Sci, Xianyang, Shaanxi, Peoples R China Australian Natl Univ, Res Sch Biol, Div Plant Sci, Canberra, ACT, Australia Battelle Mem Inst, Clin & Nonclin Res, Columbus, OH USA Southern Methodist Univ, Biol Sci, Dallas, TX 75275 USA Teikyo Univ, Inst Med Mycol, Tokyo, Japan Tempus Labs, Bioinformat, Chicago, IL USA Hunan Univ, Coll Biol, Changsha, Hunan, Peoples R China Inst Cochin, Dept Infect Immun & Inflammat, Paris, France Royal Coll Surgeons Ireland, FutureNeuro Res Ctr Physiol & Med Phys, Dublin, Ireland Univ Jyvaskyla, Gerontol Res Ctr, Jyvaskyla, Finland Heidelberg Univ, Dept Anesthesiol, Heidelberg, Germany Penn State Univ, Biol, University Pk, PA 16802 USA Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing, Peoples R China Univ Sci & Technol China, Sch Life Sci, Hefei, Anhui, Peoples R China Michigan State Univ, Anim Sci, E Lansing, MI 48824 USA SUNY Buffalo, Jacobs Sch Med & Biomed Sci, Dept Neurol, Buffalo Neuroimaging Anal Ctr, New York, NY USA Univ Rostock, Inst Biol Sci, Rostock, Germany South China Normal Univ, Sch Environm, Environm Res Inst, Guangzhou, Guangdong, Peoples R China Univ Bari, Dept Vet Med, Bari, Italy Radboud Univ Nijmegen, Med Ctr, Primary & Community Care, Nijmegen, Netherlands EcoHlth Alliance, New York, NY USA Mayo Clin, Cardiovasc Dept, Rochester, MN USA Med Univ Silesia, Sch Med Katowice, Dept Epidemiol, Katowice, Poland Univ Lleida, Anim Sci, Lleida, Spain Univ Florida, Coll Pharm, Pharmaceut Outcomes & Policy, Gainesville, FL USA Pacific Northwest Natl Lab, Earth & Biol Sci Directorate, Richland, WA 99352 USA Univ Edinburgh, Ctr Discovery Brain Sci, Edinburgh, Midlothian, Scotland Harvard Med Sch, Dept Biomed Informat, Boston, MA 02115 USA Univ Penn, Radiol, Philadelphia, PA 19104 USA Humanitas Univ & Res Hosp, Asthma & Allergy Unit, Biomed Sci Personalized Med, Rozzano, Italy Australian Natl Univ, Dept Quantum Sci, Canberra, ACT, Australia Carl von Ossietzky Univ Oldenburg, Ecol Genom, Oldenburg, Germany Int Med Univ, Paediat Dent & Orthodont, Kuala Lumpur, Malaysia Univ Ottawa, Sch Nursing, Ottawa, ON, Canada Maastricht Univ, Dept Educ Support, Maastricht, Netherlands Univ Manchester, Math, Manchester, Lancs, England Kings Coll London, Fac Life Sci & Med, Sch Populat Hlth Sci, London, England Queensland Univ Technol, Inst Hlth & Biomed Innovat, Brisbane, Qld, Australia Harbin Med Univ, Publ Hlth Sch, Epidemiol, Harbin, Heilongjiang, Peoples R China UiT Arctic Univ Norway, Dept Chem, Tromso, Norway Cornell Univ, Biol Stat & Computat Biol, Ithaca, NY USA East China Normal Univ, Sch Ecol & Environm Sci, Shanghai Key Lab Urban Ecol Proc & Ecorestorat, Shanghai, Peoples R China Johannes Gutenberg Univ Mainz, Fac Biol, Mainz, Germany Univ Massachusetts, Food Sci, Amherst, MA 01003 USA Max Planck Inst Terr Microbiol, Complex Adapt Traits Res Grp, Marburg, Germany NIHR Biomed Res Ctr Resp, Ctr Exercise & Rehabil Sci, Leicester, Leics, England Yale Univ, Dept Internal Med, Sect Endocrinol, New Haven, CT USA Sardar Patel Univ, Dept Biosci, Anand, Gujarat, India Univ Tokyo, Dept Appl Phys, Tokyo, Japan Univ Cologne, Vivo Res Facil ivRF, Cologne Excellence Cluster Cellular Stress Respon, Cologne, Germany Natl Open Univ Nigeria, Dept Publ Hlth Sci, Lagos, Nigeria Univ Hosp Regensburg, Dept Radiol, Regensburg, Germany Natl Univ Singapore, Geog, Singapore, Singapore Alfaisal Univ, Coll Med, Riyadh, Saudi Arabia Abdelmalek Essaadi Univ, Fac Sci & Techn Tangier, Biomed Genom & Oncogenet Res Lab, Tetouan, Morocco Tech Univ Munich, Fac Sport & Hlth Sci, Exercise Biol Grp, Munich, Germany Univ Santiago de Compostela, Dept Psicoloxia Social Basica & Metodoloxia, Galiza, Spain Griffith Univ, Signal Proc Lab, Brisbane, Qld, Australia Univ Ghent, Dept Neurol, Ghent, Belgium Ghent Univ Hosp, Ghent, Belgium Univ Ghent, Fac Vet Med, Merelbeke, Belgium Albert Einstein Coll Med, Inst Clin & Translat Res, New York, NY USA Anglia Ruskin Univ, Fac Med Sci, Cambridge, England Peking Univ, Coll Chem & Mol Engn, Beijing, Peoples R China Herlev & Gentofte Hosp, Dept Dermatol & Allergy, Hellerup, Denmark Lady Cilento Childrens Hosp, Med Imaging & Nucl Med, Brisbane, Qld, Australia Univ Gambia, Sch Med & Allied Hlth Sci, Nursing & Reprod Hlth, Brikama, Gambia Univ Sydney, Woolcock Inst Med Res, Sydney, NSW, Australia Wayne State Univ, Comp Sci, Detroit, MI USA Aberdeen Royal Infirm, Otolaryngol, Aberdeen, Scotland Univ Toronto, Lab Med & Pathobiol, Toronto, ON, Canada Chinese Univ Hong Kong, Inst Ageing, Hong Kong, Peoples R China Univ Nebraska Med Ctr, Emergency Med, Omaha, NE USA Univ Florida, Coll Med, Pathol, Gainesville, FL USA Univ Texas MD Anderson Canc Ctr, Radiat Oncol, Houston, TX 77030 USA Univ Pisa, Translat Res NTMS, Pisa, Italy Magna Grecia Univ, Clin & Expt Med, Catanzaro, Italy Univ Vermont, Larner Coll Med, Pediat, Burlington, VT USA Sun Yat Sen Univ, Canc Ctr, Diagnost & Intervent Ultrasound, Guangzhou, Guangdong, Peoples R China Fudan Univ, Inst Brain Sci, Shanghai, Peoples R China Shanxi Agr Univ, Coll Agron, Jinzhong, Shanxi, Peoples R China Univ Toronto, Inst Med Sci, Toronto, ON, Canada Univ Adelaide, ARCPOH, Adelaide, SA, Australia Pelita Harapan Univ, Fac Med, Cardiol & Vasc Med, Tangerang, Indonesia Inst Mental Hlth, Res Div, Singapore, Singapore UCL, MRC Clin Trials Unit, London, England Univ Padua, Dept Philosophy Sociol Educ & Appl Psychol FISPPA, Padua, Italy Univ Lubeck, Dept Psychiat & Psychotherapy, Lubeck, Germany Dalian Univ Technol, Ctr Mol Med, Dalian, Liaoning, Peoples R China Tianjin United Family Healthcare, Reprod Med, Tianjin, Peoples R China Univ Autonoma Barcelona, Dept Engn Quim Biol & Ambiental, Barcelona, Spain Sao Paulo State Univ UNESP, Dept Anim Sci, Sao Paulo, Brazil Helmholtz Zentrum Munchen, Inst Computat Biol, Canc Syst Biol, Ingolstadter Land Str 1, D-85764 Munich, Germany Univ Tokyo, Dept Cardiovasc Med, Tokyo, Japan Sao Paulo State Univ, Vet Clin, Sao Paulo, Brazil Zhejiang Univ, Inst Biotechnol, Hangzhou, Zhejiang, Peoples R China Aarhus Univ, Dept Mol Biol & Genet, Aarhus, Denmark Univ Manchester, St Marys Hosp, Maternal & Fetal Hlth, Manchester, Lancs, England Univ New Mexico, Internal Med, Albuquerque, NM 87131 USA Mayo Clin, Div Biomed Stat & Informat, Jacksonville, FL 32224 USA King Saud Univ, Plant Prod, Riyadh, Saudi Arabia Polish Acad Sci, Inst Genet & Anim Breeding, Dept Mol Biol, Warsaw, Poland Queensland Univ Technol, Optometry & Vis Sci, Brisbane, Qld, Australia Univ Nottingham, Sch Life Sci, Nottingham, England Canc Council Queensland, Canc Res Ctr, Brisbane, Qld, Australia Umea Univ, Dept Chem, Umea, Sweden Publ Hlth England, Ctr Radiat Chem & Environm Hazards, Bristol, Avon, England Univ Campania L Vanvitelli, DISTABIF, Caserta, Italy Bartshealth, Obstet & Gyanecol, London, England Univ Clermont Auvergne, GReD Lab, Clermont Ferrand, France INRA Abeilles & Environm, Avignon, France Queensland Univ Technol, Sch Publ Hlth & Social Work, Brisbane, Qld, Australia Univ Penn, Psychiat, Philadelphia, PA 19104 USA Novosibirsk State Univ, Res Inst Physiol & Basic Med, Novosibirsk, Russia UCL, Dept Chem, London, England La Trobe Univ, Anim Plant & Soil Sci, Melbourne, Vic, Australia Univ Arizona, Epidemiol & Biostat, Tucson, AZ USA Univ Groningen, Univ Med Ctr Groningen, ERIBA, Groningen, Netherlands Univ Gothenburg, Inst Clin Sci, Dept Radiat Phys, Gothenburg, Sweden SUNY Upstate Med Univ, Biochem & Mol Biol, Syracuse, NY 13210 USA Fundacao Oswaldo Cruz, Ctr Pesquisas Goncalo Moniz, Salvador, Bahia, Brazil Inst Environm Sci & Res ESR, Food Water & Environm Microbiol, Christchurch, New Zealand Univ Otago, Food Sci, Dunedin, New Zealand Florida Atlantic Univ, Biomed Sci, Boca Raton, FL 33431 USA Univ Queensland, Inst Mol Biosci, Brisbane, Qld, Australia Univ Hosp Wurzburg, Inst Clin Neurobiol, Wurzburg, Germany Inst Trop Med, Publ Hlth, Antwerp, Belgium Univ Thessaly, Sch Hlth Sci, Fac Med, Dept Rheumatol & Clin Immunol, Larisa, Greece Univ Basel, UZB Univ Ctr Dent Med, Dept Orthodont & Pediat Dent, Basel, Switzerland Sorbonne Univ, Museum Natl Hist Nat, Inst Systemat Evolut Biodiversite ISYEB, MNHN,CNRS,UMR 7205,EPHE, Paris, France CNRS, Inst Adv Biosci, Paris, France Univ Western Australia, Sch Mol Sci, Perth, WA, Australia Univ Ft Hare, Biochem & Microbiol, Alice, South Africa Univ Tubingen, Phys, Tubingen, Germany Griffith Univ, Sch Environm & Sci, Brisbane, Qld, Australia Philosoph Theol Hsch Vallendar, Stat & Standardised Methods, Vallendar, Germany Imperial Coll London, Life Sci, London, England Univ Adelaide, Adelaide Med Sch, Adelaide, SA, Australia Univ Nebraska Med Ctr, Dept Pharmacol & Expt Neurosci, Omaha, NE USA Technol Univ Dublin, FOCAS Res Inst, Dublin, Ireland INSERM, Natl Inst Hlth & Med Res, Canc Res Ctr Toulouse, Paris, France Univ Santiago de Compostela, Dept Bioloxia Func, Grp BRAINSHARK, Galiza, Spain Univ Nebraska, Biol, Kearney, NE USA Univ Autonoma Barcelona, Dept Genet & Microbiol, Barcelona, Spain Univ Pisa, Chem & Ind Chem, Pisa, Italy Univ Manchester, Wellcome Trust Ctr Cell Matrix Res, Manchester, Lancs, England Univ Montpellier, CNRS, Inst Human Genet, Montpellier, France Czech Acad Sci, Inst Organ Chem & Biochem, Prague, Czech Republic CSIC, Natl Ctr Biotechnol CNB, Computat Syst Biol Grp, Madrid, Spain Natl Cheng Kung Univ, Dept Biochem & Mol Biol, Tainan, Taiwan Harvard Med Sch, Schepens Eye Res Inst, Ophthalmol, Boston, MA 02115 USA Lanzhou Univ, Hosp 2, Dept Gen Surg, Lanzhou, Gansu, Peoples R China Univ Technol Sydney, Sch Life Sci, Sydney, NSW, Australia JT Chen Clin, Gynecol, Tokyo, Japan Univ Western Australia, Sch Agr & Environm, Perth, WA, Australia Beijing Normal Univ, Fac Geog Sci, Beijing, Peoples R China Univ Missouri, Elect Engn & Comp Sci, Columbia, MO USA Vrije Univ Amsterdam Med Ctr, Amsterdam Publ Hlth Res Inst, Dept Publ & Occupat Hlth, Amsterdam, Netherlands Semmelweis Univ, Med Biochem, Budapest, Hungary Queen Elizabeth Hosp, Dept Clin Oncol, Hong Kong, Peoples R China Univ Pittsburgh, Chem, Pittsburgh, PA USA GB Pant Inst Post Grad Med Educ & Res, Neurol, New Delhi, India Univ Copenhagen, Vet & Anim Sci, Copenhagen, Denmark Univ Palermo, Biomed Dept Internal & Specialist Med DIBIMIS, Sect Endocrinol, Palermo, Italy UCL, NPP, London, England Univ Florida, Microbiol & Cell Sci, Gainesville, FL USA Univ Salford, Sch Hlth Sci, Manchester, Lancs, England Cardiff Univ, Inst Med Genet, Cardiff, S Glam, Wales INSERM, ICO Canc Ctr, Angers, France Univ Colombo, Fac Med, Microbiol, Colombo, Sri Lanka Beijing Univ Chinese Med, Sch Chinese Mat Med, Beijing, Peoples R China Univ Porto, Fac Pharm, Porto, Portugal Univ Nottingham, Div Primary Care, Nottingham, England Univ Illinois, Pharm Syst Outcomes & Policy, Chicago, IL USA Pontificia Univ Catolica Goias, Escola Ciencias Agr & Biol, Goiania, Go, Brazil China Japan Friendship Hosp, Dept Oncol, Beijing, Peoples R China Boston Univ, Chem, Boston, MA 02215 USA Amer Univ, Environm Sci, Washington, DC 20016 USA Carleton Univ, Neurosci, Ottawa, ON, Canada Univ Regina, Chem & Biochem, Regina, SK, Canada Univ Montreal, Microbiolgy, Montreal, PQ, Canada Univ Leicester, Dept Genet & Genome Biol, Leicester, Leics, England Univ Queensland, Sch Agr & Food Sci, Gatton, Qld, Australia CNRS, BIOM, Paris, France UCL, Hatter Cardiovasc Inst, London, England Flinders Univ S Australia, Sci & Engn, Adelaide, SA, Australia Univ Warwick, Engn, Coventry, W Midlands, England Katholieke Univ Leuven, Ctr Human Genet, Leuven, Belgium Fudan Univ, Dept Macromol Sci, Shanghai, Peoples R China Dokuz Eylul Univ, Biol Educ, Izmir, Turkey Indiana Univ Sch Med, Dept Biochem & Mol Biol, Indianapolis, IN 46202 USA Mondo Med, Pulm Dis, Borgomanero, Italy US Naval, Res Lab, Ctr Bio Mol Sci & Engn, Washington, DC USA Univ Oslo, Inst Basic Med Sci, Dept Nutr, Oslo, Norway Peking Univ, Dept Mech & Engn Sci, Beijing, Peoples R China Saarland Univ, Dept Pharm Pharmaceut & Med Chem, Saarbrucken, Germany INSERM, Natl Inst Hlth & Med Res, Skin Res Inst, Paris, France Shanghai Proton & Heavy Ion Ctr, Res & Dev, Shanghai, Peoples R China Univ Georgia, Epidemiol, Athens, GA 30602 USA Univ Freiburg, Med Ctr, Dept Plast & Hand Surg, Freiburg, Germany Sidra Med, Res, Doha, Qatar Rostock Univ, Med Ctr, Dept Oral Maxillofacial & Plast Surg, Rostock, Germany Harvard Med Sch, Brigham & Womens Hosp, Emergency Med, Boston, MA 02115 USA AgResearch, Forage Sci, Palmerston North, New Zealand Univ Calif Los Angeles, Med, Los Angeles, CA USA Arizona State Univ, Biodesign Inst, Virginia G Piper Ctr Personalized Diagnost, Tempe, AZ USA Sheffield Hallam Univ, Res Inst, Mat & Engn, Sheffield, S Yorkshire, England Aneurin Bevan Univ Healthboard, Resp Med, Newport, Shrops, England Univ Calif San Francisco, Neurol Surg, San Francisco, CA 94143 USA Univ Western Australia, UWA Dent Sch, Perth, WA, Australia Fordham Univ, Biol Sci, Bronx, NY 10458 USA Univ Helsinki, Inst Biotechnol, Helsinki, Finland Fujian Normal Univ, Coll Life Sci, Fuzhou, Fujian, Peoples R China Univ Fukui, Dept Frontier Fiber Technol & Sci, Fukui, Japan Univ Southampton, Fac Med, Clin & Expt Sci, Southampton, Hants, England Univ Urbino, Dept Biomol Sci, Urbino, Italy Osped San Luigi, Allergol Unit, Turin, Italy Muljibhai Patel Urol Hosp, Dept Urol, Nadiad, Gujarat, India Univ Granada, Stratig & Paleontol, Granada, Spain Massey Univ, Sch Vet Sci, Auckland, New Zealand CNR, High Performance Comp & Networking Inst, Naples, Italy Univ Childrens Hosp Zurich, Div Metab, Zurich, Switzerland Univ Childrens Hosp Zurich, Childrens Res Ctr, Zurich, Switzerland Univ Melbourne, Biochem & Mol Biol, Parkville, Vic, Australia Inst Pasteur, Leptospirosis Res & Expertise Unit, Noumea, New Caledonia Tsinghua Univ, Sch Life Sci, Beijing, Peoples R China Cheikh Anta Diop Univ UCAD, Sci Fac, Biol Anim Dept, Dakar, Senegal Providence Portland Med Ctr, Earle A Chiles Res Inst, Portland, OR USA Agr & Agri Food Canada, Lacombe Res & Dev Ctr, Lacombe, AB, Canada Alberta Innovates, Performance Management & Evaluat, Edmonton, AB, Canada Univ Malaga, CSIC, Inst Hortofruticultura Subtrop Mediterranea La Ma, IHSM,UMA, Malaga, Spain James Cook Univ, Coll Publ Hlth Med & Vet Sci, Cairns, Qld, Australia European Commiss, Joint Res Ctr, Ispra, Italy Univ Montpellier, Montpellier, France CSIRO, Floreat, WA, Australia Sun Yat Sen Univ, Sun Yat Sen Mem Hosp, Guangzhou, Guangdong, Peoples R China Vanderbilt Univ, Pharmacol, 221 Kirkland Hall, Nashville, TN 37235 USA RIKEN, KFU RIKEN Translat Genom Unit, Yokohama, Kanagawa, Japan Univ Tubingen, Neurobiol Vocal Commun, Tubingen, Germany Univ Colorado, UCCS Ctr Biofrontiers Inst, Colorado Springs, CO 80907 USA Fred Hutchinson Canc Ctr, Div Basic Sci, Seattle, WA USA Univ Geneva, Fac Med, Primary Care Unit, Geneva, Switzerland Ernst Moritz Arndt Univ Greifswald, Dept Mol Genet & Infect Biol, Greifswald, Germany East China Univ Sci & Technol, Dept Fine Chem, Shanghai, Peoples R China Ohio State Univ, Surg, Columbus, OH 43210 USA Oragenics, R&D, Tampa, FL USA Natl Environm Agcy, Environm Hlth Inst, Singapore, Singapore Friedrich Loeffler Inst, Inst Diagnost Virol, Greifswald, Germany Queen Elizabeth Hosp, Oncol, Woodville, SA, Australia USDA, Emerging Pests & Pathogens Res Unit, Ithaca, NY USA Univ Freiburg, Med Ctr, Dept Neurosurg, Epilepsy Ctr, Freiburg, Germany Univ Hong Kong, Fac Educ, Informat & Technol Studies, Hong Kong, Peoples R China Univ Tokyo, Grad Sch Agr & life Sci, Agr & Environm Biol, Tokyo, Japan Univ Pittsburgh, Dept Med, Pittsburgh Heart Lung & Blood Vasc Med Inst, Pittsburgh, PA USA Guys & St Thomas NHS Fdn Trust, Directorate Transplant Renal & Urol, London, England Univ Sarajevo, Clin Ctr, Clin Heart Blood Vessel & Rheumat Dis, Sarajevo, Bosnia & Herceg Univ Kent, Sch Math Stat & Actuarial Sci, Canterbury, Kent, England Tokyo Inst Technol, Dept Life Sci & Technol, Tokyo, Japan Univ Appl Sci Munich, Laser Ctr Dept Appl Sci & Mechatron, Munich, Germany CIC NanoGUNE, Nanodevices, San Sebastian, Spain Vrije Univ Amsterdam Med Ctr, Gynaecol, Amsterdam, Netherlands Cardiff Univ, Med Sch, Div Populat Med, Cardiff, S Glam, Wales Karolinska Inst, Dept Med, Solna, Sweden Natl Inst Genet, Ctr Informat Biol, Mishima, Shizuoka, Japan Murdoch Univ, Harry Perkins Inst Med Res, Perth, WA, Australia Univ Limerick, Phys Educ & Sport Sci, Limerick, Ireland Ruhr Univ Bochum, Campus Clin Gynecol, Univ Str, Bochum, Germany Southwest Med Univ, Sch Publ Hlth, Epidemiol & Biostat, Luzhou, Sichuan, Peoples R China Beijing Canc Hosp, Minist Educ Beijing, Key Lab Carcinogenesis & Translat Res, Ctr Mol Diagnost, Beijing, Peoples R China Chinese Acad Sci, Chengdu Inst Biol, Herpetol Dept, Chengdu, Sichuan, Peoples R China Key Lab Nano Biol Effects & Safety, Beijing, Peoples R China NIBR, PK Sci, Basel, Switzerland Daejeon St Marys Hosp, Pain Ctr, Daejeon, South Korea Univ Western Ontario, Sch Hlth Studies, London, ON, Canada Univ Aberdeen, Hlth Psychol Grp, Aberdeen, Scotland Univ Colorado, Anesthesiol, Anschutz Med Campus, Boulder, CO 80309 USA Univ Antwerp, UZA Antwerp Univ Hosp, Crit Care Med, Edegem, Belgium Aarhus Univ Hosp, Endocrinol, Aarhus, Denmark Univ Pretoria, Ctr Transport Dev, Ind & Syst Engn, Pretoria, South Africa Duke Univ, Dept Biostat & Bioinformat, Durham, NC USA Pontificia Univ Catolica Goias, Med Pharmaceut & Biomed Sci Sch, Goiania, Go, Brazil Karolinska Inst, Danderyd Hosp, Dept Clin Sci, Div Cardiovasc Med, Stockholm, Sweden UCL, Clin Educ & Hlth Psychol, London, England KRIBB, Dev & Differentiat Res Ctr, Daejeon, South Korea Univ dArtois, Lab Barriere Hematoencephal, Arras, France AstraZeneca, IMED Biotech Unit, Discovery Sci, Quantitat Biol, Cambridge, England Pacific Northwest Natl Lab, Environm Mol Sci Lab, Richland, WA 99352 USA Coventry Univ, Appl Maths Res Ctr, Stat Phys Grp, Coventry, W Midlands, England Wilton Ctr, Invista Performance Technol, Cleveland, England Thunen Inst Forest Genet, Genome Res, Grosshansdorf, Germany Lebanese Amer Univ, Nat Sci, Byblos, Lebanon Takeda, Evidence & Value Generat, Osaka, Japan King Abdullah Int Med Res Ctr, Stem Cell & Regenerat Med, Riyadh, Saudi Arabia Univ Bahri, Ind Pulp & Paper, Khartoum, Sudan Univ Queensland, Mater Med Res Inst, Mater Res Inst, Brisbane, Qld, Australia Colorado State Univ, NREL, Ft Collins, CO 80523 USA Rzeszow Univ Hosp, Ob Gyn Dept, Rzeszow, Poland Univ Leeds, Fac Biol Sci, Leeds, W Yorkshire, England Massachusetts Gen Hosp, Endocrine Unit, Boston, MA 02114 USA Carl von Ossietzky Univ Oldenburg, Neurosci, Oldenburg, Germany UNSW, St George & Sutherland Clin Sch, Microbiome Res Ctr, Sydney, NSW, Australia NYU, Sch Med, Dept Biochem, New York, NY 10016 USA NYU, Sch Med, Dept Mol Pharmacol, New York, NY USA Univ Mississippi, Med Ctr, Med Infect Dis, Jackson, MS 39216 USA Tampere Univ, Fac Social Sci Psychol, Tampere, Finland Univ Cyprus, Dept Biol Sci, Nicosia, Cyprus Goethe Univ, Inst Med Microbiol & Infect Control, Frankfurt, Germany Charite Med Univ Berlin, Inst Radiol, Berlin, Germany Univ Cologne, Univ Hosp Cologne, Internal Med 1, Cologne, Germany Univ Calif Los Angeles, Sch Dent, Sect Periodont, Los Angeles, CA 90024 USA Aalborg Univ Hosp, Dept Clin Biochem, Aalborg, Denmark Manipal Acad Higher Educ, Pharm Practice, Manipal, Karnataka, India Univ Tokyo, Inst Med Sci, Dept Radiol, Tokyo, Japan Cukurova Univ, Family Med, Fac Med, Adana, Turkey Catholic Univ Korea, Coll Med, Dept Humanities & Social Med, Seoul, South Korea Univ Ghent, Food Technol Safety & Hlth, Ghent, Belgium UNSW Sydney, Sch Biol Earth & Environm Sci BEES, Sydney, NSW, Australia St Vincent Shoulder & Sports Clin, Res Unit, Vienna, Austria Cornell Univ, Biomed Engn, Ithaca, NY USA Leibniz Inst Plant Genet & Crop Plant Res IPK, Res Grp Bioinformat & Informat Technol, Gatersleben, Germany Univ Europea Madrid, Sch Doctoral Studies, Madrid, Spain CSIRO Mfg, Biomed Mfg, Melbourne, Vic, Australia Depaul Univ, Biol Sci, Chicago, IL 60604 USA Konkuk Univ, Dept Anim Sci & Technol, Seoul, South Korea Chang Gung Univ, Grad Inst Med Mechatron, Taoyuan, Taiwan Korea Univ, Coll Med, Psychiat, Seoul, South Korea Princeton Univ, Chem, Princeton, NJ 08544 USA Henan Univ Chinese Med, Henan Key Lab Chinese Med Resp Dis, Zhengzhou, Henan, Peoples R China Univ Med Ctr Mainz, Dept Psychiat & Psychotherapy, Mainz, Germany Monash Univ Malaysia, Sch Sci, Selangor, Malaysia Univ Mississippi, Med Ctr, Physiol & Biophys, Jackson, MS 39216 USA Univ Oslo, Dept Transplantat Med, Oslo, Norway Sichuan Agr Univ, Triticeae Res Inst, Yaan, Sichuan, Peoples R China Guangzhou Univ Chinese Med, Gastroenterol, Guangzhou, Guangdong, Peoples R China Southeast Univ, Sch Biol Sci & Med Engn, Suzhou, Jiangsu, Peoples R China Mt Allison Univ, Biol, Sackville, NB, Canada Ithaca Coll, Biol, Ithaca, NY 14850 USA Univ Cagliari, Dept Med Sci & Publ Hlth, Monserrato, Italy Univ Vienna, Chromosome Biol, Vienna, Austria Univ Zurich, Nephrol, Zurich, Switzerland Friedrich Schiller Univ, Inst Nutr Sci, Jena, Germany UNSW Sydney, Grad Sch Biomed Engn, Sydney, NSW, Australia Tulane Univ, Sch Med, Biochem & Mol Biol, 1430 Tulane Ave, New Orleans, LA 70112 USA NINDS, NIH, Bldg 36,Rm 4D04, Bethesda, MD 20892 USA NIH, NCBI, Natl Lib Med, Bldg 10, Bethesda, MD 20892 USA LOreal Res & Innovat, Aulnay Sous Bois, France Lund Univ, Dept Psychol, Malmo, Sweden Catholic Univ Louvain, Inst Rech Expt & Clin, Brussels, Belgium Georgia State Univ, Neurosci Inst, Atlanta, GA 30303 USA Univ Melbourne, Ophthalmol, Surg, Parkville, Vic, Australia Univ Western Australia, Ctr Ophthalmol & Visual Sci, Perth, WA, Australia Iran Univ Med Sci, Med Phys, Fac Med, Tehran, Iran Salk Inst Biol Studies, Cellular Neurobiol, La Jolla, CA USA Imperial Coll London, Fibrosis Res Grp, London, England Univ Texas MD Anderson Canc Ctr, Genitourinary Med Oncol, Houston, TX 77030 USA Univ Liege, GIGA Neurosci, Liege, Belgium Univ Crete, Sch Med, Urol, Iraklion, Greece Flinders Univ S Australia, Flinders Med Ctr, Dept Clin Pharmacol, Adelaide, SA, Australia Max Planck Inst Immunobiol & Epigenet, Bioinformat, Breisgau, Germany Cardiff Univ, Sch Psychol, Cardiff, S Glam, Wales Imperial Coll London, Chem Engn, London, England Lund Univ, Skane Univ Hosp, Clin Sci, Malmo, Sweden Sahlgrens Acad, Inst Clin Sci, Dept Mol & Clin Med, Gothenburg, Sweden Univ Cent Lancashire, Sch Pharm & Biomed Sci, Preston, Lancs, England Hosp Univ Doctor Peset, Psychiat & Clin Psychol, Valencia, Spain Ctr Biol Mol Severo Ochoa, Genome Dynam & Funct, Madrid, Spain Unvivers Hosp Lille, Dept Intens Care, Lille, France Kansai Med Univ, Surg, Osaka, Japan Univ Toulouse, Inst Natl Polytech Toulouse, Ecole Natl Super Agron Toulouse, Lab Genom & Biotechnol Fruit, Toulouse, France UiT Arctic Univ Norway, Inst Psychol, Tromsto, Norway Queens Univ, Ctr Publ Hlth, Belfast, Antrim, North Ireland Univ Manchester, Ctr Primary Care & Hlth Serv Res, Manchester, Lancs, England Griffith Univ, Menzies Hlth Inst, Gold Coast, Qld, Australia Anglia Ruskin Univ, FHSCE, Cambridge, England Univ Lleida, Dept Expt Med, Lleida, Spain NIEHS, Biomol Screening Branch, Div Natl Toxicol Program, POB 12233, Res Triangle Pk, NC 27709 USA Albany Med Coll, Immunol & Microbial Dis, Albany, NY 12208 USA Univ Queensland, Queensland Brain Inst, Brisbane, Qld, Australia Univ Kent, Sch Biosci, Canterbury, Kent, England Univ Bourgogne Franche Comte, INSERM, LNC, UMR 1231, Besancon, France Ritsumeikan Univ, Coll Life Sci, Dept Biotechnol, Shiga, Japan Kent State Univ, Biol Sci, Kent, OH 44242 USA Natl Inst Infect Dis, Dept Safety Res Blood & Biol Prod, Tokyo, Japan European Inst Marine Studies, Lab Microbiol Extreme Environm, Plouzane, France Univ Iowa, Dept Pharmacol, Roy J & Lucille A Carver Coll Med, Iowa City, IA 52242 USA Natl Univ Singapore, Biol Sci, Singapore, Singapore Conservatoire Natl Arts & Metiers, Lab GBA, EA4627, Paris, France Univ Michigan, Dept Human Genet, Ann Arbor, MI 48109 USA Lomonosov Moscow State Univ, Belozersky Inst Physicochem Biol, Moscow, Russia Jikei Univ, Sch Med, Dept Mol Biol, Tokyo, Japan Univ South Wales, Genom & Computat Biol, Treforest, Wales Duke Univ, Med Ctr, Obstet & Gynecol, Durham, NC USA Univ Technol Sydney, Climate Change Cluster, Sydney, NSW, Australia Nagoya Univ, Grad Sch Med, Dept Radiol, Nagoya, Aichi, Japan Western Sydney Univ, Sch Sci & Hlth, Sydney, NSW, Australia TEI Epirus, Dept Speech & Language Therapy, Ioannina, Greece Indiana Univ Purdue Univ, Orthopaed Surg, Indianapolis, IN 46202 USA Oniris, Vet Pathol, Nantes, France Royal Vet Coll, Pathobiol & Populat Sci, Hatfield, Herts, England Univ Ghent, Lab Pharmaceut Biotechnol, Ghent, Belgium Norwegian Inst Nat Res, Terr Ecol, Trondheim, Norway Univ Calif Merced, Mol & Cell Biol, Merced, CA USA Univ Dublin, Trinity Coll Dublin, Sch Engn, Ctr Transport Res, Dublin, Ireland Lund Univ, Inst Clin Sci, Nephrol, Malmo, Sweden Univ Birmingham, Mech Engn, Birmingham, W Midlands, England Lund Univ, Inst Clin Sci, OB GYN, Lund, Sweden Fdn Jimenez Diaz Hosp, Nephrol & Hypertens, Madrid, Spain Queensland Univ Technol, Sch Chem Phys & Mech Engn, Brisbane, Qld, Australia Otto von Guericke Univ, Psychol, Magdeburg, Germany Univ Med Ctr Gottingen, Dept Expt Neurodegenerat, Gottingen, Germany Harvard Med Sch, Spaulding Rehabil Hosp, Phys Med & Rehabil, Boston, MA 02115 USA Quadram Inst Biosci, Sci Operat, Norwich, Norfolk, England Ostbayer Tech Hsch Regensburg OTH Regensburg, Regensburg Med Image Comp ReMIC, Regensburg, Germany Deakin Univ, Fac Arts & Educ, Melbourne, Vic, Australia Univ Warwick, Warwick Med Sch, Coventry, W Midlands, England INSERM, Natl Inst Hlth & Med Res, Biochem & Mol Biol, Paris, France Univ Liege, Tax Inst, Liege, Belgium Univ Leeds, Sch Mol & Cellular Biol, Leeds, W Yorkshire, England IRCCS Ist Giannina Gaslini, UOC Genet Med, Genoa, Italy Res Diets Inc, Sci, New Brunswick, NJ USA Univ Perugia, Dept Phys & Geol, Perugia, Italy Walter Reed Natl Mil Med Ctr, Cellular Immunol, Bethesda, MD USA Univ Fed Santa Catarina, Biol Sci Ctr, Microbiol Immunol & Parasitol Dept, Florianopolis, SC, Brazil Univ Edinburgh, Royal Infirm, Ctr Liver & Digest Disorders, Edinburgh, Midlothian, Scotland Orion Pharma, Crit Care Proprietary Prod Div, Espoo, Finland MIT, Dept Civil & Environm Engn, 77 Massachusetts Ave, Cambridge, MA 02139 USA Univ Turin, Dept Vet Sci, Turin, Italy Univ G dAnnunzio, Dept Psychol Hlth & Territorial Sci, Chieti, Italy NYU, Sch Med, OB GYN, New York, NY USA Univ Glasgow, Inst Cardiovasc & Med Sci, Glasgow, Lanark, Scotland Univ Turku, Dept Biol, Turku, Finland Tech Univ Berlin, Bioanalyt, Berlin, Germany Univ Goettingen, Inst Phys Biophys 3, Gottingen, Germany Univ Texas MD Anderson Canc Ctr, Inst Appl Canc Sci, Translat Res Adv Therapeut & Innovat Oncol TRACTI, Houston, TX 77030 USA Univ Liege, Life Sci, Liege, Belgium Tarbiat Modares Univ, Fac Med Sci, Dept Toxicol, Tehran, Iran ARS, USDA, Stoneville, MS USA Univ Regensburg, RCI Regensburg Ctr Intervent Immunol, Regensburg, Germany Univ Nottingham, Sch Psychol, Nottingham, England NIH, Pathol Lab, Bethesda, MD 20892 USA Univ Carlos III Madrid, Elect Engn, Madrid, Spain Inst Med Mol, Chem Biol, Lisbon, Portugal Univ Costa Rica, CIET, San Jose, Costa Rica Univ Stavanger, Fac Hlth Sci, Stavanger, Norway Erasmus MC, Urol, Rotterdam, Netherlands Univ Edinburgh, Sch Biol Sci, Edinburgh, Midlothian, Scotland German Res Ctr Environm Hlth GmbH, Helmholtz Zentrum Munchen, Inst Bioinformat & Syst Biol IBIS, Ingolstadter Landstr 1, D-85764 Neuherberg, Germany Leiden Univ, Huygens Kamerlingh Onnes Lab, Leiden, Netherlands Univ Vienna, Nutr Sci, Vienna, Austria Kolling Inst Med Res, Med, St Leonards, NSW, Australia Johns Hopkins Sch Med, Biol Chem, Baltimore, MD USA Univ Montreal, Med Nutr & Microbiome Lab, Montreal, PQ, Canada GlaxoSmithKline, Cell & Gene Therapy, Stevenage, Herts, England Univ Trieste, Life Sci, Trieste, Italy Rhein Westfal TH Aachen, Dept Radiol, Aachen, Germany Univ Duisburg Essen, Univ Hosp Essen, West German Canc Ctr, Dept Med Oncol, Essen, Germany Med Univ Vienna, Obstet & Gynecol, Vienna, Austria FHI 360, Social & Behav Hlth Sci Div, Washington, DC USA KU Leuven VIB, Switch Lab, Leuven, Belgium Bielefeld Univ, Fac Technol, Bielefeld, Germany Capital Med Univ, Beijing Shijitan Hosp, Dept Clin Nutr, Dept Gastrointestinal Surg, Beijing, Peoples R China Meiji Univ, Dept Agr Chem, Kawasaki, Japan Yonsei Univ, Coll Med, Microbiol, Seoul, South Korea Johnson & Johnson EAME, Maidenhead, Berks, England Penn State Coll Med, Pediat, Hershey, PA USA Univ N Carolina, Dept Social Med, Chapel Hill, NC 27515 USA Univ Western Australia, ARC CoE Plant Energy Biol, Perth, WA, Australia Wageningen Univ, Div Human Nutr & Hlth, Wageningen, Netherlands Kings Coll London, Dept Neuroimaging, London, England Univ Murcia, Biochem & Mol Biol, Murcia, Spain Old Dominion Univ, Dept Biol Sci, Norfolk, VA 23529 USA Monash Univ, Biochem & Mol Biol, Melbourne, Vic, Australia Chinese Acad Sci, Inst Genet & Dev Biol, Beijing, Peoples R China Univ Pittsburgh, Pharmacol & Chem Biol, Pittsburgh, PA USA Univ Lausanne, Ctr Integrat Genom, Lausanne, Switzerland Univ Queensland, Sch Pharm, Brisbane, Qld, Australia Leibniz Inst Plant Genet & Crop Plant Res IPK Gat, Genebank, Gatersleben, Germany Piramal Imaging, Res & Dev, Berlin, Germany Univ Leeds, Civil Engn, Leeds, W Yorkshire, England Univ Missouri, Chem & Biochem, St Louis, MO 63121 USA US Geol Survey, Coastal & Marine Geol Program, Pacific Coastal & Marine Sci Ctr, Santa Cruz, CA USA Ajinomoto Genet Res Inst, Moscow, Russia Jagiellonian Univ, Fac Biochem Biophys & Biotechnol, Dept Plant Biotechnol, Krakow, Poland Univ Puerto Rico, Engn Sci & Mat, Mayaguez, PR USA Univ Regina, Dept Chem & Biochem, Regina, SK, Canada Argonne Natl Lab, Ctr Nanoscale Mat, 9700 S Cass Ave, Argonne, IL 60439 USA Univ Sunshine Coast, Sunshine Coast Mind & Neurosci Thompson Inst, Sippy Downs, Qld, Australia Chinese Peoples Liberat Army Gen Hosp, Dept Gastroenterol & Hepatol, Beijing, Peoples R China Griffith Univ, Griffith Ctr Social & Cultural Res, Gold Coast, Qld, Australia Tohoku Univ, Inst Dev Aging Canc, Dept Mol Oncol, Sendai, Miyagi, Japan Indiana Univ, Comp Sci, Bloomington, IN USA Fukushima Med Univ, Sch Med, Dept Pulm Med, Fukushima, Japan MEDIVIR AB, Biol, Huddinge, Sweden Western Sydney Univ, Neuroimmunol, Sydney, NSW, Australia Univ Jordan, Nutr & Food Technol, Amman, Jordan Thunen Inst Forest Genet, Fed Res Ctr Rura Areas Forestry & Fisheries, Inst Biodivers, Grosshansdorf, Germany Univ Edinburgh, Inst Cell Biol, Edinburgh, Midlothian, Scotland Univ Edinburgh, Ctr Integrat Physiol, Edinburgh, Midlothian, Scotland Univ Toronto, Struct Genom Consortium, Toronto, ON, Canada Canadian Mem Chiropract Coll, Grad Educ & Res, Toronto, ON, Canada Agilent Technol, R&D, Leuven, Belgium Univ British Columbia, Sch Nursing, Vancouver, BC, Canada Monash Univ, Monash Hlth, Sch Clin Sci, Stroke & Ageing Res,Dept Med, Melbourne, Vic, Australia French Natl Canc Inst, Innovat, Transfer, Biol, Boulogne, France Ludwig Maximilians Univ Munchen, Phys Chem, NanoBioSci, Munich, Germany Bandung Inst Technol, Sch Pharm, Med Chem, Bandung, Indonesia Univ Luxembourg, Life Sci Res Unit, Luxembourg, Luxembourg Lund Univ, Skane Univ Hosp, Dept Gastroenterol, Malmo, Sweden Millennium Hlth, Translat Genet, San Diego, CA USA Aristotle Univ Thessaloniki, Med Dept 2, Clin Res & Evidence Based Med Unit, Thessaloniki, Greece Jan Kochanowski Univ Humanities & Sci, Piotrkow Trybunalski Branch, Dept Psychol, Kielce, Poland McMaster Univ, Engn Phys, Hamilton, ON, Canada Marche Polytech Univ, Dept Agr Food & Environm Sci, Ancona, Italy Kuwait Univ, Fac Med, Microbiol, Kuwait, Kuwait Fujita Hlth Univ, Dept Breast Surg, Toyoake, Aich, Japan North West Reg Spinal Injuries Ctr, Spinal Injuries Ctr, Southport, Merseyside, England Luxembourg Inst Hlth, Competence Ctr Methodol & Stat, Luxembourg, Luxembourg Nestle Inst Hlth Sci SA, Metab Hlth, Ecublens, Vaud, Switzerland Ctr Inflammat Res VIB, Ghent, Belgium Univ Ghent, Dept Biomed Mol Biol, Ghent, Belgium Univ Lisbon, Inst Educ, Curriculo Formacao Prof & Tecnol, Lisbon, Portugal Univ Edinburgh, Ctr Inflammat Res, Edinburgh, Midlothian, Scotland Univ Melbourne, Sch BioSci, Parkville, Vic, Australia Northumbria Univ, Comp & Informat Sci, Newcastle Upon Tyne, Tyne & Wear, England Univ Valencia, Endocrinol, Valencia, Spain INRS, Inst Armand Frappier, Laval, PQ, Canada Univ Laval, INAF, Sch Nutr, Quebec City, PQ, Canada Univ Konstanz, Dept Biol, Constance, Germany Univ Cote dAzur, LAMHESS, Nice, France Scion, Syst Ecol, Christchurch, New Zealand CUNY, Grad Sch Publ Hlth & Hlth Policy, Epidemiol & Biostat, New York, NY 10021 USA Univ Queensland, Sch Dent, Brisbane, Qld, Australia George Inst Global Hlth, Renal & Metab Div, Sydney, NSW, Australia Wuhan Univ, Coll Chem & Mol Sci, Wuhan, Hubei, Peoples R China Griffith Univ, Sch Environm & Sci, Gold Coast, Qld, Australia Univ Minnesota, Radiat Oncol, Minneapolis, MN USA Goethe Univ, Fac Med, Frankfurt, Germany Natl Yunlin Univ Sci & Technol, Dept & Grad Sch Safety & Environm Engn, Touliu, Yunlin, Taiwan Massey Univ, Sch Sport Exercise & Nutr, Auckland, New Zealand Univ Florida, Wildlife Ecol & Conservat, Gainesville, FL USA Bournemouth Univ, Dept Psychol, Poole, Dorset, England Robert Koch Inst, Project Grp P2, Berlin, Germany Univ Edinburgh, MRC Inst Genet & Mol Med, Edinburgh, Midlothian, Scotland Univ Basel, Biozentrum, Basel, Switzerland Univ Wollongong, Sch Med, Wollongong, NSW, Australia Univ Cologne, Inst Human Genet, Cologne, Germany Rural Econ Branch, Econ Res Serv, Washington, DC USA Uivers Bordeaux, CNRS, Inst Neurosci Cognit & Integrat Aquitaine, Bordeaux, France Univ Calif Riverside, Dept Chem & Environm Engn, Riverside, CA 92521 USA Univ Calif Riverside, Mat Sci & Engn Program, Riverside, CA 92521 USA Mackay Med Coll, Dept Med, New Taipei, Taiwan Univ Bern, Div Anim Welf, Bern, Switzerland Oregon Hlth & Sci Univ, Dept Physiol & Pharmacol, Portland, OR 97201 USA Shanghai Univ Tradit Chinese Med, Inst Interdisciplinary Med Sci, Shanghai, Peoples R China McMaster Univ, Biol, Hamilton, ON, Canada Univ S Florida, Dept Cell Biol Microbiol & Mol Biol, Tampa, FL USA Hacettepe Univ, Inst Canc, Med Oncol, Ankara, Turkey City Univ Hong Kong, Dept Elect Engn, Hong Kong, Peoples R China Natl Taiwan Univ, Dept Entomol, Taipei, Taiwan Chinese Acad Agr Sci, Inst Environm & Sustainable Dev Agr, Ecol Secur, Beijing, Peoples R China Florida State Univ, Inst Mol Biophys, Chem & Biochem, Tallahassee, FL USA Peking Univ, Shenzhen Grad Sch, State Key Lab Chem Oncogen, Lab Computat Chem & Drug Design, Shenzhen, Peoples R China Univ Helsinki, Fac Pharm, Div Pharmaceut Chem & Technol, Drug Res Program, Helsinki, Finland Tohoku Univ, Microbial Biotechnol, Sendai, Miyagi, Japan Tianjin Med Univ, Sch Basical Med Sci, Dept Pharmacol, Tianjin, Peoples R China Dana Farber Canc Inst, Biostat & Computat Biol, Boston, MA 02115 USA Natl Hlth Res Inst, Inst Mol & Genom Med, Zhunan, Taiwan Univ Oxford, Physiol Anat & Genet, Oxford, England George Washington Univ, Phys, Washington, DC USA Univ Nebraska, Sch Biol Sci, Lincoln, NE USA Toronto Gen Hosp, Res Inst, Dept Lab Med & Pathobiol, Toronto, ON, Canada Univ Texas Dallas, Biol Sci, Richardson, TX 75083 USA NYU, Dept Chem, New York, NY USA Shandong Univ, Sch Math & Stat, Jinan, Shandong, Peoples R China Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei, Anhui, Peoples R China Purdue Univ, Med Chem & Mol Pharmacol, W Lafayette, IN 47907 USA NIBSC, Adv Therapies, Ridge, Herts, England Shanghai Jiao Tong Univ, Ruijin Hosp, Dept Pulm & Crit Care Med, Shanghai, Peoples R China Charite Med Univ Berlin, Dermatol & Allergy, Berlin, Germany Univ Hosp St Etienne, Hematol, St Etienne, France Inland Norway Univ Appl Sci, Inst Biotechnol, Elverum, Norway Univ Jordan, Pediat, Amman, Jordan Inst Pasteur, Mol Mycol Unit, Paris, France Cardiff Univ, Sch Med, Inst Psychol Med & Clin Neurosci, Med Res Council Ctr Neuropsychiat Genet & Genom, Cardiff, S Glam, Wales Zurich Univ Appl Sci, Social Work, Zurich, Switzerland Jawaharlal Nehru Univ, Sch Life Sci, New Delhi, India Univ Burgundy Franche Comte, LE2I, Dijon, France Univ Roehampton, Life Sci, London, England Ghent Univ Hosp, Gen & HPB Surg, Ghent, Belgium Univ Wurzburg, Insect Fungus Symbiosis Lab, Wurzburg, Germany Radboud Univ Nijmegen, Behav Sci Inst, Nijmegen, Netherlands Fraunhofer WKI, Applicat Ctr HOFZET, Hannover, Germany UCL, Struct & Mol Biol, London, England Univ Amsterdam, Dev Psychol, Amsterdam, Netherlands Aalborg Univ, Hlth Sci & Technol, CNAP, SMI, Aalborg, Denmark VA Pittsburgh Healthcare Syst, Ctr Hlth Equity Res & Promot, Pittsburgh, PA USA Cedars Sinai Med Ctr, Neurosurg, Los Angeles, CA 90048 USA Sun Yat Sen Univ, Sch Data & Comp Sci, Guangzhou, Guangdong, Peoples R China Dezhou Univ, Shandong Prov Key Lab Biophys, Guangzhou, Guangdong, Peoples R China Maison Teledetection, Inst Rech Dev, UMR Espace DEv, Montpellier, France Xiamen Univ, Sch Life Sci, Xiamen, Fujian, Peoples R China Nanjing Univ, Sch Med, Jinling Hosp, Natl Clin Res Ctr Kidney Dis,Dept Med Imaging, Nanjing, Jiangsu, Peoples R China Univ Kent, Sch Social Policy Sociol & Social Res, Canterbury, Kent, England Univ Fed Minas Gerais, Infect Dis & Trop Med, Belo Horizonte, MG, Brazil Univ Minho, Sch Med, Life & Hlth Sci Res Inst ICVS, Braga, Portugal Univ Montreal, Biochim & Med Mol, Montreal, PQ, Canada Johns Hopkins Bloomberg Sch Publ Hlth, Epidemiol, Baltimore, MD USA Max Planck Inst Biol Ageing, Metab & Genet Regulat Ageing, Cologne, Germany Univ Swaziland, Hlth Sci, Kwaluseni, Eswatini Queensland Univ Technol, Inst Future Environm, Brisbane, Qld, Australia Ctr Sci Monaco, Dept Biol Med, Monaco, Monaco HELIOS Hosp, Urol, Bad Saarow Pieskow, Germany Tech Univ Carolo Wilhelmina Braunschweig, Inst Microbiol, Braunschweig, Germany Univ Barcelona, Barcelona Ctr Maternal Fetal & Neonatal Med, Fetal i D Fetal Med Res Ctr, IDIBAPS BCNatal,Hosp Clin, Barcelona, Spain Univ Barcelona, Hosp St Joan de Deu, Barcelona, Spain Friedrich Loeffler Inst, Inst Bacterial Infect & Zoonoses, Jena, Germany Charite Med Univ Berlin, Neurol, Berlin, Germany Dublin City Univ, Natl Inst Cellular Biotechnol, Mol Therapeut Canc Ireland, Dublin, Ireland Schoen Clin Roseneck, Prien Am Chiemsee, Germany Univ Med Ctr Hamburg Eppendorf, Inst Sex Res & Forens Psychiat, Hamburg, Germany Nankai Univ, Sch Math Sci, Tianjin, Peoples R China Nankai Univ, LPMC, Tianjin, Peoples R China Univ Oxford, Oncol, Oxford, England Royal Holloway Univ London, Class, Egham, Surrey, England Cornell Univ, Clin Sci, Ithaca, NY USA Univ KwaZulu Natal, Pharmaceut Chem, Westville Campus, Durban, South Africa Royal Coll Surgeons Ireland, Med, Dublin, Ireland Univ Oslo, Dept Immunol, Oslo, Norway Bermuda Inst Ocean Sci, Marine Nitrogen Cycling Lab, St Georges, Bermuda Kanazawa Univ, Inst Liberal Arts & Sci, Kanazawa, Ishikawa, Japan World Hlth Org Reg Off Africa, Brazzaville, Rep Congo Univ Hosp BesanCon, Infect Control Dept, Besancon, France Galapagos NV, Clin Dev, Mechelen, Belgium Univ Tasmania, Integrated Marine Observing Syst, Hobart, Tas, Australia Georg August Univ Gottingen, Albrecht von Haller Inst Plant Sci, Dept Systemat Biodivers & Evolut Plants, Gottingen, Germany Univ Occupat & Environm Hlth, Dept Psychiat, Fukuoka, Fukuoka, Japan IMDEA Food, Program Precis Nutr & Aging, Madrid, Spain Radboud Univ Nijmegen, Med Sch, IQHealthcare, Nijmegen, Netherlands Maastricht Univ, Dept Cardiovasc Surg, Maastricht, Netherlands German Diabet Ctr, Inst Clin Biochem & Pathobiochem, Dusseldorf, Germany Juntendo Univ, Grad Sch Med, Dept Radiol, Tokyo, Japan Deakin Univ, Sch Informat Technol, Melbourne, Vic, Australia Max Planck Inst Eusenforschung, Dept Interface Chem & Surface Sci, Dusseldorf, Germany Edge Hill Univ, Dept Psychol, Ormskirk, England Aga Khan Univ, Psychiat, Karachi, Pakistan KRIBB, Korean Bioinformat Ctr, Seoul, South Korea Cardinal Hlth Specialty Solut, Hlth Econ & Outcomes Res, Dallas, TX USA Klinikum Univ Munchen, Div Clin Pharmacol, Munich, Germany Univ Pittsburgh, Neurol Surg, Pittsburgh, PA USA Rhein Westfal TH Aachen, Dept Child & Adolescent Psychiat Psychosomat & Ps, Aachen, Germany Univ Copenhagen, Inst Mol & Cellular Biol, Copenhagen, Denmark St Jude Childrens Res Hosp, Struct Biol, 332 N Lauderdale St, Memphis, TN 38105 USA Royal Shrewsbury Hosp, Colorectal Surg, Shrewsbury, Salop, England Univ Nottingham, Fac Med & Hlth Sci, Nottingham, England Karolinska Inst, Dept Physiol & Pharmacol, Solna, Sweden Chinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Electroanalyt Chem, Jilin, Jilin, Peoples R China Univ British Columbia, Pediat, Vancouver, BC, Canada Chinese Acad Agr Sci, State Key Lab Cotton Biol, Res Base Anyang Inst Technol, Cotton Germplasm Resources,Inst Cotton Res, Beijing, Peoples R China Chinese Univ Hong Kong, Anaesthesia & Intens Care, Hong Kong, Peoples R China Univ Macau, ICMS, Zhuhai, Guangdong, Peoples R China North China Elect Power Univ, Sch Renewable Energy, Beijing, Peoples R China Justus Liegbig Univ, Dept Internal Med, Giessen, Germany Aarhus Univ, Biosci, Aarhus, Denmark Univ Dublin, Trinity Coll Dublin, Irish Longitudinal Study Ageing TILDA, Dublin, Ireland Univ Groningen, Univ Med Ctr Groningen, Hematol, Groningen, Netherlands Vrije Univ Amsterdam Med Ctr, Child Neurol, Amsterdam, Netherlands EBI, EMBL, Cambridge, England Max Planck Inst Marine Microbiol, HGF MPG Joint Res Grp Deep Sea Ecol & Technol, Bremen, Germany Max Planck Inst Human Dev, Ctr Adapt Rat, Berlin, Germany King Faisal Univ, Math, Al Hufuf, Saudi Arabia Griffith Univ, Sch Nursing & Midwifery, Gold Coast, Qld, Australia Iowa State Univ, Roy J Carver Dept Biochemsitry Biophys & Mol Biol, Ames, IA USA Delft Univ Technol, Fac Mech Maritime & Mat Engn, Engn Thermodynam Proc & Energy Dept, Leeghwaterstr 39, NL-2628 CB Delft, Netherlands Univ Nebraska Med Ctr, Coll Allied Hlth Profess, Cytotechnol Educ, Omaha, NE USA Shinko Mem Hosp, Dept Cardiovasc Med, Kobe, Hyogo, Japan Imperial Coll London, Mat, London, England Tech Univ Munich, Dept Surg, Munich, Germany Chinese Acad Agr Sci, Res Inst Pomol, Minist Agr, Lab Qual & Safety Risk Assessment Fruit Xingcheng, Shenyang, Liaoning, Peoples R China James Madison Univ, Commun Sci & Disorders, Harrisonburg, VA 22807 USA Univ Hosp Ulm, Inst Orthopaed Res & Biomech, Ulm, Germany Univ Essex, Sch Hlth & Social Care, Colchester, Essex, England Alpha Altis, Res Serv, Nottingham, England Erasmus MC, Med Oncol, Rotterdam, Netherlands Fed Univ Oye, Dept Ind Chem, Ekiti, Nigeria Duke Univ, Med Ctr, Cell Biol, Durham, NC USA Univ Oxford, Nuffield Dept Clin Neurosci, Oxford, England Univ Manchester, Canc Res UK Manchester Inst, Manchester, Lancs, England Helsinki Univ Hosp, Childrens Hosp, Helsinki, Finland Univ Aveiro, CESAM Ctr Environm & Marine Studies, Dept Biol, Aveiro, Portugal Univ Botswana, Psychol, Gaborone, Botswana Univ Fed Bahia, Nursing Sch, Salvador, BA, Brazil Queen Mary Univ London, Biol & Expt Psychol, London, England Natl Univ Pharm, Med Chem Dept, Kharkov, Ukraine Univ Bolton, Dept Educ & Psychol, Bolton, England La Trobe Univ, Dept Chem & Phys, Melbourne, Vic, Australia Gen Hosp Northern Theater Command, Dept Gastroenterol, Shenyang, Liaoning, Peoples R China Doctors Hosp, Dept Nephrol, Athens, Greece Univ Hosp Essen, Pediat 3, Essen, Germany Imperial Coll London, Infect Dis Epidemiol, London, England Sorbonne Univ, Dept Psychiat, Paris, France UNSW Sydney, Educ, Sydney, NSW, Australia Stanford Univ, Dept Psychiat & Behav Sci, Palo Alto, CA 94304 USA Hannover Med Sch, Clin Laryngol Rhinol & Otol, Hannover, Germany Curtin Univ, Ctr Aboriginal Studies, Perth, WA, Australia Iran Univ Sci & Technol, Biomed Engn Dept, Tehran, Iran Univ Calif San Francisco, Anesthesiol, San Francisco, CA 94143 USA Khalifa Univ Sci & Technol, Mech Engn, Abu Dhabi, U Arab Emirates Univ Florida, Hort Sci, Gainesville, FL USA James Cook Univ, Australian Inst Trop Hlth & Med, Ctr Biodiscovery & Mol Dev Therapeut, Cairns, Qld, Australia Univ Porto, Fac Med, CINTESIS, Porto, Portugal Shaoxing Peoples Hosp, Med Res Ctr, Shaoxing, Zhejiang, Peoples R China NIH, Dept Transfus Med, Bethesda, MD 20892 USA AIIMS, Dept Biotechnol, New Delhi, India Univ Ottawa, Biochem Microbiol & Immunol, Ottawa, ON, Canada Univ Oslo, Inst Clin Med, Div Mental Hlth & Addict, Oslo, Norway Univ Groningen, Univ Med Ctr Groningen, Dept Radiol, Groningen, Netherlands Univ Hong Kong, Sch Nursing, Hong Kong, Peoples R China Tokyo Med Univ, Ibaraki Med Ctr, Urol, Tokyo, Japan Univ Hosp Zurich, Dept Radiat Oncol, Zurich, Switzerland Univ Maryland, Inst Human Virol, Div Immunotherapy, Baltimore, MD 21201 USA Univ Maryland, Dept Surg, Baltimore, MD 21201 USA Stellenbosch Univ, Fac Med & Hlth Sci, Div Mol Biol & Human Genet, Stellenbosch, South Africa China Agr Univ, Coll Biol Sci, Beijing, Peoples R China Osaka Univ, Grad Sch Pharmaceut Sci, Suita, Osaka, Japan Univ Washington, Biochem, Seattle, WA 98195 USA Natl Res Council Italy, Inst Biosci & BioResources, Naples, Italy Univ Lyon, Phys, Lyon, France Univ Basel, Fac Psychol, Ctr Social Psychol, Basel, Switzerland Queen Mary Univ London, Barts Canc Inst, Ctr Mol Oncol, London, England EBI, EMBL, Samples Phenotypes & Ontol Team, Cambridge, England Charles Sturt Univ, Fac Arts & Educ, Bathurst, NSW, Australia Shandong Univ, Helmholtz Inst Biotechnol, Sch Life Sci, State Key Lab Microbial Technol, Jinan, Shandong, Peoples R China Shantou Univ, Dept Biol, Shantou, Guangdong, Peoples R China Shanxi Univ, Inst Biomed Sci, Taiyuan, Shanxi, Peoples R China St Jude Childrens Res Hosp, Computat Biol, 332 N Lauderdale St, Memphis, TN 38105 USA Harbin Med Univ, Coll Bioinformat Sci & Technol, Harbin, Heilongjiang, Peoples R China NIH, Radiol & Imaging Sci, Bldg 10, Bethesda, MD 20892 USA Georgia Inst Technol, Dept Biol Sci, Atlanta, GA 30332 USA XtalPi Inc, Cambridge, MA USA Consejo Nacl Invest Cient & Tecn, Partner Inst Max Planck Soc, Inst Invest Biomed Buenos Aires IBioBA, Bioinformat, Buenos Aires, DF, Argentina Univ Sydney, Save Sight Inst, Sydney, NSW, Australia Univ South Australia, Canc Res Inst, Australian Ctr Precis Hlth, Adelaide, SA, Australia Jinan Univ, Inst Life & Hlth Engn, Guangdong Higher Educ Inst, Key Lab Funct Prot Res, Guangzhou, Guangdong, Peoples R China Univ Texas Hlth Sci Ctr Houston, Epidemiol Human Genet & Environm Sci, Houston, TX 77030 USA Weill Cornell Med, Dept Microbiol & Immunol, New York, NY USA Guangdong Inst Appl Biol Resources, Biotechnol Lab, Guangzhou, Guangdong, Peoples R China Shandong Normal Univ, Coll Life Sci, Jinan, Shandong, Peoples R China Shandong Univ, Life Sci Dept, Jinan, Shandong, Peoples R China South China Agr Univ, Integrat Microbiol Res Ctr, Guangzhou, Guangdong, Peoples R China Liaoning Acad Agr Sci, Crop Mol Improving Lab, Shenyang, Liaoning, Peoples R China Lawson Hlth Res Inst, Med Biophys, London, ON, Canada Univ Melbourne, Infrastruct Engn, Parkville, Vic, Australia Univ Canberra, Fac Hlth, Canberra, ACT, Australia Univ Cambridge, MRC Cognit & Brain Sci Unit, Cambridge, England Emory Univ, Biostat & Bioinformat, Atlanta, GA 30322 USA Johns Hopkins Sch Med, Anesthesiol & Crit Care Med, Baltimore, MD USA Nottingham Trent Univ, Sch Anim Rural & Environm Sci, Nottingham, England Univ Exeter, Biosci, Exeter, Devon, England Hillingdon Hosp NHS Fdn Trust, London, England Univ Glasgow, MRC CSO Social & Publ Hlth Sci Unit, Glasgow, Lanark, Scotland Natl & Kapodistrian Univ Athens, Evaggelismos Athens Hosp, ICU, Athens, Greece Univ Newcastle, Biol Sci, Callaghan, NSW, Australia Coventry Univ, Fac Hlth & Life Sci, Ctr Innovat Res Life Course, Coventry, W Midlands, England Lausanne Univ Hosp, Serv Endocrinol Diabet & Metab, Lausanne, Switzerland Charles Sturt Univ, Sch Community Hlth, Bathurst, NSW, Australia Queens Univ Belfast, Inst Global Food Secur, Belfast, Antrim, North Ireland Natl Univ Singapore, Inst Policy Studies, Singapore, Singapore Univ Penn, Intitute Med & Engn, Philadelphia, PA 19104 USA Cold Spring Harbor Lab, POB 100, Cold Spring Harbor, NY 11724 USA Univ Michigan, EECS, Ann Arbor, MI 48109 USA Univ British Columbia, Ctr Blood Res, Vancouver, BC, Canada UiT Arctic Univ Norway, Dept Hlth & Care Sci, Fac Hlth Sci, Tromso, Norway Hosp Clin Porto Alegre, Physiotherapy, Porto Alegre, RS, Brazil Univ Paris 05, Med Sch, Paris, France Chinese Acad Agr Sci, Inst Crop Sci, Natl Key Facil Crop Gene Resources & Genet Improv, Beijing, Peoples R China Univ Ghent, Expt Clin & Hlth Psychol, Ghent, Belgium Indian Inst Adv Res, Bioinformat & Struct Biol, Gandhinagar, Gujart, India Bambino Ges Childrens Res Hosp, Lab Mol Med, Rome, Italy Heidelberg Univ, Ctr Infect Dis Parasitol, Heidelberg, Germany Stanford Univ, Elect Engn, Palo Alto, CA 94304 USA Univ Cadiz, Biol, Andalucia, Spain Mansoura Univ Hosp, Gen Surg, Mansoura, Egypt Inst Pasteur, Virol Pole, Dakar, Senegal Cardiff Univ, Div Canc & Genet, Cardiff, S Glam, Wales Ctr Expertise & Biol Diagnost Cameroon, Food Safety & Environm Microbiol, Yaounde, Cameroon Swiss Fed Labs Mat Sci & Technol, Lab Thin Films & Photovolta, Dubendorf, Switzerland Assiut Univ, Assiut Urol & Nephrol Hosp, Fac Med, Assiut, Egypt UCL, GEE, London, England UCL, IHA, London, England Univ Derby, Univ Derby Online Learning, Derby, England SUNY Stony Brook, Family Populat & Prevent Med, Stony Brook, NY 11794 USA Walter & Eliza Hall Inst Med Res, Mol Med Div, Melbourne, Vic, Australia Newcastle Univ, Northern Inst Canc Res, Newcastle Upon Tyne, Tyne & Wear, England German Ctr Neurodegenerat Dis, Clin Dementia Res, Bonn, Germany Sorbonne Univ, CNRS, UMR 7144, Stn Biol, Paris, France Univ Barcelona, Odontoestomatol, Barcelona, Spain Janelia Res Campus, Comp Sci, Ashburn, VA USA Univ Oxford, Ctr Trop Med & Global Hlth, Oxford, England Univ Bern, ARTORG Ctr Biomed Engn Res, Bern, Switzerland Australian Natl Univ, Eccles Inst Neurosci, John Curtain Sch Med Res, Canberra, ACT, Australia John Innes Ctr, Metab Biol, Norwich, Norfolk, England USDA ARS, Genom & Bioinformat Res Unit, Raleigh, NC 27695 USA Med Univ Graz, Inst Med Informat Stat & Documentat, Holzinger Grp, Graz, Austria Ajou Univ, Pharm, Suwon, South Korea City Univ Hong Kong, Sch Energy & Environm, Hong Kong, Peoples R China Univ British Columbia, Sch Kinseiol, Vancouver, BC, Canada Univ Copenhagen, Marine Biol Sect, Dept Biol, Copenhagen, Denmark Univ Vienna, Dept Commun, Vienna, Austria Univ Dundee, Sch Social Sci, Dundee, Scotland Tech Univ Dresden, Inst Bot, Dresden, Germany Univ Oxford, Div Struct Biol, Oxford, England Natl Univ Hlth Syst, Med, Singapore, Singapore Univ Canterbury, Sch Biol Sci, Christchurch, New Zealand Univ Hosp Southern Denmark, Focused Res Unit Mol Diagnost & Clin Res, Odense, Denmark Univ Oxford, Primary Care Hlth Sci, Oxford, England Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA Adnan Menderes Univ Aydin, Fac Nursing, Dept Publ Hlth Nursing, Aydin, Turkey Oasi Res Inst IRCCS, Dept Neurol IC, Troina, Italy Purdue Univ, Weldon Sch Biomed Engn, W Lafayette, IN 47907 USA Kings Coll London, Kings Ctr Mil Hlth Res, London, England LSHTM, Dept Infect Dis Epidemiol, London, England Leibniz Univ Hannover, BMWZ Organ Chem, Hannover, Germany Xi An Jiao Tong Univ, Sch Basic Med Sci, Dept Physiol & Pathophysiol, Xian, Shaanxi, Peoples R China Univ South Australia, Sch Pharm & Med Sci, Adelaide, SA, Australia Univ Fed Santa Catarina, Dept Phys Educ, Florianopolis, SC, Brazil Southern Med Univ, Nanfang Hosp, Dept Oncol, Guangzhou, Guangdong, Peoples R China Stanford Univ, Hansen Expt Phys Lab, Palo Alto, CA 94304 USA Shenzhen Univ, Affiliated Hosp 1, Shenzhen Peoples Hosp 2, Inst Translat Med, Shenzhen, Guangdong, Peoples R China Univ Hong Kong, Dept Stat & Actuarial Sci, Hong Kong, Peoples R China UCL, Dept Mech Engn, London, England ASTAR, Singapore Immunol Network, Lab Microbial Immun, Singapore, Singapore Cent South Univ, State Key Lab Powder Met, Changsha, Hunan, Peoples R China Univ Aberdeen, Inst Appl Hlth Sci, Aberdeen, Scotland Univ Bridgeport, Biomed Engn, Bridgeport, CT 06601 USA Texas Tech Univ, Hlth Sci Ctr, Pharmaceut Sci, Lubbock, TX 79430 USA Univ Montana, Ecosyst & Conservat Sci, Missoula, MT 59812 USA Univ Goettingen, Dept Syst Neurosci, Gottingen, Germany NHLBI, Lab Syst Genet, Bldg 10, Bethesda, MD 20892 USA Cleveland Clin, Lou Ruvo Ctr Brain Hlth, Imaging, Las Vegas, NV USA Flinders Univ S Australia, Coll Nursing & Hlth Sci, Nutr & Dietet, Adelaide, SA, Australia Univ Padua, Dept Math, Padua, Italy Lund Univ, Fac Law, Lund, Sweden Univ Gothenburg, Dept Microbiol & Immunol, Gothenburg, Sweden NARO, Kachwekano Zardi, Entebbe, Uganda Natl Yunlin Univ Sci & Technol, Bachelor Program Interdisciplinary Studies, Touliu, Yunlin, Taiwan Aarhus Univ, Dept Biomed, Danish Res Inst Translat Neurosci DANDRITE, Aarhus, Denmark Eduardo Mondlane Univ, Math & Comp Sci, Maputo, Mozambique Univ Bern, Dept Old Age Psychiat & Psychotherapy, Bern, Switzerland RAS, Inst Cytol, Lab Cytol Unicellular Organisms, St Petersburg, Russia Beijing Inst Technol, Sch Chem & Chem Engn, Beijing, Peoples R China Univ Queensland, Queensland Alliance Agr & Food Innovat, Brisbane, Qld, Australia Fraunhofer Inst Toxicol & Expt Med ITEM, Inhalat Toxicol, Hannover, Germany Univ Hong Kong, Publ Hlth, Hong Kong, Peoples R China Univ Hlth Network, Anesthesia & Pain Med, Toronto, ON, Canada Univ Toronto, Toronto, ON, Canada Univ Bath, Dept Hlth, Bath, Avon, England Univ Copenhagen, Computat & RNA Biol, Copenhagen, Denmark Fisheries & Oceans Canada, Bedford Inst Oceanog, Dartmouth, NS, Canada Goethe Univ, CEF MC, BMLS, Phys Biol, Frankfurt, Germany Albert Einstein Coll Med, Anat & Struct Biol, New York, NY USA Queensland Govt, Dept Environm & Sci, Brisbane, Qld, Australia Uppsala Univ, Vasc Surg Sect, Dept Surg Sci, Uppsala, Sweden Childrens Canc Hosp, Res, Cairo, Egypt Leibniz Inst Nat Prod Res & Infect Biol, Bio Pilot Plant, Jena, Germany Duy Tan Univ, Inst Res & Dev, Da Nang, Vietnam Univ Helsinki, Helsinki Inst Life Sci HiLIFE, Helsinki, Finland Univ Queensland, Australian Inst Bioengn & Nanotechnol, Brisbane, Qld, Australia George Inst Global Hlth, Sydney, NSW, Australia Griffith Univ, Griffith Inst Drug Discovery, Brisbane, Qld, Australia Dezhou Univ, Coll Phys & Elect Informat, Shandong Prov Key Lab Biophys, Dezhou, Peoples R China Henan Agr Univ, Coll Life Sci, Zhengzhou, Henan, Peoples R China Univ Tokyo, Publ Hlth, Tokyo, Japan Sun Yat Sen Univ, Affiliated Hosp 1, Guangzhou, Guangdong, Peoples R China Univ Illinois, Dept Med, Chicago, IL USA Beijing Inst Microbiol & Epidemiol, State Key Lab Pathogen & Biosecur, Beijing, Peoples R China Minist Hlth, Key Lab Neonatal Dis, Shanghai, Peoples R China Covenant Univ, Dept Phys, Ota, Nigeria Prince Sattam Bin Abdulaziz Univ, Dept Phys Therapy & Hlth Rehabil, Al Kharj, Saudi Arabia Lund Univ, Cognit Sci, Malmo, Sweden Natl Open Univ Nigeria, Dept Publ & Environm Hlth, Abuja, Nigeria Peking Univ, Sch Publ Hlth, Dept Lab Sci & Technol, Beijing, Peoples R China Univ Sydney, Sch Publ Hlth, Menzies Ctr Hlth Policy, Sydney, NSW, Australia Univ Auckland, Dept Elect & Comp Engn, Auckland, New Zealand Beijing Univ Chinese Med, Res Ctr TCM Informat Engn, Beijing, Peoples R China Osped Niguarda Ca Granda, Cardiac Surg, Milan, Italy Univ Vet Med, Clin Horses, Hannover, Germany Harbin Med Univ, Lab Med Genet, Harbin, Heilongjiang, Peoples R China Univ Saskatchewan, Dept Psychol, Saskatoon, SK, Canada Univ Coimbra, Ctr Studies Geog & Spatial Planning CEGOT, Coimbra, Portugal Univ Groningen, Univ Med Ctr Groningen, Epidemiol, Groningen, Netherlands South Cent High Specialty Hosp, Dept Neurol & Neurosurg, Pemex, Mexico Shandong Agr Univ, Coll Informat Sci & Engn, Tai An, Shandong, Peoples R China Curtin Univ, Natl Drug Res Inst, Perth, WA, Australia Wageningen Bioveterinary Res, Bacteriol & Epidemiol, Lelystad, Netherlands Guangdong Second Prov Gen Hosp, Dept Rheumatol & Immunol, Guangzhou, Guangdong, Peoples R China Erasmus MC, Biomed Rngineering, Rotterdam, Netherlands Hiroshima Univ, Grad Sch Biomed & Hlth Sci, Hiroshima, Japan Univ Iceland, Sch Hlth Sci, Reykjavik, Iceland Ohio State Univ, Mat Sci & Engn, Columbus, OH 43210 USA Kathmandu Univ, Sch Med Sci, Dept Physiotherapy, Dhulikhel, Nepal Univ Queensland, Sch Biomed Sci, Brisbane, Qld, Australia Fraunhofer MEVIS, Image Guided Therapies, Bremen, Germany Natl Univ Hlth Syst, Haematol Oncol, Singapore, Singapore Sun Yat Sen Univ, Canc Ctr, Breast Oncol, Guangzhou, Guangdong, Peoples R China Med Coll Wisconsin, Pharmacol & Toxicol, Wauwatosa, WI USA Queensland Univ Technol, Sci & Engn Fac, Sch Chem Phys & Mech Engn, Brisbane, Qld, Australia Univ Turin, Dept Mol Biotechnol & Hlth Sci, Turin, Italy Univ Tehran Med Sci, Sch Rehabil, Physiotherapy Dept, Tehran, Iran Univ Helsinki, Dept Forest Sci, Helsinki, Finland Univ Messina, Human Pathol, Messina, Italy AO Papardo Hosp Messina, Messina, Italy Univ Ibadan, Coll Med, Inst Child Hlth, Ibadan, Nigeria King Faisal Univ, Coll Med, Fac Ophthalmol, Al Hasa, Saudi Arabia Univ Stirling, Inst Social Mkt, Stirling, Scotland Saveh Univ Med Sci, Social Determinants Hlth Res Ctr, Saveh, Iran Gakujutsu Shien Co Ltd, Tokyo, Japan Chinese Acad Sci, Inst Geochem, Guiyang, Guizhou, Peoples R China Univ Plymouth, Med Sch, Plymouth, Devon, England CHU Toulouse, Immunol, Toulouse, France Azorean Biodivers Grp, Ctr Ecol Evolut & Environm Changes, Azores, Portugal Univ Acores, Azores, Portugal RIKEN, Ctr Integrat Med Sci, Yokohama, Kanagawa, Japan Peking Univ, Sch Publ Hlth, Dept Global Hlth, Beijing, Peoples R China Chang Gung Univ, Chang Gung Mem Hosp, Dept Neurol, Linkou Med Ctr, Taoyuan, Taiwan Chang Gung Univ, Coll Med, Taoyuan, Taiwan Univ Malawi, Coll Med, Biomed Sci Dept, Blantyre, Malawi Univ Malawi, Coll Med, Pharm Dept, Blantyre, Malawi Bioself Commun, Biocurat, Marseille, France Peking Univ, Hosp 3, Dept Neurol, Beijing, Peoples R China Ahmadu Bello Univ, Fac Basic Clin Sci, Coll Hlth Sci, Dept Pathol, Zaria, Nigeria Dalhousie Univ, Dept Anesthesia Pain Management & Perioperat Med, Halifax, NS, Canada VisMederi Srl, Siena, Italy UCL, Canc Res UK, London, England UCL, UCL Canc Trials Ctr, London, England Univ Ottawa, Family Med, Ottawa, ON, Canada China Agr Univ, Coll Engn, Beijing, Peoples R China Leiden Univ, Leiden Acad Ctr Drug Res, Div Drug Discovery & Safety, Leiden, Netherlands Sun Yat Sen Univ, Affiliated Hosp 1, Dept Intervent Radiol, Guangzhou, Guangdong, Peoples R China Amer Univ Beirut, Med Ctr, Infect Dis, Beirut, Lebanon Sheffield Hallam Univ, Dept Social Work Social Care & Community Studies, Sheffield, S Yorkshire, England Mechnikov Res Inst Vaccines & Sera, Viral Hepatitis, Moscow, Russia Univ Ottawa, Pediat, Ottawa, ON, Canada Vreden Russian Res Inst Traumatol & Orthopaed, Dept Wound Infect Treatment & Prevent, St Petersburg, Russia Hangzhou Ctr Dis Control & Prevent, Dept TB Control & Prevent, Hangzhou, Zhejiang, Peoples R China Kaohsiung Med Univ, Dept Biotechnol, Kaohsiung, Taiwan Zoetis, Diagnost, Kalamazoo, MI USA Aintree Univ Hosp NHS Fdn Trust, Head & Neck Oncol Res, Liverpool, Merseyside, England Wrightington Hosp, Trauma & Orthopaed, Manchester, Lancs, England Loyola Univ, Med Ctr, Dept Psychiat, 2160 S 1st Ave, Maywood, IL 60153 USA Atkins Vet Serv, Microbiol, Calgary, AB, Canada Univ Porto, FADEUP, CIAFEL, Porto, Portugal Natl Univ Singapore, Saw Swee Hock Sch Publ Hlth, Singapore, Singapore Kangwon Natl Univ, Coll Biotechnol & Biosci, Dept Food Sci & Biotechnol, Chunchon, South Korea Kakatiya Med Coll, Internal Med, Warangal, Telangana, India Univ Antioquia, Vet Med Sch, CIBAV Res Grp, Medellin, Colombia IISER, Dept Phys, Soft & Act Matter Grp, Tirupati 517507, Andhra Pradesh, India Univ Rosario, Sch Med & Hlth, Ctr Studies Phys Activ Measurements, Bogota, Colombia Univ Hosp Essen, Cardiol & Vasc Med, Essen, Germany Univ Hosp Basel, Endocrinol, Basel, Switzerland Univ Tubingen, Inst Med Genet & Appl Genom, Tubingen, Germany Univ Hosp Munster, Div Gen Internal Med Nephrol & Rheumatolog, Dept Med D, Munster, Germany Univ Kentucky, Dept Nephrol, Lexington, KY USA Univ Freiburg, Dept Anaesthesiol & Crit Care, Med Ctr, Freiburg, Germany Univ Calif Irvine, Dept Med, Orange, CA 92668 USA Univ Hosp Leuven, Dept Urol, Leuven, Belgium Chinese Acad Sci, Coll Life Sci, Beijing, Peoples R China Univ Florida, Orthopaed & Rehabil, Gainesville, FL USA Chongqing Med Univ, Affiliated Hosp 1, Chongqing Key Lab Mol Oncol & Epigenet, Chongqing, Peoples R China Tsinghua Univ, Dept Chem Engn, Beijing, Peoples R China Yonsei Univ, Coll Med, Dept Pharmacol, Seoul, South Korea Childrens Hosp Kings Daughters, Eastern Virginia Med Sch, Dept Pediat, Norfolk, VA USA China Three Gorges Univ, Coll Sci, Dept Math, Yichang, Peoples R China Xiangtan Univ, Coll Informat Engn, Xiangtan, Hunan, Peoples R China Univ Hlth Network, Mood Disorders & Psychopharmacol, Toronto, ON, Canada Sao Paulo State Univ UNESP, Dept Anim Sci, Sao Paulo, Brazil Sao Paulo State Univ, Vet Clin, Sao Paulo, Brazil
Published: 2019

9. Isolation and characterization of two novel bacteriophages against carbapenem-resistant Klebsiella pneumoniae .

Author: Senhaji-Kacha A, Bernabéu-Gimeno M, Domingo-Calap P, Aguilera-Correa JJ, Seoane-Blanco M, Otaegi-Ugartemendia S, van Raaij MJ, Esteban J, and García-Quintanilla M
Subjects: Humans, Host Specificity, Sewage virology, Sewage microbiology, Anti-Bacterial Agents pharmacology, Genome, Viral, Microbial Sensitivity Tests, Klebsiella pneumoniae virology, Klebsiella pneumoniae drug effects, Bacteriophages isolation & purification, Bacteriophages physiology, Bacteriophages genetics, Carbapenem-Resistant Enterobacteriaceae isolation & purification, Carbapenem-Resistant Enterobacteriaceae virology, Phage Therapy, Klebsiella Infections microbiology, Klebsiella Infections therapy, Carbapenems pharmacology, Biofilms growth & development, Biofilms drug effects
Abstract: The increase of antibiotic-resistant bacteria has become a global health emergency and the need to explore alternative therapeutic options arises. Phage therapy uses bacteriophages to target specific bacterial strains. Phages are highly specific and can target resistant bacteria. Currently, research in this regard is focused on ensuring reliability and safety to bring this tool into clinical practice. The first step is to conduct comprehensive preclinical research. In this work, we present two novel bacteriophages vB_Kpn_F13 and vB_Kpn_F14 isolated against clinical carbapenem-resistant Klebsiella pneumoniae strains obtained from hospital sewage. Multiple studies in vitro were conducted, such as sequencing, electron microscopy, stability, host range infectivity, planktonic effect and biofilm inhibition in order to discover their ability to be used against carbapenem-resistant K. pneumoniae pathogens causing difficult-to-treat infections., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2024 Senhaji-Kacha, Bernabéu-Gimeno, Domingo-Calap, Aguilera-Correa, Seoane-Blanco, Otaegi-Ugartemendia, van Raaij, Esteban and García-Quintanilla.)
Published: 2024
Full Text: View/download PDF

10. Tricks and tips for trips.

Author: van Raaij MJ
Subjects: Crystallography, X-Ray, Humans, Specimen Handling methods
Abstract: Finding out about sample preparation and transportation of structural biology samples in Acta Crystallographica F, Structural Biology Communications.
Published: 2024
Full Text: View/download PDF

11. The importance of international collaborations in science and structural biology.

Author: Nonato MC, van Raaij MJ, and Agirre J
Subjects: Periodicals as Topic, Humans, International Cooperation
Abstract: The Acta Cryst. F - Structural Biology Communications Editors explain how important international collaborations are in science and structural biology.
Published: 2024
Full Text: View/download PDF

12. The unbearable burden of peer review?

Author: van Raaij MJ
Subjects: Crystallography, X-Ray, Peer Review
Abstract: The current situation of scientific manuscript peer review is discussed, both generally and as applied to Acta Crystallographica F - Biological Research Communications.
Published: 2024
Full Text: View/download PDF

13. Private glycan investigations and public video content.

Author: van Raaij MJ
Subjects: Crystallography, X-Ray, Polysaccharides
Abstract: Acta Cryst. F - Structural Biology Communications plans to introduce more video content to articles and Dialpuri et al. [(2024). Acta Cryst. F80, 30-35] provide an early example.
Published: 2024
Full Text: View/download PDF

14. AlphaFold and the future of structural biology.

Author: Read RJ, Baker EN, Bond CS, Garman EF, and van Raaij MJ
Subjects: Cryoelectron Microscopy, Crystallography, X-Ray, Protein Conformation, Machine Learning, Biology
Abstract: This editorial acknowledges the transformative impact of new machine-learning methods, such as the use of AlphaFold, but also makes the case for the continuing need for experimental structural biology.
Published: 2023
Full Text: View/download PDF

15. Quinate-based ligands for irreversible inactivation of the bacterial virulence factor DHQ1 enzyme-A molecular insight.

Author: Rodríguez Á, Maneiro M, Lence E, Otero JM, van Raaij MJ, Thompson P, Hawkins AR, and González-Bello C
Abstract: Irreversible inhibition of the enzyme type I dehydroquinase (DHQ1), a promising target for anti-virulence drug development, has been explored by enhancing the electrophilicity of specific positions of the ligand towards covalent lysine modification. For ligand design, we made use of the advantages offered by the intrinsic acid-base properties of the amino substituents introduced in the quinate scaffold, namely compounds 6 - 7 ( R configuration at C3), to generate a potential leaving group, as well as the recognition pattern of the enzyme. The reactivity of the C2-C3 bond (Re face) in the scaffold was also explored using compound 8 . The results of the present study show that replacement of the C3 hydroxy group of (-)-quinic acid by a hydroxyamino substituent (compound 6 ) provides a time-dependent irreversible inhibitor, while compound 7 , in which the latter functionality was substituted by an amino group, and the introduction of an oxirane ring at C2-C3 bond, compound 8 , do not allow covalent modification of the enzyme. These outcomes were supported by resolution of the crystal structures of DHQ1 from Staphylococcus aureus ( Sa -DHQ1) and Salmonella typhi ( St -DHQ1) chemically modified by 6 at a resolution of 1.65 and 1.90 Å, respectively, and of St -DHQ1 in the complex with 8 (1.55 Å). The combination of these structural studies with extensive molecular dynamics simulation studies allowed us to understand the molecular basis of the type of inhibition observed. This study is a good example of the importance of achieving the correct geometry between the reactive center of the ligand (electrophile) and the enzyme nucleophile (lysine residue) to allow selective covalent modification. The outcomes obtained with the hydroxyamino derivative 6 also open up new possibilities in the design of irreversible inhibitors based on the use of amino substituents., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2023 Rodríguez, Maneiro, Lence, Otero, van Raaij, Thompson, Hawkins and González-Bello.)
Published: 2023
Full Text: View/download PDF

16. Antibody Recognition of Different Staphylococcus aureus Wall Teichoic Acid Glycoforms.

Author: Di Carluccio C, Soriano-Maldonado P, Berni F, de Haas CJC, Temming AR, Hendriks A, Ali S, Molinaro A, Silipo A, van Sorge NM, van Raaij MJ, Codee JDC, and Marchetti R
Abstract: Wall teichoic acids (WTAs) are glycopolymers decorating the surface of Gram-positive bacteria and potential targets for antibody-mediated treatments against Staphylococcus aureus , including methicillin-resistant (MRSA) strains. Through a combination of glycan microarray, synthetic chemistry, crystallography, NMR, and computational studies, we unraveled the molecular and structural details of fully defined synthetic WTA fragments recognized by previously described monoclonal antibodies (mAbs 4461 and 4497). Our results unveiled the structural requirements for the discriminatory recognition of α- and β-GlcNAc-modified WTA glycoforms by the complementarity-determining regions (CDRs) of the heavy and light chains of the mAbs. Both mAbs interacted not only with the sugar moiety but also with the phosphate groups as well as residues in the ribitol phosphate (RboP) units of the WTA backbone, highlighting their significant role in ligand specificity. Using elongated WTA fragments, containing two sugar modifications, we also demonstrated that the internal carbohydrate moiety of α-GlcNAc-modified WTA is preferentially accommodated in the binding pocket of mAb 4461 with respect to the terminal moiety. Our results also explained the recently documented cross-reactivity of mAb 4497 for β-1,3/β-1,4-GlcNAc-modified WTA, revealing that the flexibility of the RboP backbone is crucial to allow positioning of both glycans in the antibody binding pocket., Competing Interests: The authors declare no competing financial interest., (© 2022 The Authors. Published by American Chemical Society.)
Published: 2022
Full Text: View/download PDF

17. Monomodular Pseudomonas aeruginosa phage JG004 lysozyme (Pae87) contains a bacterial surface-active antimicrobial peptide-like region and a possible substrate-binding subdomain.

Author: Vázquez R, Seoane-Blanco M, Rivero-Buceta V, Ruiz S, van Raaij MJ, and García P
Subjects: Antimicrobial Peptides, Muramidase metabolism, Pseudomonas aeruginosa, Bacteriophages metabolism, Pseudomonas Phages
Abstract: Phage lysins are a source of novel antimicrobials to tackle the bacterial antibiotic-resistance crisis. The engineering of phage lysins is being explored as a game-changing technological strategy to introduce a more precise approach in the way in which antimicrobial therapy is applied. Such engineering efforts will benefit from a better understanding of lysin structure and function. In this work, the antimicrobial activity of the endolysin from Pseudomonas aeruginosa phage JG004, termed Pae87, has been characterized. This lysin had previously been identified as an antimicrobial agent candidate that is able to interact with the Gram-negative surface and disrupt it. Further evidence is provided here based on a structural and biochemical study. A high-resolution crystal structure of Pae87 complexed with a peptidoglycan fragment showed a separate substrate-binding region within the catalytic domain, 18 Å away from the catalytic site and located on the opposite side of the lysin molecule. This substrate-binding region was conserved among phylogenetically related lysins lacking an additional cell-wall-binding domain, but not among those containing such a module. Two glutamic acids were identified to be relevant for the peptidoglycan-degradation activity, although the antimicrobial activity of Pae87 was seemingly unrelated. In contrast, an antimicrobial peptide-like region within the Pae87 C-terminus, named P87, was found to be able to actively disturb the outer membrane and display antibacterial activity by itself. Therefore, an antimicrobial mechanism for Pae87 is proposed in which the P87 peptide plays the role of binding to the outer membrane and disrupting the cell-wall function, either with or without the participation of the catalytic activity of Pae87., (open access.)
Published: 2022
Full Text: View/download PDF

18. Submission of structural biology data for review purposes.

Author: Baker EN, Bond CS, Garman EF, Newman J, Read RJ, and van Raaij MJ
Abstract: The editors discuss the submission of structural biology data., (© Baker et al. 2022.)
Published: 2021
Full Text: View/download PDF

19. Topical Reviews in Acta Crystallographica F Structural Biology Communications.

Author: Helliwell JR, Newman J, and van Raaij MJ
Subjects: Crystallography, X-Ray, Biology, Publishing
Published: 2021
Full Text: View/download PDF

20. Contamination or serendipity - doing the wrong thing by chance.

Author: Newman J and van Raaij MJ
Subjects: Cyanates chemistry, Cyanates metabolism, Escherichia coli metabolism, Escherichia coli Proteins genetics, Escherichia coli Proteins metabolism, Gene Expression, Humans, Hydro-Lyases genetics, Hydro-Lyases metabolism, Recombinant Proteins genetics, Recombinant Proteins metabolism, Recombinant Proteins ultrastructure, Serratia genetics, Serratia metabolism, Artifacts, Crystallography, X-Ray standards, Escherichia coli genetics, Escherichia coli Proteins ultrastructure, Hydro-Lyases ultrastructure, Transgenes
Published: 2020
Full Text: View/download PDF

21. Innovation versus practice in biological crystallization.

Author: Newman J and van Raaij MJ
Subjects: Creativity, Crystallography, X-Ray, Crystallization methods, Proteins chemistry
Published: 2020
Full Text: View/download PDF

22. Self-Immolation of a Bacterial Dehydratase Enzyme by its Epoxide Product.

Author: Lence E, Maneiro M, Sanz-Gaitero M, van Raaij MJ, Thompson P, Hawkins AR, and González-Bello C
Subjects: Bacteria metabolism, Catalysis, Drug Discovery, Hydro-Lyases metabolism, Lysine, Molecular Dynamics Simulation, Bacteria chemistry, Enzyme Inhibitors chemistry, Epoxy Compounds chemistry, Hydro-Lyases chemistry
Abstract: Disabling the bacterial capacity to cause infection is an innovative approach that has attracted significant attention to fight against superbugs. A relevant target for anti-virulence drug discovery is the type I dehydroquinase (DHQ1) enzyme. It was shown that the 2-hydroxyethylammonium derivative 3 has in vitro activity since it causes the covalent modification of the catalytic lysine residue of DHQ1. As this compound does not bear reactive electrophilic centers, how the chemical modification occurs is intriguing. We report here an integrated approach, which involves biochemical studies, X-ray crystallography and computational studies on the reaction path using combined quantum mechanics/molecular mechanics Umbrella Sampling Molecular Dynamics, that evidences that DHQ1 catalyzes its self-immolation by transforming the unreactive 2-hydroxyethylammonium group in 3 into an epoxide that triggers the lysine covalent modification. This finding might open opportunities for the design of lysine-targeted irreversible inhibitors bearing a 2-hydroxyethylammonium moiety as an epoxide proform, which to our knowledge has not been reported previously., (© 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Published: 2020
Full Text: View/download PDF

23. Molecular anatomy of the receptor binding module of a bacteriophage long tail fiber.

Author: Islam MZ, Fokine A, Mahalingam M, Zhang Z, Garcia-Doval C, van Raaij MJ, Rossmann MG, and Rao VB
Subjects: Animals, Mice, Porins metabolism, Receptors, Virus metabolism, Bacteriophage T4 genetics, Bacteriophage T4 metabolism, Bacteriophage T4 ultrastructure, Escherichia coli virology, Virus Attachment
Abstract: Tailed bacteriophages (phages) are one of the most abundant life forms on Earth. They encode highly efficient molecular machines to infect bacteria, but the initial interactions between a phage and a bacterium that then lead to irreversible virus attachment and infection are poorly understood. This information is critically needed to engineer machines with novel host specificities in order to combat antibiotic resistance, a major threat to global health today. The tailed phage T4 encodes a specialized device for this purpose, the long tail fiber (LTF), which allows the virus to move on the bacterial surface and find a suitable site for infection. Consequently, the infection efficiency of phage T4 is one of the highest, reaching the theoretical value of 1. Although the atomic structure of the tip of the LTF has been determined, its functional architecture and how interactions with two structurally very different Escherichia coli receptor molecules, lipopolysaccharide (LPS) and outer membrane protein C (OmpC), contribute to virus movement remained unknown. Here, by developing direct receptor binding assays, extensive mutational and biochemical analyses, and structural modeling, we discovered that the ball-shaped tip of the LTF, a trimer of gene product 37, consists of three sets of symmetrically alternating binding sites for LPS and/or OmpC. Our studies implicate reversible and dynamic interactions between these sites and the receptors. We speculate that the LTF might function as a "molecular pivot" allowing the virus to "walk" on the bacterium by adjusting the angle or position of interaction of the six LTFs attached to the six-fold symmetric baseplate., Competing Interests: The authors have declared that no competing interests exist.
Published: 2019
Full Text: View/download PDF

24. Taking biological structure communications into the third dimension.

Author: van Raaij MJ and Newman J
Subjects: Humans, Protein Domains, Imaging, Three-Dimensional, Proteins chemistry
Published: 2019
Full Text: View/download PDF

25. Inhibition of L. monocytogenes Biofilm Formation by the Amidase Domain of the Phage vB_LmoS_293 Endolysin.

Author: Pennone V, Sanz-Gaitero M, O'Connor P, Coffey A, Jordan K, van Raaij MJ, and McAuliffe O
Subjects: Amidohydrolases genetics, Endopeptidases chemistry, Endopeptidases genetics, Enzyme Activation, Hydrogen-Ion Concentration, Listeria monocytogenes classification, Recombinant Proteins, Substrate Specificity, Temperature, Amidohydrolases metabolism, Bacteriophages enzymology, Biofilms, Endopeptidases metabolism, Host-Pathogen Interactions, Listeria monocytogenes physiology, Listeria monocytogenes virology
Abstract: Listeria monocytogenes is a ubiquitous Gram-positive bacterium that is a major concern for food business operators because of its pathogenicity and ability to form biofilms in food production environments. Bacteriophages (phages) have been evaluated as biocontrol agents for L. monocytogenes in a number of studies and, indeed, certain phages have been approved for use as anti-listerial agents in food processing environments (ListShield and PhageGuard Listex). Endolysins are proteins produced by phages in the host cell. They cleave the peptidoglycan cell wall, thus allowing release of progeny phage into the environment. In this study, the amidase domain of the phage vB_LmoS_293 endolysin (293-amidase) was cloned and expressed in E scherichia . coli (E. coli) . Muralytic activity at different concentrations, pH and temperature values, lytic spectrum and activity against biofilms was determined for the purified 293-amidase protein. The results showed activity on autoclaved cells at three different temperatures (20 °C, 37 °C and 50 °C), with a wider specificity ( L. monocytogenes 473 and 3099, a serotype 4b and serogroup 1/2b-3b-7, respectively) compared to the phage itself, which targets only L. monocytogenes serotypes 4b and 4e. The protein also inhibits biofilm formation on abiotic surfaces. These results show the potential of using recombinant antimicrobial proteins against pathogens in the food production environment., Competing Interests: The authors declare no conflict of interest.
Published: 2019
Full Text: View/download PDF

26. Introducing Methods Communications, a new category of contributions to Acta Crystallographica F.

Author: Newman J and van Raaij MJ
Subjects: Humans, Crystallography, X-Ray methods, Periodicals as Topic standards, Publishing statistics & numerical data
Published: 2019
Full Text: View/download PDF

27. Still Something to Discover: Novel Insights into Escherichia coli Phage Diversity and Taxonomy.

Author: Korf IHE, Meier-Kolthoff JP, Adriaenssens EM, Kropinski AM, Nimtz M, Rohde M, van Raaij MJ, and Wittmann J
Subjects: Coliphages isolation & purification, Coliphages ultrastructure, Genome, Viral, Genomics methods, Host Specificity, Humans, Phylogeny, Viral Tropism, Biodiversity, Coliphages classification, Coliphages physiology, DNA Barcoding, Taxonomic, Escherichia coli virology
Abstract: The aim of this study was to gain further insight into the diversity of Escherichia coli phagesfollowed by enhanced work on taxonomic issues in that field. Therefore, we present the genomiccharacterization and taxonomic classification of 50 bacteriophages against E. coli isolated fromvarious sources, such as manure or sewage. All phages were examined for their host range on a setof different E. coli strains, originating, e.g., from human diagnostic laboratories or poultry farms.Transmission electron microscopy revealed a diversity of morphotypes (70% Myo-, 22% Sipho-, and8% Podoviruses), and genome sequencing resulted in genomes sizes from ~44 to ~370 kb.Annotation and comparison with databases showed similarities in particular to T4- and T5-likephages, but also to less-known groups. Though various phages against E. coli are already describedin literature and databases, we still isolated phages that showed no or only few similarities to otherphages, namely phages Goslar, PTXU04, and KWBSE43-6. Genome-based phylogeny andclassification of the newly isolated phages using VICTOR resulted in the proposal of new generaand led to an enhanced taxonomic classification of E. coli phages.
Published: 2019
Full Text: View/download PDF

28. Findable Accessible Interoperable Re-usable (FAIR) diffraction data are coming to protein crystallography.

Author: Helliwell JR, Minor W, Weiss MS, Garman EF, Read RJ, Newman J, van Raaij MJ, Hajdu J, and Baker EN
Subjects: Databases, Factual, Humans, Information Dissemination, Proteins chemistry, Reproducibility of Results, X-Ray Diffraction, Crystallography, X-Ray methods, Image Processing, Computer-Assisted methods, Imaging, Three-Dimensional methods, Information Storage and Retrieval methods, Proteins ultrastructure
Published: 2019
Full Text: View/download PDF

29. Welcoming Janet Newman with a BLAST on crystallization strategy.

Author: van Raaij MJ
Subjects: Crystallography, X-Ray, Surface Properties, Crystallization, Proteins chemistry, Publishing
Published: 2019
Full Text: View/download PDF

30. The so far farthest reaches of the double jelly roll capsid protein fold.

Author: San Martín C and van Raaij MJ
Subjects: Bacteriophages genetics, Capsid Proteins genetics, DNA Viruses genetics, Genome, Viral, Protein Structure, Tertiary, Bacteriophages chemistry, Capsid Proteins chemistry, Metagenomics
Abstract: Background: During the last two decades, structural biology analyses have shown that viruses infecting hosts far apart in evolution share similar architectural features, prompting a new virus classification based on structural lineages. Until recently, only a few prokaryotic viruses had been described for one of the lineages, whose main characteristic is a capsid protein with a perpendicular double jelly roll., Main Body: Metagenomics analyses are showing that the variety of prokaryotic viruses encoding double jelly roll capsid proteins is much larger than previously thought. The newly discovered viruses have novel genome organisations with interesting implications for virus structure, function and evolution. There are also indications of their having a significant ecological impact., Conclusion: Viruses with double jelly roll capsid proteins that infect prokaryotic hosts form a large part of the virosphere that had so far gone unnoticed. Their discovery by metagenomics is only a first step towards many more exciting findings. Work needs to be invested in isolating these viruses and their hosts, characterizing the structure and function of the proteins their genomes encode, and eventually access the wealth of biological information they may hold.
Published: 2018
Full Text: View/download PDF

31. Quo vadis, Acta Crystallographica F?

Author: van Raaij MJ
Subjects: Cryoelectron Microscopy, Magnetic Resonance Spectroscopy, Crystallography, X-Ray, Serial Publications
Published: 2018
Full Text: View/download PDF

32. Structure and N-acetylglucosamine binding of the distal domain of mouse adenovirus 2 fibre.

Author: Singh AK, Nguyen TH, Vidovszky MZ, Harrach B, Benkő M, Kirwan A, Joshi L, Kilcoyne M, Berbis MÁ, Cañada FJ, Jiménez-Barbero J, Menéndez M, Wilson SS, Bromme BA, Smith JG, and van Raaij MJ
Subjects: Animals, Crystallography, X-Ray, Mice, Protein Binding, Protein Conformation, Acetylglucosamine metabolism, Capsid Proteins chemistry, Capsid Proteins metabolism, Protein Domains, Receptors, Virus metabolism
Abstract: Murine adenovirus 2 (MAdV-2) infects cells of the mouse gastrointestinal tract. Like human adenoviruses, it is a member of the genus Mastadenovirus, family Adenoviridae. The MAdV-2 genome has a single fibre gene that expresses a 787 residue-long protein. Through analogy to other adenovirus fibre proteins, it is expected that the carboxy-terminal virus-distal head domain of the fibre is responsible for binding to the host cell, although the natural receptor is unknown. The putative head domain has little sequence identity to adenovirus fibres of known structure. In this report, we present high-resolution crystal structures of the carboxy-terminal part of the MAdV-2 fibre. The structures reveal a domain with the typical adenovirus fibre head topology and a domain containing two triple β-spiral repeats of the shaft domain. Through glycan microarray profiling, saturation transfer difference nuclear magnetic resonance spectroscopy, isothermal titration calorimetry and site-directed mutagenesis, we show that the fibre specifically binds to the monosaccharide N-acetylglucosamine (GlcNAc). The crystal structure of the complex reveals that GlcNAc binds between the AB and CD loops at the top of each of the three monomers of the MAdV-2 fibre head. However, infection competition assays show that soluble GlcNAc monosaccharide and natural GlcNAc-containing polymers do not inhibit infection by MAdV-2. Furthermore, site-directed mutation of the GlcNAc-binding residues does not prevent the inhibition of infection by soluble fibre protein. On the other hand, we show that the MAdV-2 fibre protein binds GlcNAc-containing mucin glycans, which suggests that the MAdV-2 fibre protein may play a role in viral mucin penetration in the mouse gut.
Published: 2018
Full Text: View/download PDF

33. Carbohydrate structure hits the groove.

Author: Agirre J and van Raaij MJ
Subjects: Animals, Crystallography methods, Humans, Carbohydrates chemistry, Glycoproteins chemistry
Published: 2018
Full Text: View/download PDF

34. A novel amyloid designable scaffold and potential inhibitor inspired by GAIIG of amyloid beta and the HIV-1 V3 loop.

Author: Kokotidou C, Jonnalagadda SVR, Orr AA, Seoane-Blanco M, Apostolidou CP, van Raaij MJ, Kotzabasaki M, Chatzoudis A, Jakubowski JM, Mossou E, Forsyth VT, Mitchell EP, Bowler MW, Llamas-Saiz AL, Tamamis P, and Mitraki A
Subjects: Crystallography, X-Ray, Humans, Protein Structure, Secondary, Amyloid beta-Peptides chemistry, HIV Envelope Protein gp120 chemistry, HIV-1 chemistry
Abstract: The GAIIG sequence, common to the amyloid beta peptide (residues 29-33) and to the HIV-1 gp120 (residues 24-28 in a typical V3 loop), self-assembles into amyloid fibrils, as suggested by theory and the experiments presented here. The longer YATGAIIGNII sequence from the V3 loop also self-assembles into amyloid fibrils, of which the first three and the last two residues are outside the amyloid GAIIG core. We postulate that this sequence, with suitably selected modifications at the flexible positions, can serve as a designable scaffold for novel amyloid-based materials. Moreover, we report the single crystal X-ray structure of the beta-breaker peptide GAIPIG at 1.05 Å resolution. The structural information provided in this study could serve as the basis for structure-based design of potential inhibitors of amyloid formation., (© 2018 Federation of European Biochemical Societies.)
Published: 2018
Full Text: View/download PDF

35. Contractile injection systems of bacteriophages and related systems.

Author: Taylor NMI, van Raaij MJ, and Leiman PG
Subjects: Bacteriophage T4 genetics, Biological Evolution, Cell Membrane chemistry, Cell Membrane metabolism, Genome, Viral, Gram-Negative Bacteria chemistry, Gram-Negative Bacteria genetics, Gram-Negative Bacteria physiology, Pyocins chemistry, Pyocins metabolism, Type VI Secretion Systems chemistry, Type VI Secretion Systems genetics, Type VI Secretion Systems physiology, Viral Tail Proteins genetics, X-Ray Diffraction, Bacteriophage T4 chemistry, Bacteriophage T4 physiology, Viral Tail Proteins chemistry, Viral Tail Proteins physiology
Abstract: Contractile tail bacteriophages, or myobacteriophages, use a sophisticated biomolecular structure to inject their genome into the bacterial host cell. This structure consists of a contractile sheath enveloping a rigid tube that is sharpened by a spike-shaped protein complex at its tip. The spike complex forms the centerpiece of a baseplate complex that terminates the sheath and the tube. The baseplate anchors the tail to the target cell membrane with the help of fibrous proteins emanating from it and triggers contraction of the sheath. The contracting sheath drives the tube with its spiky tip through the target cell membrane. Subsequently, the bacteriophage genome is injected through the tube. The structural transformation of the bacteriophage T4 baseplate upon binding to the host cell has been recently described in near-atomic detail. In this review we discuss structural elements and features of this mechanism that are likely to be conserved in all contractile injection systems (systems evolutionary and structurally related to contractile bacteriophage tails). These include the type VI secretion system (T6SS), which is used by bacteria to transfer effectors into other bacteria and into eukaryotic cells, and tailocins, a large family of contractile bacteriophage tail-like compounds that includes the P. aeruginosa R-type pyocins., (© 2018 John Wiley & Sons Ltd.)
Published: 2018
Full Text: View/download PDF

36. Target highlights from the first post-PSI CASP experiment (CASP12, May-August 2016).

Author: Kryshtafovych A, Albrecht R, Baslé A, Bule P, Caputo AT, Carvalho AL, Chao KL, Diskin R, Fidelis K, Fontes CMGA, Fredslund F, Gilbert HJ, Goulding CW, Hartmann MD, Hayes CS, Herzberg O, Hill JC, Joachimiak A, Kohring GW, Koning RI, Lo Leggio L, Mangiagalli M, Michalska K, Moult J, Najmudin S, Nardini M, Nardone V, Ndeh D, Nguyen TH, Pintacuda G, Postel S, van Raaij MJ, Roversi P, Shimon A, Singh AK, Sundberg EJ, Tars K, Zitzmann N, and Schwede T
Subjects: Animals, Bacteria chemistry, Crystallography, X-Ray, Humans, Protein Folding, Software, Computational Biology methods, Models, Molecular, Protein Conformation, Proteins chemistry
Abstract: The functional and biological significance of the selected CASP12 targets are described by the authors of the structures. The crystallographers discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP12 experiment., (© 2017 Wiley Periodicals, Inc.)
Published: 2018
Full Text: View/download PDF

37. Structure of a Reptilian Adenovirus Reveals a Phage Tailspike Fold Stabilizing a Vertebrate Virus Capsid.

Author: Menéndez-Conejero R, Nguyen TH, Singh AK, Condezo GN, Marschang RE, van Raaij MJ, and San Martín C
Subjects: Amino Acid Sequence, Animals, Atadenovirus genetics, Capsid Proteins genetics, Cryoelectron Microscopy, Crystallography, X-Ray, Mass Spectrometry, Models, Molecular, Protein Structure, Secondary, Atadenovirus chemistry, Capsid chemistry, Capsid Proteins chemistry, Reptiles virology
Abstract: Although non-human adenoviruses (AdVs) might offer solutions to problems posed by human AdVs as therapeutic vectors, little is known about their basic biology. In particular, there are no structural studies on the complete virion of any AdV with a non-mammalian host. We combine mass spectrometry, cryo-electron microscopy, and protein crystallography to characterize the composition and structure of a snake AdV (SnAdV-1, Atadenovirus genus). SnAdV-1 particles contain the genus-specific proteins LH3, p32k, and LH2, a previously unrecognized structural component. Remarkably, the cementing protein LH3 has a trimeric β helix fold typical of bacteriophage host attachment proteins. The organization of minor coat proteins differs from that in human AdVs, correlating with higher thermostability in SnAdV-1. These findings add a new piece to the intriguing puzzle of virus evolution, hint at the use of cell entry pathways different from those in human AdVs, and will help development of new, thermostable SnAdV-1-based vectors., (Copyright © 2017 Elsevier Ltd. All rights reserved.)
Published: 2017
Full Text: View/download PDF

38. Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34.

Author: Granell M, Namura M, Alvira S, Kanamaru S, and van Raaij MJ
Subjects: Crystallography, X-Ray, Models, Molecular, Protein Conformation, Bacteriophage T4 chemistry, Viral Tail Proteins chemistry
Abstract: Long tail fibers of bacteriophage T4 are formed by proteins gp34, gp35, gp36, and gp37, with gp34 located at the phage-proximal end and gp37 at the phage-distal, receptor-binding end. We have solved the structure of the carboxy-terminal region of gp34, consisting of amino acids 894-1289, by single-wavelength anomalous diffraction and extended the structure to amino acids 744-1289 using data collected from crystals containing longer gp34-fragments. The structure reveals three repeats of a mixed α-β fibrous domain in residues 744 to 877. A triple-helical neck connects to an extended triple β-helix domain (amino acids 900-1127) punctuated by two β-prism domains. Next, a β-prism domain decorated with short helices and extended β-helices is present (residues 1146-1238), while the C -terminal end is capped with another short β-helical region and three β-hairpins. The structure provides insight into the stability of the fibrous gp34 protein., Competing Interests: The authors declare no conflict of interest. The funding sponsors had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, and in the decision to publish the results.
Published: 2017
Full Text: View/download PDF

39. The Eighth Central European Conference "Chemistry towards Biology": Snapshot.

Author: Perczel A, Atanasov AG, Sklenář V, Nováček J, Papoušková V, Kadeřávek P, Žídek L, Kozłowski H, Wątły J, Hecel A, Kołkowska P, Koča J, Svobodová-Vařeková R, Pravda L, Sehnal D, Horský V, Geidl S, Enriz RD, Matějka P, Jeništová A, Dendisová M, Kokaislová A, Weissig V, Olsen M, Coffey A, Ajuebor J, Keary R, Sanz-Gaitero M, van Raaij MJ, McAuliffe O, Waltenberger B, Mocan A, Šmejkal K, Heiss EH, Diederich M, Musioł R, Košmrlj J, Polański J, and Jampílek J
Subjects: Drug Delivery Systems, Drug Design, Epigenesis, Genetic, Structure-Activity Relationship, Systems Biology, Chemistry, Pharmaceutical methods, Proteins chemistry
Abstract: The Eighth Central European Conference "Chemistry towards Biology" was held in Brno, Czech Republic, on August 28-September 1, 2016 to bring together experts in biology, chemistry and design of bioactive compounds; promote the exchange of scientific results, methods and ideas; and encourage cooperation between researchers from all over the world. The topics of the conference covered "Chemistry towards Biology", meaning that the event welcomed chemists working on biology-related problems, biologists using chemical methods, and students and other researchers of the respective areas that fall within the common scope of chemistry and biology. The authors of this manuscript are plenary speakers and other participants of the symposium and members of their research teams. The following summary highlights the major points/topics of the meeting., Competing Interests: The authors declare no conflict of interest.
Published: 2016
Full Text: View/download PDF

40. Some of the most interesting CASP11 targets through the eyes of their authors.

Author: Kryshtafovych A, Moult J, Baslé A, Burgin A, Craig TK, Edwards RA, Fass D, Hartmann MD, Korycinski M, Lewis RJ, Lorimer D, Lupas AN, Newman J, Peat TS, Piepenbrink KH, Prahlad J, van Raaij MJ, Rohwer F, Segall AM, Seguritan V, Sundberg EJ, Singh AK, Wilson MA, and Schwede T
Subjects: Bacteria chemistry, Computational Biology methods, Computer Graphics, Crystallography, X-Ray, Databases, Protein, Humans, International Cooperation, Protein Folding, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Secondary, Sequence Homology, Amino Acid, Viruses chemistry, Computational Biology statistics & numerical data, Models, Molecular, Models, Statistical, Proteins chemistry, Software
Abstract: The Critical Assessment of protein Structure Prediction (CASP) experiment would not have been possible without the prediction targets provided by the experimental structural biology community. In this article, selected crystallographers providing targets for the CASP11 experiment discuss the functional and biological significance of the target proteins, highlight their most interesting structural features, and assess whether these features were correctly reproduced in the predictions submitted to CASP11. Proteins 2016; 84(Suppl 1):34-50. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc., (© 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.)
Published: 2016
Full Text: View/download PDF

41. Fasciola hepatica calcium-binding protein FhCaBP2: structure of the dynein light chain-like domain.

Author: Nguyen TH, Thomas CM, Timson DJ, and van Raaij MJ
Subjects: Animals, Calcium-Binding Proteins genetics, Calcium-Binding Proteins metabolism, Crystallography, X-Ray, Dyneins genetics, Dyneins metabolism, EF Hand Motifs, Fasciola hepatica genetics, Helminth Proteins chemistry, Helminth Proteins genetics, Helminth Proteins metabolism, Humans, Models, Molecular, Protein Domains, Recombinant Proteins, Calcium-Binding Proteins chemistry, Dyneins chemistry, Fasciola hepatica metabolism, Fascioliasis parasitology
Abstract: The common liver fluke Fasciola hepatica causes an increasing burden on human and animal health, partly because of the spread of drug-resistant isolates. As a consequence, there is considerable interest in developing new drugs to combat liver fluke infections. A group of potential targets is a family of calcium-binding proteins which combine an N-terminal domain with two EF-hand motifs and a C-terminal domain with predicted similarity to dynein light chains (DLC-like domain). The function of these proteins is unknown, although in several species, they have been localised to the tegument, an important structure at the host-parasite interface. Here, we report the X-ray crystal structure of the DLC-like domain of F. hepatica calcium-binding protein 2 (FhCaBP2), solved using single-wavelength anomalous diffraction and refined at 2.3 Å resolution in two different crystal forms. The FhCaBP2 DLC-like domain has a structure similar to other DLC domains, with an anti-parallel β-sheet packed against an α-helical hairpin. Like other DLC domains, it dimerises through its β2-strand, which extends in an arch and forms the fifth strand in an extended β-sheet of the other monomer. The structure provides molecular details of the dimerisation of FhCaBP2, the first example from this family of parasite proteins.
Published: 2016
Full Text: View/download PDF

42. Crystal structure of raptor adenovirus 1 fibre head and role of the beta-hairpin in siadenovirus fibre head domains.

Author: Nguyen TH, Ballmann MZ, Do HT, Truong HN, Benkő M, Harrach B, and van Raaij MJ
Subjects: Adenoviridae chemistry, Adenoviridae classification, Adenoviridae genetics, Animals, Crystallography, X-Ray, Humans, Inverted Repeat Sequences, Models, Molecular, Nucleic Acid Conformation, Phylogeny, Protein Domains, Raptors virology, Viral Proteins genetics, Viral Proteins metabolism, Adenoviridae metabolism, Adenoviridae Infections veterinary, Adenoviridae Infections virology, Viral Proteins chemistry
Abstract: Background: Most adenoviruses recognize their host cells via an interaction of their fibre head domains with a primary receptor. The structural framework of adenovirus fibre heads is conserved between the different adenovirus genera for which crystal structures have been determined (Mastadenovirus, Aviadenovirus, Atadenovirus and Siadenovirus), but genus-specific differences have also been observed. The only known siadenovirus fibre head structure, that of turkey adenovirus 3 (TAdV-3), revealed a twisted beta-sandwich resembling the reovirus fibre head architecture more than that of other adenovirus fibre heads, plus a unique beta-hairpin embracing a neighbouring monomer. The TAdV-3 fibre head was shown to bind sialyllactose., Methods: Raptor adenovirus 1 (RAdV-1) fibre head was expressed, crystallized and its structure was solved and refined at 1.5 Å resolution. The structure could be solved by molecular replacement using the TAdV-3 fibre head structure as a search model, despite them sharing a sequence identity of only 19 %. Versions of both the RAdV-1 and TAdV-3 fibre heads with their beta-hairpin arm deleted were prepared and their stabilities were compared with the non-mutated proteins by a thermal unfolding assay., Results: The structure of the RAdV-1 fibre head contains the same twisted ABCJ-GHID beta-sandwich and beta-hairpin arm as the TAdV-3 fibre head. However, while the predicted electro-potential surface charge of the TAdV-3 fibre head is mainly positive, the RAdV-1 fibre head shows positively and negatively charged patches and does not appear to bind sialyllactose. Deletion of the beta-hairpin arm does not affect the structure of the raptor adenovirus 1 fibre head and only affects the stability of the RAdV-1 and TAdV-3 fibre heads slightly., Conclusions: The high-resolution structure of RAdV-1 fibre head is the second known structure of a siadenovirus fibre head domain. The structure shows that the siadenovirus fibre head structure is conserved, but differences in the predicted surface charge suggest that RAdV-1 uses a different natural receptor for cell attachment than TAdV-3. Deletion of the beta-hairpin arm shows little impact on the structure and stability of the siadenovirus fibre heads.
Published: 2016
Full Text: View/download PDF

43. Characterization of a Bacteriophage-Derived Murein Peptidase for Elimination of Antibiotic-Resistant Staphylococcus aureus.

Author: Keary R, Sanz-Gaitero M, van Raaij MJ, O'Mahony J, Fenton M, McAuliffe O, Hill C, Ross RP, and Coffey A
Subjects: Animals, Biofilms drug effects, Endopeptidases chemistry, Humans, Anti-Bacterial Agents pharmacology, Methicillin-Resistant Staphylococcus aureus drug effects, N-Acetylmuramoyl-L-alanine Amidase metabolism, Staphylococcus Phages enzymology
Abstract: Staphylococcus aureus is a major cause of infection in humans and animals, causing a wide variety of diseases, from local inflammations to fatal sepsis. The bacterium is commonly multi-drug resistant and thus many front-line antibiotics have been rendered ineffective for treating such infections. Research on murein/peptidoglycan hydrolases, derived from bacterial viruses (bacteriophages), has demonstrated that such proteins are attractive candidates for development as novel antibacterial agents for combatting Gram-positive pathogens. Here we review the research produced to-date on the bacteriophage-derived CHAPK murein peptidase. Initially, we sequenced and annotated the genome of anti-staphylococcal bacteriophage K and cloned the gene for the bacteriophage endolysin, a murein hydrolase which plays a role in cell killing during the bacteriophage life cycle. An highly active domain of the enzyme, a cysteine, histidine-dependent amido hydrolase/peptidase (CHAPK), was cloned, overexpressed in E. coli and purified. This CHAPK enzyme was demonstrated to rapidly lyse several strains of methicillin resistant S. aureus and both disrupted and prevented the formation of a staphylococcal biofilm. The staphylolytic activity of the peptidase was demonstrated in vivo using a mouse model, without adverse effects on the animals. The crystal structure of the enzyme was elucidated, revealing a calcium ion close to the active site. Site-directed mutagenesis indicated that this calcium ion is involved in the catalytic mechanism of the enzyme. The crystal structure of this enzyme is a valuable source of information for efficient engineering of this and similar CHAP-domain-containing proteins. Overall, the data collected to date on CHAPK has demonstrated its strong potential as a novel therapeutic candidate for treatment of staphylococcal infections and has provided us with insight into the fundamental enzymatic mechanisms of CHAP domain-containing peptidoglycan hydrolases.
Published: 2016
Full Text: View/download PDF

44. Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone.

Author: Garcia-Doval C, Castón JR, Luque D, Granell M, Otero JM, Llamas-Saiz AL, Renouard M, Boulanger P, and van Raaij MJ
Subjects: Caudovirales chemistry, Caudovirales physiology, Crystallography, X-Ray, Models, Molecular, Molecular Chaperones genetics, Mutant Proteins chemistry, Mutant Proteins genetics, Protein Conformation, Siphoviridae physiology, Viral Tail Proteins genetics, Virus Attachment, Molecular Chaperones chemistry, Siphoviridae chemistry, Viral Tail Proteins chemistry
Abstract: Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970-1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 Å resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 Å structure solved by molecular replacement. The additional chaperone domain (residues 1263-1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition.
Published: 2015
Full Text: View/download PDF

45. Structure and Sialyllactose Binding of the Carboxy-Terminal Head Domain of the Fibre from a Siadenovirus, Turkey Adenovirus 3.

Author: Singh AK, Berbís MÁ, Ballmann MZ, Kilcoyne M, Menéndez M, Nguyen TH, Joshi L, Cañada FJ, Jiménez-Barbero J, Benkő M, Harrach B, and van Raaij MJ
Subjects: Amino Acid Sequence, Binding Sites genetics, Calorimetry methods, Carbohydrate Conformation, Carbohydrate Sequence, Crystallography, X-Ray, Lactose chemistry, Lactose metabolism, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Mutation, Polysaccharides chemistry, Polysaccharides metabolism, Protein Binding, Siadenovirus genetics, Siadenovirus pathogenicity, Sialic Acids metabolism, Thermodynamics, Viral Proteins genetics, Viral Proteins metabolism, Virulence genetics, Lactose analogs & derivatives, Protein Structure, Tertiary, Siadenovirus metabolism, Sialic Acids chemistry, Viral Proteins chemistry
Abstract: The virulent form of turkey adenovirus 3 (TAdV-3), also known as turkey hemorrhagic enteritis virus (THEV), is an economically important poultry pathogen, while the avirulent form is used as a vaccine. TAdV-3 belongs to the genus Siadenovirus. The carboxy-terminal region of its fibre does not have significant sequence similarity to any other adenovirus fibre heads of known structure. Two amino acid sequence differences between virulent and avirulent TAdV-3 map on the fibre head: where virulent TAdV-3 contains Ile354 and Thr376, avirulent TAdV-3 contains Met354 and Met376. We determined the crystal structures of the trimeric virulent and avirulent TAdV-3 fibre head domains at 2.2 Å resolution. Each monomer contains a beta-sandwich, which, surprisingly, resembles reovirus fibre head more than other adenovirus fibres, although the ABCJ-GHID topology is conserved in all. A beta-hairpin insertion in the C-strand of each trimer subunit embraces its neighbouring monomer. The avirulent and virulent TAdV-3 fibre heads are identical apart from the exact orientation of the beta-hairpin insertion. In vitro, sialyllactose was identified as a ligand by glycan microarray analysis, nuclear magnetic resonance spectroscopy, and crystallography. Its dissociation constant was measured to be in the mM range by isothermal titration calorimetry. The ligand binds to the side of the fibre head, involving amino acids Glu392, Thr419, Val420, Lys421, Asn422, and Gly423 binding to the sialic acid group. It binds slightly more strongly to the avirulent form. We propose that, in vivo, the TAdV-3 fibre may bind a sialic acid-containing cell surface component.
Published: 2015
Full Text: View/download PDF

46. Chemical Modification of a Dehydratase Enzyme Involved in Bacterial Virulence by an Ammonium Derivative: Evidence of its Active Site Covalent Adduct.

Author: González-Bello C, Tizón L, Lence E, Otero JM, van Raaij MJ, Martinez-Guitian M, Beceiro A, Thompson P, and Hawkins AR
Subjects: Ammonium Compounds metabolism, Cell Line, Enzyme Inhibitors chemistry, Enzyme Inhibitors metabolism, Enzyme Inhibitors pharmacology, Humans, Hydro-Lyases metabolism, Molecular Dynamics Simulation, Salmonella typhi pathogenicity, Virulence, Ammonium Compounds chemistry, Ammonium Compounds pharmacology, Catalytic Domain drug effects, Hydro-Lyases antagonists & inhibitors, Hydro-Lyases chemistry, Salmonella typhi enzymology, Staphylococcus aureus enzymology
Abstract: The first example of an ammonium derivative that causes a specific modification of the active site of type I dehydroquinase (DHQ1), a dehydratase enzyme that is a promising target for antivirulence drug discovery, is described. The resolution at 1.35 Å of the crystal structure of DHQ1 from Salmonella typhi chemically modified by this ammonium derivative revealed that the ligand is covalently attached to the essential Lys170 through the formation of an amine. The detection by mass spectroscopy of the reaction intermediates, in conjunction with the results of molecular dynamics simulations, allowed us to explain the inhibition mechanism and the experimentally observed differences between S. typhi and Staphylococcus aureus enzymes. The results presented here reveal that the replacement of Phe225 in St-DHQ1 by Tyr214 in Sa-DHQ1 and its hydrogen bonding interaction with the conserved water molecule observed in several crystal structures protects the amino adduct against further dehydration/aromatization reactions. In contrast, for the St-DHQ1 enzyme, the carboxylate group of Asp114, with the assistance of this water molecule, would trigger the formation of a Schiff base that can undergo further dehydration reactions until full aromatization of the cyclohexane ring is achieved. Moreover, in vitro antivirulence studies showed that the reported compound is able to reduce the ability of Salmonella Enteritidis to kill A459 respiratory cells. These studies have identified a good scaffold for the design of irreversible inhibitors that can be used as drugs and has opened up new opportunities for the development of novel antivirulence agents by targeting the DHQ1 enzyme.
Published: 2015
Full Text: View/download PDF

47. Crystal structure of the fibre head domain of bovine adenovirus 4, a ruminant atadenovirus.

Author: Nguyen TH, Vidovszky MZ, Ballmann MZ, Sanz-Gaitero M, Singh AK, Harrach B, Benkő M, and van Raaij MJ
Subjects: Animals, Cattle, Crystallography, X-Ray, Models, Molecular, Protein Conformation, Atadenovirus chemistry, Capsid Proteins chemistry
Abstract: Background: In adenoviruses, primary host cell recognition is generally performed by the head domains of their homo-trimeric fibre proteins. This first interaction is reversible. A secondary, irreversible interaction subsequently takes place via other adenovirus capsid proteins and leads to a productive infection. Although many fibre head structures are known for human mastadenoviruses, not many animal adenovirus fibre head structures have been determined, especially not from those belonging to adenovirus genera other than Mastadenovirus., Methods: We constructed an expression vector for the fibre head domain from a ruminant atadenovirus, bovine adenovirus 4 (BAdV-4), consisting of amino acids 414-535, expressed the protein in Escherichia coli, purified it by metal affinity and cation exchange chromatography and crystallized it. The structure was solved using single isomorphous replacement plus anomalous dispersion of a mercury derivative and refined against native data that extended to 1.2 Å resolution., Results: Like in other adenoviruses, the BAdV-4 fibre head monomer contains a beta-sandwich consisting of ABCJ and GHID sheets. The topology is identical to the fibre head of the other studied atadenovirus, snake adenovirus 1 (SnAdV-1), including the alpha-helix in the DG-loop, despite of them having a sequence identity of only 15 %. There are also differences which may have implications for ligand binding. Beta-strands G and H are longer and differences in several surface-loops and surface charge are observed., Conclusions: Chimeric adenovirus fibres have been used to retarget adenovirus-based anti-cancer and gene therapy vectors. Ovine adenovirus 7 (OAdV-7), another ruminant atadenovirus, is intensively tested as a basis for such a vector. Here, we present the high-resolution atomic structure of the BAdV-4 fibre head domain, the second atadenovirus fibre head structure known and the first of an atadenovirus that infects a mammalian host. Future research should focus on the receptor-binding properties of these fibre head domains.
Published: 2015
Full Text: View/download PDF

48. Conformational changes leading to T7 DNA delivery upon interaction with the bacterial receptor.

Author: González-García VA, Pulido-Cid M, Garcia-Doval C, Bocanegra R, van Raaij MJ, Martín-Benito J, Cuervo A, and Carrascosa JL
Subjects: Bacteriophage T7 chemistry, Bacteriophage T7 genetics, DNA Packaging, DNA, Viral chemistry, DNA, Viral genetics, Escherichia coli ultrastructure, Kinetics, Microbial Interactions, Models, Molecular, Nucleic Acid Conformation, Transduction, Genetic, Virion chemistry, Virion genetics, Virion ultrastructure, Bacteriophage T7 ultrastructure, DNA, Viral ultrastructure, Escherichia coli virology, Genome, Viral, Lipopolysaccharides metabolism, Receptors, Virus metabolism
Abstract: The majority of bacteriophages protect their genetic material by packaging the nucleic acid in concentric layers to an almost crystalline concentration inside protein shells (capsid). This highly condensed genome also has to be efficiently injected into the host bacterium in a process named ejection. Most phages use a specialized complex (often a tail) to deliver the genome without disrupting cell integrity. Bacteriophage T7 belongs to the Podoviridae family and has a short, non-contractile tail formed by a tubular structure surrounded by fibers. Here we characterize the kinetics and structure of bacteriophage T7 DNA delivery process. We show that T7 recognizes lipopolysaccharides (LPS) from Escherichia coli rough strains through the fibers. Rough LPS acts as the main phage receptor and drives DNA ejection in vitro. The structural characterization of the phage tail after ejection using cryo-electron microscopy (cryo-EM) and single particle reconstruction methods revealed the major conformational changes needed for DNA delivery at low resolution. Interaction with the receptor causes fiber tilting and opening of the internal tail channel by untwisting the nozzle domain, allowing release of DNA and probably of the internal head proteins., (© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.)
Published: 2015
Full Text: View/download PDF

49. Irreversible covalent modification of type I dehydroquinase with a stable Schiff base.

Author: Tizón L, Maneiro M, Peón A, Otero JM, Lence E, Poza S, van Raaij MJ, Thompson P, Hawkins AR, and González-Bello C
Subjects: Bacterial Proteins antagonists & inhibitors, Catalytic Domain, Crystallography, X-Ray, Enzyme Inhibitors chemical synthesis, Epoxy Compounds chemical synthesis, Histidine chemistry, Hydro-Lyases antagonists & inhibitors, Hydrogen Bonding, Kinetics, Ligands, Lysine chemistry, Molecular Dynamics Simulation, Protein Binding, Salmonella typhi chemistry, Salmonella typhi enzymology, Static Electricity, Bacterial Proteins chemistry, Enzyme Inhibitors chemistry, Epoxy Compounds chemistry, Hydro-Lyases chemistry, Schiff Bases chemistry
Abstract: The irreversible inhibition of type I dehydroquinase (DHQ1), the third enzyme of the shikimic acid pathway, is investigated by structural, biochemical and computational studies. Two epoxides, which are mimetics of the natural substrate, were designed as irreversible inhibitors of the DHQ1 enzyme and to study the binding requirements of the linkage to the enzyme. The epoxide with the S configuration caused the covalent modification of the protein whereas no reaction was obtained with its epimer. The first crystal structure of DHQ1 from Salmonella typhi covalently modified by the S epoxide, which is reported at 1.4 Å, revealed that the modified ligand is surprisingly covalently attached to the essential Lys170 by the formation of a stable Schiff base. The experimental and molecular dynamics simulation studies reported here highlight the huge importance of the conformation of the C3 carbon of the ligand for covalent linkage to this type of aldolase I enzyme, revealed the key role played by the essential His143 as a Lewis acid in this process and show the need for a neatly closed active site for catalysis.
Published: 2015
Full Text: View/download PDF

50. Crystal structure of the fibre head domain of the Atadenovirus Snake Adenovirus 1.

Author: Singh AK, Menéndez-Conejero R, San Martín C, and van Raaij MJ
Subjects: Animals, Carrier Proteins chemistry, Crystallography, X-Ray, Protein Binding, Snakes, Adenoviridae, Capsid Proteins chemistry, Models, Molecular, Protein Conformation, Protein Interaction Domains and Motifs
Abstract: Adenoviruses are non-enveloped icosahedral viruses with trimeric fibre proteins protruding from their vertices. There are five known genera, from which only Mastadenoviruses have been widely studied. Apart from studying adenovirus as a biological model system and with a view to prevent or combat viral infection, there is a major interest in using adenovirus for vaccination, cancer therapy and gene therapy purposes. Adenoviruses from the Atadenovirus genus have been isolated from squamate reptile hosts, ruminants and birds and have a characteristic gene organization and capsid morphology. The carboxy-terminal virus-distal fibre head domains are likely responsible for primary receptor recognition. We determined the high-resolution crystal structure of the Snake Adenovirus 1 (SnAdV-1) fibre head using the multi-wavelength anomalous dispersion (MAD) method. Despite the absence of significant sequence homology, this Atadenovirus fibre head has the same beta-sandwich propeller topology as other adenovirus fibre heads. However, it is about half the size, mainly due to much shorter loops connecting the beta-strands. The detailed structure of the SnAdV-1 fibre head and other animal adenovirus fibre heads, together with the future identification of their natural receptors, may lead to the development of new strategies to target adenovirus vectors to cells of interest.
Published: 2014
Full Text: View/download PDF

Catalog

Books, media, physical & digital resources

See catalog results

Searchworks

Select search scope, currently: Articles Catalog books, media & more in Jio Institute collections Articles journal articles & other e-resources

Search

Search Constraints

Refine your results

Search Limiters

Topic

Publication Year Range

Language

Publication Type

Journal

Region

Database

Publisher

132 results on '"van Raaij MJ"'

Search Results

Catalog

Select search scope, currently: Articles

Catalog

books, media & more in Jio Institute collections

Articles

journal articles & other e-resources