1,413 results on '"Potempa, Jan"'
Search Results
102. Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus
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Burchacka, Ewa, Zdzalik, Michal, Niemczyk, Justyna-Stec, Pustelny, Katarzyna, Popowicz, Grzegorz, Wladyka, Benedykt, Dubin, Adam, Potempa, Jan, Sienczyk, Marcin, Dubin, Grzegorz, and Oleksyszyn, Jozef
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- 2014
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103. Heightened immune response to autocitrullinated Porphyromonas gingivalis peptidylarginine deiminase: a potential mechanism for breaching immunologic tolerance in rheumatoid arthritis
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Quirke, Anne-Marie, Lugli, Elena Birgitta, Wegner, Natalia, Hamilton, Bart C, Charles, Peter, Chowdhury, Muslima, Ytterberg, A Jimmy, Zubarev, Roman A, Potempa, Jan, Culshaw, Shauna, Guo, Yonghua, Fisher, Benjamin A, Thiele, Geoffrey, Mikuls, Ted R, and Venables, Patrick JW
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- 2014
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104. Carbamylation of Integrin ?IIb?3: The Mechanistic Link to Platelet Dysfunction in ESKD
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Binder, Veronika, Chru?cicka-Smaga, Barbara, Bergum, Brith, Jaisson, St?phane, Gillery, Philippe, Sivertsen, Joar, Hervig, Tor, Kaminska, Marta, Tilvawala, Ronak, Nemmara, Venkatesh V., Thompson, Paul R., Potempa, Jan, Marti, Hans-Peter, and Mydel, Piotr
- Abstract
Dialysis is lifesaving for patients with ESKD, but replaces only 10% of normal kidney function, leaving these patients with a chronic urea overload. One unavoidable consequence of excess urea is carbamylation, a post-translational modification that interferes with biologic functions of proteins. In this study, the authors found that platelets from patients with ESKD exhibit carbamylation-triggered structural alterations in integrin ?IIb?3, associated with a fibrinogen-binding defect and impaired platelet aggregation. Given that lysine 185 in the ?3subunit seems to play a pivotal role in receptor activation, carbamylation of this residue may represent a mechanistic link between uremia and dysfunctional primary hemostasis in patients. Supplementation of free amino acids prevented loss of ?IIb?3function, suggesting amino acid administration may have a beneficial effect on uremic platelet dysfunction.
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- 2022
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105. Verification of a topology model of PorT as an integral outer-membrane protein in Porphyromonas gingivalis
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Nguyen, Ky-Anh, Zylicz, Jasiek, Szczesny, Pawel, Sroka, Aneta, Hunter, Neil, and Potempa, Jan
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Anaerobic bacteria -- Research ,Membrane proteins -- Analysis ,Mutagenesis -- Research ,Gene expression -- Research ,Biological sciences - Abstract
PorT is a membrane-associated protein shown to be essential for the maturation and secretion of a class of cysteine proteinases, the gingipains, from the periodontal pathogen Porphyromonas gingivalis. It was previously reported that PorT is located on the periplasmic surface of the inner membrane to function as a chaperone for the maturing proteinases. Our modelling suggested it to be an integral outer-membrane protein with eight anti-parallel, membrane-traversing [beta]-strands. In this report, the outer-membrane localization model was confirmed by the structural and functional tolerance of PorT to hexahistidine (6xHis) tag insertions at selected locations within the protein using site-directed mutagenesis. Interestingly, those PorT mutations adversely affecting gingipain secretion enhanced expression of the porT gene but at the same time suppressed the transcription of the gingipain rgpB gene. Further, PorT mutants deficient in gingipain activities produced significantly more di- and triaminopeptidase activities. PorT homologues have been found in restricted members of the Bacteroidetes phylum where there is potential for PorT to participate in the maturation and secretion of proteins with characteristic C-terminal domains (CTDs). Knowledge of the cellular localization of PorT will enable analysis of the role of this protein in a new secretory pathway for the export of gingipains and other CTD-class proteins.
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- 2009
106. A unique bacterial secretion machinery with multiple secretion centers.
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Liqiang Song, Perpich, John D., Chenggang Wu, Doan, Thierry, Nowakowska, Zuzanna, Potempa, Jan, Christie, Peter J., Cascales, Eric, Lamont, Richard J., and Bo Hu
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SECRETION ,PORPHYROMONAS gingivalis ,ASSEMBLY machines ,PERIODONTAL disease ,PROTEIN transport - Abstract
The Porphyromonas gingivalis type IX secretion system (T9SS) promotes periodontal disease by secreting gingipains and other virulence factors. By in situ cryoelectron tomography, we report that the P. gingivalis T9SS consists of 18 PorM dimers arranged as a large, caged ring in the periplasm. Near the outer membrane, PorM dimers interact with a PorKN ring complex of ∼52 nm in diameter. PorMKN translocation complexes of a given T9SS adopt distinct conformations energized by the proton motive force, suggestive of different activation states. At the inner membrane, PorM associates with a cytoplasmic complex that exhibits 12-fold symmetry and requires both PorM and PorL for assembly. Activated motors deliver substrates across the outer membrane via one of eight Sov translocons arranged in a ring. The T9SSs are unique among known secretion systems in bacteria and eukaryotes in their assembly as supramolecular machines composed of apparently independently functioning translocation motors and export pores. [ABSTRACT FROM AUTHOR]
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- 2022
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107. Porphyromonas gingivalis HmuY and HmuR: further characterization of a novel mechanism of heme utilization
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Olczak, Teresa, Sroka, Aneta, Potempa, Jan, and Olczak, Mariusz
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- 2008
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108. Acriflavine, a clinically aproved drug, inhibits SARS-CoV-2 and other betacoronaviruses
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Napolitano, Valeria, primary, Dabrowska, Agnieszka, additional, Schorpp, Kenji, additional, Mourão, André, additional, Barreto-Duran, Emilia, additional, Benedyk, Malgorzata, additional, Botwina, Pawel, additional, Brandner, Stefanie, additional, Bostock, Mark, additional, Chykunova, Yuliya, additional, Czarna, Anna, additional, Dubin, Grzegorz, additional, Fröhlich, Tony, additional, Hoelscher, Michael, additional, Jedrysik, Malwina, additional, Matsuda, Alex, additional, Owczarek, Katarzyna, additional, Pachota, Magdalena, additional, Plettenburg, Oliver, additional, Potempa, Jan, additional, Rothenaigner, Ina, additional, Schlauderer, Florian, additional, Szczepanski, Artur, additional, Mohn, Kristin Greve-Isdahl, additional, Blomberg, Bjorn, additional, Sattler, Michael, additional, Hadian, Kamyar, additional, Popowicz, Grzegorz Maria, additional, and Pyrc, Krzysztof, additional
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- 2021
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109. Murine myeloid cell MCPIP1 suppresses autoimmunity by regulating B-cell expansion and differentiation
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Dobosz, Ewelina, primary, Lorenz, Georg, additional, Ribeiro, Andrea, additional, Würf, Vivian, additional, Wadowska, Marta, additional, Kotlinowski, Jerzy, additional, Schmaderer, Christoph, additional, Potempa, Jan, additional, Fu, Mingui, additional, Koziel, Joanna, additional, and Lech, Maciej, additional
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- 2021
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110. MCPIP-1 Restricts Inflammation via Promoting Apoptosis of Neutrophils
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Dobosz, Ewelina, primary, Wadowska, Marta, additional, Kaminska, Marta, additional, Wilamowski, Mateusz, additional, Honarpisheh, Mohsen, additional, Bryzek, Danuta, additional, Potempa, Jan, additional, Jura, Jolanta, additional, Lech, Maciej, additional, and Koziel, Joanna, additional
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- 2021
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111. PorZ, an Essential Component of the Type IX Secretion System of Porphyromonas gingivalis , Delivers Anionic Lipopolysaccharide to the PorU Sortase for Transpeptidase Processing of T9SS Cargo Proteins
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Madej, Mariusz, primary, Nowakowska, Zuzanna, additional, Ksiazek, Miroslaw, additional, Lasica, Anna M., additional, Mizgalska, Danuta, additional, Nowak, Magdalena, additional, Jacula, Anna, additional, Bzowska, Monika, additional, Scavenius, Carsten, additional, Enghild, Jan J., additional, Aduse-Opoku, Joseph, additional, Curtis, Michael A., additional, Gomis-Rüth, F. Xavier, additional, and Potempa, Jan, additional
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- 2021
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112. Mammalian-like type II glutaminyl cyclases in Porphyromonas gingivalis and other oral pathogenic bacteria as targets for treatment of periodontitis
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Taudte, Nadine, primary, Linnert, Miriam, additional, Rahfeld, Jens-Ulrich, additional, Piechotta, Anke, additional, Ramsbeck, Daniel, additional, Buchholz, Mirko, additional, Kolenko, Petr, additional, Parthier, Christoph, additional, Houston, John A., additional, Veillard, Florian, additional, Eick, Sigrun, additional, Potempa, Jan, additional, Schilling, Stephan, additional, Demuth, Hans-Ulrich, additional, and Stubbs, Milton T., additional
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- 2021
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113. Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia
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Zak, Krzysztof M., primary, Bostock, Mark J., additional, Waligorska, Irena, additional, Thøgersen, Ida B., additional, Enghild, Jan J., additional, Popowicz, Grzegorz M., additional, Grudnik, Przemyslaw, additional, Potempa, Jan, additional, and Ksiazek, Miroslaw, additional
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- 2021
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114. Additional file 2 of Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia
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Philips, Anna, Stolarek, Ireneusz, Handschuh, Luiza, Nowis, Katarzyna, Juras, Anna, Trzciński, Dawid, Nowaczewska, Wioletta, Wrzesińska, Anna, Potempa, Jan, and Figlerowicz, Marek
- Abstract
Additional file 2. Supplementary Material “Anthropological description of analyzed individuals” and Supplementary Figures.
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- 2020
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115. Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of gram-negative bacteria?
- Author
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Nguyen, Ky-Anh, Travis, James, and Potempa, Jan
- Subjects
Bacterial proteins -- Research ,Gram-negative bacteria -- Research ,Proteases -- Research ,Membrane proteins -- Research ,Biological sciences - Abstract
The mature 507-residue RgpB protein belongs to an important class of extracellular outer membraneassociated proteases, the gingipains, from the oral pathogen Porphyromonas gingivalis that has been shown to play a central role in the virulence of the organism. The C termini of these gingipains along with other outer membrane proteins from the organism share homologous sequences and have been suggested to function in attachment of these proteins to the outer membrane. In this report, we have created a series of truncated and site-directed mutants of the C terminus from a representative member of this class, the RgpB protease, to investigate its role in the maturation of these proteins. Truncation of the last two residues (valyl-lysine) from the C terminus is sufficient to create an inactive version of the protein that lacks the posttranslational glyeosylation seen in the wild type, and the protein remains trapped behind the outer membrane. Alanine scanning of the last five residues revealed the importance of the C-terminal motif in mediating correct posttranslational modification of the protein. This result may have a wider implication in a novel secretory pathway in distinct members of the Cytophaga-Flavobacterium-Bacteroidetes phylum.
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- 2007
116. Karilysin
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Potempa, Jan, primary, Gomis-Rüth, F. Xavier, additional, and Karim, Abdulkarim Y., additional
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- 2013
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117. Staphopain B
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Kantyka, Tomasz, primary, Shaw, Lindsey N., additional, and Potempa, Jan, additional
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- 2013
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118. Interpain A
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Potempa, Jan, primary and Manandhar, Surya P., additional
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- 2013
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119. Staphopain A
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Kantyka, Tomasz, primary, Shaw, Lindsey N., additional, and Potempa, Jan, additional
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- 2013
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120. Gingipain K
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Pike, Robert N., primary and Potempa, Jan, additional
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- 2013
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121. Gingipain R
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Nguyen, Ky-Anh, primary and Potempa, Jan, additional
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- 2013
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122. The IgA Protease of Clostridium ramosum
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Potempa, Jan, primary and Poulsen, Knud, additional
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- 2013
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123. Contributors
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Abbott, Catherine Anne, primary, Abraham, Carmela R., additional, Adachi, Hideki, additional, Adachi, Osao, additional, Adam, Zach, additional, Adams, Michael W.W., additional, Adang, Michael J., additional, Adham, Ibrahim M., additional, Aducci, Patrizia, additional, Agard, David A., additional, Agranovsky, Alexey A., additional, Akamatsu, Tetsuya, additional, Akiyama, Yoshinori, additional, Albrechtsen, Reidar, additional, Alejo, Alí, additional, Amberg, Sean M., additional, Amerik, Alexander Y., additional, Amparyup, Piti, additional, Andrade, Felipe, additional, Andrés, Germán, additional, Andrews, Daniel M., additional, Andrews, Robert K., additional, Antalis, Toni M., additional, Anthony, Colin S., additional, Aoki, Naoya, additional, Apte, Suneel S., additional, Arima, Kazunari, additional, Arlaud, Gérard, additional, Arni, Raghuvir Krishnaswamy, additional, Arnoux, Pascal, additional, Aronson, Nathan N., additional, Arthur, Michel, additional, Asano, Yasuhisa, additional, Ascenzi, Paolo, additional, Assakura, Marina T., additional, Auld, David S., additional, Ávila, Veridiana de Melo Rodrigues, additional, Avilés, Francesc X., additional, Awad, William M., additional, Bachhawat, Anand K., additional, Bai, Shan, additional, Baird, Teaster T., additional, Bajaj, S. Paul, additional, Baker, Susan C., additional, Banbula, Agnieszka, additional, Barrett, Alan J., additional, Barrowman, Jemima, additional, Bartlett, John D., additional, Bartsch, Jörg W., additional, Baschuk, Nikola, additional, Baskova, Isolda P., additional, Batra, Jyotsna, additional, Bauer, Karl, additional, Baumann, Ulrich, additional, Baumeister, Wolfgang, additional, Bauvois, Cédric, additional, Bayés, Alex, additional, Beauvais, Anne, additional, Becker-Pauly, Christoph, additional, Begley, Tadhg P., additional, Békés, Miklós, additional, Belas, Robert, additional, Beleford, Daniah, additional, Beppu, Teruhiko, additional, Bergmann, Ernst M., additional, Bernard, Bruno A., additional, Bernard, Dominique, additional, Berndt, Michael C., additional, Berruti, Giovanna, additional, Berry, Colin, additional, Bertenshaw, Greg P., additional, Betzel, Christian, additional, Bhaskarla, Chetana, additional, Bhosale, Manoj, additional, Bierbaum, Gabriele, additional, Bjarnason Jón, B., additional, Blaber, Michael, additional, Blackman, Michael J., additional, Blinkovsky, Alexander, additional, Boeke, Jef D., additional, Bogyo, Matthew, additional, Bohn, Stefan, additional, Boileau, Guy, additional, Boland, Mike, additional, Bolken, Tové C., additional, Bond, Judith S., additional, Bondeson, Jan, additional, Bordallo, Javier, additional, Borelli, Claudia, additional, Botelho, Tiago O., additional, Bott, Richard R., additional, Bourne, David G., additional, Bovenschen, Niels, additional, Bradshaw, Ralph A., additional, Breddam, Klaus, additional, Brew, Keith, additional, Brindley, Paul J., additional, Brinkman, Diane L., additional, Britton, Collette, additional, Broadbent, Jeff R., additional, Broadhurst, Anne, additional, Brómme, Dieter, additional, Broom, Murray, additional, Brown, Jeremy S., additional, Brown, Mark A., additional, Bruchhaus, Iris, additional, Burleigh, Barbara A., additional, Burns, Kristin E., additional, Burrows, James F., additional, Butler, Michael J., additional, Buttle, David J., additional, Byrd, Chelsea M., additional, Byun, Tony, additional, Cadel, Sandrine, additional, Caffrey, Conor R., additional, Cal, Santiago, additional, Caldentey, Javier, additional, Candela, Thomas, additional, Capasso, Clemente, additional, Capriogilio, Daniel R., additional, Carginale, Vincenzo, additional, Carmona, Adriana Karaoglanovic, additional, Carruthers, Vern B., additional, Castellino, Francis J., additional, Catanese, Joseph J., additional, Caterson, Bruce, additional, Caughey, George H., additional, Cawley, Naimh X., additional, Cawston, Tim E., additional, Cazzulo, Juan José, additional, Chai, Jijie, additional, Chai, Karl X., additional, Chaim, Olga Meiri, additional, Chang, L.S., additional, Chao, Julie, additional, Chapot-Chartier, Marie-Pierre, additional, Charli, Jean-Louis, additional, Charlier, Paulette, additional, Chave, Karen J., additional, Chen, Jian-Min, additional, Chen, Jinq-May, additional, Chen, Li-Mei, additional, Chen, Ya-Wen, additional, Chen, Yu-Yen, additional, Chevrier, Bernard, additional, Chich, Jean-François, additional, Chien, Jeremy, additional, Chimalapati, Suneeta, additional, Cho, Ki Joon, additional, Choi, Kwan Yong, additional, Chuang, Woei-Jer, additional, Chung, Chin Ha, additional, Chung, Ivy Yeuk Wah, additional, Clamagirand, Christine, additional, Clark, Ian M., additional, Clarke, Adrian K., additional, Clarke, Nicola E., additional, Clarke, Steven Gerard, additional, Clauziat, Philippe, additional, Clements, Judith A., additional, Coffinier, Catherine, additional, Cohen, Paul, additional, Colige, Alain, additional, Collignon, Anne, additional, Colloms, Sean D., additional, Conzelmann, Andreas, additional, Coombs, Graham H., additional, Cooney, Jakki C., additional, Cooper, Jonathan B., additional, Cooper, Max D., additional, Copeland, Nikki A., additional, Cottrell, Graeme S., additional, Coyle, Joseph T., additional, Craik, Charles S., additional, Creemers, John W.M., additional, Cretu, Daniela, additional, Croce, Jenifer, additional, Cross, Keith J., additional, Cueva, Rosario, additional, Cui, Sheng, additional, Cunha, Luis, additional, Cutting, Simon, additional, d’Enfert, Christophe, additional, D’Orchymont, Hugues, additional, Dahlbäck, Björn, additional, Dai, Shujia, additional, Dalbey, Ross E., additional, Dalton, John P., additional, Dando, Pam M., additional, Daniel, R.M., additional, Danilov, Sergei M., additional, Davies, Donna E., additional, De Araujo, Heloisa S., additional, De los Santos, Teresa, additional, de Luca, Viviana, additional, De Meester, Ingrid, additional, de Oliveira, Ana Karina, additional, de Oliveira, Eduardo Brandt, additional, De Oliveira, Pedro Lagerblad, additional, de Vos, Sarah, additional, Declercq, Jeroen, additional, Declercq, Wim, additional, Deghmane, Ala-Eddine, additional, Dekker, Niek, additional, Del Prete, Sonia, additional, Del Rosal, Marina, additional, Delmas, Bernard, additional, DeLotto, Robert, additional, Demidyuk, Ilya V., additional, Denison, Mark R., additional, Deussing, Jan M., additional, Devi, Lakshmi A., additional, Diamandis, Eleftherios P., additional, Diaz, Isabel, additional, Díaz-Perales, Araceli, additional, Dijkstra, Bauke W., additional, Ding, Yan, additional, Dixon, Jack E., additional, Dodt, Johannes, additional, Dokland, Terje, additional, Dolenc, Iztok, additional, Dong, Ningzheng, additional, Dong, Tran Cat, additional, Dong, Ying, additional, Dongre, Mitesh, additional, Donovan, Mark, additional, Dore, Timothy M., additional, Dorstyn, Loretta, additional, Dou, Hong, additional, Dou, Zhicheng, additional, Dougall, Annette M., additional, Drag, Marcin, additional, Dudley, Edward G., additional, Dunn, Ben M., additional, Dupuy, Bruno, additional, Duque-Magalhāes, Maria Conceicāo, additional, Durá, M. Asunción, additional, Eeckhout, Yves, additional, Eijsink, Vincent, additional, Eisen, Arthur Z., additional, Eissa, Azza, additional, Eklund, Sandra, additional, Eletr, Ziad M., additional, Ellis, Vincent, additional, Engel, Wolfgang, additional, Erdös, Ervin G., additional, Escalante, Teresa, additional, Estell, David A., additional, Etscheid, Michael, additional, Evans, Herbert J., additional, Everett, Roger D., additional, Faesen, Alex C., additional, Fahrenholz, Falk, additional, Fanjul-Fernández, Miriam, additional, Farady, Christopher J., additional, Feller, Georges, additional, Feng, Hong, additional, Fenster, Kurt M., additional, Férec, Claude, additional, Ferrari, Silvia, additional, Fingleton, Barbara, additional, Fisher, Jed F., additional, Fives-Taylor, Paula M., additional, Fong, Loren G., additional, Forneris, F., additional, Forster, Brian M., additional, Forster, Friedrich, additional, Foster, Simon J., additional, Foulon, Thierry, additional, Foundling, Stephen I., additional, Fox, Jay William, additional, Franzetti, Bruno, additional, Frasch, Alejandra P., additional, Freeze, Hudson H., additional, Frère, Jean-Marie, additional, Frey, Teryl K., additional, Fricke, Beate, additional, Fricker, Lloyd D., additional, Fridman, Rafael, additional, Froelich, Christopher J., additional, Fröhlich, Camilla, additional, Fu, Hsueh-Liang, additional, Fuhrmann, Cynthia N., additional, Fujimura, Satoshi, additional, Fujiwara, Hiroshi, additional, Fukushima, Jun, additional, Fukuyama, Keiichi, additional, Fuller, Robert S., additional, Fusek, Martin, additional, Gaboriaud, Christine, additional, Gache, Christian, additional, Gakh, Oleksandr, additional, Gal, Peter, additional, Gao, Junjun, additional, García-Sastre, Adolfo, additional, Gardiner, Donald L., additional, Gatehouse, John A., additional, Gaucher, G.M., additional, Gauthier, Francis, additional, Ghuysen, Jean-Marie, additional, Gibson, Wade, additional, Gillies, Jennifer, additional, Glaser, Elzbieta, additional, Glaser, Fabian, additional, Glickman, Michael H., additional, Goettig, Peter, additional, Goffin, Colette, additional, Gohda, Eiichi, additional, Goldberg, Alfred L., additional, Goldberg, Daniel E., additional, Goldberg, Gregory I., additional, Goldfarb, Nathan E., additional, Gomis-Rüth, F. Xavier, additional, Gopal, B., additional, Gorbalenya, Alexander E., additional, Gordon, Stuart G., additional, Gorrell, Mark D., additional, Götz, Friedrich, additional, Goulas, Theodoros, additional, Gouzy-Darmon, Cécile, additional, Govind, K., additional, Gráf, Lászlo, additional, Granados, Robert R., additional, Gräwert, Melissa Ann, additional, Gray, Douglas A., additional, Graycar, Thomas P., additional, Green, Jonathan A., additional, Gremski, Luiza Helena, additional, Groll, Michael, additional, Gromova, Tania Yu, additional, Gros, P., additional, Grubman, Marvin J., additional, Grunden, Amy M., additional, Gudmundsdóttir, Ágústa, additional, Guinand, Micheline, additional, Gully, Djamel, additional, Gustchina, Alla, additional, Gutiérrez, José María, additional, Ha, Byung Hak, additional, Haeggström, Jesper Z., additional, Hageman, James H., additional, Haiko, Johanna, additional, Hailfinger, Stephan, additional, Haitchi, Hans Michael, additional, Han, Ji Seon, additional, Hanquez, Chantal, additional, Harada, Minoru, additional, Hara-Nishimura, Ikuko, additional, Harboe, Marianne, additional, Härd, Torleif, additional, Harris, David A., additional, Hassiepen, Ulrich, additional, Hata, Shoji, additional, Hattori, Akira, additional, He, Rong-Qiao, additional, Heck, Albert J.R., additional, Hendricks, Dirk F., additional, Henrich, Bernhard, additional, Henriet, Patrick, additional, Hernández-Arana, Andrés, additional, Herrera-Camacho, Irma, additional, Heussipp, Gerhard, additional, Hibino, Toshihiko, additional, Hicks, P.M., additional, Hillman, Bradley I., additional, Hiraoka, B. Yukihiro, additional, Hiratake, Jun, additional, Hizukuri, Yohei, additional, Ho, Heng-Chien, additional, Hoa, Ngo Thi, additional, Hochstrasser, Mark, additional, Hodge, Kathryn M., additional, Hofmann, Theo, additional, Hohn, Thomas, additional, Hoidal, John R., additional, Höltje, Joachim-Volker, additional, Homma, Koichi J., additional, Honek, John F., additional, Hook, Vivian Y.H., additional, Hooper, John D., additional, Hooper, Nigel M., additional, Hosoi, Kazuo, additional, Howe, Christopher J., additional, Hruby, Dennis E., additional, Hseih, James J.-D., additional, Hsu, Chun-Chieh, additional, Huang, Tony T., additional, Huang, Tur-Fu, additional, Huet, Yoann, additional, Hughes, Clare, additional, Hugonnet, Jean-Emmanuel, additional, Huston, Adrienne L., additional, Ibrahim-Granet, Oumaïma, additional, Ichishima, Eiji, additional, Ikehara, Yukio, additional, Inagami, Tadashi, additional, Ingram, Jessica, additional, Isaac, R.E., additional, Isaya, Grazia, additional, Isaza, Clara E., additional, Ishii, Shin-ichi, additional, Isnard, Amandine, additional, Ito, Kiyoshi, additional, Ito, Koreaki, additional, Itoh, Yoshifumi, additional, Iturrioz, Xavier, additional, Iwanaga, Sadaaki, additional, Jack, Ralph W., additional, Jackson, Mel C., additional, James, Michael N.G., additional, Janata, Jiří, additional, Janoir, Claire, additional, Janska, Hanna, additional, Jarrell, Ken F., additional, Jaskolski, Mariusz, additional, Jaswal, Sheila S., additional, Jean, Ying Y., additional, Jenne, Dieter E., additional, Jeon, Young Joo, additional, Jiang, Ping, additional, Johnson, John E., additional, Johnson, Michael D., additional, Johnston, James A., additional, Jones, Amanda, additional, Jones, Elizabeth W., additional, Joudiou, Carine, additional, Juliano, Luiz, additional, Jung, Hea-Jin, additional, Jupp, Ray, additional, Kagawa, Todd F., additional, Kalbacher, Hubert, additional, Kamata, Yayoi, additional, Kaminogawa, Shuichi, additional, Kamio, Yoshiyuki, additional, Kaneda, Makoto, additional, Kang, Sung Gyun, additional, Kang, Sung Hwan, additional, Kania, Mary, additional, Kantyka, Tomasz, additional, Kanzawa, Nobuyuki, additional, Karim, Abdulkarim Y., additional, Kasumi, Takafumi, additional, Kataoka, Hiroaki, additional, Kaur, Hardeep, additional, Kawabata, Shun-Ichiro, additional, Kawaguchi, Mari, additional, Kay, John, additional, Kaynar, Murat, additional, Keiler, Kenneth C., additional, Kelly, R.M., additional, Kenton, Nathaniel T., additional, Kerr, Michael A., additional, Kersse, Kristof, additional, Kervinen, Jukka, additional, Kessler, Benedikt M., additional, Kessler, Efrat, additional, Khoronen, Timo K., additional, Kidd, Simon, additional, Kikkert, Marjolein, additional, Kilian, Mogens, additional, Kim, Do-Hyung, additional, Kim, Doyoun, additional, Kim, Eunice EunKyeong, additional, Kim, In Seop, additional, Kim, Jung-Gun, additional, Kim, Kyeong Kyu, additional, Kim, Kyung Hyun, additional, Kimber, Matthew S., additional, Kimura, Yukio, additional, Kirschke, Heidrun, additional, Kiso, Yoshiaki, additional, Kleanthous, Colin, additional, Klein, Jürgen R., additional, Klemba, Michael, additional, Kmiec, Beata, additional, Kobayashi, Hideyuki, additional, Kodama, Hiroyuki, additional, Koelsch, Gerald, additional, Kok, Jan, additional, Kolattukody, P.E., additional, Kolb, Fabrice A., additional, Kolmar, Harald, additional, Komori, Yumiko, additional, Konvalinka, Jan, additional, Korkmaz, Brice, additional, Kostrov, Sergey V., additional, Kräusslich, Hans-Georg, additional, Krczal, Gabi, additional, Kress, Lawrence F., additional, Kristjánsson, Magnüs Már, additional, Kučera, Tomáš, additional, Kukday, Sayali S., additional, Kumagai, Hidehiko, additional, Kumar, Sharad, additional, Kumarasiri, Malika, additional, Kumazaki, Takashi, additional, Kümmerer, Beate M., additional, Kuno, Kouji, additional, Kurkinen, Markku, additional, Kutejová, Eva, additional, Kveiborg, Marie, additional, Kwarciak, Agnieszka, additional, Laakkonen, Liisa, additional, Labrou, Nikolaos E., additional, Laing, Gavin D., additional, Lamppa, Gayle, additional, Langer, Thomas, additional, Laursen, Richard A., additional, Lawrenson, Richard A., additional, Layne, Matthew D., additional, Le Bonniec, Bernard F., additional, Leal, María C., additional, Lechan, Ronald M., additional, Lee, David H., additional, Lee, Irene, additional, Lee, Jae, additional, Lee, Kye Joon, additional, Lee, Soohee, additional, Lei, Xiaobo, additional, Leis, Jonathan, additional, LeMosy, Ellen K., additional, Lepage, Thierry, additional, Leppla, Stephen H., additional, Lesner, Adam, additional, Lessard, Ivan A.D., additional, Lhomond, Guy, additional, Li, Huilin, additional, Li, Shu-Ming, additional, Li, Weiguo, additional, Liao, Ta-Hsiu, additional, Liddington, Robert C., additional, Lieber, Toby, additional, Lijnen, H.R., additional, Lima, Christopher D., additional, Lin, Chen-Yong, additional, Lin, Gang, additional, Lin, Ming T., additional, Lin, Xinli, additional, Lin, Yee-Shin, additional, Lindsay, L.L., additional, Lipscomb, William N., additional, Little, John W., additional, Liu, Ching-Chuan, additional, Liu, Chuan-ju, additional, Lively, Mark O., additional, Livnat-Levanon, Nurit, additional, Ljungdahl, Per O., additional, Llorens-Cortes, Catherine, additional, Lobel, Peter, additional, Loh, Y. Peng, additional, Lohi, Jouko, additional, Lomonossoff, G.P., additional, Looze, Yvan, additional, López-Otin, Carlos, additional, Lopez-Quezada, Landys, additional, Loukas, Alex, additional, Lu, Long-Sheng, additional, Lundwall, Áke, additional, Luo, Liu-Ying, additional, Lupas, Andrei, additional, Luthe, Dawn S., additional, Lynch, Nicholas J., additional, Lyons, Peter J., additional, MacKay, Vivian L., additional, Macleod, Jesica M. Levingston, additional, Magdolen, Viktor, additional, Mainardi, Jean-Luc, additional, Mäkinen, Kauko K., additional, Mallari, Jeremy P., additional, Manandhar, Surya P., additional, Mandelbaum, Fajga R., additional, Manicone, Anne M., additional, Mansfeld, Johanna, additional, Marcotrigiano, Joseph, additional, Mares, Michael, additional, Marfany, Gemma, additional, Markland, Francis S., additional, Marokházi, Judith, additional, Marquis, Hélène, additional, Marr, Robert A., additional, Martegani, Enzo, additional, Martin, Erik W., additional, Martinez, Manuel, additional, Martins, L. Miguel, additional, Maruyama, Masato, additional, Maruyama, Masugi, additional, Maruyama, Sususmu, additional, Masaki, Takeharu, additional, Massoumi, Ramin, additional, Mathew, Rency T., additional, Matrisian, Lynn M., additional, Matsuda, Yoshihiro, additional, Matsushita, Osamu, additional, Matuschek, Marco, additional, Matušková, Anna, additional, Matúz, Krisztina, additional, Mauch, Cornelia, additional, Maurizi, Michael R., additional, Mayr, Lorenz M., additional, McCafferty, Dewey G., additional, McDonald, J. Ken, additional, McKerrow, James H., additional, McMillan, David, additional, Mecham, Robert P., additional, Mehta, Darshini P., additional, Meisinger, Chris, additional, Mellors, Alan, additional, Melton, Roger G., additional, Melvin, Jeffrey A., additional, Ménard, Robert, additional, Menéndez-Arias, Luis, additional, Menezes, Milene C., additional, Mesecar, Andrew, additional, Mesnage, Stéphane, additional, Meyer, Diane H., additional, Meyers, Gregor, additional, Michaelis, Susan, additional, Michalska, Karolina, additional, Mielicki, Wojciech P., additional, Mierau, Igor, additional, Mikoulinskaia, Galina V., additional, Miller, Charles G., additional, Miller, Lydia K., additional, Mills, John, additional, Mills, Kenneth V., additional, Min, Jinrong, additional, Mistou, Michel-Yves, additional, Misumi, Yoshio, additional, Miyoshi, Shin-ichi, additional, Mizutani, Shigehiko, additional, Mobashery, Shahriar, additional, Mochizuki, Satsuki, additional, Mock, William L., additional, Möhrlen, Frank, additional, Moiré, Nathalie, additional, Monahan, Paul E., additional, Moncada-Pazos, Angela, additional, Monnet, Véronique, additional, Monod, Michel, additional, Montecucco, Cesare, additional, Morelli, Laura, additional, Mori, Sumiko, additional, Morita, Takashi, additional, Morrissey, James H., additional, Morse, Richard J., additional, Mort, John S., additional, Mortensen, Uffe H., additional, Morty, Rory E., additional, Moss, Joel, additional, Motoshima, Hidemasa, additional, Mottram, Jeremy C., additional, Moura-da-Silva, Ana M., additional, Mudgett, Mary Beth, additional, Mundt, Egbert, additional, Murakami, Kazuo, additional, Murakami, Mario Tyago, additional, MurakamiMurofoshi, Kimiko, additional, Murao, Sawao, additional, Murphy, Gillian, additional, Murthy, M.R.N., additional, Muta, Tatsushi, additional, Myburgh, Elmarie, additional, Mzhavia, Nino, additional, Nabi, A.H.M. Nurun, additional, Nagase, Hideaki, additional, Nagle, Michael W., additional, Nägler, Dorit K., additional, Naik, Rajesh R., additional, Nair, Divya B., additional, Nakai, Toshiki, additional, Nakajima, Yoshitaka, additional, Nakamura, Yukio, additional, Nakatogawa, Hitoshi, additional, Nakayama, Toru, additional, Nalivaeva, Natalia N., additional, Nandi, Dipankar, additional, Nascimento-Silva, Maria Clara Leal, additional, Nasmyth, Kim, additional, Nathan, Carl F., additional, Navarro-García, Fernando, additional, Naves, Dayane Lorena, additional, Nedialkova, Danny D., additional, Neuman, Keir C., additional, Nguyen, Jeffrey-Tri, additional, Nguyen, Ky-Anh, additional, Niemirowicz, Gabriela T., additional, Nikai, Toshiaki, additional, Nishi, Eiichiro, additional, Nishii, Wataru, additional, Nishiyama, Makoto, additional, Nishiyama, Yasuhiro, additional, Noda, Masatoshi, additional, Nomura, Seiji, additional, Norioka, Shigemi, additional, Nsangou, Desire M.M., additional, O’Brien, Amornrat, additional, O’Connor, Michael B., additional, Oda, Kohei, additional, Odinokova, Irina V., additional, Oetjen, Joyce, additional, Ogura, Teru, additional, Ohman, Dennis E, additional, Ohsumi, Yoshinori, additional, Ojha, Mukti, additional, Okabe, Akinobu, additional, Okada, Yasunori, additional, Okamoto, Keinosuke, additional, Okuda, Kenji, additional, Okumura, Nobuaki, additional, Okuno, Takashi, additional, Oleson, Kjeld, additional, Oliveira de Giuseppe, Priscila, additional, Olivier, Martin, additional, Ono, Yasuko, additional, Oroszlan, Stephen, additional, Ota, Nobuyuki, additional, Ovadia, Michael, additional, O-Wang, Jiyang, additional, Oxvig, Claus, additional, Packer, Jeremy C.L., additional, Padilla-López, Sergio, additional, Paetzel, Mark, additional, Page, Michael J., additional, Page-McCaw, Andrea, additional, Paine, Mark J.I., additional, Park, Byoung Chul, additional, Park, Eunyong, additional, Park, John E., additional, Park, Pyong Woo, additional, Park, Sung Goo, additional, Parkin, Kirk L., additional, Parks, William C, additional, Paschoalin, Thaysa, additional, Pastore, Annalisa, additional, Patananan, Alexander Nikolich, additional, Paul, Sudhir, additional, Paulson, Henry L., additional, Pawel-Rammingen, Ulrich von, additional, Pearce, David A., additional, Pearson, Mark S., additional, Pei, Duanqing, additional, Pejler, Gunnar, additional, Pemberton, Alan D., additional, Peng, Jianhao, additional, Pernier, Julien, additional, Peters, Jan-Michael, additional, Pfirrmann, Thorsten, additional, Pham, Viet-Laï, additional, Pichová, Iva, additional, Pickering, Darren, additional, Piesse, Christophe, additional, Pignol, David, additional, Pike, Robert N., additional, Pinck, Lothaire, additional, Pirkle, Hubert, additional, Pitot, Henry C., additional, Plaut, Andrew G., additional, Ploegh, Hidde, additional, Polgár, László, additional, Porter, Corrine, additional, Postina, Rolf, additional, Potempa, Jan, additional, Poulsen, Knud, additional, Power, Scott D., additional, Pratt, Rex. F., additional, Prehna, Gerd, additional, Prévost, Gilles, additional, Pshezhetsky, Alexey V., additional, Qasim, Mohammad A., additional, Qian, Feng, additional, Qiu, Jiazhou, additional, Quesada, Víctor, additional, Radisky, Evette S., additional, Rader, Stephen D., additional, Raman, Kavita, additional, Ramsay, Andrew J., additional, Rancourt, Derrick E., additional, Ranjit, Najju, additional, Rao, Narayanam V., additional, Ratia, Kiira, additional, Rawlings, Neil D., additional, Rawson, Robert B., additional, Reddy, Vijay, additional, Redman, Colvin M., additional, Regonesi, Maria Elena, additional, Reichert, Andreas S., additional, Reichl, Antonia P., additional, Remaut, Han, additional, Remington, S. James, additional, Renatus, Martin, additional, Reverter, David, additional, Reynolds, Eric C., additional, Rholam, Mohamed, additional, Rice, Charles M., additional, Ridky, Todd W., additional, Riezman, Howard, additional, Rijken, D.C., additional, Rio, Marie-Christine, additional, Ritchie, Alison, additional, Robert-Baudouy, Janine, additional, Robinson, Mark W., additional, Robinson, Michael, additional, Rodriguez-Romero, Adela, additional, Rodriques, Renata Santos, additional, Rogers, John C., additional, Rojas, Camilo, additional, Romesberg, Floyd E., additional, Roper, David J., additional, Rosas-Murrieta, Nora, additional, Rose, A.M., additional, Rosenthal, Philip J., additional, Rosing, J., additional, Rossetto, Ornella, additional, Rossi, Véronique, additional, Roth, Richard A., additional, Rottensteiner, Hanspeter, additional, Rowan, Andrew D., additional, Rozanov, Mikhail, additional, Rucavado, Alexandra, additional, Ruecker, Andrea, additional, Rul, Françoise, additional, Rümenapf, Till, additional, Russo, Ilaria, additional, Ryan, Martin D., additional, Sacco, Elena, additional, Sadler, J. Evan, additional, Saenger, W., additional, Sahl, Hans-Georg, additional, Sajid, Mohammed, additional, Sakaguchi, Masayoshi, additional, Sakiyama, Fumio, additional, Salas, Maria L., additional, Salgado, Maria Cristina O., additional, Salvesen, Guy S., additional, Sánchez, Edith, additional, Sanchez, Eladio F., additional, Sang, Qing-Xiang Amy, additional, Sankaran, Krishnan, additional, Sarkar, Susanta K., additional, Sarras, Michael P., additional, Sasagawa, Yoshikiyo, additional, Satohiko, Araki, additional, Sauvage, Eric, additional, Saveanu, Loredana, additional, Savithri, H.S., additional, Sawada, Hitoshi, additional, Sawers, R. Gary, additional, Scarisbrick, Isobel A., additional, Schaller, Andreas, additional, Scheer, Justin M., additional, Scheiflinger, Friedrich, additional, Schiene-Fischer, Cordelia, additional, Schlomann, Uwe, additional, Schlösser, Manfred, additional, Schmaier, Alvin H., additional, Schmidt, Walter K., additional, Schneemann, Anette, additional, Schnellmann, Rick G., additional, Scholze, Henning, additional, Schomburg, Lutz, additional, Schwaeble, Wilhelm J., additional, Scott, Christopher J., additional, Scudiero, Rosaria, additional, Sehara-Fujisawa, Atsuko, additional, Seidah, Nabil G., additional, Seiki, Motoharu, additional, Sekiguchi, Junichi, additional, Senff-Ribeiro, Andrea, additional, Seong, Ihn Sik, additional, Serpe, Mihaela, additional, Serrano, Solange M.T., additional, Setlow, Peter, additional, Shahian, Tina, additional, Shanks, M., additional, Shao, Feng, additional, Shapiro, Steven D., additional, Sharma, Navneet, additional, Shaw, Lindsey N., additional, Shen, Aimee, additional, Shen, Lei, additional, Sherwood, Roger F., additional, Shi, Yun-Bo, additional, Shimoi, Hitoshi, additional, Shimura, Yoichiro, additional, Shirras, A.D., additional, Shridhar, Viji, additional, Shukla, Jinal K., additional, Siigur, Ene, additional, Siigur, Jüri, additional, Silmon de Monerri, Natalie C., additional, Sim, Robert B., additional, Simmer, James P., additional, Simmons, William H., additional, Singh, Jaspreet, additional, Singleton, Alison, additional, Sirakova, Tatiana D., additional, Sixma, Titia K., additional, Skern, Tim, additional, Skidgel, Randal A., additional, Slack, Jeffrey, additional, Sleat, David E., additional, Slusher, Barbara S., additional, Smith, Janet L., additional, Smith, Matthew A., additional, Smyth, Mark J., additional, Snijder, Erik J., additional, Sobhanifar, Solmaz, additional, Söderhaäll, Kenneth, additional, Sohar, Istvan, additional, Sonderegger, Peter, additional, Sorgine, Marcos Henrique Ferreira, additional, Sorimachi, Hiroyuki, additional, Soukhodolets, Karen E., additional, Souza, Tatiana de Arruda Campos Brasil de, additional, Sperka, Tamás, additional, Sriskandan, Shiranee, additional, St. Geme, Joseph W., additional, St. Leger, Raymond J., additional, Staib, Peter, additional, Steele, James L., additional, Stefansson, Bjarki, additional, Steinkühler, Christian, additional, Stenberg, Leisa M., additional, Stenflo, Johan, additional, Stennicke, Henning R., additional, Stepanov, Valentin M., additional, Stepnaya, Olga A., additional, Steven, Frank, additional, Stevens, Richard L., additional, Stevenson, Kenneth J., additional, St-Louis, Mathieu, additional, Stobart, Christopher C., additional, Stöcker, Walter, additional, Storer, Andrew C., additional, Sträter, Norbert, additional, Strauss, Ellen G., additional, Strauss, James H., additional, Stříšovský, Kvido, additional, Strynadka, Natalie C.J., additional, Sturrock, Edward D., additional, Su, Dan, additional, Su, Xiao-Dong, additional, Suárez-Rendueles, Paz, additional, Sulea, Traian, additional, Sundararajan, Venkatesh, additional, Suno, Ryoji, additional, Suzuki, Carolyn K., additional, Suzuki, Fumiaki, additional, Suzuki, Hideyuki, additional, Suzuki, Nobuhiro, additional, Swenson, Stephen, additional, Szabady, Rose L., additional, Szecsi, Pal Bela, additional, Szilágyi, Lászlo, additional, Taha, Muhamed-Kheir, additional, Takahashi, Eizo, additional, Takahashi, Kenji, additional, Takai, Toshiro, additional, Takeda, Atsushi, additional, Takeda, Soichi, additional, Tame, Jeremy J.R.H., additional, Tamura, Tomohiro, additional, Tan, Fulong, additional, Tanaka, Keiji, additional, Tanase, Carmen, additional, Tang, Jordan, additional, Tanizaki, Martha M., additional, Tannich, Egbert, additional, Tans, Guido, additional, Tarentino, Anthony L., additional, Tassanakajon, Anchalee, additional, Tatsumi, Hiroki, additional, Tautz, Norbert, additional, Taylor, Erin Bassford, additional, Teixeira, Pedro Filipe, additional, Telugu, Bhanu Prakash V.L., additional, Templin, Markus F., additional, Terada, Shigeyuki, additional, Tetsuya, Uchikoba, additional, Thacker, C., additional, Thaker, Maulik, additional, Thiel, Heinz-Jürgen, additional, Thielens, Nicole, additional, Thierry, Gonzales, additional, Thivierge, Karine, additional, Thomas, Mark D., additional, Thome, Margot, additional, Thorsness, Mary K., additional, Thorsness, Peter E., additional, Tigue, Natalie J., additional, Todi, Sokol V., additional, Tomkinson, Birgitta, additional, Tonello, Fiorella, additional, Tong, Liang, additional, Toogood, H.S., additional, Tortora, Paolo, additional, Tözsèr, József, additional, Travassos, Luiz Rodolpho, additional, Travis, James, additional, Trevisan-Silva, Dilza, additional, Trinchella, Francesca, additional, Trivedi, Neil N., additional, Troy, Carol M., additional, Tschesche, Harald, additional, Tseng, Yu-Lun, additional, Tsujimoto, Masafumi, additional, Tu, Anthony T., additional, Tumelty, Kathleen E., additional, Turk, Boris, additional, Turk, Dusan, additional, Turk, Vito, additional, Turner, Anthony J., additional, Uchikoba, Tetsuya, additional, Ueno, Takayuki, additional, Ugalde, Alejandro P., additional, Uitto, Veli-Jukka, additional, Urban, Sinisa, additional, Valdenaire, Olivier, additional, Valli, Adrian, additional, Van Beeumen, Jozef, additional, Van den Burg, Bertus, additional, Van der Hoorn, Renier A.L., additional, van Dijl, Jan Maarten, additional, Van Endert, Peter, additional, Van Raam, Bram J., additional, Van Wart, Harold E., additional, Vanden Berghe, Tom, additional, Vandenabeele, Peter, additional, Vanoni, Margo, additional, Veiga, Silvio Sanches, additional, Velander, William H., additional, Velasco, Gloria, additional, Vendrell, Josep, additional, Venekei, I. István, additional, Vetvicka, Vaclav, additional, Vögtle, F.-Nora, additional, Vollmer, Waldemar, additional, Wada, Kei, additional, Wagner, Fred W., additional, Wai, Sun Nyunt, additional, Wai, Timothy, additional, Wainwright, Shane, additional, Walker, Kenneth W., additional, Walker, Stephen J., additional, Wallach, Jean, additional, Walling, Linda L., additional, Walsh, Peter N., additional, Wang, Hai-Yan, additional, Wang, Hengbin, additional, Wang, Jianwei, additional, Wang, Peng, additional, Wang, Ping, additional, Wassenegger, Michael, additional, Watanabe, Kunihiko, additional, Webb, Helen, additional, Weber, Joseph M., additional, Weber, Niklas, additional, Webster, Daniel R., additional, Wei, Shuo, additional, Welch, Rodney A., additional, Wells, James A., additional, Wenzel, Herbert, additional, Wertz, Ingrid E., additional, Wewer, Ulla W., additional, Whyteside, Alison R., additional, Wilk, Sherwin, additional, Wilkin, Jean-Marc, additional, Wilmes, Claudia, additional, Winther, Jakob R., additional, Wishart, David S., additional, Wlodawer, Alexander, additional, Woessner, J. Fred, additional, Wolfe, Michael S., additional, Wong, Wilson, additional, Woodgate, Roger, additional, Wright, Gerry, additional, Wu, Jiunn-Jong, additional, Wu, Qingyu, additional, Wysocka, Magdalena, additional, Xu, Chao, additional, Xu, Zhenghong, additional, Yahori, Kinnosuke, additional, Yamada, Shoji, additional, Yamaguchi, Nozomi, additional, Yamaguchi, Shinji, additional, Yamakawa, Yoshio, additional, Yamamoto, Hiroki, additional, Yana, Ikao, additional, Yang, Maozhou, additional, Yang, Na, additional, Yao, Chenjuan, additional, Yao, Tingting, additional, Yasuda, Noriko, additional, Yasuhara, Toshimasa, additional, Yasumasu, Shigeki, additional, Yeh, Edward T.H., additional, Yiallouros, Irene, additional, Yin, Jiang, additional, Yonezawa, Hiroo, additional, Yoo, Soon Ji, additional, Yoshimoto, Tadashi, additional, Young, Michael W., additional, Young, Stephen G., additional, Zaidi, Nousheen, additional, Zavalova, Ludmila L., additional, Zavodszky, Peter, additional, Zhang, Aidong, additional, Zhang, Xianming, additional, Zhang, Yi-Zheng, additional, Zheng, Dominick, additional, Zhong, Guangming, additional, Zhong, Rong, additional, Zhou, Yuan, additional, Zhou, Zhaohui Sunny, additional, Zick, Michael, additional, Zigrino, Paola, additional, and Zimin, Andrei A., additional
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- 2013
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124. Dipeptidyl-Peptidase 7 of Porphyromonas gingivalis
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Potempa, Jan, primary, Banbula, Agnieszka, additional, and Travis, James, additional
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- 2013
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125. Aureolysin
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Potempa, Jan, primary and Shaw, Lindsey N., additional
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- 2013
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126. Investigations into [[sigma].sup.B]-modulated regulatory pathways governing extracellular virulence determinant production in Staphylococcus aureus
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Shaw, Lindsey N., Aish, Joanne, Davenport, Jessica E., Brown, Melanie C., Lithgow, James K., Simmonite, Kay, Crossley, Howard, Travis, James, Potempa, Jan, and Foster, Simon J.
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Staphylococcus aureus -- Physiological aspects ,Staphylococcus aureus -- Genetic aspects ,Chromosome deletion -- Research ,Genetic research ,Biological sciences - Abstract
The commonly used Staphylococcus aureus laboratory strain 8325-4 bears a naturally occurring 11-bp deletion in the [[sigma].sup.B]-regulating phosphatase rsbU. We have previously published a report (M. J. Horsburgh, J. L. Aish, I. J. White, L. Shaw, J. K. Lithgow, and S. J. Foster, J. Bacteriol. 184:5457-5467, 2002) on restoring the rsbU deletion, producing a [[sigma].sup.B]-functional 8325-4 derivative, SH1000. SH1000 is pleiotropically altered in phenotype from 8325-4, displaying enhanced pigmentation, increased growth yields, and a marked decrease in secreted exoproteins. This reduction in exoprotein secretion appears to result from a sixfold reduction in agr expression. In this study we have undertaken transposon mutagenesis of SH1000 to identify components involved in the modulation of extracellular proteases and [alpha]-hemolysin compared to 8325-4. In total, 13 genes were identified displaying increased [alpha]-hemolysin transcription and extracellular proteolysis. Phenotypic analysis revealed that each mutant also had decreased pigmentation and a general increase in protein secretion. Interestingly this phenotype was not identical in each case but was variable from mutant to mutant. None of the genes identified encoded classic regulatory proteins but were predominantly metabolic enzymes involved in amino acid biosynthesis and transport. Further analysis revealed that all of these mutations were clustered in a 35-kb region of the chromosome. By complementation and genetic manipulation we were able to demonstrate the validity of these mutations. Interestingly transcriptional analysis revealed that rather than being regulated by [[sigma].sup.B], these genes appeared to have a role in the regulation of [[sigma].sup.B] activity. Thus, we propose that the loss of individual genes in this chromosomal hot spot region results in a destabilization of cellular harmony and disruption of the [[sigma].sup.B] regulatory, cascade.
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- 2006
127. Citrullination-Resistant LL-37 Is a Potent Antimicrobial Agent in the Inflammatory Environment High in Arginine Deiminase Activity
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Bryzek, Danuta, primary, Golda, Anna, additional, Budziaszek, Joanna, additional, Kowalczyk, Dominik, additional, Wong, Alicia, additional, Bielecka, Ewa, additional, Shakamuri, Priyanka, additional, Svoboda, Pavel, additional, Pohl, Jan, additional, Potempa, Jan, additional, and Koziel, Joanna, additional
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- 2020
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128. Epigenetic regulation of inflammation in periodontitis: cellular mechanisms and therapeutic potential
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Jurdziński, Krzysztof T., primary, Potempa, Jan, additional, and Grabiec, Aleksander M., additional
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- 2020
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129. Kallikrein 13 serves as a priming protease during infection by the human coronavirus HKU1
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Milewska, Aleksandra, primary, Falkowski, Katherine, additional, Kulczycka, Magdalena, additional, Bielecka, Ewa, additional, Naskalska, Antonina, additional, Mak, Pawel, additional, Lesner, Adam, additional, Ochman, Marek, additional, Urlik, Maciej, additional, Diamandis, Elftherios, additional, Prassas, Ioannis, additional, Potempa, Jan, additional, Kantyka, Tomasz, additional, and Pyrc, Krzysztof, additional
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- 2020
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130. Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype
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Shaw, Lindsey N., Golonka, Ewa, Szmyd, Grzegorz, Foster, Simon J., Travis, James, and Potempa, Jan
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Proteins -- Research ,Pleiotropy -- Research ,Staphylococcus aureus -- Genetic aspects ,Genetic research ,Biological sciences - Abstract
The cytoplasmic protein SspC of Staphylococcus aureus, referred to as staphostatin B, is a very specific, tightly binding inhibitor of the secreted protease staphopain B (SspB). SspC is hypothesized to protect intracellular proteins against proteolytic damage by prematurely folded and activated staphopain B (M. Rzychon, A. Sabat, K. Kosowska, J. Potempa, and A. Dubin, Mol. Microbiol. 49:1051-1066, 2003). Here we provide evidence that elimination of intracellular staphopain B activity is indeed the function of SspC. An isogenic sspC mutant of S. aureus 8325-4 exhibits a wide range of striking pleiotropic alterations in phenotype, which distinguish it from the parent. These changes include a defect in growth, a less structured peptidoglycan layer within the cell envelope, severely decreased autolytic activity, resistance to lysis by S. aureus phages, extensively diminished sensitivity to lysis by lysostaphin, the ability to form a biofilm, and a total lack of extracellular proteins secreted into the growth media. The same phenotype was also engineered by introduction of sspB into an 8325-4 sspBC mutant. In contrast, sspC inactivation in the SH1000 strain did not yield any significant changes in the mutant phenotype, apparently due to strongly reduced expression of sspB in the sigma B-positive background. The exact pathway by which these diverse aberrations are exerted in 8325-4 is unknown, but it is apparent that a very small amount of staphopain B (less than 20 ng per 200 [micro]g of cell proteins) is sufficient to bring about these widespread changes. It is proposed that the effects observed are modulated through the proteolytic degradation of several cytoplasmic proteins within cells lacking the inhibitor. Seemingly, some of these proteins may play a role in protein secretion; hence, their proteolytic inactivation by SspB has pleiotropic effects on the SspC-deficient mutant.
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- 2005
131. Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities
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Kawalec, Magdalena, Potempa, Jan, Moon, Jonathan L., Travis, James, and Murray, Barbara E.
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Enterococcus -- Research ,Enzymes -- Research ,Biological sciences - Abstract
A previously identified gene sprE of Enterococcus faecalis strain OG1 was shown to encode an extracellular serine protease that appears to belong to the glutamyl endopeptidase I staphylococcal group. A single form of SprE with a molecular mass of 25 kDa and a pH optimum between 7.0 and 7.5 was isolated from culture supernatant of wild-type E. faecalis strain OG1RF (TX4002); this form was apparently generated by cleavage of the [Ser.sup.-1]-[Leu.sup.1] and [Arga.sup.230]-[Leu.sup.231] peptide bonds of the secreted zymogen. In contrast, the culture supernatant of the gelatinase-null mutant, TX5264, with a nonpolar deletion of gelE which encodes the E. faecalis gelatinase, was found to contain several forms of SprE proteolytically processed on both the N and C termini; in addition to a full-length zymogen and a truncated zymogen, three mature forms of the SprE proteinase, [Leu.sup.1]-[Ala.sup.237], [Ser.sup.-1]-[Glu.sup.227], and [Leu.sup.1]-[Glu.sup.227], were identified. As with the V8 proteinase of Staphylococcus aureus, the closest homologue of SprE, all of the active forms cleaved specifically Glu-Xaa peptide bonds but with substantially different efficiencies, while none was able to hydrolyze peptide bonds with Asp in the P1 position. The most active of all these enzyme forms against several substrates, including human fibrinogen and [beta]-chain insulin, was the [Ser.sup.-1]-[Glu.sup.227] ([sup.-1]S-SprE) isolated from TX5264; [sup.-1]S-SprE, in contrast to other forms of SprE, was unstable at 37[degrees]C, apparently due to autodegradation. In conclusion, our results demonstrate that sprE encodes a highly specific serine-type glutamyl endopeptidase, the maturation of which is dependent on the presence of gelatinase. In the absence of gelatinase activity, the aberrant processing of pro-SprE results in the appearance of a 'superactive' form of the enzyme, [sup.-1]S-SprE.
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- 2005
132. The role and regulation of the extracellular proteases of Staphylococcus aureus
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Shaw, Lindsey, Golonka, Ewa, Potempa, Jan, and Foster, Simon J.
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Biological sciences - Abstract
Staphylococcus aureus has several extracellular proteases with proposed roles in virulence. SspA (serine protease), SspB (cysteine protease) and Aur (metalloprotease) have been characterized previously and SspA and SspB were found to be cotranscribed. The coding region for the cysteine protease ScpA has been identified and characterized. It is in a probable bi-cistronic operon with scpA located immediately upstream of a coding region for a 108 aa protein that is a specific inhibitor of ScpA. Using primer extension analysis promoters have been mapped and it was found that [[sigma].sup.A] is the only sigma factor involved in the transcription of scpA, sspABC and aur. The transcription of all the genes occurs maximally at post-exponential phase, being positively regulated by agr (accessory gene regulator) and negatively regulated by sarA (staphylococcal accessory regulator). Furthermore [[sigma].sup.B] represses transcription from the aur and scp operons similarly to the previously shown effect on ssp [Horsburgh, M., Aish, J., White, I., Shaw, L., Lithgow, J. & Foster, S. (2002). J Bacteriol 184, 5457-5467]. Using mutations in each protease gene the proteolytic cascade of activation has been analysed. Aur, SspA, SspB and ScpA are all produced as zymogens, activated by proteolytic cleavage. Although the metalloprotease, Aur, does catalyse activation of the SspA zymogen, it is not the sole agent capable of conducting this process. Site-directed mutagenesis revealed that Aur is not capable of undergoing auto-proteolysis to achieve activation. The cysteine protease, ScpA, appears to reside outside this cascade of activation, as mature ScpA was observed in the aur, sspA and sspB mutant strains. Using a mouse abscess model, it has been shown that insertional inactivation of sspA or sspB results in significant attenuation of virulence, whilst mutations in aur or scpA do not. It is likely the attenuation observed in the sspA strain is due to polarity on the sspB gene.
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- 2004
133. Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis
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Zhou, Xiao-Yan, Gao, Jin-Long, Hunter, Neil, Potempa, Jan, and Nguyen, Ky-Anh
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- 2013
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134. The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine
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Carroll, Ronan K., Veillard, Florian, Gagne, Danielle T., Lindenmuth, Jarrod M., Poreba, Marcin, Drag, Marcin, Potempa, Jan, and Shaw, Lindsey N.
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- 2013
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135. 19 Kinins in bacterial infections
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Potempa, Jan, primary and Herwald, Heiko, additional
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- 2011
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136. Human SCCA Serpins Inhibit Staphylococcal Cysteine Proteases by Forming Classic “Serpin-Like” Covalent Complexes
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Kantyka, Tomasz, primary and Potempa, Jan, additional
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- 2011
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137. Gingipain aminopeptidase activities in Porphyromonas gingivalis
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Veillard, Florian, Potempa, Barbara, Poreba, Marcin, Drag, Marcin, and Potempa, Jan
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- 2012
- Full Text
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138. Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes
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Sztukowska, Maryta, Veillard, Florian, Potempa, Barbara, Bogyo, Matthew, Enghild, Jan J., Thogersen, Ida B., Nguyen, Ky-Anh, and Potempa, Jan
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- 2012
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139. Protease-dependent mechanisms of complement evasion by bacterial pathogens
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Potempa, Michal and Potempa, Jan
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- 2012
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140. Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis
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Sroka, Aneta, Sztukowska, Maryta, Potempa, Jan, Travis, James, and Genco, Caroline Attardo
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Bacteriology -- Research ,Bacteria -- Physiological aspects ,Hemoproteins -- Physiological aspects ,Lysine -- Physiological aspects ,Cysteine proteinases -- Physiological aspects ,Haptoglobin -- Physiological aspects ,Transferrin -- Physiological aspects ,Serum -- Physiological aspects ,Biological sciences - Abstract
Research has been conducted on the lysine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis (Kgp). Results demonstrate the ability of the Kgp to bind and degrade hemoglobin, soluble haptoglobin, hemopexin and transferrin present in human serum.
- Published
- 2001
141. Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence
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Kantyka, Tomasz, Plaza, Karolina, Koziel, Joanna, Florczyk, Danuta, Stennicke, Hennig R., Thogersen, Ida B., Enghild, Jan J., Silverman, Gary A., Pak, Stephen C., and Potempa, Jan
- Published
- 2011
142. The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases
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Cerdà-Costa, Núria, Guevara, Tibisay, Karim, Abdulkarim Y., Ksiazek, Miroslaw, Nguyen, Ky-Anh, Arolas, Joan L., Potempa, Jan, and Gomis-Rüth, Xavier F.
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- 2011
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143. Mechanisms of vascular damage by systemic dissemination of the oral pathogen Porphyromonas gingivalis
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Farrugia, Cher, primary, Stafford, Graham P., additional, Potempa, Jan, additional, Wilkinson, Robert N., additional, Chen, Yan, additional, Murdoch, Craig, additional, and Widziolek, Magdalena, additional
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- 2020
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144. The essential Porphyromonas gingivalis type IX secretion system component PorZ delivers anionic-lipopolysaccharide to the PorU sortase for transpeptidase processing of cargos
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Madej, Mariusz, primary, Nowakowska, Zuzanna, additional, Ksiazek, Miroslaw, additional, Lasica, Anna M., additional, Mizgalska, Danuta, additional, Nowak, Magdalena, additional, Jacula, Anna, additional, Scavenius, Carsten, additional, Enghild, Jan J., additional, Aduse-Opoku, Joseph, additional, Curtis, Michael A., additional, Gomis-Rüth, F. Xavier, additional, and Potempa, Jan, additional
- Published
- 2020
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145. Application of the In Vitro HoxB8 Model System to Characterize the Contributions of Neutrophil–LPS Interaction to Periodontal Disease
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Sochalska, Maja, primary, Stańczyk, Magdalena B., additional, Użarowska, Maria, additional, Zubrzycka, Natalia, additional, Kirschnek, Susanne, additional, Grabiec, Aleksander M., additional, Kantyka, Tomasz, additional, and Potempa, Jan, additional
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- 2020
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146. Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)—A CleavEx Based Analysis
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Falkowski, Katherine, primary, Bielecka, Ewa, additional, Thøgersen, Ida B., additional, Bocheńska, Oliwia, additional, Płaza, Karolina, additional, Kalińska, Magdalena, additional, Sąsiadek, Laura, additional, Magoch, Małgorzata, additional, Pęcak, Aleksandra, additional, Wiśniewska, Magdalena, additional, Gruba, Natalia, additional, Wysocka, Magdalena, additional, Wojtysiak, Anna, additional, Brzezińska-Bodal, Magdalena, additional, Sychowska, Kamila, additional, Pejkovska, Anastasija, additional, Rehders, Maren, additional, Butler, Georgina, additional, Overall, Christopher M, additional, Brix, Klaudia, additional, Dubin, Grzegorz, additional, Lesner, Adam, additional, Kozik, Andrzej, additional, Enghild, Jan J., additional, Potempa, Jan, additional, and Kantyka, Tomasz, additional
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- 2020
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147. Apolipoprotein E Triggers Complement Activation in Joint Synovial Fluid of Rheumatoid Arthritis Patients by Binding C1q
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Vogt, Leonie M., primary, Kwasniewicz, Ewa, additional, Talens, Simone, additional, Scavenius, Carsten, additional, Bielecka, Ewa, additional, Ekdahl, Kristina N., additional, Enghild, Jan J., additional, Mörgelin, Matthias, additional, Saxne, Tore, additional, Potempa, Jan, additional, and Blom, Anna M., additional
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- 2020
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148. Proteolysis of Gingival Keratinocyte Cell Surface Proteins by Gingipains Secreted From Porphyromonas gingivalis – Proteomic Insights Into Mechanisms Behind Tissue Damage in the Diseased Gingiva
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Hočevar, Katarina, primary, Vizovišek, Matej, additional, Wong, Alicia, additional, Kozieł, Joanna, additional, Fonović, Marko, additional, Potempa, Barbara, additional, Lamont, Richard J., additional, Potempa, Jan, additional, and Turk, Boris, additional
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- 2020
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149. Kallikrein-related peptidase 14 activates zymogens of membrane type matrix metalloproteinases (MT-MMPs) - a CleavEx library-based analysis
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Falkowski, Katherine, primary, Bielecka, Ewa, additional, Thøgersen, Ida B., additional, Bocheńska, Oliwia, additional, Płaza, Karolina, additional, Kalińska, Magdalena, additional, Sąsiadek, Laura, additional, Magoch, Małgorzata, additional, Pęcak, Aleksandra, additional, Wiśniewska, Magdalena, additional, Gruba, Natalia, additional, Wysocka, Magdalena, additional, Wojtysiak, Anna, additional, Brzezińska-Bodal, Magdalena, additional, Sychowska, Kamila, additional, Pejkovska, Anastasija, additional, Rehders, Maren, additional, Butler, Georgina, additional, Overall, Christopher M, additional, Brix, Klaudia, additional, Dubin, Grzegorz, additional, Lesner, Adam, additional, Kozik, Andrzej, additional, Enghild, Jan J., additional, Potempa, Jan, additional, and Kantyka, Tomasz, additional
- Published
- 2020
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150. Peptidylarginine Deiminase of Porphyromonas gingivalis Modulates the Interactions between Candida albicans Biofilm and Human Plasminogen and High-Molecular-Mass Kininogen
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Karkowska-Kuleta, Justyna, primary, Surowiec, Magdalena, additional, Gogol, Mariusz, additional, Koziel, Joanna, additional, Potempa, Barbara, additional, Potempa, Jan, additional, Kozik, Andrzej, additional, and Rapala-Kozik, Maria, additional
- Published
- 2020
- Full Text
- View/download PDF
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