264 results on '"Vallone B"'
Search Results
2. Cryo-EM structure of holo-PdxR from Bacillus clausii bound to its target DNA in the half-closed conformation
- Author
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Freda, I., primary, Montemiglio, L.C., additional, Tramonti, A., additional, Contestabile, R., additional, Vallone, B., additional, Savino, C., additional, Exertier, C., additional, Bolognesi, M., additional, and Chaves Sanjuan, A., additional
- Published
- 2023
- Full Text
- View/download PDF
3. CRYSTAL STRUCTURE OF FERRIC MURINE NEUROGLOBIN CDLESS MUTANT
- Author
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Exertier, C., primary, Freda, I., additional, Montemiglio, L.C., additional, Savino, C., additional, Cerutti, G., additional, Gugole, E., additional, and Vallone, B., additional
- Published
- 2022
- Full Text
- View/download PDF
4. OleP mutant S240Y in complex with 6DEB
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Savino, C., primary, Montemiglio, L.C., additional, Vallone, B., additional, Exertier, C., additional, Freda, I., additional, and Gugole, E., additional
- Published
- 2022
- Full Text
- View/download PDF
5. OleP mutant G92W in complex with 6DEB
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Savino, C., primary, Montemiglio, L.C., additional, Vallone, B., additional, Exertier, C., additional, Freda, I., additional, and Gugole, E., additional
- Published
- 2022
- Full Text
- View/download PDF
6. OleP mutant E89Y in complex with 6DEB
- Author
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Savino, C., primary, Montemiglio, L.C., additional, Vallone, B., additional, Exertier, C., additional, Freda, I., additional, and Gugole, E., additional
- Published
- 2022
- Full Text
- View/download PDF
7. Neuroglobin, seven years after
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Brunori, M. and Vallone, B.
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- 2007
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8. Crystallographic structure of oligosaccharide dehydrogenase from Pycnoporus cinnabarinus, glucose-bound form
- Author
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Cerutti, G., primary, Savino, C., additional, Montemiglio, L.C., additional, Vallone, B., additional, and Sciara, G., additional
- Published
- 2021
- Full Text
- View/download PDF
9. Crystallographic structure of oligosaccharide dehydrogenase from Pycnoporus cinnabarinus, ligand-free form
- Author
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Cerutti, G., primary, Savino, C., additional, Montemiglio, L.C., additional, Sciara, G., additional, and Vallone, B., additional
- Published
- 2021
- Full Text
- View/download PDF
10. Crystallographic structure of oligosaccharide dehydrogenase from Pycnoporus cinnabarinus, laminaribiose-bound form
- Author
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Cerutti, G., primary, Savino, C., additional, Montemiglio, L.C., additional, Vallone, B., additional, and Sciara, G., additional
- Published
- 2021
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- View/download PDF
11. Structural Dynamics of Myoglobin
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Brunori, M., primary, Bourgeois, D., additional, and Vallone, B., additional
- Published
- 2008
- Full Text
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12. Crystal structure of OleP-oleandolide(DEO) bound to L-rhamnose
- Author
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Montemiglio, L.C., primary, Savino, C., additional, Vallone, B., additional, Parisi, G., additional, and Freda, I., additional
- Published
- 2020
- Full Text
- View/download PDF
13. OleP-oleandolide(DEO) in low salt crystallization conditions
- Author
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Savino, C., primary, Montemiglio, L.C., additional, Vallone, B., additional, Parisi, G., additional, and Cecchetti, C., additional
- Published
- 2020
- Full Text
- View/download PDF
14. OleP-oleandolide(DEO) in high salt crystallization conditions
- Author
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Montemiglio, L.C., primary, Savino, C., additional, Vallone, B., additional, Parisi, G., additional, and Cecchetti, C., additional
- Published
- 2020
- Full Text
- View/download PDF
15. Crystal structure of OleP-6DEB bound to L-rhamnose
- Author
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Montemiglio, L.C., primary, Savino, C., additional, Vallone, B., additional, Parisi, G., additional, and Freda, I., additional
- Published
- 2020
- Full Text
- View/download PDF
16. murine Neuroglobin under 2 kBar of argon
- Author
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Prange, T., primary, Colloc'h, N., additional, Carpentier, P., additional, and Vallone, B., additional
- Published
- 2020
- Full Text
- View/download PDF
17. Ferric murine neuroglobin Gly-loop44-47/F106A mutant
- Author
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Exertier, C., primary, Freda, I., additional, Montemiglio, L.C., additional, Savino, C., additional, and Vallone, B., additional
- Published
- 2020
- Full Text
- View/download PDF
18. Neuroglobin under every kind of pressure
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Colloc'h, N, Girard, E, Carpentier, P, Prangé, T, Vallone, B, Imagerie et Stratégies Thérapeutiques des pathologies Cérébrales et Tumorales (ISTCT), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), and Brunaud, Carole
- Subjects
[SDV] Life Sciences [q-bio] ,[SDV]Life Sciences [q-bio] - Abstract
CERVOXY; National audience
- Published
- 2019
19. Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments
- Author
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Ardiccioni, C., Arcovito, A., Longa, S. D., Van Der Linden, P., Bourgeois, D., Weik, M., Montemiglio, L. C., Savino, C., Avell, G., Exertier, C., Carpentier, P., Prange, T., Brunori, M., Colloc'h, N., Vallone, B., Arcovito A. (ORCID:0000-0002-8384-4844), Ardiccioni, C., Arcovito, A., Longa, S. D., Van Der Linden, P., Bourgeois, D., Weik, M., Montemiglio, L. C., Savino, C., Avell, G., Exertier, C., Carpentier, P., Prange, T., Brunori, M., Colloc'h, N., Vallone, B., and Arcovito A. (ORCID:0000-0002-8384-4844)
- Abstract
A combined biophysical approach was applied to map gas-docking sites within murine neuroglobin (Ngb), revealing snapshots of events that might govern activity and dynamics in this unique hexacoordinate globin, which is most likely to be involved in gas-sensing in the central nervous system and for which a precise mechanism of action remains to be elucidated. The application of UV-visible microspectroscopy in crystallo, solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15-40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation. Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton. Notably, no other secondary sites were observed under our experimental conditions.
- Published
- 2019
20. Contributory presentations/posters
- Author
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Gries, A., Singh, Balwinder, Nakazawal, Chicko, Genest, D., Getzoff, E. D., Matsuo, H., Kaur, Harpreet, Borst, J. W., Chadha, K. C., Tingyun, Kuang, Jagannadham, M. V., Leijon, Mikael, Sato, S., Bhakuni, Vlnod, Vijayan, M., Surolia, A., Suguna, K., Manoj, N., Srinivas, V. R., Ravishankar, R., Laggner, P., Prassl, R., Schwarzenbacher, R., Zeth, K., Kostner, G. M., Taylor, Susan S., Xuong, Nguyen-huu, Akamine, Pearl, Sagar, Bidva M., Saikrishnan, K., Purnapatre, K., Handa, P., Roy, S., Varshney, U., Biswal, B. K., Sukumar, N., Rao, J. K. Mohana, Johnson, A., Pattabhi, Vasantha, Murthy, M. R. N., Krishna, Sri S., Savithri, H. S., Sastri, Mira, Hosur, M. V., Pillai, Bindu, Kannan, K. K., Kumar, Mukesh, Patwardhan, Swati, Padmanabhaa, B., Sasaki-Sugio, S., Matsuzaki, T., Nukaga, M., Singh, T. P., Sharma, A. K., Srinivasan, A., Khan, J. A., Paramasivam, M., Kumar, P., Karthikevan, S., Sharma, S., Yadav, S., Srintvasan, A., Alam, Neelima, Gourinath, S., Kaur, Punit, Chandra, Vikas, Betzel, Ch., Ghosh, S., Bera, A. K., Pal, A. K., Baneriee, Asok, Mukhopadhyay, B. P., Bhattacharya, S., Chakraborty, S., Haldar, U., Dey, I., Solovicova, Adriana, Sevcik, Jozef, Sekar, K., Sundaralingam, M., Genov, N., Liang, Dong-cai, Zhang, Ji-ping, Jiang, Tao, Chang, Wen-rui, Blommers, Marcel, Jahnke, Wolfgang, Hosur, R. V., Panchal, S. C., Pillay, Bindu, Jaganathan, N. R., Mathur, Puniti, Srivatsun, S., Joshi, Ratan Mani, Chauhan, V. S., Govil, Girjesh, Atreya, H. S., Sahu, S. C., Quinjou, Éric, Adjadj, Elisabeth, Mispelter, Joël, Izadi-Pruneyre, Nadia, Blouquit, Yves, Heyd, Bernadette, Lerat, Guilhem, Desmadreil, Michel, Milnard, Philippe, Lin, Y., Rao, B. D. Nageswara, Raghunathan, Vidva, Chau, Mei H., Coutinho, Evans, Pesais, Prashant, Srivastava, Sudha, Saran, Anil, Srikrishnan, Thamarapu, Lijima, Herbert, Gesme, Jayson, Sapico, Leizl F., Paxton, Raymond, Grace, C. R., Nagenagowda, G., Lynn, A. M., Cowsik, Sudha M., Govil, G., Sahu, Sarata C., Bhattacharya, A., Chauhan, S., Kumar, Anil, Zuiderweg, Erik R. P., Pellecchia, Maurizio, Nitta, Katsutoshi, Ohnishi, Atsushi, Kawano, Keiichi, Hikichi, Kunio, Fujitani, Naoki, Ohkubo, Tadayasu, Aizawa, Tomoyasu, Kumaki, Yasuhiro, Hayakawa, Yoichi, Parvathy, Rani V., Kini, R. M., Nakagawa, Astushi, Tanaka, Isao, Demura, Makoto, Yao, Min, Koshiba, Takumi, Kobashigawa, Yoshihiro, Kuwajima, Kunihiro, Linge, Jens, Nilges, Michael, Donoghue, Seán O., Chakshusmathi, G., Ratnaparkhi, Girish S., Madhu, P. K., Varadarajan, R., Tetreau, C., Tourbez, M., Lavalette, D., Bulone, D., Manno, M., Emanuele, A., Palma-Vittorelli, M. B., Palma, M. U., Vaiana, S. M., Martorana, V., Biagio, P. L. San, Chang, D. K., Cheng, S. F., Yang, S. H., Francis, S., Trivedi, V. D., Chien, W. J., Manstein, Dietmar J., Batra, Renn, Geeves, Michael A., Geller, Maciej, Trvlska, Joanna, Grochowski, Pawel, Lesyng, B., Ginalski, K., Grochowski, P., Lavalette, P., Blouquit, Y., Roccatano, D., Berendsen, H. J. C., Amadei, A., Nola, Di A., Ho, Bosco, Curmi, P. M. G., Berry, H., Pelta, J., Pauthe, E., Lairez, D., Srinivasan, M., Sahi, Shakti, Kothekar, V., Madhusudnan, Kartha S., Nandel, Fateh S., Jain, D. V. S., Berendsen, Herman J. C., Feenstra, Anton K., Tama, F., Sanejouand, Y.-H., Go, N., Sharma, Deepak, Pasha, Santosh, Sharma, Sunita, Brahmachari, Samir K., Makker, Jyoti, Viiavaraghavan, R., Kumar, S., Dey, Sharmisllia, Krishnamoorthy, G., Lakshmikanth, G. S., Zaitseva, E. M., Mazhul, V. M., Kierdaszuk, Borys, Widengren, J., Rigler, R., Terry, B., Mets, Ü., Swaminathan, R., Yathindra, N., Thamotharan, S., Chosrowjan, H., Mataga, N., Shibata, Y., Morisima, I., Xiao, Ming, Selvin, Paul, Chakraharty, Tania, Cooke, Roger, Faraone, A., Branca, C., Maisano, G., Migliardo, P., Magazù, S., Villari, V., Behere, Digambar V., Deva, Sharique Zahida Waheed M., Vallone, B., Savino, C., Travaglini-Allocatelli, C., Cutruzzolà, F., Brunori, M., Gibson, Q. H., Mazumdar, Shyamalava, Mitra, Samaresh, Prasad, Swati, Soto, P., Fayad, R., Tyulkova, N. A., Sukovataya, I. E., Mamedov, Sh. V., Aksakal, B., Canturk, M., Aktas, B., Yilgin, R., Bogutska, K. I., Miroshnichenko, N. S., Wein, A. J., Hypolite, J. A., DiSanto, M., Chacko, S., Zheng, Y-M., Antosiewicz, J., Wojciechowski, M., Grycuk, T., Di Nola, Alfredo, Ceruso, Marc A., Chatterjee, Bishnu P., Bandvopadhvay, Subhasis, Choudhury, Devapriva, Khight, Stefan, Thompson, Andrew, Stojanoff, Vivian, Pinkner, Jerome, Hultgren, Scott, Flatters, Delphine, Goodfellow, Julia, Takazawatt, Fumi, Kanehisa, Minoru, Sasai, Masaki, Nakamura, Hironori, Wang, Bao Han, Pan, xin Min, Zheng, Yuan, Wang, Zhi Xin, Ahmad, Atta, Kulkarni, Sangeeta, Prakash, Koodathingal, Prajapati, Shashi, Surin, Alexey, Kihara, Hiroshi, Yang, Li, Matsumoto, Tomoharu, Nakagawa, Yuki, Semisotnov, Gennady V., Kimura, Kazumoto, Amemiya, Yoshiyuki, Tayyab, Saad, Muzammil, Salman, Kumar, Yogesh, Bhakuni, Vinod, Sundd, Monica, Kundu, Suman, Jagannadham, Medicherla V., Chandani, Bina, Warrier, Deepti, Sinha, Lalankumar, Dhar, Ruby, Mehrotra, Sonam, Khandelwal, Purnima, Seth, Subhendu, Gidwani, Arun, Prabha, Ratna C., Sasidhar, Y. U., Madhusudan, K. P., Nishikawa, Ken, Kinjo, Akira R., Varadarajan, Raghavan, Chakravarty, Suvobrata, Van Dael, H., Noyelle, K., Joniau, M., Haezebrouck, P., Jha, Indra Brata, Bhat, Rajiv, Dash, Sheffali, Mohanty, Prasanna, Bandyopadhyay, A. K., Sonawat, H. M., Rao, Ch. Mohan, Datta, Siddhartha, Raman, B., Rajaraman, K., Ramakrishna, T., Pande, A., Benedek, G., King, J., Betts, S., Pande, J., Asherie, N., Ogun, O., Kalacheva, G. S., Sokolova, I. V., Mitaku, Shigeki, Sonoyama, Masashi, Taira, Kunihiro, Yokoyama, Yasunori, Sasakil, Takanori, Kamo, Naoki, Mukai, Yuri, Dalal, Seema, Regan, Lynne, Mituku, Shigeki, Kumar, Devesh, Roychoudhury, Mihir, Lőrinczv, Dénes, Könczöl, Franciska, Farkas, László, Belagyi, Joseph, Schick, Christoph, Thomson, Christy A., Ananthanarayanan, Vettai S., Alirzayeva, E. G., Baba-Zade, S. N., Sarai, A., Kono, H., Uedaira, H., An, J., Gromiha, Michael M., Oobatake, M., Yutani, Katsuhide, Takano, Kazufumi, Yamagata, Yuriko, Jas, Gouri S., Hofrichter, James, Muñoz, Victor, Eaton, William A., Penoyar, Jonathan, Lo Verde, Philip T., Bódi, Á., Venekei, I., Kardos, J., Gráf, L., Závodszky, P., Szilágyi, András, Závodszky, Péter, Woolfson, D. N., Walshaw, J., Allan, R. D., Funahashi, Jun, Gupta, Savan, Di Nola, A., Mangoni, M., Roccatano, P., Ramachandraiah, Gosu, Chandra, Nagasuma R., Ciani, Barbara, Woolfson, Derek N., Nair, Usha B., Salunke, Dinakar M., Kaur, Kanwal J., Swaminathan, Chittoor P., Surolia, Avadhesha, Pramanik, A., Jörnvall, H., Nygren, P.-Å., Jonasson, P., Ståhl, S., Johansson, B.-L., Kratz, G., Wahren, J., Ekberg, K., Uhlén, M., Jansson, O. T., Uhlén, S., Misselwitz, Rolf, Welfle, Heinz, Welfle, Karin, Höhne, Wolfgang, Kurganov, B. I., Mitskevich, L. G., Fedurkina, N. V., Jarori, Gotam K., Maity, Haripada, Guharay, J., Sengupta, P. K., Sengupta, B., Sridevi, K., Kasturi, S. R., Gupta, S. P., Agarwal, Gunjan, Briehl, Robin W., Kwong, Suzanne, Tyulkova, N A., Ismailova, O. I., Parola, A. H., Yayon, A., Hariharan, C., Pines, D., Pines, E., Zamai, M., Cohen-Luria, R., Woolfeon, D. N., Spooner, G. A., Padya, M. J., Bharadwaj, D. K., Bakshi, Panchan, Jagannathan, N. R., Sharma, U., Srivastava, N., Barthwal, R., Matsuda, Keiko, Nishioka, Takaaki, Go, Nobuhiro, Urata, S., Aita, T., Husimi, Y., Majumder, Mainak, Subirana, Juan A., Malinina, Lucy, Abrescia, Nicola G. A., Aymami, Juan, Coll, Miquel, Eritxa, Ramón, Premraj, B. J., Thenmalarchelvi, R., Gautham, N., Kumar, Satheesh P., Kan, Lou-Sing, Hou, Ming, Lin, Shwu-Bin, Roy, Kanal B., Sana, Tapas, Bruant, N., Flatters, D., Lavery, R., Sklenar, Heinz, Rons, Remo, Lavery, Richard, Thakur, Ashoke Ranjan, Kundu, Sudip, Bandyopadhyay, Debashree, Bhattacharyya, Dhananjay, Majumdar, Rabi, Barceló, F., Portugal, J., Rao, B. J., Ramanathan, Sunita, Gliosli, Mahua, Varshney, Umesh, Kumar, Vinay N., Pataskar, Shashank S., Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Kolmdaivel, P., Maiti, Motilal, Das, Suman, Sen, Anjana, Xodo, Luigi, Suraci, Chiara, Del Terra, Elisa, Quadrifoglio, Franco, Diviacco, Silvia, Ray, Arghya, Rao, Basuthkar J., Karthikeyan, G., Chary, Kandala V. R., Mujeeb, Anwer, James, Thomas L., Bogdanov, A., Zanina, A., Haya, E. E. F., Kasyanenko, N., Cornélio, M. L., Bugs, M. R., Tolstorukov, Ye. M., Sanval, Nitish K., Tiwari, S. N., Sanyal, Nitish K., Choudhury, Mihir Roy, Patel, P. K., Bhavesh, Neel S., Gabrielian, Anna, Rigler, Rudolf, Edman, Lars, Wennmalm, Stefan, Constantinescu, B., Gazdaru, D., Radulcscu, I., Radu, L., Wärmländer, Sebastian, Aoki, Setsuyuki, Ishiura, Masahiro, Kondo, Takao, Pashinskaya, V. A., Kosevich, M. V., Shelkovsky, V. S., Blagoy, Yu. P., Wang, Ji-hua, Malathi, R., Chandrasekhar, K., Kandimalla, E. R., Agrawal, S., Rastogi, V. K., Palafox, Alcolea M., Singh, Chatar, Beniaminov, A. D., Minyat, E. E., Zdobnov, E. M., Ulyanov, N. B., Bondarenko, S. A., Ivanov, V. I., Singh, J. S., Tewari, Ravindra, Sonawane, Kailas D., Grosjean, Henri, Sonavane, Uddhavesh B., Morin, Annie, Doherty, Elizabeth A., Doudna, Jennifer A., Tochio, H., Shirakawa, M., Kyogoku, Y., Das, Achintya, Javaram, B., Kalra, Parul, Shukla, Piyush, Dixit, Surjit B., Beveridge, David L., McConnell, Kevin, Davidson, B. E., Chan, R. Y. S., Sawyer, W. H., Eccelston, J. F., Yan, Yuling, Norden, Bengt, Tuite, Eimer, Nielsen, Peter, Takahashi, Masayuki, Ghosh, Anirban, Bansal, Manju, Pingoud, Alfred, Christ, Frauke, Thole, Hubert, Pingoud, Vera, Wende, Wolfgang, Luthra, Pratibha Mehta, Chandra, Ramesh, Sen, Ranjan, Weisberg, Robert, King, Rodney, Gobets, Bas, van Amerongen, Herbert, van Stokkum, Ivo H. M., Larsen, Olaf F. A., van Grondelle, Rienk, Hilbers, Cornelis W., Heus, Hans A., Berends, Jos, Sngrvan, H E., Khudaverdian, N. V., Babayan, Yu. S., Pichierri, F., Gromiha, M., Prabakaran, P., Aida, M., Sayano, K., Merkienė, Eglė, Vilkaitis, Giedrius, Klimašauskas, Saulius, Serva, Saulius, Weinhold, Elmar, Bandiera, Antonella, Marsich, Eleonora, Manzini, Giorgio, Potikyan, G., Arakelyan, V., Babayan, Yu., Ninaber, Alex, Goodfellow, Julia M., Ohta, Shigeru, Ito, Yoichiro, Husimi, Yuzuru, Usukura, J., Aiba, H., Tagami, H., Nunes, Elia, Suarez, Mougli, Candreva, Carmen E., Keszenman, Deborah, Thyberg, Per, Földes-Papp, Zeno, Joshi, Amita, Singh, Dinesh, Rajeswari, M. R., Amenitsch, H., Pregetter, M., Chapman, J., Mishra, K. P., Pandev, B. N., Tonevitsky, A. G., Pohl, E. E., Agapov, I. I., Sun, J., Pohl, P., Dennison, S. M., Gorbeako, G. P., Dynbko, T. S., Mishra, A. K., Pappavee, N., Luis, Loura, Rodrigo, Almeida, Manuel, Prieto, Gendel, Ya. L., Kleszczyńska, H., Kuczera, J., Przestalski, S., Kral, T., Chernitsky, E. A., Senkovich, O. A., Rosin, V. V., Gasanov, R. A., Allakhverdieva, Y. M., Papageorgiou, G. C., Savopol, Tudor, Apetrei, Calin, Balea, Marius, Cucu, D., Mihailescu, D., Ramanathan, K. V., Bačić, Goran, Genest, Monique, Sajot, Nicolas, Garnier, Norbert, Crouzy, Serge, Zsiros, O., Várkonyi, Z. S., Combos, Z., Farkas, T., Cribier, Sophie, de Paula, F., Fraceto, I. F., Schreier, S., Spisni, A., Sevšek, F., Žekš, B., Gomišček, G., Svetina, S., Arrigler, V., Hotani, Hirokazu, Nomura, Fumimasa, Takiguchi, Kingo, Nagata, Miki, Panicker, Lata, Parvathanathan, P. S., Hotani, H., Takiguchi, K., Ishino, A., Saitoh, A., Afonin, S., Takahashi, A., Takizawa, T., Nakato, Y., Marathe, Dipti, Jørgensen, Kent, Chattopadhyay, Amitabha, Rukmini, R., Rawat, Satinder S., Pečar, S., Štrancar, J., Šentiurc, M., Stolič, Z., Filipin, K., Biswas, S. C., Samanta, Anunay, Sana, Satyen, Kinoshita, Koji, Yamazaki, Masahito, Ohki, Kazuo, Goto, Akira, Kiuchi, Tai, Kumeta, Takaaki, Ohba, Tetsuhiko, Sugar, I. P., Thompson, K. K., Biltonen, R. L., Thompson, T. E., Ichinose, H., Suezaki, Y., Akivama, M., Matuoka, S., Tsuchihashi, K., Gasa, S., Pike, H. M., Mattjus, P., Brown, R. E., Molotkovsky, J. G., Arora, Ashish, Kleinschmidt, Jörg H., Tamm, Lukas K., Kruglyakova, K. E., Luneva, O. G., Fedin, V. A., Kuptsoya, O. S., Visser, A. J. W. G., Visser, N. V., Dyubko, T. S., Ogihara, Toshihiko, Mishima, Kiyoshi, Shvaleva, A. L., Radenović, Č. N., Jeremić, M. G., Radenović, N. Č., Minić, P. M., Salakhutdinov, B. A., Aripov, T. F., Tadjibaeva, E. T., Zamaraeva, M. V., Vagina, O. N., Basak, A. K., Cole, A., Naylor, C., Poppofl, M., Titball, R., Naylor, C. E., Moss, D. S., Eaton, J. T., Justin, N., Titball, R. W., Nomura, F., Nagata, M., Ishjkawa, S., Takahashi, S., Obuchi, Kaoru, Staudegger, Erich, Lohner, Karl, Kriechbaum, Manfred, Waring, Alan J., Lehrer, Robert I., Mayer, Bernd, Köhler, Gottfried, Gangl, Susanne, Shobini, J., Hu, B., Lortz, B., Sackmann, E., Guttenberg, Z., Antonovich, A. N., Slobozhanina, E. I., Lukyanenko, L. M., Kozlova, N. M., Krylov, Andrey V., Kotova, Elena A., Antonenko, Yuri N., Yaroslavov, Alexander A., Ghosh, Subhendu, Bera, Amal K., Das, Sudipto, Urbánková, Eva, Freeman, Karl, Jelokhani-Niaraki, Masood, Jezek, Petr, Usmanov, P. B., Tonkikh, A. K., Ongarbaev, A., Pohl, Peter, Saparov, Sapar M., Harikumar, P., Reeves, J. P., Sikdar, S. K., Rao, S., Ghatpande, A. S., Corsso, C., Varanda, W. A., ElHamel, C., Dé, E., Molle, G., Saint, N., Varshney, Anurae, Mathew, M. K., Isacoff, E. Y., Loots, E., Kasai, Michiki, Yamaguchi, Naohiro, Ghosh, Paramita, Tigyi, Joseph, Miledi, Ricardo, Tigyi, Gabor, Liliom, Karoly, Djurisic, Maja R., Andjus, Pavle R., Shrivastava, Indira H., Sansom, M. S. P., Barrias, C., Oliveira, P. F., Lopes, I. A., Mauricio, A. C., Fedorovich, S. V., Konev, S. V., Sholukh, M. V., Chubanov, V. S., Klevets, M., Fedirko, N., Shvinka, N., Manko, V., Prabhananda, B. S., Kombrabail, Mamata H., Aravamudhan, S., Venegas-Cotero, Berenice, Blake, Ivan Ortega, Zhou, Han-qing, Hu, Xiao-jian, Zhang, Zhi-hong, Feng, Hang-fang, Cheng, Wei-ying, Zalyvsky, I. A., Dubitsky, L. O., Vovkanvch, L. S., Savio-Galimberti, E., Ponce-Homos, J. E., Bonazzola, P., Capurro, Claudia, Parisi, Mario, Toriano, Roxana, Thomas, David D., Ready, Laxma G., Jones, Larry R., Tashmukhamedov, B. A., Sagdullaev, B. T., Heitzmann, D., Bleich, M., Warth, R., Ferreira, H. G., Ferreira, K. T. G., Greger, R., Parola, Abraham H., Alfahel, Essa, Zagoory, Orna, Priel, Zvi, Hama-Inaba, H., Ohyama, H., Hayata, I., Choi, K., Haginoya, K., Mori, M., Wang, R., Yukawa, O., Nakajima, T., Joshi, Nanda B., Kannurpatti, Sridhar K., Sinha, Mau, Joshi, Preeti G., Bei, Ling, Hu, Tianhui, Shen, Xun, Knetsch, Menno L. W., Schäfers, Nicole, Sandblom, John, Galvanovskis, Juris, Kovacs, Eugenia, Dinu, Alexandra, Pologea-Moraru, Roxana, Sanghvi, S. H., Jazbinšek, V., Tronteli, Z., Thiel, G., Wübeller, G., Müller, W., Brumen, Milan, Fajmut, Leš, Marhl, Marko, Volotovski, I. D., Sokolovski, S. G., Knight, M. R., Chalyi, Alexander V., Vasilʼev, Alexei N., Sharma, P., Pant, H. C., Sharma, M., Amin, N. D., Albers, R. W., Steinbach, P. J., Barchir, J., Balasubramanyam, M., Gardner, J. P., Condrescu, M., Pilarczyk, Gotz, Greulich, K. O., Monajembashi, Shamci, El-Awadi, A. I., El-Refaei, F. M., Talaat, M. M., Ali, F. M., Zahradniková, Alexandra, Tahradník, Ivan, Pavelková, Jana, Zhorov, Boris S., Ananthanaravanan, Vettai S., Weiss, D. G., Martin, D., Gornik, E., Neu, E., Michailov, Ch. M., Welscher, U., Seidenbusch, W., Jellali, A., Pattnaik, B. R., Hicks, D., Dreyfus, H., Sahel, J., Picaud, S., Forster, V., Wang, Hong-Wei, Sui, Sen-fang, Luther, Pradeep K., Morris, Ed, Barry, John, Squire, John, Sundari, Sivakama C., Balasubramanian, D., Christlet, Hema Thanka T., Veluraia, K., Suresh, Xavier M., Laretta-Garde, V., Krilov, Dubravka, Herak, Janko N., Stojanović, Nataša, Ferrone, Frank A., Ivanova, Maria, Jasuja, Ravi, Mirchev, Rossen, Stopar, David, Wolfs, Cor J. A. M., Hemminga, Marcus A., Spruijt, Ruud B., Arcovito, G., De Spirito, M., Frank, Joachim, Heagle, Amy B., Grassucci, Robert, Penczek, Pawel, Agrawal, Rajendra K., Sharma, Manjuli R., Wagenknecht, Terence, Jeyakumar, Loice H., Fleischer, Sidney, Knupp, Carlo, Squire, John M., Ezra, Eric, Munro, Peter M. G., Kitazawa, Hidefumi, Ichihara, Koji, Itoh, Tomohiko J., Iguchi, Yusuke, Pifat, Greta, Kveder, Marina, Pečar, Slavko, Schara, Milan, Nair, Deepak, Singh, Kavita, Rao, Kanury V. S., Sundaravadivel, B., Jain, Deepti, Kaur, Kanwaljeet, Salunke, D. M., Goel, Manisha, Kovalenko, E. I., Semenkova, G. N., Cherenkevich, S. N., Loganathan, D., Lakshmanan, T., Sriram, D., Srinivasan, S., Lebrón, J. A., Bjorkman, P. J., Ramalingam, T. S., Singh, A. K., Gayatri, T. N., Bisch, Paulo M., Caffarena, Ernesto R., Grigera, Raul J., Fromherz, P., Kiessling, V., Suresh, C. G., Rao, K. N., Khan, M. I., Gaikwad, S. M., Elanthiraiyan, M., Kaliannan, P., Payne, J., Chadha, K., Ambrus, J. L., Nair, M. P. N., Nair, Madhavan P. N., Hewitt, R., Schwartz, S. A., Mahajan, S., Macherel, D., Bourguignon, J., Neuburger, M., Douce, R., Cohen-Addad, C., Faure, M., Ober, R., Sieker, L., Gurumurthy, D. S., Velmurugan, S., Lobo, Z., Phadke, Ratna S., Desai, Prashant, Alieva, D. R., Guseinova, I. M., Zulfugarov, I. S., Aliev, J. A., Ismayilov, M. A., Novruzova, S. N., Savchenko, T. V., Suleimanov, Yu. S., Bartošková, Hana, Nauš, Jan, Ilík, Petr, Kouřil, Roman, Vidyasagar, P. B., Thomas, Sarah, Gaikwad, Jvoti U., Cseh, Z., Mustárdy, L., Garab, G., Simidjiev, I., Rajagopal, S., Várkonyi, Zs., Holzenburg, A., Stoylova, S., Papp, E., Millar, D. P., Bruder, R., Woo, T. T., Genick, U. K., Gerwert, K., Jávorfí, Tamás, Garab, Győző, Naqvi, Razi K., Gaikwad, Jyoti, Kalimullah, Md., Semwal, Manoj, Naus, Man, Ilik, Petr, Kouril, Roman, Horváth, Gábor, Bernard, Gary D., Pomozi, István, Wehner, Rüdiger, Damjanović, Ana, Schulten, Klaus, Ritz, Thorsten, Yandao, Gong, Jushuo, Wang, Nanming, Zhao, Jixiu, Shan, Freiberg, Arvi, Timpmann, Kõu, Woodbury, Neal W., Ruus, Rein, Nemtseva, E. V., Kudryasheva, N. S., Sizykh, A. G., Tikhomirov, A. A., Nesterenko, T. V., Shikhov, V. N., Forti, Giorgio, Furia, Alberto, Finazzi, Giovanni, Barbagallo, Romina Paola, Agalarov, R., Gasanov, R., Iskenderova, S., Nobuhiro, G. O., Osamu, Miyashita, Ramrakhiani, M., Soni, R. K., Yoshida, Masasuke, Akutsu, Hideo, Yagi, Hiromasa, Tozawa, Kacko, Sekino, Nobuaki, Iwabuchi, Tomoyuki, Kaulen, A. D., Avetisyan, A. V., Feniouk, B. A., Skulachev, V. P., Breyton, Cécile, Kühlbrandt, Werner, Gräslund, Astrid, Assarsson, Maria, Libisch, B., Horváth, G., Gombos, Z., Budagovskaya, N. V., Kudryasheva, N., Fukunishi, Arima, Harada, Erisa, Fukuoka, Yuki, Ohmura, Tomoaki, Kawai, Gota, Watanabe, Kimitsuna, Žekš, Boštjan, Božič, Bojan, Derganc, Jure, Svetina, Saša, Hoh, J. F. Y., Li, Z. B., Rossmanith, G. H., Frederix, P. L. T. M., de Beer, E. L., Treijtel, B. W., Blangè, T., Galtet, F., Hénon, S., Isabey, D., Planus, E., Laurent, V., Rath, L. S., Raval, M. K., Dash, P. K., Ramakrishnan, C., Balaram, R., Basak, Kanika, Balaban, Alexandra T., Nandy, Ashesh, Grunwald, Gregory D., Vracko, Marjan, Randic, Milan, Basak, Subhash C., Amic, Dragan, Beslo, Drago, Trinajstic, Nenad, Nikolic, Sonja, Walahaw, J., Lensink, Marc F. J., Reddy, Boojala V. B., Shindylov, Ilya N., Bourne, Philip E., Grigera, J. R., de Xammar Oro, J., Donnamaria, M. C., Neagu, Monica, Neagu, Adrian, Janežič, Dušanka, Praprotnik, Matej, Nilsson, Lennart, Mark, Pekka, Fata, La L., Dardenne, Laurent E., Werneck, Araken S., Neto, Marçal de O., Kannan, N., Vishveshwara, S., Veluraja, K., Opitz, David, Balasubramanian, Krishnan, Gute, Brian D., Mills, Denise, Lungeanu, Diana, Mihalas, G. I., Macovievici, G., Gruia, Raluca, Dalcin, B., Cortez-Maghelly, C., Passos, E. P., Ljubisavljevic, M., Blesic, S., Milosevic, S., Stratimirovic, D. J., Bachhawat, Nandita, Mande, Shekhar C., Nandy, A., Nishigaki, Koichi, Saito, Ayumu, Naimuddin, Mohammed, Takaesu, Hirotomo, Ono, Mitsuo, Hirokawa, Takatsugu, Eissa, A. M., Ahmed, Abdalla S., El Gohary, M. I., Nakashima, Hiroshi, Raghava, G. P. S., Kurgalvuk, N., Goryn, O., Gerstman, Bernard S., Kratasyuk, V. A., Esimbekova, E. N., Gritsenko, E. V., Remmel, N. N., Maznyak, O. M., German, A., Tikhonov, A., Tchitchkan, D., Koulchitsky, S., Pashkevich, S., Pletnev, S., Kulchitsky, V., Pesotskaya, Y., Shapiro, Erik M., Borthakur, Arijitt, Dimitrov, Ivan, Leigh, John S., Rizi, Rahim, Reddy, Ravinder, Charagundla, Sridhar, Duvvuri, Umamaheswar, Degaonkar, M., Khubchandani, M., Kumar, Mahesh, Jagannathan, N R., Raghunathan, P., Jayasundar, Rama, Coshic, O., Rath, O. K., Julka, P. K., Iliescu, Karina Roxana, Sajin, Maria, Petcu, Ileana, Moisoi, Nicolcta, Kuzmenko, A. I., Donchenko, G. V., Nikolenko, I. A., Morozova, R. P., Rahman, M. K., Ahmed, M. M., Watanabe, Takehiro, Uretzky, G., Ammar, R., Sharony, R., Rubin, Y., Gilboa, H., Mallick, H. N., Kumar, Mohan V., Begum, Gulnaz M., Degaonkar, Mahaveer N., Govindasamy, S., Kumosani, T. A., Lupusoru, C., Titescu, G., Haulica, I., Stefanescu, I., Iliescu, R., Nastasa, V., Bild, W., Khetawat, Gopal, Nealen, M., Faraday, N., Bray, P. F., Noga, S., Lycholat, E. A., Ananieva, T. V., Kosevich, M V., Stepanyan, S. G., Antonyuk, S. V., Khachatryan, A., Kumar, A., Arakelian, H., Khachatryan, R., Agadjanyan, S., Ayrapetyan, S., Mkheyan, V., Rajan, S. S., Kabaleeswaran, V., Gopalakrishnan, Geetha, Govindachari, T. R., Ramrakhiani, Meera, Cullen, David C., Lowe, Phillip, Badley, Andrew, Hermel, H., Möhwald, H., Schmahl, W., Singh, Anil K., Das, Joydip, Majumdar, Nirmalya, Dér, András, Oroszi, László, Kelemen, Loránd, Ormos, Pál, Hámori, András, Ramsden, Jeremy J., Mitra, Chanchal K., Savitri, D., Yanagida, Toshio, Esaki, Seiji, Sowa, Yosiyuki, Nishida, Tomoyuki, Kimura, Yuji, Radu, M., Laukhina, E. E., Kasumova, L. A., Koltover, V. K., Bubnov, V. P., Estrin, Ya. I., Dotta, Rajiv, Zahradník, Ivan, Marko, Milan, Novák, Pavel, Miyata, Hidetake, Hirata, Hiroaki, Sengupta, P., Maiti, S., Balaji, J., Banerjee, S., Barker, A. L., Winlove, C. P., OʼHare, D., Macpherson, J. V., Gonsalves, M., Unwin, P. R., Phillip, R., Kumar, Ravindra G., Murata, K., Nagayaka, K., Danev, R., Sugitani, S., Gősch, Michael, Thyberg, P., Földes-Papp, Z., Björk, G., Blom, H., Holm, J., Heino, T., Inagaki, Fuyuhiko, Yokochi, Masashi, Kusunoki, Masami, Matthews, E. K., Pines, J., Chukova, Yu. P., Koltover, Vitaly K., Kang, B. P. S., Bansal, Geetanjali, Bansal, M. P., Singh, U., Singh, Uma, Nakata, Kotoko, Nakano, Tastuya, Kaminuma, Tsuguchika, Kirn, Bonn, Potocnik, Neja, Stare, Vito, Shukla, Latal, Sastry, M. D., Natarajan, V., Devasagayam, T. P. A., Kesavan, P. C., Sayfutdinov, R., Degermendzhy, A. G., Adamovich, V. V., Rogozin, Yu. D., Khetrapal, C. L., Gowda, G. A. Nagana, Ghimire, Kedar Nath, Masaru, Ishida, Fujita, H., Ishiwata, S., Suzuki, M., Kawahara, S., Kirino, Y., Kishimoto, Y., Mori, H., Mishina, M., Ohshima, H., Dukhin, A. S., Goetz, P. J., Shilov, V. N., and Mishra, R. K.
- Published
- 1999
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21. Determinants of neuroglobin plasticity highlighted by high pressure crystallography and crystallography under moderate gas pressure
- Author
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Colloc'h, N, Girard, E, Prangé, T, Carpentier, P, Sacquin-Mora, S, Vallone, B, Brunaud, Carole, Imagerie et Stratégies Thérapeutiques des pathologies Cérébrales et Tumorales (ISTCT), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), European Synchrotron Radiation Facility (ESRF), Couteau, Florence, and Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)
- Subjects
[SDV] Life Sciences [q-bio] ,[SDV]Life Sciences [q-bio] - Abstract
CERVOXY COLL; International audience
- Published
- 2018
22. Crystal structure of murine neuroglobin bound to CO at 15K under illumination using optical fiber
- Author
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Savino, C., primary, Montemiglio, L.C., additional, Ardiccioni, C., additional, Exertier, C., additional, and Vallone, B., additional
- Published
- 2019
- Full Text
- View/download PDF
23. Carbomonoxy murine neuroglobin F106A mutant
- Author
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Exertier, C., primary, Vallone, B., additional, Savino, C., additional, Freda, I., additional, Montemiglio, L.C., additional, Cerutti, G., additional, Scaglione, A., additional, and Parisi, G., additional
- Published
- 2019
- Full Text
- View/download PDF
24. Ferric murine neuroglobin F106A mutant
- Author
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Exertier, C., primary, Vallone, B., additional, Savino, C., additional, Freda, I., additional, Montemiglio, L.C., additional, Cerutti, G., additional, Scaglione, A., additional, and Parisi, G., additional
- Published
- 2019
- Full Text
- View/download PDF
25. Ferric murine neuroglobin Gly-loop mutant
- Author
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Exertier, C., primary, Vallone, B., additional, Savino, C., additional, Freda, I., additional, Montemiglio, L.C., additional, Cerutti, G., additional, Scaglione, A., additional, and Parisi, G., additional
- Published
- 2019
- Full Text
- View/download PDF
26. Carbomonoxy murine neuroglobin Gly-loop mutant
- Author
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Exertier, C., primary, Vallone, B., additional, Savino, C., additional, Freda, I., additional, Montemiglio, L.C., additional, Cerutti, G., additional, Scaglione, A., additional, and Parisi, G., additional
- Published
- 2019
- Full Text
- View/download PDF
27. Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex at 5.5 Angstrom resolution.
- Author
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Testi, C., primary, Montemiglio, L.C., additional, Vallone, B., additional, Des Georges, A., additional, Boffi, A., additional, Mancia, F., additional, and Baiocco, P., additional
- Published
- 2019
- Full Text
- View/download PDF
28. Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex.
- Author
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Testi, C., primary, Montemiglio, L.C., additional, Vallone, B., additional, Des Georges, A., additional, Boffi, A., additional, Mancia, F., additional, Baiocco, P., additional, and Savino, C., additional
- Published
- 2019
- Full Text
- View/download PDF
29. Probing Conformational Transitions in Interface α1β2 of Human Hemoglobin by Site-Directed Mutagenesis
- Author
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Vallone, B., primary, Cavalli, V., additional, and Brunori, M., additional
- Published
- 1993
- Full Text
- View/download PDF
30. Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography
- Author
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Colloc'h, N., Sacquin-Mora, S., Avella, G., Dhaussy, A.C., Prangé, T., Vallone, B., Girard, E., Imagerie et Stratégies Thérapeutiques des pathologies Cérébrales et Tumorales ( ISTCT ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ), Laboratoire de biochimie théorique [Paris] ( LBT ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Department of Biochemical Sciences, Università degli Studi di Roma 'La Sapienza' [Rome]-Réseau International des Instituts Pasteur ( RIIP ) -Institut Pasteur - Fondation Cenci Bolognetti, Laboratoire de cristallographie et sciences des matériaux ( CRISMAT ), Centre National de la Recherche Scientifique ( CNRS ) -Ecole Nationale Supérieure d'Ingénieurs de Caen ( ENSICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ) -Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ), Laboratoire de cristallographie et RMN biologiques ( LCRB - UMR 8015 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de biologie structurale ( IBS - UMR 5075 ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ) -Université Joseph Fourier - Grenoble 1 ( UJF ), Imagerie et Stratégies Thérapeutiques des pathologies Cérébrales et Tumorales (ISTCT), Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de biochimie théorique [Paris] (LBT (UPR_9080)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Institut de biologie physico-chimique (IBPC (FR_550)), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Laboratoire de cristallographie et sciences des matériaux (CRISMAT), École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC), Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7)-Institut de biologie physico-chimique (IBPC), Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Université de Caen Normandie (UNICAEN), Normandie Université (NU), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Hypoxie, physiopathologies cérébrovasculaire et tumorale ( CERVOxy ), Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biochimie Théorique, CNRS UPR9080, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005, Paris, France., Centre National de la Recherche Scientifique ( CNRS ), Instituto Pasteur-Fondazione Cenci Bolognetti and Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Sapienza Università di Roma, 5 piazzale Aldo Moro, 00185, Roma, Italy., Université de Rome la Sapienza, BIOGEM Research Institute, Ariano Irpino, Italy., Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Institut de biologie physico-chimique (IBPC (FR_550)), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche sur les Matériaux Avancés (IRMA), Normandie Université (NU)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Rouen Normandie (UNIROUEN), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
- Subjects
Models, Molecular ,Neuroglobin ,high-pressure crystallography ,protein structural dynamics ,synchrotron ,Protein Conformation ,Science ,Biophysics ,Heme ,PRESSURE ,Crystallography, X-Ray ,Article ,Mice ,Structure-Activity Relationship ,Pressure ,PROTEIN CRYSTAL STRUCTURE ANALYSIS ,Computational models ,Animals ,Humans ,X-ray crystallography ,[ SDV ] Life Sciences [q-bio] ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM] ,Mutation ,PROTEIN CRYSTALLOGRAPHER ,Medicine ,[ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM] - Abstract
CERVOXY; International audience; Investigating the effect of pressure sheds light on the dynamics and plasticity of proteins, intrinsically correlated to functional efficiency. Here we detail the structural response to pressure of neuroglobin (Ngb), a hexacoordinate globin likely to be involved in neuroprotection. In murine Ngb, reversible coordination is achieved by repositioning the heme more deeply into a large internal cavity, the “heme sliding mechanism”. Combining high pressure crystallography and coarse-grain simulations on wild type Ngb as well as two mutants, one (V101F) with unaffected and another (F106W) with decreased affinity for CO, we show that Ngb hinges around a rigid mechanical nucleus of five hydrophobic residues (V68, I72, V109, L113, Y137) during its conformational transition induced by gaseous ligand, that the intrinsic flexibility of the F-G loop appears essential to drive the heme sliding mechanism, and that residue Val 101 may act as a sensor of the interaction disruption between the heme and the distal histidine.
- Published
- 2017
31. Structural and functional characterization of OleP in complex with 6DEB in sodium formate
- Author
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Parisi, G., primary, Savino, C., additional, Montemiglio, L.C., additional, and Vallone, B., additional
- Published
- 2018
- Full Text
- View/download PDF
32. metNeuroglobin under oxygen at 50 bar
- Author
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Prange, T., primary, Colloc'h, N., additional, Carpentier, P., additional, and Vallone, B., additional
- Published
- 2017
- Full Text
- View/download PDF
33. Crystal structure of murine neuroglobin under 100 bar krypton
- Author
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Colloc'h, N., primary, Prange, T., additional, Vallone, B., additional, and Carpentier, P., additional
- Published
- 2017
- Full Text
- View/download PDF
34. Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure
- Author
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Savino, C., primary, Vallone, B., additional, Scaglione, A., additional, Parisi, G., additional, Montemiglio, L.C., additional, Fullone, M.R., additional, and Grgurina, I., additional
- Published
- 2017
- Full Text
- View/download PDF
35. Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, apo structure
- Author
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Savino, C., primary, Vallone, B., additional, Scaglione, A., additional, Parisi, G., additional, Montemiglio, L.C., additional, Fullone, M.R., additional, and Grgurina, I., additional
- Published
- 2017
- Full Text
- View/download PDF
36. Time-resolved X-ray scattering as a tool to probe heme proteins structural dynamics in solution
- Author
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LEVANTINO, Matteo, CUPANE, Antonio, Cammarata, M, Vallone, B, Brunori, M, Levantino, M, Cammarata, M, Vallone, B, Brunori, M, and Cupane, A.
- Subjects
Dynamic Structural Science ,Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) - Abstract
Time-resolved wide-angle X-ray scattering (TR-WAXS) is a recently developed technique allowing to probe global structural changes of proteins in solution. We have used TR-WAXS to investigate large conformational changes of heme proteins (wild-type and mutant hemoglobin, neuroglobin, etc.) that cannot take place when these macromolecules are in a crystalline environment. Our data revealed detailed information on kinetic and thermodynamic properties of the investigated proteins and demonstrate the potentiality of the TR-WAXS technique.
- Published
- 2013
37. Neuroglobin-Prion protein interaction: what’s the function?
- Author
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Palladino P., Scaglione G. L., Arcovito A., Vitale R. M., Amodeo P., Vallone B., Brunori M., Benedetti E., ROSSI, FILOMENA, Ettore Benedetti, P., Palladino, G. L., Scaglione, A., Arcovito, R., Vitale, P., Amodeo, B., Vallone, M., Brunori, E., Benedetti, Rossi, Filomena, Palladino, P., Scaglione, G. L., Arcovito, A., Vitale, R. M., Amodeo, P., Vallone, B., Brunori, M., and Benedetti, E.
- Subjects
neuroglobin ,neuroglobina ,prion protein ,peptidi sintetici ,proteina prionica ,MD ,molecular recognition - Abstract
Neuroglobin and cellular prion protein (PrPC) are expressed in the nervous system and co-localized in the retinal ganglion cell layer. Both proteins do not have an unambiguously assigned function, and it was recently reported that PrPC aggregates rapidly in the presence of neuroglobin, whereas it does not aggregate in the presence of myoglobin, another globin with different tissue specificity. Electrostatic complementarity between the unstructured PrPCN-terminus and neuroglobin has been proposed to mediate this specific interaction. To verifythis hypothesis experimentally, we have used a combined approach of automated docking and molecular dynamics (MD) studies carried out on short stretches of prion protein (PrP) N-terminus to identify the minimal electrostatically interacting aminoacidic sequences with neuroglobin. Subsequently, we have performed the synthesis of these peptides by solid phase methods, and we tested their interaction with neuroglobin by surface plasmon resonance (SPR). Preliminary results confirm unequivocally the specific interaction between synthetic PrP peptides and neuroglobin suggesting a crucial role of PrPC positively charged regions in thisprotein–protein association.
- Published
- 2010
38. Crystal structure of murine neuroglobin at ambient pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, and Vallone, B., additional
- Published
- 2016
- Full Text
- View/download PDF
39. Crystal structure of murine neuroglobin mutant V101F at ambient pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
40. Crystal structure of murine neuroglobin at 310 MPa pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
41. Crystal structure of murine neuroglobin mutant F106W at 310 MPa pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
42. Crystal structure of murine neuroglobin mutant F106W at 280 MPa pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
43. Crystal structure of murine neuroglobin at 270 MPa pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
44. Crystal structure of murine neuroglobin mutant F106W at ambient pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
45. Crystal structure of murine neuroglobin mutant V101F at 150 MPa pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
46. Crystal structure of murine neuroglobin mutant V101F at 240 MPa pressure
- Author
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Colloc'h, N., primary, Girard, E., additional, Vallone, B., additional, and Prange, T., additional
- Published
- 2016
- Full Text
- View/download PDF
47. Structure of the adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in streptomyces sp. Oh-5093, ligand bound structure
- Author
-
Savino, C., primary, Scaglione, A., additional, Montemiglio, L.C., additional, Parisi, G., additional, Grgurina, I., additional, Fullone, M.R., additional, and Vallone, B., additional
- Published
- 2016
- Full Text
- View/download PDF
48. Structure of the adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in streptomyces sp. Oh-5093, apo structure
- Author
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Savino, C., primary, Scaglione, A., additional, Montemiglio, L.C., additional, Parisi, G., additional, Grgurina, I., additional, Fullone, M.R., additional, and Vallone, B., additional
- Published
- 2016
- Full Text
- View/download PDF
49. Investigating the structural plasticity of a cytochrome P450: 3D structure of EryK and binding to its physiological substrate and inhibitors
- Author
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Montemiglio, LC [ 1 ], Vallone, B [ 1 ], Gianni, S [ 2 ], and Savino, C
- Published
- 2011
50. Neuroglobin-prion protein interaction: what's the function?
- Author
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Palladino P, Scaglione GL, Arcovito A, Vitale RM, Amodeo P, Vallone B, Brunori M, Benedetti E, and Rossi F.
- Subjects
animal diseases ,nervous system diseases - Abstract
Neuroglobin and cellular prion protein (PrPC) are expressed in the nervous system and co-localized in the retinal ganglion cell layer. Both proteins do not have an unambiguously assigned function, and it was recently reported that PrPC aggregates rapidly in the presence of neuroglobin, whereas it does not aggregate in the presence of myoglobin, another globin with different tissue specificity. Electrostatic complementarity between the unstructured PrPC N-terminus and neuroglobin has been proposed to mediate this specific interaction. To verify this hypothesis experimentally, we have used a combined approach of automated docking and molecular dynamics (MD) studies carried out on short stretches of prion protein (PrP) N-terminus to identify the minimal electrostatically interacting aminoacidic sequences with neuroglobin. Subsequently, we have performed the synthesis of these peptides by solid phase methods, and we tested their interaction with neuroglobin by surface plasmon resonance (SPR). Preliminary results confirm unequivocally the specific interaction between synthetic PrP peptides and neuroglobin suggesting a crucial role of PrPC positively charged regions in this proteinprotein association.
- Published
- 2011
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