Zobrazeno 1 - 10
of 229
pro vyhledávání: '"Joël Janin"'
Publikováno v:
IUCrJ, Vol 2, Iss 6, Pp 643-652 (2015)
Protein interactions are essential in all biological processes. The changes brought about in the structure when a free component forms a complex with another molecule need to be characterized for a proper understanding of molecular recognition as wel
Externí odkaz:
https://doaj.org/article/690dc8ee6ce7415699362ddf4771cdde
Autor:
Joël Janin
Publikováno v:
Protein Science. 23:1813-1817
A minimal model of protein-protein binding affinity that takes into account only two structural features of the complex, the size of its interface, and the amplitude of the conformation change between the free and bound subunits, is tested on the 144
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c41555183476e808e31bbe1a86ca7cb5
https://doi.org/10.1002/pro.2560
https://doi.org/10.1002/pro.2560
Autor:
Joël Janin
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:2075-2081
Eight CAPRI prediction rounds with a total of 15 targets were held in the years 2010–2012. Only five of the targets were protein assemblies comparable with those of earlier CAPRI rounds. In one target, the solvent positions at the interface had to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::579a7101a688767c89a05e896869bb98
https://doi.org/10.1002/prot.24375
https://doi.org/10.1002/prot.24375
Publikováno v:
Protein Science. 22:1655-1663
Oligomeric proteins are more abundant in nature than monomeric proteins, and involved in all biological processes. In the absence of an experimental structure, their subunits can be modeled from their sequence like monomeric proteins, but reliable pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fb166452957860622b19e82d6e1f149
https://doi.org/10.1002/pro.2361
https://doi.org/10.1002/pro.2361
Publikováno v:
Protein Science. 22:1453-1457
The buried surface area (BSA), which measures the size of the interface in a protein-protein complex may differ from the accessible surface area (ASA) lost upon association (which we call DSA), if conformation changes take place. To evaluate the DSA,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d5bd6de96919d464451f536cd060cdf
https://doi.org/10.1002/pro.2330
https://doi.org/10.1002/pro.2330
Autor:
Howook Hwang, Shiyong Liu, Xiaoqin Zou, Huan-Xiang Zhou, Hideaki Umeyama, Paul A. Bates, Hahnbeom Park, Yangyu Huang, Xiaolei Zhu, Marianne Rooman, Rudi Agius, David Baker, Sarel J. Fleishman, Dimitri Gillis, Eiji Kanamori, Yuko Tsuchiya, Sandor Vajda, Panagiotis L. Kastritis, Brian Jimenez, Thom Vreven, Xiufeng Yang, Hiromitsu Shimoyama, Nan Zhao, Zhiping Weng, Sheng-You Huang, Mikael Trellet, Chaok Seok, Samuel C. Flores, Miguel Romero-Durana, Sanbo Qin, Michael S. Pacella, Julie C. Mitchell, Mayuko Takeda-Shitaka, Dmitri Beglov, Jeffrey J. Gray, Shoshana J. Wodak, Rocco Moretti, Martin Zacharias, Dmitry Korkin, Dima Kozakov, João P. G. L. M. Rodrigues, Haruki Nakamura, Juan Esquivel-Rodríguez, Mieczyslaw Torchala, Yves Dehouck, Alexandre M. J. J. Bonvin, David R. Hall, Mitsuo Iwadate, Krishna Praneeth Kilambi, Jamica Sarmiento, Daron M. Standley, Joël Janin, Omar N. A. Demerdash, Brian G. Pierce, Chiara Pallara, Meng Cui, Shusuke Teraguchi, Petr Popov, Hasup Lee, Haotian Li, Juan Fernández-Recio, Laura Pérez-Cano, Sergei Grudinin, Sameer Velankar, Daisuke Kihara, Xiaofeng Ji, Genki Terashi, Yi Xiao, Shide Liang, Iain H. Moal
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 81:1980-1987
Community-wide blind prediction experiments such as CAPRI and CASP provide an objective measure of the current state of predictive methodology. Here we describe a community-wide assessment of methods to predict the effects of mutations on protein-pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c35f351f56e60c23e4c4383987063979
https://doi.org/10.1002/prot.24356
https://doi.org/10.1002/prot.24356
Autor:
Joël Janin, Shoshana J. Wodak
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:357-358
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::458c9d8869596e5aec9fce770e20533e
https://doi.org/10.1002/prot.25233
https://doi.org/10.1002/prot.25233
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:2861-2870
We perform an analysis of the quaternary structure and dimer/dimer interface in the crystal structures of 165 human hemoglobin tetramers; 112 are in the T, 17 the R, 14 the Y (or R2) state; 11 are high-affinity T state mutants, and 11 may either be i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::253b371a0ff4f8347f8659d7fd24df50
https://doi.org/10.1002/prot.23112
https://doi.org/10.1002/prot.23112
Autor:
Iain H. Moal, Paul A. Bates, Zhiping Weng, Alexandre M. J. J. Bonvin, Panagiotis L. Kastritis, Howook Hwang, Joël Janin
Publikováno v:
Protein Science. 20:482-491
We have assembled a nonredundant set of 144 protein–protein complexes that have high-resolution structures available for both the complexes and their unbound components, and for which dissociation constants have been measured by biophysical methods
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f49c2b85d3e099141f5efff80a45a28
https://doi.org/10.1002/pro.580
https://doi.org/10.1002/pro.580
Autor:
Joël Janin
Publikováno v:
Crystallography Reviews. 20:233-235
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77ba98495354a67b675b84572403c62d
https://doi.org/10.1080/0889311x.2014.882330
https://doi.org/10.1080/0889311x.2014.882330