Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Manasi A. Pethe"'
Publikováno v:
PLoS Computational Biology, Vol 13, Iss 6, p e1005614 (2017)
Multispecificity-the ability of a single receptor protein molecule to interact with multiple substrates-is a hallmark of molecular recognition at protein-protein and protein-peptide interfaces, including enzyme-substrate complexes. The ability to per
Externí odkaz:
https://doaj.org/article/ce70dcfad2324096a4b4914339068a33
Publikováno v:
Journal of Molecular Biology. 429:220-236
Characterizing the substrate specificity of protease enzymes is critical for illuminating the molecular basis of their diverse and complex roles in a wide array of biological processes. Rapid and accurate prediction of their extended substrate specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::152f316f44aa962df8b83e7981d629da
https://doi.org/10.1016/j.jmb.2016.11.031
https://doi.org/10.1016/j.jmb.2016.11.031
Autor:
Jack Maguire, Ragul Gowthaman, Marion F. Sauer, Georg Kuenze, Tanja Kortemme, Benjamin Basanta, Indigo Chris King, Jens Meiler, Rhiju Das, Ora Schueler-Furman, Nicholas A. Marze, Brandon Frenz, Christoffer Norn, Julia Koehler Leman, Jason W. Labonte, Kala Bharath Pilla, Lei Shi, Sergey Lyskov, Brian D. Weitzner, Nir London, Karen R. Khar, Jaume Bonet, Nawsad Alam, Andreas Scheck, Alexander M. Sevy, Lars Malmström, Thomas Huber, Christopher Bystroff, Lior Zimmerman, Lorna Dsilva, Bruno E. Correia, Roland L. Dunbrack, Sergey Ovchinnikov, Rocco Moretti, Scott Horowitz, Phil Bradley, Frank DiMaio, Noah Ollikainen, Brian Kuhlman, Jeffrey J. Gray, Melanie L. Aprahamian, Andrew Leaver-Fay, Santrupti Nerli, Brian Koepnick, Xingjie Pan, Manasi A. Pethe, Andrew M. Watkins, Summer B. Thyme, Enrique Marcos, Vikram Khipple Mulligan, Hahnbeom Park, Po-Ssu Huang, David K. Johnson, Daniel-Adriano Silva, Patrick Barth, Shannon Smith, Caleb Geniesse, Jason K. Lai, Patrick Conway, Amelie Stein, Jeliazko R. Jeliazkov, David Baker, Dominik Gront, Kalli Kappel, Firas Khatib, Robert Kleffner, Brian J. Bender, Richard Bonneau, Kyle A. Barlow, Joseph H. Lubin, Shourya S. Roy Burman, Nikolaos G. Sgourakis, Yuval Sedan, Ryan E. Pavlovicz, Kristin Blacklock, Seth Cooper, Barak Raveh, Alisa Khramushin, John Karanicolas, Justin B. Siegel, Sharon L. Guffy, Brian G. Pierce, Alex Ford, Darwin Y. Fu, Orly Marcu, Gideon Lapidoth, Brian Coventry, René M. de Jong, Shane O’Conchúir, Thomas W. Linsky, William R. Schief, Rebecca F. Alford, Scott E. Boyken, Sagar D. Khare, Maria Szegedy, Ray Yu-Ruei Wang, Steven M. Lewis, Hamed Khakzad, Timothy M. Jacobs, Frank D. Teets, Lukasz Goldschmidt, Daisuke Kuroda, Steffen Lindert, P. Douglas Renfrew, Yifan Song, Jared Adolf-Bryfogle, Michael S. Pacella, Aliza B. Rubenstein
Publikováno v:
Nat Methods
The Rosetta software for macromolecular modeling, docking and design is extensively used in laboratories worldwide. During two decades of development by a community of laboratories at more than 60 institutions, Rosetta has been continuously refactore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c561276e840d68005d2aab06fb9642da
https://pubmed.ncbi.nlm.nih.gov/32483333
https://pubmed.ncbi.nlm.nih.gov/32483333
Autor:
He Chen, Chuan Kao, Beidi Lu, Ronald M. Levy, Manasi A. Pethe, Yijie Niu, Peng He, Jie Zhu, Fitzgerald Michael, Yang Gao, Malathi Kalyanikar, Haoyuan Chen, Emilio Gallicchio
Publikováno v:
Journal of Computer-Aided Molecular Design. 29:315-325
The Binding Energy Distribution Analysis Method (BEDAM) protocol has been employed as part of the SAMPL4 blind challenge to predict the binding free energies of a set of octa-acid host-guest complexes. The resulting predictions were consistently judg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85d3035b00fccafddc679adb8f5e908d
https://doi.org/10.1007/s10822-014-9795-2
https://doi.org/10.1007/s10822-014-9795-2
Biophysical interactions between proteins and peptides are key determinants of genotype-fitness landscapes, but an understanding of how molecular structure and residue-level energetics at protein-peptide interfaces shape functional landscapes remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb11eb243db26b45da5ac163c20708fa
https://doi.org/10.1101/172197
https://doi.org/10.1101/172197
Publikováno v:
PLoS Computational Biology
PLoS Computational Biology, Vol 13, Iss 6, p e1005614 (2017)
PLoS Computational Biology, Vol 13, Iss 6, p e1005614 (2017)
Multispecificity–the ability of a single receptor protein molecule to interact with multiple substrates–is a hallmark of molecular recognition at protein-protein and protein-peptide interfaces, including enzyme-substrate complexes. The ability to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d4fd4adb3941d4b91b945e81a68bdef
http://europepmc.org/articles/PMC5507473
http://europepmc.org/articles/PMC5507473
Publikováno v:
Biophysical Journal. 110:345a
The substrate specificity of protease enzymes constitutes the molecular basis of their diverse and complex biological roles. Rapid and accurate prediction of extended substrate specificity would also enable the design of custom enzymes capable of sel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fbf0a2f6301584f5d31b0ae7a50664e
https://doi.org/10.1016/j.bpj.2015.11.1858
https://doi.org/10.1016/j.bpj.2015.11.1858