Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Victoria A Feher"'
Autor:
Victoria A Feher, Arlo Randall, Pierre Baldi, Robin M Bush, Luis M de la Maza, Rommie E Amaro
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e68934 (2013)
Chlamydia trachomatis is the most prevalent cause of bacterial sexually transmitted diseases and the leading cause of preventable blindness worldwide. Global control of Chlamydia will best be achieved with a vaccine, a primary target for which is the
Externí odkaz:
https://doaj.org/article/bee4dddb0a6b4a688b0735296995d89d
Autor:
Mads Gabrielsen, Katherine S H Beckham, Victoria A Feher, Caroline E Zetterström, Dai Wang, Sylke Müller, Mikael Elofsson, Rommie E Amaro, Olwyn Byron, Andrew J Roe
Publikováno v:
PLoS ONE, Vol 7, Iss 2, p e32217 (2012)
Thiol peroxidase, Tpx, has been shown to be a target protein of the salicylidene acylhydrazide class of antivirulence compounds. In this study we present the crystal structures of Tpx from Y. pseudotuberculosis (ypTpx) in the oxidised and reduced sta
Externí odkaz:
https://doaj.org/article/f1d1bcf768034b47ad2805c83446d23a
Autor:
Samantha Ottavi, Sarah M. Scarry, John Mosior, Yan Ling, Julia Roberts, Amrita Singh, David Zhang, Laurent Goullieux, Christine Roubert, Eric Bacqué, H. Rachel Lagiakos, Jeremie Vendome, Francesca Moraca, Kelin Li, Andrew J. Perkowski, Remya Ramesh, Matthew M. Bowler, William Tracy, Victoria A. Feher, James C. Sacchettini, Ben S. Gold, Carl F. Nathan, Jeffrey Aubé
Publikováno v:
Journal of Medicinal Chemistry. 65:1996-2022
Autor:
Christopher Higgs, Victoria A. Feher, Ishita Aloni, Kyle Marshall, Piotr Rotkiewicz, Daniel Cappel, Gerhard Hessler, Matthew P. Repasky, Hans Matter, Eric Feyfant, Anatoly M. Ruvinsky
Publikováno v:
ChemMedChem. 13:2684-2693
Mechanisms of protein-carbohydrate recognition attract a lot of interest due to their roles in various cellular processes and metabolism disorders. We have performed a large-scale analysis of protein structures solved in complex with glucose, galacto
Capturing Invisible Motions in the Transition from Ground to Rare Excited States of T4 Lysozyme L99A
Publikováno v:
Biophysical journal, vol 111, iss 8
Proteins commonly sample a number of conformational states to carry out their biological function, often requiring transitions from the ground state to higher-energy states. Characterizing the mechanisms that guide these transitions at the atomic lev
Autor:
Kristian Jensen, Wayne Tang, Mary Grimes, David Calkins, W. George Lai, Sayan Mondal, Victoria A. Feher, Jeff Bell, Wu Yin, Fiona M. McRobb, Shulu Feng, Michael Trzoss, Goran Krilov, Hamish Wright, Andrew Placzek, Robert Pelletier, Morgan Lawrenz, Nie Zhe, Aleksey Gerasyuto, Karen Akinsanya
Publikováno v:
Blood. 136:30-30
Introduction: MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1), was identified as a translocation protein fused with cIAP2 in mucosa-associated lymphoid tissue (MALT) B cell lymphomas. MALT1, a key mediator of NF-κB signali
Autor:
Robert D. Malmstrom, Rommie E. Amaro, Jeffrey R. Wagner, Jacob D. Durrant, Victoria A. Feher, Christopher T. Lee
Publikováno v:
Chemical Reviews
Allosteric drug development holds promise for delivering medicines that are more selective and less toxic than those that target orthosteric sites. To date, the discovery of allosteric binding sites and lead compounds has been mostly serendipitous, a
Autor:
Rommie E. Amaro, Nathan Mih, Daniel J. Mermelstein, Victoria A. Feher, J. Andrew McCammon, Levi C. T. Pierce, Jamie M. Schiffer
Publikováno v:
Biophysical journal, vol 116, iss 2
The atomic-level mechanisms that coordinate ligand release from protein pockets are only known for a handful of proteins. Here, we report results from accelerated molecular dynamics simulations for benzene dissociation from the buried cavity of the T
Autor:
Shuai Liu, Rommie E. Amaro, Michael Chiu, Chenghua Shao, Markus G. Rudolph, W. Patrick Walters, Bernd Kuhn, Victoria A. Feher, Stephen K. Burley, Zied Gaieb, Michael K. Gilson, Symon Gathiaka, Huanwang Yang
The Drug Design Data Resource (D3R) ran Grand Challenge 2 (GC2) from September 2016 through February 2017. This challenge was based on a dataset of structures and affinities for the nuclear receptor farnesoid X receptor (FXR), contributed by F. Hoffm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cc3af3963874d770a5972effd5f46f7
https://europepmc.org/articles/PMC5767524/
https://europepmc.org/articles/PMC5767524/
Gaussian Accelerated Molecular Dynamics: Unconstrained Enhanced Sampling and Free Energy Calculation
Publikováno v:
Journal of chemical theory and computation, vol 11, iss 8
Journal of Chemical Theory and Computation
Miao, Y; Feher, VA; & McCammon, JA. (2015). Gaussian Accelerated Molecular Dynamics: Unconstrained Enhanced Sampling and Free Energy Calculation. Journal of Chemical Theory and Computation, 11(8), 3584-3595. doi: 10.1021/acs.jctc.5b00436. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/3hn7r4rv
Journal of Chemical Theory and Computation
Miao, Y; Feher, VA; & McCammon, JA. (2015). Gaussian Accelerated Molecular Dynamics: Unconstrained Enhanced Sampling and Free Energy Calculation. Journal of Chemical Theory and Computation, 11(8), 3584-3595. doi: 10.1021/acs.jctc.5b00436. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/3hn7r4rv
© 2015 American Chemical Society. A Gaussian accelerated molecular dynamics (GaMD) approach for simultaneous enhanced sampling and free energy calculation of biomolecules is presented. By constructing a boost potential that follows Gaussian distribu