Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Christopher L McClendon"'
Autor:
Hiruy S Meharena, Xiaorui Fan, Lalima G Ahuja, Malik M Keshwani, Christopher L McClendon, Angela M Chen, Joseph A Adams, Susan S Taylor
Publikováno v:
PLoS Biology, Vol 14, Iss 11, p e2000127 (2016)
Eukaryotic protein kinases regulate most cellular functions by phosphorylating targeted protein substrates through a highly conserved catalytic core. In the active state, the catalytic core oscillates between open, intermediate, and closed conformati
Externí odkaz:
https://doaj.org/article/a9ecdc8883d341479d40aa5acbc5baa1
Autor:
Sabeeha Hasnain, Christopher L McClendon, Monica T Hsu, Matthew P Jacobson, Pradipta Bandyopadhyay
Publikováno v:
PLoS ONE, Vol 9, Iss 9, p e106466 (2014)
A new coarse-grained model of the E. coli cytoplasm is developed by describing the proteins of the cytoplasm as flexible units consisting of one or more spheres that follow Brownian dynamics (BD), with hydrodynamic interactions (HI) accounted for by
Externí odkaz:
https://doaj.org/article/2214fb70256d4962b71009c5610d201b
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 4, p e1003022 (2013)
The Janus Kinase 2 (JAK2) plays essential roles in transmitting signals from multiple cytokine receptors, and constitutive activation of JAK2 results in hematopoietic disorders and oncogenesis. JAK2 kinase activity is negatively regulated by its pseu
Externí odkaz:
https://doaj.org/article/f1e01e537402430cbfda52ce21bb4408
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e57804 (2013)
Post-translational modification by the addition of an oxoanion functional group, usually a phosphate group and less commonly a sulfate group, leads to diverse structural and functional consequences in protein systems. Building upon previous studies o
Externí odkaz:
https://doaj.org/article/93bc85c5c2b04314932f0068f072fa67
Autor:
Faruck Morcos, Santanu Chatterjee, Christopher L McClendon, Paul R Brenner, Roberto López-Rendón, John Zintsmaster, Maria Ercsey-Ravasz, Christopher R Sweet, Matthew P Jacobson, Jeffrey W Peng, Jesús A Izaguirre
Publikováno v:
PLoS Computational Biology, Vol 6, Iss 12, p e1001015 (2010)
Protein-protein interactions are often mediated by flexible loops that experience conformational dynamics on the microsecond to millisecond time scales. NMR relaxation studies can map these dynamics. However, defining the network of inter-converting
Externí odkaz:
https://doaj.org/article/36ac1f3e72a34aa9a5a8d601fa14b349
Autor:
Jordan M. Mattheisen, Chris Limberakis, Roger B. Ruggeri, Matthew S. Dowling, Christopher W. am Ende, Emilie Ceraudo, Thomas Huber, Christopher L. McClendon, Thomas P. Sakmar
Publikováno v:
Journal of the American Chemical Society. 145:11173-11184
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cc5b00c6a565fcfee5f02177fdc5ebb
https://doi.org/10.1021/jacs.3c00972
https://doi.org/10.1021/jacs.3c00972
Autor:
Christopher Pfleger, Holger Gohlke, Alexander Minges, Markus Boehm, Christopher L. McClendon, Rubben Torella
Publikováno v:
Journal of Chemical Theory and Computation. 13:6343-6357
Allostery describes the functional coupling between sites in biomolecules. Recently, the role of changes in protein dynamics for allosteric communication has been highlighted. A quantitative and predictive description of allostery is fundamental for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3c6ecfe48ce0a29eb109b74d09772a4
https://doi.org/10.1021/acs.jctc.7b00529
https://doi.org/10.1021/acs.jctc.7b00529
Publikováno v:
Journal of chemical theory and computation 15(5), 3331–3343 (2019). doi:10.1021/acs.jctc.8b01295
Modulating protein activity with small molecules binding to cryptic pockets offers great opportunities to overcome hurdles in drug design. Cryptic sites are atypical binding sites in proteins that are closed in the absence of a stabilizing ligand and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33970944e93124d36ae99a9e89b5c94f
https://hdl.handle.net/2128/22180
https://hdl.handle.net/2128/22180
Autor:
Gianluigi Veglia, Leanna R. McDonald, Atul K. Srivastava, Larry R. Masterson, Alessandro Cembran, Christopher L. McClendon, Susan S. Taylor, Jonggul Kim
Publikováno v:
Structure. 22(12):1735-1743
Conformational fluctuations play a central role in enzymatic catalysis. However, it is not clear how the rates and the coordination of the motions affect the different catalytic steps. Here, we used NMR spectroscopy to analyze the conformational fluc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94486280d4dea7b86be22e3296bf5d57
Autor:
Lalima G. Ahuja, Christopher L. McClendon, Susan S. Taylor, Gianluigi Veglia, Alexandr P. Kornev
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 114, iss 6
The expertise of protein kinases lies in their dynamic structure, wherein they are able to modulate cellular signaling by their phosphotransferase activity. Only a few hundreds of protein kinases regulate key processes in human cells, and protein kin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a15b11f426df00f76dcc991a9e395f8
https://escholarship.org/uc/item/793623jn
https://escholarship.org/uc/item/793623jn