Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Brian W Beck"'
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e97115 (2014)
Specific protein interactions are responsible for most biological functions. Distinguishing Functionally Linked Interfaces of Proteins (FLIPs), from Functionally uncorrelated Contacts (FunCs), is therefore important to characterizing these interactio
Externí odkaz:
https://doaj.org/article/0768fd0657754636a15d21bd3c2e2a35
Autor:
Edwin Skidmore, J. Eric Coulter, Suresh Marru, Jeremy Fischer, Matthew W. Vaughn, David Y. Hancock, Marlon Pierce, Nirav Merchant, John Michael Lowe, Brian W. Beck, Gwen A. Jacobs, Winona Snapp-Childs
Publikováno v:
PEARC
Jetstream2 will be a category I production cloud resource that is part of the National Science Foundation’s Innovative HPC Program. The project’s aim is to accelerate science and engineering by providing “on-demand” programmable infrastructur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85c0759db57d2ad3234f925a4cd4bf0f
https://doi.org/10.1145/3437359.3465565
https://doi.org/10.1145/3437359.3465565
Autor:
Jordan A. McConnell, Jairus M. Reddy, Brian W. Beck, Cristina P. Reddy, DiAnna L. Hynds, Filsy Samuel
Publikováno v:
Cellular Signalling. 27:630-637
Rac1 is an important regulator of axon extension, cell migration and actin reorganization. Like all Rho guanine triphosphatases (GTPases), Rac1 is targeted to the membrane by the addition of a geranylgeranyl moiety, an action thought to result in Rac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::304d30f642cda1684862e85135cb80c1
https://doi.org/10.1016/j.cellsig.2014.11.033
https://doi.org/10.1016/j.cellsig.2014.11.033
Autor:
Isha D. Mehta, Brian W. Beck
Publikováno v:
Biophysical Journal. 110(3)
Proteins perform numerous cellular activities either individually or by interacting with other proteins. The function carried out by participating oligomers is representative of their structural stability and interaction specificity. One general goal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55977db8b124151f81f67bded9c4bba8
Publikováno v:
Biopolymers. 85:241-252
The dynamics and structure of Serratia marcescens endonuclease and its neighboring solvent are investigated by molecular dynamics (MD). Comparisons are made with structural and biochemical experiments. The dimer form is physiologic and functions more
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e522dc3e03980c31df930d152caf205
https://doi.org/10.1002/bip.20641
https://doi.org/10.1002/bip.20641
Publikováno v:
Journal of Biological Chemistry. 281:38801-38811
In the presence of ATP, unphosphorylated smooth muscle myosin can form a catalytically inactive monomer that sediments at 10 Svedbergs (10 S). The tail of 10 S bends into thirds and interacts with the regulatory domain. ADP-Pi is “trapped” at the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa9d7dcb4b32d4453a85af90e4763ca4
https://doi.org/10.1074/jbc.m606555200
https://doi.org/10.1074/jbc.m606555200
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 62:982-995
The monomer and dimer of the bacterium Serratia marcescens endonuclease (SMnase) are each catalytically active and the two subunits of the dimer function independently of each other. Specific interfacial waters may play a role in stability, complex f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8ae4e5897ae56dd18ef4cd42326e868
https://doi.org/10.1002/prot.20694
https://doi.org/10.1002/prot.20694
Publikováno v:
Biophysical Journal. 112:489a
Protein-protein interactions (PPI) play essential roles in virtually all biological processes. While modern structural determination methods such as x-ray crystallography and NMR provide valuable information that can aid in our understanding of these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a58ece8b74ec14f5da4c7322ba9a862
https://doi.org/10.1016/j.bpj.2016.11.2645
https://doi.org/10.1016/j.bpj.2016.11.2645
Autor:
Isha D. Mehta, Brian W. Beck
Publikováno v:
Biophysical Journal. 112:345a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b33026d7105da57a32deb20c3a3e289
https://doi.org/10.1016/j.bpj.2016.11.1871
https://doi.org/10.1016/j.bpj.2016.11.1871
Publikováno v:
Biophysical Journal. 81(2):601-613
A sequence determinant of reduction potentials is reported for bacterial [4Fe-4S]-type ferredoxins. The residue that is four residues C-terminal to the fourth ligand of either cluster is generally an alanine or a cysteine. In five experimental ferred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fb3565ea3d6329ae077998ef6d40aa2