Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Leslie A. Bush-Pelc"'
Publikováno v:
Biophysical chemistry
(2007).
info:cnr-pdr/source/autori:Gianni S, Ivarsson Y, Bah A, Bush-Pelc LA, Di Cera E./titolo:Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics./doi:/rivista:Biophysical chemistry (Print)/anno:2007/pagina_da:/pagina_a:/intervallo_pagine:/volume
(2007).
info:cnr-pdr/source/autori:Gianni S, Ivarsson Y, Bah A, Bush-Pelc LA, Di Cera E./titolo:Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics./doi:/rivista:Biophysical chemistry (Print)/anno:2007/pagina_da:/pagina_a:/intervallo_pagine:/volume
The interaction of Na(+) and K(+) with proteins is at the basis of numerous processes of biological importance. However, measurement of the kinetic components of the interaction has eluded experimentalists for decades because the rate constants are t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52c099ccf6d0d8aa37e335d0521a3058
https://doi.org/10.1016/j.bpc.2007.09.009
https://doi.org/10.1016/j.bpc.2007.09.009
Autor:
Agustin O. Pineda, Leslie A. Bush-Pelc, Francesca Marino, Zhi-wei Chen, F. Scott Mathews, Enrico Di Cera
Publikováno v:
Journal of Biological Chemistry. 282:27165-27170
Little is known on the role of disulfide bonds in the catalytic domain of serine proteases. The Cys-191-Cys-220 disulfide bond is located between the 190 strand leading to the oxyanion hole and the 220-loop that contributes to the architecture of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e810ddc4744044d20e6de7ceb695f5e
https://doi.org/10.1074/jbc.m703202200
https://doi.org/10.1074/jbc.m703202200
Autor:
Zhi-wei Chen, Can E. Ergenekan, Francesca Marino, Enrico Di Cera, F. Scott Mathews, Leslie A. Bush-Pelc
Publikováno v:
Journal of Biological Chemistry. 282:16355-16361
Unlike human thrombin, murine thrombin lacks Na+ activation due to the charge reversal substitution D222K in the Na+ binding loop. However, the enzyme is functionally stabilized in a Na+-bound form and is highly active toward physiologic substrates.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abba7180d92608082831dae7288a1269
https://doi.org/10.1074/jbc.m701323200
https://doi.org/10.1074/jbc.m701323200
The molecular mechanism of thrombin activation by Na(+) remains elusive. Its kinetic formulation requires extension of the classical Botts-Morales theory for the action of a modifier on an enzyme to correctly account for the contribution of the E*, E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f3afecf506c21ff453fc031bc5a2b65
https://europepmc.org/articles/PMC2794733/
https://europepmc.org/articles/PMC2794733/
Autor:
Leslie A. Bush-Pelc, Enrico Di Cera, Tara C. White, Michelle A. Berny, Erik I. Tucker, Andras Gruber, Owen J. T. McCarty
Publikováno v:
Arteriosclerosis, thrombosis, and vascular biology. 28(2)
Objective— Thrombin containing the mutations Trp215Ala and Glu217Ala (WE) selectively activates protein C and has potent antithrombotic effects in primates. The aim of this study was to delineate the molecular mechanism of direct WE–platelet inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f685cff7351daf55beaf024658b58ee
https://pubmed.ncbi.nlm.nih.gov/18216328
https://pubmed.ncbi.nlm.nih.gov/18216328
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 104(28)
It has been proposed that the cleaved form of protease-activated receptor 3 (PAR3) acts as a cofactor for thrombin cleavage and activation of PAR4 on murine platelets, but the molecular basis of this physiologically important effect remains elusive.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36f0b9579b353fee6487c9a3755c6015
https://pubmed.ncbi.nlm.nih.gov/17606903
https://pubmed.ncbi.nlm.nih.gov/17606903
Publikováno v:
Physical Chemistry Chemical Physics (PCCP); Mar2007, Vol. 9 Issue 11, p1291-1306, 16p