Zobrazeno 1 - 10
of 143
pro vyhledávání: '"Peter G.W. Gettins"'
Autor:
Marija Backovic, Peter G.W. Gettins
Publikováno v:
The Scientific World Journal, Vol 2, Pp 112-114 (2002)
Externí odkaz:
https://doaj.org/article/1fd5f292b1f94550875d551cac6ff921
Publikováno v:
Biochemistry. 60:1201-1213
Antithrombin is unique among serpin family protein protease inhibitors with respect to the major reactive center loop (RCL) and core conformational changes that mediate allosteric activation of its anticoagulant function by heparin. A critical role f
Autor:
Gonzalo Izaguirre, Susan Clark Bock, Peter G.W. Gettins, Ryan Roth, Richard Swanson, Steven T. Olson
Publikováno v:
Journal of Biological Chemistry. 290:28020-28036
Past studies have suggested that a key feature of the mechanism of heparin allosteric activation of the anticoagulant serpin, antithrombin, is the release of the reactive center loop P14 residue from a native state stabilizing interaction with the hy
Autor:
Mateusz S. Wietecha, Lin Chen, Luisa A. DiPietro, Mateusz J. Król, Peter G.W. Gettins, Elizabeth R. Michalczyk
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 309:H812-H826
During dermal wound repair, hypoxia-driven proliferation results in dense but highly permeable, disorganized microvascular networks, similar to those in solid tumors. Concurrently, activated dermal fibroblasts generate an angiopermissive, provisional
Autor:
Peter G.W. Gettins, Giulia Isetti, Richard Swanson, Gonzalo Izaguirre, Alexey Dementiev, Steven T. Olson, Ryan Roth
Publikováno v:
Journal of Biological Chemistry. 288:33611-33619
Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin. These are accompanied by CD, fluorescence, an
Publikováno v:
Journal of Biological Chemistry. 288:32020-32035
Serpin protein protease inhibitors inactivate their target proteases through a unique mechanism in which a major serpin conformational change, resulting in a 70-A translocation of the protease from its initial reactive center loop docking site to the
Publikováno v:
Journal of Biological Chemistry. 288:24081-24090
Although lysines are known to be critical for ligand binding to LDL receptor family receptors, relatively small reductions in affinity have been found when such lysines have been mutated. To resolve this paradox, we have examined the specific binding
Autor:
Peter G.W. Gettins, Steven T. Olson
Publikováno v:
The Biochemical journal. 473(15)
Serpins are a widely distributed family of high molecular mass protein proteinase inhibitors that can inhibit both serine and cysteine proteinases by a remarkable mechanism-based kinetic trapping of an acyl or thioacyl enzyme intermediate that involv
Autor:
Peter G.W. Gettins, Klavs Dolmer
Publikováno v:
The Journal of biological chemistry. 291(2)
Plasminogen activator inhibitor 1 (PAI-1) is a serpin inhibitor of the plasminogen activators urokinase-type plasminogen activator (uPA) and tissue plasminogen activator, which binds tightly to the clearance and signaling receptor low density lipopro
Autor:
Steven T. Olson, Sophia Schedin-Weiss, Peter G.W. Gettins, Benjamin Richard, Gonzalo Izaguirre
Publikováno v:
Biochimie. 92:1587-1596
Serpin family protein proteinase inhibitors regulate the activity of serine and cysteine proteinases by a novel conformational trapping mechanism that may itself be regulated by cofactors to provide a finely-tuned time and location-dependent control