Zobrazeno 1 - 10
of 84
pro vyhledávání: '"Peter G.W. Gettins"'
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:
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
Publikováno v:
Biochemical Journal
Jensen, J K, Dolmer, K, Schar, C & Gettins, P G W 2009, ' Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP ', Biochemical Journal, vol. 421, no. 2, pp. 273-82 . https://doi.org/10.1042/BJ20090175
Jensen, J K, Dolmer, K, Schar, C & Gettins, P G W 2009, ' Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP ', Biochemical Journal, vol. 421, no. 2, pp. 273-82 . https://doi.org/10.1042/BJ20090175
RAP (receptor-associated protein) is a three domain 38 kDa ER (endoplasmic reticulum)-resident protein that is a chaperone for the LRP (low-density lipoprotein receptor-related protein). Whereas RAP is known to compete for binding of all known LRP li
Autor:
Ninh Doan, Peter G.W. Gettins
Publikováno v:
Journal of Biological Chemistry. 283:28747-28756
α-Macroglobulins (αMs) are large glycoproteins that have been identified in a wide range of vertebrate and invertebrate species and are mostly thiol ester containing proteinase inhibitors. A recent analysis of bacterial genomes (Budd, A., Blandin,
Autor:
Ninh Doan, Peter G.W. Gettins
Publikováno v:
Biochemical Journal. 407:23-30
Human alpha2M (alpha2-macroglobulin) and the complement components C3 and C4 are thiol ester-containing proteins that evolved from the same ancestral gene. The recent structure determination of human C3 has allowed a detailed prediction of the locati
Publikováno v:
Journal of Biological Chemistry. 282:19502-19509
Maspin is a member of the serpin family with a reactive center loop that is incompatible with proteinase inhibition by the serpin conformational change mechanism. Despite this there are reports that maspin might regulate uPA-dependent processes in vi
Autor:
Manikanahally P. Raghavendra, Christopher J. Froelich, Richard Swanson, Steven T. Olson, Peter G.W. Gettins, Weiqing Zhang
Publikováno v:
Journal of Biological Chemistry. 282:2305-2313
CrmA is a "cross-class" serpin family inhibitor of the proapoptotic serine protease, granzyme B, as well as cysteine proteases of the caspase family. To determine whether crmA inhibits these structurally diverse proteases by a common conformational t