Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Peter G.W. Gettins"'
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:
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
Publikováno v:
Biological Chemistry. 383:1677-1682
Pigment epitheliumderived factor is a member of the serpin superfamily of proteins, but one that lacks inhibitory properties against either serine or cysteine proteinases. Nevertheless it possesses a number of physiological properties that make it a
Publikováno v:
Journal of Virology. 76:2848-2856
Tva is the cellular receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A). The viral receptor function of Tva is determined by a 40-residue, cysteine-rich motif called the LDL-A module. Here we report the solution structure of the LDL-A m
Publikováno v:
Biochemistry. 40:6680-6687
Activation of antithrombin by high-affinity heparin as an inhibitor of factor Xa has been ascribed to an allosteric switch between two conformations of the reactive center loop. However, we have previously shown that other, weaker binding, charged po
Publikováno v:
Biochemistry. 40:6284-6292
We have used [(1)H-(15)N]-HSQC NMR to investigate the structural changes that occur in both serpin and proteinase in forming the kinetically trapped covalent protein-protein complex that is the basis for serpin inhibition of serine proteinases. By al
Publikováno v:
Journal of Biological Chemistry. 275:2698-2704
The binding of pentasaccharide heparin to antithrombin induces a conformational change that is transmitted to the reactive center loop and increases the rate of inhibition of factor Xa by approximately 300-fold. The mechanism of such transmission is
Publikováno v:
Archives of Biochemistry and Biophysics. 294:511-518
From the cDNA sequence of bovine glutathione peroxidase [ G. T. Mullenbach, A. Tabrizi, B. D. Irvine, G. I. Bell, J. A. Tainer, and R. A. Hallewell (1988) Protein Eng. 2, 239–246 ], it is known that the full transcript represents a 205-residue prot
Autor:
Peter G.W. Gettins, Angela Horne
Publikováno v:
Carbohydrate Research. 223:81-98
Two tetrasaccharides, two hexasaccharides, and a disaccharide have been purified from heparinase digests of porcine intestinal mucosal heparin in sufficient quantities to permit 13 C-n.m.r. characterization of the species. The two tetrasacchrides are
Autor:
Peter G.W. Gettins, Steven T. Olson
Publikováno v:
The Journal of biological chemistry. 284(31)
Serpins form an enormous superfamily of 40-60-kDa proteins found in almost all types of organisms, including humans. Most are one-use suicide substrate serine and cysteine proteinase inhibitors that have evolved to finely regulate complex proteolytic