Zobrazeno 1 - 10
of 137
pro vyhledávání: '"Steven T Olson"'
Autor:
Steven T. Olson, Lawrence Leung, Yan Xiong, Richard Swanson, Tianquan Jin, Yung-Jen Chuang, Weiqing Zhang
Antithrombin, a serpin family protease inhibitor crucial to hemostasis, acquires antiangiogenic properties on undergoing conformational alterations induced by limited proteolysis or elevated temperature. To better understand the biochemical mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f35cf6fa37f23060d68b4dfb7f0b9595
https://doi.org/10.1158/0008-5472.c.6494417.v1
https://doi.org/10.1158/0008-5472.c.6494417.v1
Autor:
Steven T. Olson, Lawrence Leung, Yan Xiong, Richard Swanson, Tianquan Jin, Yung-Jen Chuang, Weiqing Zhang
Supplementary Tables 1-2 from Antiangiogenic Antithrombin Induces Global Changes in the Gene Expression Profile of Endothelial Cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51e6e4425efeeb6fb010db5615972312
https://doi.org/10.1158/0008-5472.22364885
https://doi.org/10.1158/0008-5472.22364885
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
Publikováno v:
The Journal of biological chemistry. 298(6)
Protein Z (PZ)-dependent protease inhibitor (ZPI) is a plasma anticoagulant protein of the serpin superfamily, which is activated by its cofactor, PZ, to rapidly inhibit activated factor X (FXa) on a procoagulant membrane surface. ZPI is also activat
Autor:
Sebastian Pernal, Sean C. Morris, Francis M. Creighton, Alexander Willis, Sabo Michael E, Laura M Moore, Herbert H Engelhard, Steven T. Olson
Publikováno v:
International Journal of Nanomedicine. 15:1549-1568
Background Thrombotic events continue to be a major cause of morbidity and mortality worldwide. Tissue plasminogen activator (tPA) is used for the treatment of acute ischemic stroke and other thrombotic disorders. Use of tPA is limited by its narrow
Publikováno v:
Journal of Biological Chemistry. 292:14625-14635
Lipid oxidation due to oxidative stress plays an important role in the pathogenesis of inflammatory and thrombotic cardiovascular diseases. Several findings suggest that lipid peroxidation can alter the function of coagulation proteins and contribute
Autor:
Dudley K. Strickland, Steven T. Olson
Publikováno v:
Journal of Thrombosis and Haemostasis. 18:262-263
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
Heparin allosterically activates the anticoagulant serpin, antithrombin, by binding through a sequence-specific pentasaccharide and inducing activating conformational changes in the protein. Three basic residues of antithrombin, Lys114, Lys125 and Ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f5f9032f5993c5ec324f2e9171771b1
https://europepmc.org/articles/PMC6363533/
https://europepmc.org/articles/PMC6363533/
Publikováno v:
Journal of Biological Chemistry. 290:9906-9918
Background: ZPI-protein Z complex is a critical anticoagulant regulator of membrane-associated factor Xa. Results: The energetics and multistep kinetics of the ZPI-protein Z interaction were characterized with fluorescently labeled K239C ZPI. Conclus