Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Susan Clark Bock"'
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:
Susan Clark Bock
Publikováno v:
Trauma Induced Coagulopathy ISBN: 9783319283067
To sustain blood circulation and continue on with life after a serious traumatic injury, it is equally necessary to prevent hemorrhage and exsanguination, and to check the development of subsequent systemic thrombosis by escaped clotting enzymes. Com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::031d1ac9a4f826000b1acfee6d3c9a41
https://doi.org/10.1007/978-3-319-28308-1_2
https://doi.org/10.1007/978-3-319-28308-1_2
Autor:
Ingemar Björk, Steven T. Olson, Aiqin Lu, Susan Clark Bock, Mohamad Aman Jairajpuri, Umesh R. Desai
Publikováno v:
Journal of Biological Chemistry. 278:15941-15950
The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor's binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contri
Publikováno v:
Trends in Cardiovascular Medicine. 12:198-205
The serpin, antithrombin, and its polysaccharide activator, heparin, are essential anticoagulant regulators of blood-clotting cascade proteases and thereby critical for maintaining hemostasis. The relative importance of the molecular interactions tha
Publikováno v:
Journal of Biological Chemistry. 275:18976-18984
The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln. R129H and R129Q antithrombins bound pentasacch
Publikováno v:
Biochemistry. 34:8433-8440
Two antithrombin III (ATIII) isoforms occur naturally in human plasma. The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192. The beta-ATIII isoform lacks carbohydrate on asparagine-135 (N135), which
Autor:
Allen P. Kaplan, Susan Clark Bock, Marc Schapira, William R. Wikoff, Francisca Tausk, Karen Skriver, Philip A. Patston
Publikováno v:
Journal of Biological Chemistry. 266:9216-9221
The serine protease inhibitor (serpin) C1 inhibitor inactivates enzymes involved in the regulation of vascular permeability. A patient from the Ma family with the genetic disorder hereditary angioedema inherited a dysfunctional C1 inhibitor allele. R
Publikováno v:
The Journal of biological chemistry. 281(42)
The native conformation of antithrombin III (ATIII) is a poor inhibitor of its coagulation pathway target enzymes because of the partial insertion of its reactive center loop (RCL) in its central A beta-sheet. This study focused on tyrosine 131, whic
Publikováno v:
The Journal of biological chemistry. 276(47)
Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active