Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Steven J. Orcutt"'
Autor:
Steven J. Orcutt, Aran F. Labrijn, Adam Zwolak, Mark L. Chiu, William M. Atkins, Theo Rispens, Dennis R. Goulet, Rob N. de Jong
Publikováno v:
The Journal of Biological Chemistry
Journal of biological chemistry, 293(2), 651-661. American Society for Biochemistry and Molecular Biology Inc.
Journal of biological chemistry, 293(2), 651-661. American Society for Biochemistry and Molecular Biology Inc.
Bispecific antibodies (bsAbs) combine the antigen specificities of two distinct Abs and demonstrate therapeutic promise based on novel mechanisms of action. Among the many platforms for creating bsAbs, controlled Fab-arm exchange (cFAE) has proven us
Membrane Binding by Prothrombin Mediates Its Constrained Presentation to Prothrombinase for Cleavage
Publikováno v:
Journal of Biological Chemistry. 288:27789-27800
Long-standing dogma proposes a profound contribution of membrane binding by prothrombin in determining the rate at which it is converted to thrombin by prothrombinase. We have examined the action of prothrombinase on full-length prothrombin variants
Autor:
George P. Vlasuk, Hassan Mahmoud Elokdah, Steven J. Orcutt, Stephen J. Gardell, Thomas A. Antrilli, Julie A. Krueger, David L. Crandall, Scott Mayer
Publikováno v:
Molecular Pharmacology. 72:897-906
PAI-749 is a potent and selective synthetic antagonist of plasminogen activator inhibitor 1 (PAI-1) that preserved tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA) activities in the presence of PAI-1 (IC 50 value
Autor:
Steven J. Orcutt, Sriram Krishnaswamy
Publikováno v:
Journal of Biological Chemistry. 279:54927-54936
Thrombin formation results from cleavage of prothrombin following Arg(271) and Arg(320). Both bonds are accessible for cleavage, yet the sequential action of prothrombinase on Arg(320) followed by Arg(271) is implied by the intermediate observed duri
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 705
The preparation of sufficient amounts of high-quality protein samples is the major bottleneck for structural proteomics. The use of recombinant proteins has increased significantly during the past decades. The most commonly used host, Escherichia col
Publikováno v:
Methods in Molecular Biology ISBN: 9781617379666
The preparation of sufficient amounts of high-quality protein samples is the major bottleneck for structural proteomics. The use of recombinant proteins has increased significantly during the past decades. The most commonly used host, Escherichia col
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a52c8a3c27b6ae2f17e6c62a4e461267
https://doi.org/10.1007/978-1-61737-967-3_2
https://doi.org/10.1007/978-1-61737-967-3_2
Prothrombinase catalyzes thrombin formation by the ordered cleavage of two peptide bonds in prothrombin. Although these bonds are likely ≈36 Å apart, sequential cleavage of prothrombin at Arg-320 to produce meizothrombin, followed by its cleavage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e66e44df341f68c4e70c3967dd036bc
https://europepmc.org/articles/PMC1174926/
https://europepmc.org/articles/PMC1174926/
Publikováno v:
The Journal of biological chemistry. 277(48)
The specific action of serine proteinases on protein substrates is a hallmark of blood coagulation and numerous other physiological processes. Enzymic recognition of substrate sequences preceding the scissile bond is considered to contribute dominant
Publikováno v:
Blood. 104:1717-1717
The conversion of human prothrombin to thrombin requires the cleavage of two peptide bonds. When catalyzed by prothrombinase, the reaction proceeds almost exclusively via initial cleavage at R 320 followed by cleavage at R 271 yielding meizothrombin
Autor:
Steven J. Orcutt, Sriram Krishnaswamy
Publikováno v:
Blood. 104:1712-1712
Thrombin formation is catalyzed by human prothrombinase almost exclusively through sequential cleavage at Arg320 followed by cleavage at Arg271 in prothrombin. Activation site mutants in which the individual sites have been rendered uncleavable indic