Výsledky vyhledávání - "Parvathi Kamath"

Ligand Binding Shuttles Thrombin along a Continuum of Zymogen- and Proteinase-like States

Autor: Parvathi Kamath, James A. Huntington, Sriram Krishnaswamy

Publikováno v: Journal of Biological Chemistry. 285:28651-28658

The critical and multiple roles of thrombin in blood coagulation are regulated by ligands and cofactors. Zymogen activation imparts proteolytic activity to thrombin and also affects the binding of ligands to its two principal exosites. We have used t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5872ea5717929f33d01562236497c53e
https://doi.org/10.1074/jbc.m110.154914

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Fate of Membrane-bound Reactants and Products during the Activation of Human Prothrombin by Prothrombinase*

Autor: Sriram Krishnaswamy, Parvathi Kamath

Membrane binding by prothrombin, mediated by its N-terminal fragment 1 (F1) domain, plays an essential role in its proteolytic activation by prothrombinase. Thrombin is produced in two cleavage reactions. One at Arg(320) yields the proteinase meizoth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef275135305e59d124baa15d1fe51a9c
https://europepmc.org/articles/PMC2573076/

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Long-Range Allosteric Linkage Between Exosites Reciprocally Regulates the Zymogenicity of Prothrombin Derivatives

Autor: Anuja Khan, Joseph A. Micucci, Sriram Krishnaswamy, Parvathi Kamath, Paul E. Bock

Publikováno v: Blood. 126:122-122

The binding of ligands to anion binding exosite I (ABEI) and exosite II (ABEII) on prothrombin (II) derivatives plays an integral role in regulating their function. These exosites are located on opposite faces of the proteinase domain and exhibit uni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6deb74d02fcd48dc4487453a832acd29
https://doi.org/10.1182/blood.v126.23.122.122

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Driving Thrombin From a Protease-Like State to a Zymogen-Like State and Back

Autor: Sriram Krishnaswamy, Parvathi Kamath

Publikováno v: Blood. 114:852-852

Abstract 852 Thrombin (IIa) possesses two anion binding exosites, ABEI and ABEII that play key roles in binding ligands and regulating protease function. Thrombomodulin and hirugen (Hir) are among the established ligands for ABEI. ABEII binds to frag

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1bfdaa8113c5f096632e6cbbed8556a7
https://doi.org/10.1182/blood.v114.22.852.852

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Fate of Membrane-Bound Reactants and Products during Prothrombin Activation by Prothrombinase

Autor: Sriram Krishnaswamy, Parvathi Kamath

Publikováno v: Blood. 110:2692-2692

The activation of prothrombin by the prothrombinase complex yields the protease thrombin (IIa) and the activation peptide fragment 1.2 (F1.2). IIa and F1.2 are established to interact noncovalently through the fragment 2 (F2) domain. Since membrane b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::828830fe2d75b04ab427cb6aa47ec336
https://doi.org/10.1182/blood.v110.11.2692.2692

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