Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains.
about
Protease-activated receptor-4 uses dual prolines and an anionic retention motif for thrombin recognition and cleavageStructural basis for the anticoagulant activity of the thrombin-thrombomodulin complexCrystal structures of murine thrombin in complex with the extracellular fragments of murine protease-activated receptors PAR3 and PAR4Targeting the GPIbα binding site of thrombin to simultaneously induce dual anticoagulant and antiplatelet effectsMolecular mapping of the thrombin-heparin cofactor II complexMolecular recognition mechanisms of thrombin.Autoantibodies to thrombin directed against both of its cryptic exosites.Further characterization of ADAMTS-13 inactivation by thrombin.Thrombin hydrolysis of human osteopontin is dependent on thrombin anion-binding exosites.Thrombin mutant W215A/E217A treatment improves neurological outcome and reduces cerebral infarct size in a mouse model of ischemic stroke.A thrombin receptor function for platelet glycoprotein Ib-IX unmasked by cleavage of glycoprotein V.Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation.Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin.Thrombomodulin.Ligand binding to anion-binding exosites regulates conformational properties of thrombin.Thrombin.Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets.Structure-function relationships in thrombin-activatable fibrinolysis inhibitor.The roles of selected arginine and lysine residues of TAFI (Pro-CPU) in its activation to TAFIa by the thrombin-thrombomodulin complexPolyphosphate binds with high affinity to exosite II of thrombin.The thrombin epitope recognizing thrombomodulin is a highly cooperative hot spot in exosite I.Mutations in the fourth EGF-like domain affect thrombomodulin-induced changes in the active site of thrombin.An extensive interaction interface between thrombin and factor V is required for factor V activation.Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively.Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C.A critical role for Gly25 in the B chain of human thrombin.Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain.RNA aptamer to thrombin binds anion-binding exosite-2 and alters protease inhibition by heparin-binding serpins.Identification of a thrombomodulin interaction site on thrombin-activatable fibrinolysis inhibitor that mediates accelerated activation by thrombin.Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate.Reversible covalent direct thrombin inhibitors
P2860
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P2860
Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Thrombin interacts with thromb ...... specific and distinct domains.
@en
type
label
Thrombin interacts with thromb ...... specific and distinct domains.
@en
prefLabel
Thrombin interacts with thromb ...... specific and distinct domains.
@en
P2093
P2860
P356
P1476
Thrombin interacts with thromb ...... specific and distinct domains.
@en
P2093
P2860
P304
25510-25516
P356
10.1074/JBC.274.36.25510
P407
P577
1999-09-01T00:00:00Z