Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin.
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Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzymeFibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexesCrystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitorRole of corin and atrial natriuretic peptide in preeclampsiaMechanism of the Anticoagulant Activity of Thrombin Mutant W215A/E217AStabilization of the E* Form Turns Thrombin into an AnticoagulantMolecular basis of thrombomodulin activation of slow thrombinAutoactivation of Thrombin PrecursorsExposure of R169 controls protein C activation and autoactivationStructure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bugINP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype.Hageman factor, platelets and polyphosphates: early history and recent connectionIdentification of protein-protein interfaces by decreased amide proton solvent accessibility.Low anticoagulant heparin blocks thrombin-induced endothelial permeability in a PAR-dependent mannerAntithrombotic effects of thrombin-induced activation of endogenous protein C in primates.Crystal structures of thrombin with thiazole-containing inhibitors: probes of the S1' binding site.An allosteric switch controls the procoagulant and anticoagulant activities of thrombinActivation of factor XI by products of prothrombin activationMolecular mapping of the heparin-binding exosite of thrombin.Relative antithrombotic and antihemostatic effects of protein C activator versus low-molecular-weight heparin in primates.Structural resiliency of an EGF-like subdomain bound to its target protein, thrombinSignaling-mediated cooperativity between glycoprotein Ib-IX and protease-activated receptors in thrombin-induced platelet activationSelection of a suppressor mutation that restores affinity of an oligonucleotide inhibitor for thrombin using in vitro genetics.Antibody-probed conformational transitions in the protease domain of human factor IX upon calcium binding and zymogen activation: putative high-affinity Ca(2+)-binding site in the protease domainBio-inspired liposomal thrombomodulin conjugate through bio-orthogonal chemistry.Thrombin.Exosites in the substrate specificity of blood coagulation reactions.Proexosite-1 on prothrombin is a factor Va-dependent recognition site for the prothrombinase complex.The thrombin epitope recognizing thrombomodulin is a highly cooperative hot spot in exosite I.Glycosaminoglycans and the regulation of blood coagulation.Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains.Cellular consequences of thrombin-receptor activation.Expression and folding of recombinant bovine prethrombin-2 and its activation to thrombin.Thrombomodulin is required for the antithrombotic activity of thrombin mutant W215A/E217A in a mouse model of arterial thrombosis.Functional mapping of the surface residues of human thrombin.The serine protease granzyme A does not induce platelet aggregation but inhibits responses triggered by thrombin.An extensive interaction interface between thrombin and factor V is required for factor V activation.Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C.The elusive role of the potential factor X cation-binding exosite-1 in substrate and inhibitor interactions.N-glycosylation in the protease domain of trypsin-like serine proteases mediates calnexin-assisted protein folding.
P2860
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P2860
Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Single amino acid substitution ...... activities of human thrombin.
@en
Single amino acid substitution ...... activities of human thrombin.
@nl
type
label
Single amino acid substitution ...... activities of human thrombin.
@en
Single amino acid substitution ...... activities of human thrombin.
@nl
prefLabel
Single amino acid substitution ...... activities of human thrombin.
@en
Single amino acid substitution ...... activities of human thrombin.
@nl
P2093
P2860
P356
P1476
Single amino acid substitution ...... activities of human thrombin.
@en
P2093
P2860
P304
P356
10.1073/PNAS.88.15.6775
P407
P577
1991-08-01T00:00:00Z