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Transglutaminases: crosslinking enzymes with pleiotropic functions
Blood coagulation, skin-barrier formation, hardening of the fertilization envelope, extracellular-matrix assembly and other important biological processes are dependent on the rapid generation ofExpand
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Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders.
The human transglutaminase (TG) family consists of a structural protein, protein 4.2, that lacks catalytic activity, and eight zymogens/enzymes, designated factor XIII-A (FXIII-A) and TG1-7, thatExpand
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Structural origins of fibrin clot rheology.
The origins of clot rheological behavior associated with network morphology and factor XIIIa-induced cross-linking were studied in fibrin clots. Network morphology was manipulated by varying theExpand
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Mechanism of allosteric regulation of transglutaminase 2 by GTP
Allosteric regulation is a fundamental mechanism of biological control. Here, we investigated the allosteric mechanism by which GTP inhibits cross-linking activity of transglutaminase 2 (TG2), aExpand
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Identification of a Novel Recognition Sequence for Fibronectin within the NH2-terminal β-Sandwich Domain of Tissue Transglutaminase*
Tissue transglutaminase belongs to the multigene transglutaminase family of Ca2+-dependent protein cross-linking enzymes. Unlike other transglutaminases, it is involved in cell-matrix interactionsExpand
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ACTIVATION OF THE FIBRIN STABILIZING FACTOR OF PLASMA BY THROMBIN.
Abstract Two new reactions in the final stages of blood coagulation that involve the fibrin stabilizing factor of plasma are described. The factor is first activated by thrombin in the presence ofExpand
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Factor XIII: Structure, Activation, and Interactions with Fibrinogen and Fibrin
  • L. Lorand
  • Medicine, Chemistry
  • Annals of the New York Academy of Sciences
  • 1 June 2001
Abstract: Fibrin stabilizing factor (factor XIII or FXIII) plays a critical role in the generation of a viable hemostatic plug. Following exposure to thrombin and calcium, the zymogen is activated toExpand
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Hydrolysis of γ:ε Isopeptides by Cytosolic Transglutaminases and by Coagulation Factor XIIIa*
Nε-(γ-glutamyl)lysine cross-links, connecting various peptide chain segments, are frequently the major products in transglutaminase-catalyzed reactions. We have now investigated the effectiveness ofExpand
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Ca2+-related regulatory function of fibrinogen.
Fibrinogen displays a regulation of considerable physiological significance by lowering the Ca2+ requirement for the conversion of the fibrin-stabilizing factor (Factor XIII) zymogen to the range ofExpand
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Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin.
Complex formation between the human erythrocyte transglutaminase (protein-glutamine:amine gamma-glutamyltransferase, EC 2.3.2.13) and fibronectin or its fragments was examined by immunoanalyticalExpand
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