Activation and characterization of procarboxypeptidase B from human plasma
about
Plasma carboxypeptidases as regulators of the plasminogen systemFlexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein SubstratesElucidation of the molecular mechanisms of two nanobodies that inhibit thrombin-activatable fibrinolysis inhibitor activation and activated thrombin-activatable fibrinolysis inhibitor activityActivated human plasma carboxypeptidase B is retained in the blood by binding to alpha2-macroglobulin and pregnancy zone proteinTAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complexTwo naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme.Gene expression profiling in hepatic tissue of newly weaned pigs fed pharmacological zinc and phytase supplemented diets.Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage.A phosphorylation tag for uranyl mediated protein purification and photo assisted tag removalBiochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI).A novel metallocarboxypeptidase-like enzyme from the marine annelid Sabellastarte magnifica--a step into the invertebrate world of proteases.Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation.Association of a single nucleotide polymorphism in CPB2 encoding the thrombin-activable fibrinolysis inhibitor (TAF1) with blood pressure.Carboxypeptidase U at the interface between coagulation and fibrinolysis.TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots.Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine lifeKinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sitesCarboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy?An overview of enzymatic reagents for the removal of affinity tags.Thrombin-activatable procarboxypeptidase B regulates activated complement C5a in vivo.Targeted disruption of the gene encoding the murine small subunit of carboxypeptidase N (CPN1) causes susceptibility to C5a anaphylatoxin-mediated shock.Thrombin-thrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon.Molecular characterization of the carboxypeptidase B1 of Anopheles stephensi and its evaluation as a target for transmission-blocking vaccines.In vivo regulation of plasminogen function by plasma carboxypeptidase B.Enhancement of rabbit jugular vein thrombolysis by neutralization of factor XI. In vivo evidence for a role of factor XI as an anti-fibrinolytic factorThe roles of selected arginine and lysine residues of TAFI (Pro-CPU) in its activation to TAFIa by the thrombin-thrombomodulin complexSelective modulation of thrombin-activatable fibrinolysis inhibitor (TAFI) activation by thrombin or the thrombin-thrombomodulin complex using TAFI-derived peptides.Acute phase mediators modulate thrombin-activable fibrinolysis inhibitor (TAFI) gene expression in HepG2 cells.Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties.Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis.Carboxypeptidases: new regulators of plasminogen activation in vivo?Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes.Secretion and antifibrinolytic function of thrombin-activatable fibrinolysis inhibitor from human platelets.cpbAg1 encodes an active carboxypeptidase B expressed in the midgut of Anopheles gambiae.Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro.Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin.A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis.Antithrombotic agents in the treatment of severe sepsis.Proteolytic cleavage of carboxypeptidase N markedly increases its antifibrinolytic activity.The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability.
P2860
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P2860
Activation and characterization of procarboxypeptidase B from human plasma
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Activation and characterization of procarboxypeptidase B from human plasma
@ast
Activation and characterization of procarboxypeptidase B from human plasma
@en
Activation and characterization of procarboxypeptidase B from human plasma
@nl
type
label
Activation and characterization of procarboxypeptidase B from human plasma
@ast
Activation and characterization of procarboxypeptidase B from human plasma
@en
Activation and characterization of procarboxypeptidase B from human plasma
@nl
prefLabel
Activation and characterization of procarboxypeptidase B from human plasma
@ast
Activation and characterization of procarboxypeptidase B from human plasma
@en
Activation and characterization of procarboxypeptidase B from human plasma
@nl
P356
P1433
P1476
Activation and characterization of procarboxypeptidase B from human plasma
@en
P2093
P304
P356
10.1021/BI00017A012
P407
P577
1995-05-02T00:00:00Z