Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C.
about
Increased tissue factor-initiated prothrombin activation as a result of the Arg506 --> Gln mutation in factor VLEIDENThe discovery of activated protein C resistanceImplication of protein S thrombin-sensitive region with membrane binding via conformational changes in the gamma-carboxyglutamic acid-rich domainProthrombotic phenotype of protein Z deficiencyEffects of protein S and factor Xa on peptide bond cleavages during inactivation of factor Va and factor VaR506Q by activated protein CActive site-labeled prothrombin inhibits prothrombinase in vitro and thrombosis in vivo.Factor Va, bound to microparticles released during platelet storage, is resistant to inactivation by activated protein C.Inhibition of thrombin formation by active site mutated (S360A) activated protein C.An engineered factor Va prevents bleeding induced by anticoagulant wt activated protein CModeling of human factor Va inactivation by activated protein C.Cleavage at both Arg306 and Arg506 is required and sufficient for timely and efficient inactivation of factor Va by activated protein C.Molecular recognition in the protein C anticoagulant pathway.Erythrocyte-derived microparticles supporting activated protein C-mediated regulation of blood coagulationNotecarin D binds human factor V and factor Va with high affinity in the absence of membranes.Binding of calcium to anticoagulant protein S: role of the fourth EGF moduleThe role of thrombin exosites I and II in the activation of human coagulation factor V.Phosphorylation of protein S by platelet kinases enhances its activated protein C cofactor activity.Low plasma levels of tissue factor pathway inhibitor in patients with congenital factor V deficiency.Mechanisms of anticoagulant and cytoprotective actions of the protein C pathway.Dissociation of activated protein C functions by elimination of protein S cofactor enhancement.HIV replication alters the composition of extrinsic pathway coagulation factors and increases thrombin generationAmino acid region 1000-1008 of factor V is a dynamic regulator for the emergence of procoagulant activity.APC resistance: biological basis and acquired influences.Down-regulation of the clotting cascade by the protein C pathwayThe protein C pathway in intestinal barrier function: challenging the hemostasis paradigm.Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein CPro- and anticoagulant properties of factor V in pathogenesis of thrombosis and bleeding disorders.Association of Hemostatic Gene Polymorphisms With Early-Onset Ischemic Heart Disease in Egyptian Patients.Detailed mechanisms of the inactivation of factor VIIIa by activated protein C in the presence of its cofactors, protein S and factor V.Mapping of the factor Xa binding site on factor Va by site-directed mutagenesisFactor V is an anticoagulant cofactor for activated protein C during inactivation of factor Va.Function of the activated protein C (APC) autolysis loop in activated FVIII inactivation.Conformational changes in activated protein C caused by binding of the first epidermal growth factor-like module of protein S.Protein C activation on endothelial cells by prothrombin activation products generated in situ: meizothrombin is a better protein C activator than alpha-thrombin.Regulation of platelet factor Va-dependent thrombin generation by activated protein C at the surface of collagen-adherent platelets.Secondary substrate-binding exosite in the serine protease domain of activated protein C important for cleavage at Arg-506 but not at Arg-306 in factor Va.Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C.Defining the factor Xa-binding site on factor Va by site-directed glycosylation.Importance of protein S and phospholipid for activated protein C-mediated cleavages in factor Va.The risk of venous thromboembolism associated with the factor V Leiden mutation and low B-vitamin status.
P2860
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P2860
Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C.
description
1995 nî lūn-bûn
@nan
1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի սեպտեմբերին 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
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@ast
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@en
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@nl
type
label
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@ast
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@en
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@nl
prefLabel
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@ast
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@en
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@nl
P2093
P2860
P356
P1476
Peptide bond cleavages and los ...... aR506Q by activated protein C.
@en
P2093
Nicolaes GA
Pabinger I
Schwarz HP
Thomassen MC
P2860
P304
21158-21166
P356
10.1074/JBC.270.36.21158
P407
P577
1995-09-01T00:00:00Z