Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized.
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Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junctionStructural basis of coagulation factor V recognition for cleavage by RVV-VNew insights into the spatiotemporal localization of prothrombinase in vivo.Factor V Leiden improves in vivo hemostasis in murine hemophilia models.Regulated cleavage of prothrombin by prothrombinase: repositioning a cleavage site reveals the unique kinetic behavior of the action of prothrombinase on its compound substrateThe factor V light chain mediates the binding and endocytosis of plasma-derived factor V by megakaryocytes.Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase.Recombinant canine B-domain-deleted FVIII exhibits high specific activity and is safe in the canine hemophilia A model.Improved hemostasis in hemophilia mice by means of an engineered factor Va mutantIdentification of the MMRN1 binding region within the C2 domain of human factor V.The molecular basis of factor V and VIII procofactor activationProcoagulant adaptation of a blood coagulation prothrombinase-like enzyme complex in australian elapid venom.Blood coagulation factors V and VIII: Molecular Mechanisms of Procofactor Activation.Zymogen-like factor Xa variants restore thrombin generation and effectively bypass the intrinsic pathway in vitroNotecarin D binds human factor V and factor Va with high affinity in the absence of membranes.Hemostatic agents of broad applicability produced by selective tuning of factor Xa zymogenicity.A bipartite autoinhibitory region within the B-domain suppresses function in factor VMeizothrombin is an unexpectedly zymogen-like variant of thrombin.Restricted active site docking by enzyme-bound substrate enforces the ordered cleavage of prothrombin by prothrombinase.The role of thrombin exosites I and II in the activation of human coagulation factor V.Factor VIII accelerates proteolytic cleavage of von Willebrand factor by ADAMTS13.Safety, Stability and Pharmacokinetic Properties of (super)Factor Va, a Novel Engineered Coagulation Factor V for Treatment of Severe Bleeding.Membrane binding by prothrombin mediates its constrained presentation to prothrombinase for cleavageMembrane-dependent interaction of factor Xa and prothrombin with factor Va in the prothrombinase complex.Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptidesVenom factor V from the common brown snake escapes hemostatic regulation through procoagulant adaptations.Amino acid region 1000-1008 of factor V is a dynamic regulator for the emergence of procoagulant activity.Novel factor VIII variants with a modified furin cleavage site improve the efficacy of gene therapy for hemophilia A.Spatiotemporal regulation of coagulation and platelet activation during the hemostatic response in vivo.Rethinking events in the haemostatic process: role of factor V and TFPI.The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly.Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin.The critical role of the 185-189-loop in the factor Xa interaction with Na+ and factor Va in the prothrombinase complex.Engineered factor Xa variants retain procoagulant activity independent of direct factor Xa inhibitors.Mass spectrometry-assisted study reveals that lysine residues 1967 and 1968 have opposite contribution to stability of activated factor VIII.Fate of membrane-bound reactants and products during the activation of human prothrombin by prothrombinase.Factor V has an anticoagulant cofactor activity that targets the early phase of coagulation.Prothrombotic skeletal muscle myosin directly enhances prothrombin activation by binding factors Xa and Va.Tick spit shines a light on the initiation of coagulation.A rapid pro-hemostatic approach to overcome direct oral anticoagulants.
P2860
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P2860
Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Removal of B-domain sequences ...... cofactor function is realized.
@en
type
label
Removal of B-domain sequences ...... cofactor function is realized.
@en
prefLabel
Removal of B-domain sequences ...... cofactor function is realized.
@en
P2860
P356
P1476
Removal of B-domain sequences ...... cofactor function is realized.
@en
P2093
Raffaella Toso
Rodney M Camire
P2860
P304
21643-21650
P356
10.1074/JBC.M402107200
P407
P577
2004-03-05T00:00:00Z