Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
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Trp2313-His2315 of Factor VIII C2 Domain Is Involved in Membrane Binding: STRUCTURE OF A COMPLEX BETWEEN THE C2 DOMAIN AND AN INHIBITOR OF MEMBRANE BINDINGDomain organization of membrane-bound factor VIII.Cysteamine enhances the procoagulant activity of Factor VIII-East Hartford, a dysfunctional protein due to a light chain thrombin cleavage site mutation (arginine-1689 to cysteine)Differential proteolytic activation of factor VIII-von Willebrand factor complex by thrombinLipid nanotechnologies for structural studies of membrane-associated proteinsDimeric Organization of Blood Coagulation Factor VIII bound to Lipid Nanotubes.Suppression of FVIII inhibitor formation in hemophilic mice by delivery of transgene modified apoptotic fibroblasts.Structural model of porcine factor VIII and factor VIIIa molecules based on scanning transmission electron microscope (STEM) images and STEM mass analysisDirect characterization of factor VIII in plasma: detection of a mutation altering a thrombin cleavage site (arginine-372----histidine).The molecular basis of factor V and VIII procofactor activationBlood coagulation factors V and VIII: Molecular Mechanisms of Procofactor Activation.A1 subunit-mediated regulation of thrombin-activated factor VIII A2 subunit dissociation.A single chain variant of factor VIII Fc fusion protein retains normal in vivo efficacy but exhibits altered in vitro activity.Molecular basis of factor VIII inhibition by human antibodies. Antibodies that bind to the factor VIII light chain prevent the interaction of factor VIII with phospholipid.Gene therapy for hemophilia A: production of therapeutic levels of human factor VIII in vivo in mice.Factor VIII-East Hartford (arginine 1689 to cysteine) has procoagulant activity when separated from von Willebrand factor.Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIaThe diversity of the immune response to the A2 domain of human factor VIIIAntiphospholipid antibodies: laboratory and pathogenetic aspects.The heparin-binding exosite of factor IXa is a critical regulator of plasma thrombin generation and venous thrombosisHemophilia A due to mutations that create new N-glycosylation sites.Molecular characterization of mild-to-moderate hemophilia A: detection of the mutation in 25 of 29 patients by denaturing gradient gel electrophoresis.Novel factor VIII variants with a modified furin cleavage site improve the efficacy of gene therapy for hemophilia A.Mutations and a polymorphism in the factor VIII gene discovered by denaturing gradient gel electrophoresisIdentification and functional requirement of Cu(I) and its ligands within coagulation factor VIII.Detailed mechanisms of the inactivation of factor VIIIa by activated protein C in the presence of its cofactors, protein S and factor V.Haemophilia A: database of nucleotide substitutions, deletions, insertions and rearrangements of the factor VIII geneRemoval of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized.Intracellular retention of a factor VIII protein with an Arg2307-->Gln mutation as a cause of haemophilia A.Structural and functional characterization of Factor VIII-delta II, a new recombinant Factor VIII lacking most of the B-domain.Function of the activated protein C (APC) autolysis loop in activated FVIII inactivation.Characterization of des-(741-1668)-factor VIII, a single-chain factor VIII variant with a fusion site susceptible to proteolysis by thrombin and factor Xa.Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P1 siteFour hydrophobic amino acids of the factor VIII C2 domain are constituents of both the membrane-binding and von Willebrand factor-binding motifs.Sequencing of the factor 8(F8) coding regions in 10 Turkish hemophilia A patients reveals three novel pathological mutations, and one rediagnosis of von Willebrand's disease type 2N.Development of a novel automated screening method for detection of FVIII Inhibitors.Abnormal factor VIII Hiroshima: defect in crucial proteolytic cleavage by thrombin at Arg1689 detected by a novel ELISA.Biological activity of recombinant factor VIII variants lacking the central B-domain and the heavy-chain sequence Lys713-Arg740: discordant in vitro and in vivo activity.Expression of blood clotting factor VIII:C gene in capillary endothelial cells.Proteolysis of factor VIII heavy chain polypeptides in plasma and concentrates.
P2860
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P2860
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
description
1988 nî lūn-bûn
@nan
1988 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@ast
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@en
Proteolytic requirements for thrombin activation of anti-hemophilic factor
@nl
type
label
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@ast
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@en
Proteolytic requirements for thrombin activation of anti-hemophilic factor
@nl
prefLabel
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@ast
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@en
Proteolytic requirements for thrombin activation of anti-hemophilic factor
@nl
P921
P356
P1476
Proteolytic requirements for thrombin activation of anti-hemophilic factor (factor VIII)
@en
P2093
D D Pittman
R J Kaufman
P304
P356
10.1073/PNAS.85.8.2429
P407
P577
1988-04-01T00:00:00Z