Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity.
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Replacing the factor VIII C1 domain with a second C2 domain reduces factor VIII stability and affinity for factor IXaCofactor activity in factor VIIIa of the blood clotting pathway is stabilized by an interdomain bond between His281 and Ser524 formed in factor VIII.Structural investigation of zymogenic and activated forms of human blood coagulation factor VIII: a computational molecular dynamics studyFactor VIII lacking the C2 domain retains cofactor activity in vitroThe crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.A Glu113Ala mutation within a factor VIII Ca2+-binding site enhances cofactor interactions in factor Xase.Increasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.The role of P4-P3' residues flanking Arg336 in facilitating activated protein C-catalyzed cleavage and inactivation of factor VIIIaSequences flanking Arg336 in factor VIIIa modulate factor Xa-catalyzed cleavage rates at this site and cofactor function.P3-P3' residues flanking scissile bonds in factor VIII modulate rates of substrate cleavage and procofactor activation by thrombinMembrane-binding properties of the Factor VIII C2 domain.Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface.Acidic residues C-terminal to the A2 domain facilitate thrombin-catalyzed activation of factor VIII.Blood Clotting Factor VIII: From Evolution to Therapy.Identification of residues contributing to A2 domain-dependent structural stability in factor VIII and factor VIIIaModification of interdomain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activityCleavage at Arg-1689 influences heavy chain cleavages during thrombin-catalyzed activation of factor VIII.Combining mutations of charged residues at the A2 domain interface enhances factor VIII stability over single point mutationsStabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway.pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2+.Molecular orientation of factor VIIIa on the phospholipid membrane surface determined by fluorescence resonance energy transfer.Role of P1 residues Arg336 and Arg562 in the activated-Protein-C-catalysed inactivation of Factor VIIIa.Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P1 siteIdentification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain.Factor VIII (FVIII) gene mutations in 120 patients with hemophilia A: detection of 26 novel mutations and correlation with FVIII inhibitor development.Differential contributions of Glu96, Asp102 and Asp111 to coagulation factor V/Va metal ion binding and subunit stability.Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa.Proteolysis at Arg740 facilitates subsequent bond cleavages during thrombin-catalyzed activation of factor VIII.Enhanced factor VIIIa stability of A2 domain interface variants results from an increased apparent affinity for the A2 subunit. Results from an increased apparent affinity for the A2 subunit.
P2860
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P2860
Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@en
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@nl
type
label
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@en
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@nl
prefLabel
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@en
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@nl
P2093
P2860
P356
P1476
Residues 110-126 in the A1 dom ...... equired for cofactor activity.
@en
P2093
Hironao Wakabayashi
Philip J Fay
P2860
P304
12677-12684
P356
10.1074/JBC.M311042200
P407
P577
2004-01-13T00:00:00Z