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Factor VIII Lacking the C2 Domain Retains Cofactor Activity in Vitro

The Journal of biological chemistry, 2010-08, Vol.285 (33), p.25176-25184

2010

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Contribution of factor VIII light-chain residues 2007-2016 to an activated protein C-interactive site

Thrombosis and haemostasis, 2013-02, Vol.109 (2), p.187-198

2013

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Residues 110–126 in the A1 Domain of Factor VIII Contain a Ca2+ Binding Site Required for Cofactor Activity

The Journal of biological chemistry, 2004-03, Vol.279 (13), p.12677-12684

2004

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Residues Surrounding Arg336 and Arg562 Contribute to the Disparate Rates of Proteolysis of Factor VIIIa Catalyzed by Activated Protein C

The Journal of biological chemistry, 2007-07, Vol.282 (28), p.20264-20272

2007

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Mechanisms of Factor Xa-catalyzed Cleavage of the Factor VIIIa A1 Subunit Resulting in Cofactor Inactivation

The Journal of biological chemistry, 2003-05, Vol.278 (19), p.16502-16509

2003

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Mechanisms of Interactions of Factor X and Factor Xa with the Acidic Region in the Factor VIII A1 Domain

The Journal of biological chemistry, 2004-08, Vol.279 (32), p.33104-33113

2004

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Metal Ion-independent Association of Factor VIII Subunits and the Roles of Calcium and Copper Ions for Cofactor Activity and Inter-Subunit Affinity

Biochemistry (Easton), 2001-08, Vol.40 (34), p.10293-10300

2001

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Identification of a Factor Xa-interactive Site within Residues 337–372 of the Factor VIII Heavy Chain

The Journal of biological chemistry, 2004-04, Vol.279 (16), p.15763-15771

2004

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Modification of Interdomain Interfaces within the A3C1C2 Subunit of Factor VIII Affects Its Stability and Activity

Biochemistry (Easton), 2013-06, Vol.52 (22), p.3921-3929

2013

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Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa

Thrombosis and haemostasis, 2014-07, Vol.112 (1), p.43-52

2014

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The mild phenotype in severe hemophilia A with Arg1781His mutation is associated with enhanced binding affinity of factor VIII for factor X

Thrombosis and haemostasis, 2013-06, Vol.109 (6), p.1007-1015

2013

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Sequences Flanking Arg336 in Factor VIIIa Modulate Factor Xa-catalyzed Cleavage Rates at this Site and Cofactor Function

The Journal of biological chemistry, 2012-05, Vol.287 (19), p.15409-15417

2012

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The role of P4-P3’ residues flanking Arg336 in facilitating activated protein C-catalyzed cleavage and inactivation of factor VIIIa

Thrombosis research, 2011-11, Vol.128 (5), p.470-476

2011

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Membrane-binding properties of the Factor VIII C2 domain

Biochemical journal, 2011-04, Vol.435 (1), p.187-196

2011

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Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P1 site

Blood, 2005-06, Vol.105 (11), p.4362-4368

2005

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Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity

Biochemistry (Easton), 2002-07, Vol.41 (26), p.8485-8492

2002

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pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2

Biochimica et biophysica acta, 2006-06, Vol.1764 (6), p.1094-1101

2006

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Role of P1 residues Arg336 and Arg562 in the activated-Protein-C-catalysed inactivation of Factor VIIIa

Biochemical journal, 2006-06, Vol.396 (2), p.355-362

2006

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A Glu113Ala Mutation within a Factor VIII Ca2+-Binding Site Enhances Cofactor Interactions in Factor Xase

Biochemistry (Easton), 2005-08, Vol.44 (30), p.10298-10304

2005

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Factor VIII Lacking the C2 Domain Retains Cofactor Activity in Vitro

Contribution of factor VIII light-chain residues 2007-2016 to an activated protein C-interactive site

Residues 110–126 in the A1 Domain of Factor VIII Contain a Ca2+ Binding Site Required for Cofactor Activity

Residues Surrounding Arg336 and Arg562 Contribute to the Disparate Rates of Proteolysis of Factor VIIIa Catalyzed by Activated Protein C

Mechanisms of Factor Xa-catalyzed Cleavage of the Factor VIIIa A1 Subunit Resulting in Cofactor Inactivation

Mechanisms of Interactions of Factor X and Factor Xa with the Acidic Region in the Factor VIII A1 Domain

Metal Ion-independent Association of Factor VIII Subunits and the Roles of Calcium and Copper Ions for Cofactor Activity and Inter-Subunit Affinity

Identification of a Factor Xa-interactive Site within Residues 337–372 of the Factor VIII Heavy Chain

Modification of Interdomain Interfaces within the A3C1C2 Subunit of Factor VIII Affects Its Stability and Activity

Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa

The mild phenotype in severe hemophilia A with Arg1781His mutation is associated with enhanced binding affinity of factor VIII for factor X

Sequences Flanking Arg336 in Factor VIIIa Modulate Factor Xa-catalyzed Cleavage Rates at this Site and Cofactor Function

The role of P4-P3’ residues flanking Arg336 in facilitating activated protein C-catalyzed cleavage and inactivation of factor VIIIa

Membrane-binding properties of the Factor VIII C2 domain

Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P1 site

Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity

pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2

Role of P1 residues Arg336 and Arg562 in the activated-Protein-C-catalysed inactivation of Factor VIIIa

A Glu113Ala Mutation within a Factor VIII Ca2+-Binding Site Enhances Cofactor Interactions in Factor Xase

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