W. H. Kane

The factor VCI domain is involved in membrane binding: identification of functionally important amino acid residues within the CI domain of factor V using alanine scanning mutagenesis (2004)

Saleh,M., Peng,W. M., Quinn-Allen,M. A., Macedo-Ribeiro,S., Fuentes-Prior,P., Bode,W., ...

The factor VCI domain is involved in membrane binding: identification of functionally important amino acid residues within the CI domain of factor V using alanine scanning mutagenesis (2004)

Saleh, M., Peng, W. M., Quinn-Allen, M. A., Macedo-Ribeiro, S., Fuentes-Prior, P., Bode, W., ...

Solvent exposed hydrophobic amino acids in the factor VC1 and C2 domains are critical for membrane dependent prothrombinase assembly, but not for prothrombin activation in solution. (2003)

Peng,W. M., Quinn-Allen,M. A., Fuentes-Prior,P., Kane,W. H.

Solvent exposed hydrophobic amino acids in the factor VC1 and C2 domains are critical for membrane dependent prothrombinase assembly, but not for prothrombin activation in solution. (2003)

Peng, W. M., Quinn-Allen, M. A., Fuentes-Prior, P., Kane, W. H.

Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator.

Rodgers, G M, Kane, W H

Vascular endothelium possesses multiple procoagulant properties, including synthesis and expression of Factor V. We studied the effects of homocysteine on the regulation of endothelial cell Factor V...

Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin.

Kane, W H, Davie, E W

Coagulation factor V is a high molecular weight plasma glycoprotein that participates as a cofactor in the conversion of prothrombin to thrombin by factor Xa. A phage lambda gt11 Hep G2 cell cDNA...

Formation of factor Va by atherosclerotic rabbit aorta mediates factor Xa-catalyzed prothrombin activation.

Rodgers, G M, Kane, W H, Pitas, R E

Vascular cell procoagulant activity may be important in the pathogenesis of atherosclerosis. In previous studies, we described the ability of the atherogenic metabolite homocysteine to activate...

Characterization of an acquired inhibitor to coagulation factor V. Antibody binding to the second C-type domain of factor V inhibits the binding of factor V to phosphatidylserine and neutralizes procoagulant activity.

Ortel, T L, Quinn-Allen, M A, Charles, L A, Devore-Carter, D, Kane, W H

Coagulation Factor V is an essential component of the prothrombinase complex, which activates the zymogen prothrombin to thrombin. A patient was described who developed a Factor V inhibitor that...

Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator.

Rodgers, G M, Kane, W H

Vascular endothelium possesses multiple procoagulant properties, including synthesis and expression of Factor V. We studied the effects of homocysteine on the regulation of endothelial cell Factor V...

Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin.

Kane, W H, Davie, E W

Coagulation factor V is a high molecular weight plasma glycoprotein that participates as a cofactor in the conversion of prothrombin to thrombin by factor Xa. A phage lambda gt11 Hep G2 cell cDNA...

Formation of factor Va by atherosclerotic rabbit aorta mediates factor Xa-catalyzed prothrombin activation.

Rodgers, G M, Kane, W H, Pitas, R E

Vascular cell procoagulant activity may be important in the pathogenesis of atherosclerosis. In previous studies, we described the ability of the atherogenic metabolite homocysteine to activate...

Characterization of an acquired inhibitor to coagulation factor V. Antibody binding to the second C-type domain of factor V inhibits the binding of factor V to phosphatidylserine and neutralizes procoagulant activity.

Ortel, T L, Quinn-Allen, M A, Charles, L A, Devore-Carter, D, Kane, W H

Coagulation Factor V is an essential component of the prothrombinase complex, which activates the zymogen prothrombin to thrombin. A patient was described who developed a Factor V inhibitor that...