M. A. Quinn-Allen

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.

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...

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...