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Journal Articles

Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface

Hironao Wakabayashi, Fatbardha Varfaj, Jennifer DeAngelis, Philip J. Fay

Blood (2008) 112 (7): 2761–2769.

https://doi.org/10.1182/blood-2008-02-142158

Published: 2008

Journal Articles

P2 and P2′ Residues Are Important for the Efficient Proteolysis of Factor VIIIa at Arg336 Catalyzed by Activated Protein C.

Fatbardha Varfaj, Ph.D., Jennifer DeAngelis, BS, Hironao Wakabayashi, Ph.D., Philip J. Fay, Ph.D.

Blood (2007) 110 (11): 2689.

https://doi.org/10.1182/blood.V110.11.2689.2689

Published: 2007

Journal Articles

The Mutation Leu335Pro in Factor VIII Results in Its Rapid Inactivation by Thrombin-Catalyzed Proteolysis at Arg336.

Fatbardha Varfaj, Ph.D., Hironao Wakabayashi, Ph.D., Philip J. Fay, PhD

Blood (2007) 110 (11): 2690.

https://doi.org/10.1182/blood.V110.11.2690.2690

Published: 2007

Journal Articles

A3 Domain Residue Glu1829 Contributes to A2 Subunit Retention in Factor VIIIa.

Hironao Wakabayashi, PhD, Qian Zhou, M. S., Fatbardha Varfaj, M. S., Philip J. Fay, Ph.D.

Blood (2006) 108 (11): 1690.

https://doi.org/10.1182/blood.V108.11.1690.1690

Published: 2006

Journal Articles

Contribution of P4-P3′ Residues Surrounding P1 Residues Arg336 and Arg562 in the Activated Protein C-Catalyzed Inactivation of Factor VIIIa.

Fatbardha Varfaj, MS, Hironao Wakabayashi, Ph.D., Philip J. Fay, Ph.D.

Blood (2006) 108 (11): 1693.

https://doi.org/10.1182/blood.V108.11.1693.1693

Published: 2006

Journal Articles

pH-Dependent Association of Factor VIII Chains: Enhancement of Affinity at Physiological pH by Cu 2+ .

Hironao Wakabayashi, MD, PhD, Qian Zhou, MS, Keiji Nogami, MD, Charles Ansong, MS, Fatbardha Varfaj, MS, Stephen Miles, PhD, Philip J. Fay, PhD

Blood (2005) 106 (11): 1015.

https://doi.org/10.1182/blood.V106.11.1015.1015

Published: 2005

Journal Articles

Exosite Interactions Contribute to the Activated Protein C-Catalyzed Inactivation of Factor VIIIa.

Fatbardha Varfaj, Julie Neuberg, Hironao Wakabayashi, Ph.D., Philip J. Fay, Ph. D.

Blood (2004) 104 (11): 1739.

https://doi.org/10.1182/blood.V104.11.1739.1739

Published: 2004

NARROW

Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface

P2 and P2′ Residues Are Important for the Efficient Proteolysis of Factor VIIIa at Arg336 Catalyzed by Activated Protein C.

The Mutation Leu335Pro in Factor VIII Results in Its Rapid Inactivation by Thrombin-Catalyzed Proteolysis at Arg336.

A3 Domain Residue Glu1829 Contributes to A2 Subunit Retention in Factor VIIIa.

Contribution of P4-P3′ Residues Surrounding P1 Residues Arg336 and Arg562 in the Activated Protein C-Catalyzed Inactivation of Factor VIIIa.

pH-Dependent Association of Factor VIII Chains: Enhancement of Affinity at Physiological pH by Cu 2+ .

Exosite Interactions Contribute to the Activated Protein C-Catalyzed Inactivation of Factor VIIIa.

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ASH Publications

American Society of Hematology

Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface

P2 and P2′ Residues Are Important for the Efficient Proteolysis of Factor VIIIa at Arg336 Catalyzed by Activated Protein C.

The Mutation Leu335Pro in Factor VIII Results in Its Rapid Inactivation by Thrombin-Catalyzed Proteolysis at Arg336.

A3 Domain Residue Glu1829 Contributes to A2 Subunit Retention in Factor VIIIa.

Contribution of P4-P3′ Residues Surrounding P1 Residues Arg336 and Arg562 in the Activated Protein C-Catalyzed Inactivation of Factor VIIIa.

pH-Dependent Association of Factor VIII Chains: Enhancement of Affinity at Physiological pH by Cu 2+ .

Exosite Interactions Contribute to the Activated Protein C-Catalyzed Inactivation of Factor VIIIa.

Email alerts

ASH Publications

American Society of Hematology

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