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Journal Articles

Noncovalent stabilization of the factor VIII A2 domain enhances efficacy in hemophilia A mouse vascular injury models

Lilley Leong, Derek Sim, Chandra Patel, Katherine Tran, Perry Liu, Elena Ho, Thomas Thompson, Peter J. Kretschmer, Hironao Wakabayashi, Philip J. Fay, John E. Murphy

Blood (2015) 125 (2): 392–398.

https://doi.org/10.1182/blood-2014-02-555656

Published: 2015

Includes: Supplemental data

Journal Articles

Stabilizing Factor VIIIa By Combining Mutations That Modulate Inter-Subunit Interactions and Proteolytic Inactivation

Hironao Wakabayashi, MD, PhD, Jennifer Wintermute, Philip J. Fay, PhD

Blood (2013) 122 (21): 3572.

https://doi.org/10.1182/blood.V122.21.3572.3572

Published: 2013

Journal Articles

Reduced Affinity To VWF Induced By a Novel Mutation At Pro1809Leu (factor VIII-Tenri) Is The Cause Of Mild Hemophilia A Developing Anti-Factor VIII Inhibitor

Koji Yada, MD, PhD, Keiji Nogami, MD, PhD, Masahiro Takeyama, MD, PhD, Hiroaki Minami, MD, Philip J. Fay, PhD, Midori Shima, MD, PhD

Blood (2013) 122 (21): 2343.

https://doi.org/10.1182/blood.V122.21.2343.2343

Published: 2013

Journal Articles

A Coagulation Mechanism for the Mild Bleeding Tendency in a Patient with Severe Hemophilia A Possessing an Arg1781His Mutation.

Koji Yada, MD, Keiji Nogami, MD, PhD, Kenichi Ogiwara, MD, PhD, Hironao Wakabayashi, MD, PhD, Philip J. Fay, PhD, Midori Shima, MD, PhD

Blood (2012) 120 (21): 2213.

https://doi.org/10.1182/blood.V120.21.2213.2213

Published: 2012

Journal Articles

Residues Surrounding Arg372, Arg740, and Arg1689 Contribute to the Rates of Thrombin-Catalyzed Cleavage of Factor VIII.

Jennifer L. Newell, PhD, Amy E. Griffiths, MS, Philip J. Fay, PhD

Blood (2009) 114 (22): 847.

https://doi.org/10.1182/blood.V114.22.847.847

Published: 2009

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

Thrombin-Catalyzed Cleavages of Factor VIII at Arg372 and Arg1689 Are Facilitated by the Acidic Residues Glu720-Asp725.

Jennifer Newell, MS, Qian Zhou, M.S., Philip J. Fay, Ph.D.

Blood (2007) 110 (11): 2686.

https://doi.org/10.1182/blood.V110.11.2686.2686

Published: 2007

Journal Articles

Contributions of Residues in the 558-Loop of Factor VIIIa A2 Subunit to Interactions with Factor IXa in Factor Xase.

H. Travis Ichikawa, Ph.D., Sandeep Chadha, MS, Qian Zhou, M.S., Philip J. Fay, Ph.D.

Blood (2007) 110 (11): 2688.

https://doi.org/10.1182/blood.V110.11.2688.2688

Published: 2007

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

Localization of Factor VIII Residues Contributing to Factor VIII and/or VIIIa Structural Stability as Detected by Rates of Activity Decay.

Hironao Wakabayashi, MD, PhD, Philip J. Fay, PhD

Blood (2007) 110 (11): 1763.

https://doi.org/10.1182/blood.V110.11.1763.1763

Published: 2007

Journal Articles

A Cluster of Basic Residues in the Factor VIIIa A2 Subunit Function in Substrate Binding and Product Release during the Activation of Factor X by Factor Xase.

H. Travis Ichikawa, PhD, Qian Zhou, M. S., Philip J. Fay, Ph. D.

Blood (2006) 108 (11): 196.

https://doi.org/10.1182/blood.V108.11.196.196

Published: 2006

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

Cleavage at Arg740 Appears Essential for Thrombin-Catalyzed Cleavage at Arg372 during the Activation of Factor VIII.

Jennifer Newell, BS, Philip J. Fay, Ph.D.

Blood (2006) 108 (11): 1692.

https://doi.org/10.1182/blood.V108.11.1692.1692

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

Mapping Factor VIIIa Inter-Subunit Interactions Using Chemical Modification and Zero-Length Cross-Linking.

Stephen M. Miles, PhD, Jan Freas, BS, Philip J. Fay, PhD

Blood (2005) 106 (11): 1016.

https://doi.org/10.1182/blood.V106.11.1016.1016

Published: 2005

Journal Articles

Factor VIII A2 Domain Residues 497–510 and 584–593 Comprise the R8B12 Epitope.

Charles Ansong, MS, Stephen Miles, PhD, Philip J. Fay, PhD

Blood (2005) 106 (11): 4028.

https://doi.org/10.1182/blood.V106.11.4028.4028

Published: 2005

Journal Articles

Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P 1 site

Keiji Nogami, Qian Zhou, Hironao Wakabayashi, Philip J. Fay

Blood (2005) 105 (11): 4362–4368.

https://doi.org/10.1182/blood-2004-10-3939

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

Noncovalent stabilization of the factor VIII A2 domain enhances efficacy in hemophilia A mouse vascular injury models

Stabilizing Factor VIIIa By Combining Mutations That Modulate Inter-Subunit Interactions and Proteolytic Inactivation

Reduced Affinity To VWF Induced By a Novel Mutation At Pro1809Leu (factor VIII-Tenri) Is The Cause Of Mild Hemophilia A Developing Anti-Factor VIII Inhibitor

A Coagulation Mechanism for the Mild Bleeding Tendency in a Patient with Severe Hemophilia A Possessing an Arg1781His Mutation.

Residues Surrounding Arg372, Arg740, and Arg1689 Contribute to the Rates of Thrombin-Catalyzed Cleavage of Factor VIII.

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

Thrombin-Catalyzed Cleavages of Factor VIII at Arg372 and Arg1689 Are Facilitated by the Acidic Residues Glu720-Asp725.

Contributions of Residues in the 558-Loop of Factor VIIIa A2 Subunit to Interactions with Factor IXa in Factor Xase.

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.

Localization of Factor VIII Residues Contributing to Factor VIII and/or VIIIa Structural Stability as Detected by Rates of Activity Decay.

A Cluster of Basic Residues in the Factor VIIIa A2 Subunit Function in Substrate Binding and Product Release during the Activation of Factor X by Factor Xase.

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

Cleavage at Arg740 Appears Essential for Thrombin-Catalyzed Cleavage at Arg372 during the Activation of Factor VIII.

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+ .

Mapping Factor VIIIa Inter-Subunit Interactions Using Chemical Modification and Zero-Length Cross-Linking.

Factor VIII A2 Domain Residues 497–510 and 584–593 Comprise the R8B12 Epitope.

Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P 1 site

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

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American Society of Hematology

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ASH Publications

American Society of Hematology

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