Modification of Interdomain Interfaces within the A3C1C2 Subunit of Factor VIII Affects Its Stability and Activity-Reference-Cited by-同舟云学术

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

Published:2013-05-21 Issue:22 Volume:52 Page:3921-3929
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wakabayashi Hironao¹,Fay Philip J.¹

Affiliation:

1. Department of Biochemistry and Biophysics, University of Rochester School of Medicine, 601 Elmwood Avenue, Rochester, New York 14642, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi400295x

Reference27 articles.

1. Activation of factor VIII and mechanisms of cofactor action

2. Reconstitution of human factor VIII from isolated subunits

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

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

5. pH-dependent association of factor VIII chains: Enhancement of affinity at physiological pH by Cu2+

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1. Prediction of hemophilia A severity using a small-input machine-learning framework;npj Systems Biology and Applications;2021-05-25

2. Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway;Journal of Thrombosis and Haemostasis;2016-03-21

3. Cofactor Activity in Factor VIIIa of the Blood Clotting Pathway Is Stabilized by an Interdomain Bond between His281 and Ser524 Formed in Factor VIII;Journal of Biological Chemistry;2014-05

4. Replacing the Factor VIII C1 Domain with a Second C2 Domain Reduces Factor VIII Stability and Affinity for Factor IXa;Journal of Biological Chemistry;2013-10