Associated Papers
Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway.
Monaghan M et al.
Journal of Thrombosis and Haemostasis : Jth, 2016
Enhanced factor VIIIa stability of A2 domain interface variants results from an increased apparent affinity for the A2 subunit. Results from an increased apparent affinity for the A2 subunit.
Monaghan M et al.
Thrombosis and Haemostasis, 2014
Role of hydrophobic mutations on the binding affinity and stability of blood coagulation factor VIIIa: a computational molecular dynamics and free-energy analysis.
Venkateswarlu D
Biochemical and Biophysical Research Communications, 2014
Enhancing factor VIII and VIIIa stability by combining mutations at the A2 domain interface and A1-C2 domain interface.
Wakabayashi H et al.
Journal of Thrombosis and Haemostasis : Jth, 2012
Combining mutations of charged residues at the A2 domain interface enhances factor VIII stability over single point mutations.
Wakabayashi H et al.
Journal of Thrombosis and Haemostasis : Jth, 2009
Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface.
Wakabayashi H et al.
Blood, 2008
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