Associated Papers
Engineered coagulation factor VIII with enhanced secretion and coagulation potential for hemophilia A gene therapy.
Kashiwakura Y et al.
Blood, 2026
41198051 (PubMed )
Supplement: BLOOD_BLD-2025-028481-mmc1.pdf
Factor IXa and factor X influence factor VIIIa stability and inactivation mechanisms in vitro and in vivo.
Morris JJ et al.
Blood, 2025
The combination of Asp519Val/Glu665Val and Lys1813Ala mutations in FVIII markedly increases coagulation potential.
Nakajima Y et al.
Blood Advances, 2024
Factor VIII mutated with Lys1813Ala within the factor IXa-binding region enhances intrinsic coagulation potential.
Nakajima Y et al.
Blood Advances, 2023
The 3.2 Å structure of a bioengineered variant of blood coagulation factor VIII indicates two conformations of the C2 domain.
Smith IW et al.
Journal of Thrombosis and Haemostasis : Jth, 2020
Protein-Engineered Coagulation Factors for Hemophilia Gene Therapy.
Samelson-Jones BJ et al.
Molecular Therapy. Methods & Clinical Development, 2019
Noncovalent stabilization of the factor VIII A2 domain enhances efficacy in hemophilia A mouse vascular injury models.
Leong L et al.
Blood, 2015
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
Effects of replacement of factor VIII amino acids Asp519 and Glu665 with Val on plasma survival and efficacy in vivo.
Kosloski MP et al.
The Aaps Journal, 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
Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa.
Wakabayashi H et al.
Thrombosis and Haemostasis, 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
The regulation of factor IXa by supersulfated low molecular weight heparin.
Misenheimer TM et al.
Biochemistry, 2010
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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