The role of β-barrels 1 and 2 in the enzymatic activity of factor XIII A-subunit

Author:

Hethershaw E. L.1ORCID,Adamson P. J.1,Smith K. A.1,Goldsberry W. N.2,Pease R. J.1,Radford S. E.3,Grant P. J.1,Ariëns R. A. S.1,Maurer M. C.2,Philippou H.1

Affiliation:

1. Discovery and Translational Science Department; Leeds Institute for Cardiovascular and Metabolic Medicine; Faculty of Medicine and Health; University of Leeds; Leeds UK

2. Chemistry Department; University of Louisville; Louisville KY USA

3. Astbury Centre for Structural Molecular Biology; School of Molecular and Cellular Biology; University of Leeds; Leeds UK

Funder

National Institutes of Health

British Heart Foundation

Publisher

Wiley

Subject

Hematology

Reference50 articles.

1. Factor XIII: structure, activation, and interactions with fibrinogen and fibrin;Lorand;Ann N Y Acad Sci,2001

2. Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor;Sakata;J Clin Invest,1980

3. Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor;Kimura;J Biol Chem,1986

4. Factor V is a substrate for the transamidase factor XIIIa;Francis;J Biol Chem,1986

5. Covalent crosslinking of human coagulation factor V by activated factor XIII from guinea pig megakaryocytes and human plasma;Huh;Blood,1988

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