Kringles of the plasminogen–prothrombin gene family share conformational epitopes with recombinant apolipoprotein (a): specificity of the fibrin-binding site

Author:

Dominguez Miguel,Rojas Gertrudis,Loyau Stéphane,Bazurco Martin,Sorell Luis,Anglés-Cano Eduardo

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference38 articles.

1. Evolution of proteases of blood coagulation and fibrinolysis by assembly from modules;Patthy;Cell,1985

2. Modes of evolution in the protease and kringle domains of the plasminogen-prothrombin family;Hughes;Mol. Phylogenet. Evol.,2000

3. Location of the intermediate and high affinity ω-aminocarboxylic acid-binding sites in human plasminogen;Vali;J. Biol. Chem.,1982

4. The plasminogen activator/plasmin system;Vassalli;J. Clin. Invest.,1991

5. Partial amino acid sequence of apolipoprotein (a) shows that it is homologous to plasminogen;Eaton;Biochemistry,1987

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