Structure of prothrombin fragment 1 refined at 2.8 Å resolution
- 1 August 1988
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 202 (4) , 885-901
- https://doi.org/10.1016/0022-2836(88)90565-7
Abstract
No abstract availableThis publication has 70 references indexed in Scilit:
- Proton magnetic resonance study of lysine-binding to the kringle 4 domain of human plasminogenJournal of Molecular Biology, 1987
- Structure and order of the protein and carbohydrate domains of prothrombin fragment 1FEBS Letters, 1987
- cDNA sequence of human apolipoprotein(a) is homologous to plasminogenNature, 1987
- Complete assignment of the aromatic proton magnetic resonance spectrum of the kringle 1 domain from human plasminogen: the structure of the ligand-binding siteBiochemistry, 1987
- Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modulesCell, 1985
- Amino acid sequence of bovine protein Z: a vitamin K‐dependent serine protease homologFEBS Letters, 1985
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2.8 Å resolutionJournal of Molecular Biology, 1982
- A low resolution model of fragment 1 from bovine prothrombinFEBS Letters, 1982
- Kringle 5 of human plasminogen carries a benzamidine-binding siteBiochemical and Biophysical Research Communications, 1981