Plasmin Reduction by Phosphoglycerate Kinase Is a Thiol-independent Process
Open Access
- 1 March 2002
- journal article
- Published by Elsevier
- Vol. 277 (11) , 9062-9068
- https://doi.org/10.1074/jbc.m111531200
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- A Truncated Plasminogen Activator Inhibitor-1 Protein Induces and Inhibits Angiostatin (Kringles 1–3), a Plasminogen Cleavage ProductJournal of Biological Chemistry, 2001
- A 1.8 Å resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure11Edited by R. HuberJournal of Molecular Biology, 2001
- Regulation of Angiostatin Production by Matrix Metalloproteinase-2 in a Model of Concomitant ResistancePublished by Elsevier ,1999
- Generation of Angiostatin by Reduction and Proteolysis of PlasminPublished by Elsevier ,1997
- Patterns and Emerging Mechanisms of the Angiogenic Switch during TumorigenesisPublished by Elsevier ,1996
- Protein disulphide isomerase: building bridges in protein foldingTrends in Biochemical Sciences, 1994
- Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 ÅActa Crystallographica Section D-Biological Crystallography, 1994
- An investigation of large inhibitors binding to phosphoglycerate kinase and their effect on anion activationEuropean Journal of Biochemistry, 1992
- The two fast‐reacting thiols of 3‐phosphoglycerate kinase are structurally juxtaposedEuropean Journal of Biochemistry, 1987
- Structure of horse muscle phosphoglycerate kinase: Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 Å Fourier mapJournal of Molecular Biology, 1974