The effect of the one-chain to two-chain conversion in tissue plasminogen activator: Characterization of mutations at position 275
- 1 February 1990
- journal article
- research article
- Published by Elsevier in Thrombosis Research
- Vol. 57 (4) , 527-539
- https://doi.org/10.1016/0049-3848(90)90070-s
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- The single-chain form of tissue-type plasminogen activator has catalytic activity: studies with a mutant enzyme that lacks the cleavage siteBiochemistry, 1989
- 279 Characterization of tissue plasminogen activator variants with all amino acid possibilities at position 275Fibrinolysis, 1988
- The effect of polymerised fibrin on the catalytic activities of one-chain tissue-type plasminogen activator as revealed by an analogue resistant to plasmin cleavageBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesisBiochemistry, 1987
- Construction and characterization of an active factor VIII variant lacking the central one-third of the moleculeBiochemistry, 1986
- Proteolytic activation of tissue plasminogen activator by plasma and tissue enzymesFEBS Letters, 1984
- Different base/base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coliCell, 1984
- [32] Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectorsPublished by Elsevier ,1983
- Cloning and expression of human tissue-type plasminogen activator cDNA in E. coliNature, 1983
- Studies on the kinetics of plasminogen activation by tissue plasminogen activatorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982