The Activation-resistant Conformation of Recombinant Human Plasminogen Is Stabilized by Basic Residues in the Amino-terminal Hinge Region
Open Access
- 1 June 1995
- journal article
- Published by Elsevier
- Vol. 270 (26), 15770-15776
- https://doi.org/10.1074/jbc.270.26.15770
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Positive co-operative binding at two weak lysine-binding sites governs the Glu-plasminogen conformational changeBiochemical Journal, 1992
- Conformation of Lys-plasminogen and the kringle 1-3 fragment of plasminogen analyzed by small-angle neutron scatteringBiochemistry, 1991
- Characterization of an Extremely Large, Ligand-Induced Conformational Change in PlasminogenScience, 1990
- Plasmin-mediated fibrinolysis by variant recombinant tissue plasminogen activators.Proceedings of the National Academy of Sciences, 1989
- Mutants of human tissue-type plasminogen activator (t-PA): Structural aspects and functional propertiesFibrinolysis, 1988
- High expression of functional adenovirus DNA polymerase and precursor terminal protein using recombinant vaccinia virusNucleic Acids Research, 1988
- Molecular cloning and characterization of a full‐length cDNA clone for human plasminogenFEBS Letters, 1987
- The gapped duplex DNA approach to oligonucleotide-directed mutation constructionNucleic Acids Research, 1984
- On the Regulation and Control of FibrinolysisThrombosis and Haemostasis, 1980
- Molecular mechanism of physiological fibrinolysisNature, 1978