Design of potent reversible inhibitors for thermolysin. Peptides containing zinc coordinating ligands and their use in affinity chromatography
- 2 October 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (20) , 4340-4347
- https://doi.org/10.1021/bi00587a012
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Peptide hydroxamic acids as inhibitors of thermolysinBiochemistry, 1978
- By-product analogs for bovine carboxypeptidase BBiochemistry, 1978
- Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acidsBiochemistry, 1977
- Characterization of the "microprotease" from Bacillus cereus. A zinc neutral endoproteaseBiochemistry, 1977
- A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substratesJournal of Molecular Biology, 1977
- Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysisBiochemistry, 1977
- Synthesis and structure-activity relations of bestatin analogs, inhibitors of aminopeptidase BJournal of Medicinal Chemistry, 1977
- Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomerArchives of Biochemistry and Biophysics, 1976
- Structure-activity studies on sulfamate sweetenersJournal of Medicinal Chemistry, 1976
- Structure of carboxypeptidase B at 2.8 Å resolutionJournal of Molecular Biology, 1976