The selective inactivation of thiol proteasesin vitro andin vivo
- 1 February 1984
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 3 (1), 109-120
- https://doi.org/10.1007/bf01024841
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Structure and stereochemistry of tetrahedral inhibitor complexes of papain by direct NMR observationJournal of the American Chemical Society, 1983
- A prolyl endopeptidase from murine macrophages, its assay and specific inactivationArchives of Biochemistry and Biophysics, 1983
- The thiol proteinase inhibitors, Z-Phe-PheCHN2 and Z-Phe-AlaCHN2, inhibit lysosomal protein degradation in isolated rat hepatocytesBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- The regulation of proteolysis in normal fibroblasts as they approach confluence. Evidence for the participation of the lysosomal systemBiochemical Journal, 1982
- N-α-carbobenzoxy pyroglutamyl diazomethyl ketone as active-site-directed inhibitor for pyroglutamyl peptidaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Characterization of proline endopeptidase from rat brainBiochemistry, 1980
- Mechanism of the reaction of papain with substrate-derived diazomethyl ketones. Implications for the difference in site specificity of halomethyl ketones for serine proteinases and cysteine proteinases and for stereoelectronic requirements in the papain catalytic mechanismBiochemical Journal, 1978
- Binding of chloromethyl ketone substrate analogs to crystalline papainBiochemistry, 1976
- The Kinetics and Mechanism of Papain-Catalyzed Hydrolyses1Journal of the American Chemical Society, 1966
- Azaserine-reactive Sulfhydryl Group of 2-Formamido-N-ribosylacetamide 5'-Phosphate:l-Glutamine Amido-ligase (Adenosine Diphosphate)Published by Elsevier ,1963