The Caspase-like Sites of Proteasomes, Their Substrate Specificity, New Inhibitors and Substrates, and Allosteric Interactions with the Trypsin-like Sites
Open Access
- 1 September 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (38) , 35869-35877
- https://doi.org/10.1074/jbc.m303725200
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Definition of the Extended Substrate Specificity Determinants for β-Tryptases I and IIJournal of Biological Chemistry, 2001
- Evidence for the Existence of a Non-catalytic Modifier Site of Peptide Hydrolysis by the 20 S ProteasomeJournal of Biological Chemistry, 2000
- Purification and catalytic properties of human caspase family membersCell Death & Differentiation, 1999
- DEGRADATION OF CELL PROTEINS AND THE GENERATION OF MHC CLASS I-PRESENTED PEPTIDESAnnual Review of Immunology, 1999
- Conformational constraints for protein self-cleavage in the proteasomeJournal of Molecular Biology, 1998
- Kinetic Studies of the Branched Chain Amino Acid Preferring Peptidase Activity of the 20S Proteasome: Development of a Continuous Assay and Inhibition by Tripeptide Aldehydes and clasto-Lactacystin β-LactoneBiochemistry, 1998
- Bovine Spleen Multicatalytic Proteinase Complex (Proteasome)Journal of Biological Chemistry, 1997
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997
- Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acidsBiochemistry, 1993
- A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytesNature, 1992