Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes
- 1 June 1998
- journal article
- Published by Elsevier in Chemistry & Biology
- Vol. 5 (6), 307-320
- https://doi.org/10.1016/s1074-5521(98)90169-7
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- 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
- Reactions of [14C]-3,4-Dichloroisocoumarin with Subunits of Pituitary and Spleen Multicatalytic Proteinase Complexes (Proteasomes)Biochemistry, 1997
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997
- The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the CytosolCell, 1996
- Mechanistic Studies on the Inactivation of the Proteasome by LactacystinJournal of Biological Chemistry, 1996
- Potent α-ketocarbonyl and boronic ester derived inhibitors of proteasomeBioorganic & Medicinal Chemistry Letters, 1996
- Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å ResolutionScience, 1995
- A 3,4-dichloroisocoumarin-resistant component of the multicatalytic proteinase complexBiochemistry, 1992
- The LMP antigens: A stable MHC-controlled multisubunit protein complexHuman Immunology, 1986
- Regel zur Abschätzung der chemischen Verschiebung von Protonen an einer DoppelbindungHelvetica Chimica Acta, 1966