title: Ubiquitin-mediated protein modification and degradation.
abstract: Ubiquitin is a small, 8 kD protein found in all eukaryotic cells. It is involved in a wide variety of regulatory roles within the cell, including gene expression, ribosome biosynthesis, receptor expression, and the stress response. The best understood of these is that of ubiquitin-mediated proteolysis, in which ubiquitin is covalently attached to specific protein target substrates that are then recognized and degraded by a high molecular weight protease.
authors.affiliation: Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: A L
authors.initials: AL
authors.lastname: Schwartz
authors.forename: A
authors.initials: A
authors.lastname: Ciechanover
mesh_terms: D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D008025:Ligases / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex; D011506:Proteins / Q000378:metabolism*; D013379:Substrate Specificity; D044767:Ubiquitin-Protein Ligases; D014452:Ubiquitins / Q000378:metabolism*
chemical_list: D009097:Multienzyme Complexes; D011506:Proteins; D014452:Ubiquitins; D044767:Ubiquitin-Protein Ligases; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D008025:Ligases