Proteasomes and their kin: proteases in the machine age.
Pickart
Cecile M
CM
Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, 615 North Wolfe Street, Baltimore, Maryland 21205, USA. cpickart@jhmi.edu
Cohen
Robert E
RE
D001426:Bacterial Proteins / Q000502:physiology; D003546:Cysteine Endopeptidases / Q000378:metabolism / Q000502:physiology*; D010450:Endopeptidases / Q000378:metabolism*; D005656:Fungal Proteins / Q000502:physiology; D008854:Microscopy, Electron; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism / Q000502:physiology*; D010447:Peptide Hydrolases / Q000502:physiology; D010455:Peptides / Q000737:chemistry; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D015398:Signal Transduction; D013329:Structure-Activity Relationship; D025801:Ubiquitin / Q000378:metabolism
D001426:Bacterial Proteins; D005656:Fungal Proteins; D009097:Multienzyme Complexes; D010455:Peptides; D025801:Ubiquitin; D010450:Endopeptidases; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease