Ubiquitin at Fox Chase

Cell Death and Differentiation

Volumn 12, Issue 9, 2005, Pages 1198-1201

  Rose, I ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Ubiquitin

Indexed keywords

CELL ENZYME; HISTONE H2A; LIGAND; PROTEASOME; PROTEIN P53; TYROSINE AMINOTRANSFERASE; UBIQUITIN; UBIQUITIN ACTIVATING ENZYME E1; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

CELL FREE SYSTEM; CELL LYSATE; COMPLEX FORMATION; COVALENT BOND; ENZYME ACTIVITY; ENZYME MECHANISM; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN STABILITY; RETICULOCYTE; REVIEW; UNITED STATES;

ANIMALS; BIOCHEMISTRY; HISTORY, 20TH CENTURY; HUMANS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN STRUCTURE, TERTIARY; UBIQUITIN; UNITED STATES;

EID: 23944469919     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401710     Document Type: Review

References (20)

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2. Schimke RT and Doyle D (1970) Control of enzyme levels in animal tissues. Annu. Rev. Biochem. 39: 929-976
3. Simpson MV (1953) Control of enzyme levels in animal tissues. J. Biol. Chem. 20: 143-154
4. See previous autobiographical chapter
5. Rose IA et al. (1974) Determination of the rate of hexokinase-glucose dissociation by the isotope-trapping method. J. Biol. Chem. 249: 5163-5168
6. Etlinger JD and Goldberg AL (1977) A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc. Natl. Acad. Sci. USA 86: 7751-7755
7. Ciechanover A, Hod Y and Hershko A (1978) A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem. Biophys. Res. Commun. 81: 1100-1105
8. Hershko A, Ciechanover A, Heller H, Haas AL and Rose IA (1980) Proposed role of ATP in protein breakdown: conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc. Natl. Acad. Sci. USA 77: 1783-1786
9. Wilkinson KD, Urban MK and Haas AL (1980) Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes. J. Biol. Chem. 255: 7529-7532
10. Haas AL, Murphy KE and Bright PM (1985) The inactivation of ubiquitin accounts for the inability to demonstrate ATP, ubiquitin-dependent proteolysis in liver extracts. J. Biol. Chem. 260: 4694-4703
11. Haas AL, Warms JVB, Hershko A and Rose IA (1982) Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257: 2543-2548
12. Haas AL and Rose IA (1982) The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J. Biol. Chem. 257: 10329-10337
13. Haas AL, Warms JVB and Rose IA (1983) Biochemistry 22: 4388-4394
14. Hershko A, Ciechanover A and Rose IA (1981) Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown. J. Biol. Chem. 256: 1525-1528
15. Rose IA and Warms JVB (1983) Biochemistry 22: 4288-4294
16. Pickart CM and Rose IA (1985) Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J. Biol. Chem. 260: 7903-7910
17. Pickart CM and Rose IA (1986) Mechanism of ubiquitin carboxyl-terminal hydrolase. Borohydride and hydroxylamine inactivate in the presence of ubiquitin. J. Biol. Chem. 261: 10210-10217
18. Johnston SC, Riddle SM, Cohen RE and Hill CP (1999) Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18: 3877-3887
19. Hu M, Li P, Li M, Li W, Yao T, Wu J-W, Gu W, Cohen RE and Shi Y (2002) Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111: 1041-1054
20. Johnston SC, Larsen CN, Cook WJ, Wilkinson KD and Hill CP (1997) Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J. 16: 3787-3796