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Volumn 300, Issue 5617, 2003, Pages 342-344

Polyubiquitination of p53 by a ubiquitin ligase activity of p300

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CELLS; DEGRADATION; TUMORS;

EID: 0037432773     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1080386     Document Type: Article
Times cited : (395)

References (25)
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    • note
    • E3 enzymes catalyze the conjugation of Ub moieties by using isopeptide linkage to ε-amino groups on target protein lysines. Mono- or polyubiquitination may occur. E4 enzymes elongate shorter (<4 Ub moieties) Ub chains to form polyubiquitin conjugates on specific substrates.
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    • note
    • Materials and methods are available as supporting material on Science Online.
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    • note
    • Autoubiquitination reactions contain URC and a potential E3, without the addition of a specific substrate. Two potential products of such a reaction are ubiquitinated forms of the E3 and polymerized Ub, where Ub itself is the substrate.
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    • note
    • We thank E. Kieff, M. Ewen, and R. Drapkin for their critical reading of this manuscript; C. Prives for pS3-expressing baculovirus; G. Lozano for MDM2-null MEFs; and S. Sadis for helpful suggestions. This work was supported by a National Cancer Institute (NCI) Howard Temin Award (S.R.G.), an NCI grant CA15751 (D.M.L.), the Claudia Adams Barr Program (S.R.G. and A.L.K.), and the Harcourt General Charitable Foundation (S.R.G.).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.