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Titolo:
Protein regulation by monoubiquitin
Autore:
Hicke, L;
Indirizzi:
Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ Evanston IL USA 60208 Cell Biol, Evanston, IL 60208 USA
Titolo Testata:
NATURE REVIEWS MOLECULAR CELL BIOLOGY
fascicolo: 3, volume: 2, anno: 2001,
pagine: 195 - 201
SICI:
1471-0072(200103)2:3<195:PRBM>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
UBIQUITIN-CONJUGATING ENZYME; DNA-REPAIR; MULTIUBIQUITIN CHAIN; SACCHAROMYCES-CEREVISIAE; NEGATIVE REGULATOR; GENE-EXPRESSION; FACTOR RECEPTOR; ENDOCYTOSIS; YEAST; LIGASE;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
72
Recensione:
Indirizzi per estratti:
Indirizzo: Hicke, L Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, 2153 Sheridan Rd, Evanston, IL 60208 USA Northwestern Univ 2153 Sheridan Rd Evanston IL USA 60208 0208 USA
Citazione:
L. Hicke, "Protein regulation by monoubiquitin", NAT REV MOL, 2(3), 2001, pp. 195-201

Abstract

Multi-ubiquitin chains at least four subunits long are required for efficient recognition and degradation of ubiquitylated proteins by the proteasome, but other functions of ubiquitin have been discovered that do not involvethe proteasome. Some proteins are modified by a single ubiquitin or short ubiquitin chains. Instead of sending proteins to their death through the proteasome, monoubiquitylation regulates processes that range from membrane transport to transcriptional regulation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/08/20 alle ore 08:09:46