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Titolo:
NEGATIVE REGULATION OF SP1 TRANSACTIVATION IS CORRELATED WITH THE BINDING OF CELLULAR PROTEINS TO THE AMINO-TERMINUS OF THE SP1 TRANSACTIVATION DOMAIN
Autore:
MURATA Y; KIM HG; ROGERS KT; UDVADIA AJ; HOROWITZ JM;
Indirizzi:
DUKE UNIV,MED CTR,DEPT MOLEC CANC BIOL,BOX 3686 DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT MOLEC CANC BIOL DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT MICROBIOL DURHAM NC 27710
Titolo Testata:
The Journal of biological chemistry
fascicolo: 32, volume: 269, anno: 1994,
pagine: 20674 - 20681
SICI:
0021-9258(1994)269:32<20674:NROSTI>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETINOBLASTOMA GENE-PRODUCT; TRANSCRIPTION FACTOR; DNA-BINDING; FUNCTIONAL-ANALYSIS; RB PROTEIN; EXPRESSION; PURIFICATION; COACTIVATORS; INACTIVATION; ANTIONCOGENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
Y. Murata et al., "NEGATIVE REGULATION OF SP1 TRANSACTIVATION IS CORRELATED WITH THE BINDING OF CELLULAR PROTEINS TO THE AMINO-TERMINUS OF THE SP1 TRANSACTIVATION DOMAIN", The Journal of biological chemistry, 269(32), 1994, pp. 20674-20681

Abstract

Sp1 is a well characterized and ubiquitously expressed transcription factor that regulates the constitutive and induced expression of a variety of mammalian genes. It is unclear whether Sp1 activity is regulated in vivo; the mechanism by which Sp1 interacts with the basal transcription complex has not been firmly established. We report the identification of a ubiquitously expressed and evolutionarily conserved nuclear protein, p74, that specifically binds Sp1 in vivo and in vitro. p74interacts with several portions of the Sp1 trans-activation domain invitro, and we correlate the binding of p74 to the amino-terminal serine/threonine-rich subdomain of Sp1 with the inhibition of Sp1-mediatedtranscription in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 05:01:16