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Titolo:
TRANSACTIVATION AND TRANSFORMATION BY MYB ARE NEGATIVELY REGULATED BYA LEUCINE-ZIPPER STRUCTURE
Autore:
KANEIISHII C; MACMILLAN EM; NOMURA T; SARAI A; RAMSAY RG; AIMOTO S; ISHII S; GONDA TJ;
Indirizzi:
INST PHYS & CHEM RES,TSUKUBA LIFE SCI CTR TSUKUBA IBARAKI 305 JAPAN INST MED & VET SCI,HANSON CTR CANC RES ADELAIDE SA 5000 AUSTRALIA OSAKA UNIV,INST PROT RES SUITA OSAKA 565 JAPAN ROYAL MELBOURNE HOSP,LUDWIG INST CANC RES,TUMOR BIOL BRANCH PARKVILLEVIC 3050 AUSTRALIA
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 7, volume: 89, anno: 1992,
pagine: 3088 - 3092
SICI:
0027-8424(1992)89:7<3088:TATBMA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
C-MYB; V-MYB; TRANSCRIPTIONAL ACTIVATOR; CELLULAR PROGENITOR; NUCLEOTIDE-SEQUENCE; ONCOGENE PRODUCT; PROTO-ONCOGENE; BINDING; JUN; GENE;
Keywords:
ONCOGENE; DNA-BINDING PROTEIN; NEGATIVE REGULATORY DOMAIN; POINT MUTANTS; INHIBITORS;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
C. Kaneiishii et al., "TRANSACTIVATION AND TRANSFORMATION BY MYB ARE NEGATIVELY REGULATED BYA LEUCINE-ZIPPER STRUCTURE", Proceedings of the National Academy of Sciences of the United Statesof America, 89(7), 1992, pp. 3088-3092

Abstract

The negative regulatory domain of the c-myb protooncogene product (c-Myb) normally represses transcriptional activation by c-Myb. We show here that a leucine-zipper structure is a component of the negative regulatory domain, because its disruption markedly increases both the transactivating and transforming capacities of c-Myb. We also demonstratethat this leucine-zipper structure can interact with cellular proteins. Our results suggest that an inhibitor that suppresses transactivation binds to c-Myb through the leucine zipper and that c-Myb can be oncogenically activated by missense mutation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:37:04