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Titolo:
Epstein-Barr virus nuclear protein 2 has at least two N-terminal domains that mediate self-association
Autore:
Harada, S; Yalamanchili, R; Kieff, E;
Indirizzi:
Brigham & Womens Hosp, Program Virol, Channing Lab, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 nning Lab, Boston, MA 02115 USA Brigham & Womens Hosp, Dept Med & Microbiol, Channing Lab, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 nning Lab, Boston, MA 02115 USA Brigham & Womens Hosp, Dept Mol Genet, Channing Lab, Boston, MA 02115 USA Brigham & Womens Hosp Boston MA USA 02115 nning Lab, Boston, MA 02115 USA Harvard Univ, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115Harvard Univ, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 5, volume: 75, anno: 2001,
pagine: 2482 - 2487
SICI:
0022-538X(200103)75:5<2482:EVNP2H>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-BINDING-PROTEIN; LYMPHOCYTE GROWTH TRANSFORMATION; NUCLEAR-PROTEIN-2 ACIDIC DOMAIN; RBP-J-KAPPA; C-MYB; TRANSACTIVATION; ANTIGEN-2; PROMOTER; INTERACT; ELEMENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Kieff, E Brigham & Womens Hosp, Program Virol, Channing Lab, 181 Longwood Ave, Boston, MA 02115 USA Brigham & Womens Hosp 181 Longwood Ave Boston MA USA 02115 15 USA
Citazione:
S. Harada et al., "Epstein-Barr virus nuclear protein 2 has at least two N-terminal domains that mediate self-association", J VIROLOGY, 75(5), 2001, pp. 2482-2487

Abstract

Previous genetic and biochemical analyses have indicated that the Epstein-Barr virus EBNA-2 amino terminus is important for primary B-lymphocyte growth transformation and may be involved in self-association, We now report that EBNA-2 has at least two domains, amino acids 1 to 60 and 96 to 210, which independently mediate homotypic association, 1 to 60 with 1 to 60 and 96 to 210 with 96 to 210, EBNA-2 self-association is likely to be critical to the ability of EBNA-2 to interact simultaneously with multiple cellular transcription factors, coactivators, and histone acetyltransferases through its RBPJ kappa binding and acidic activating domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 01:31:43