The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation.

about

EBF1 binds to EBNA2 and promotes the assembly of EBNA2 chromatin complexes in B cells.Species-specific functions of Epstein-Barr virus nuclear antigen 2 (EBNA2) reveal dual roles for initiation and maintenance of B cell immortalization.

P2860

Q41926654-B90728F0-604B-4E82-A4E6-1933AFD64C5B Q47271015-7FF10409-A2E9-45DD-A06F-CEEB73DA3AEC

P2860

The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation.

Item

http://www.wikidata.org/entity/Q35664999

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@ast

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@en

type

Item

label

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@ast

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@en

prefLabel

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@ast

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@en

P1476

The EBNA-2 N-Terminal Transact ...... ed for Target Gene Activation.

@en

P2093

Bettina Kempkes

http://www.w3.org/2001/XMLSchema#string

Elfriede Nössner

http://www.w3.org/2001/XMLSchema#string

Janosch Hennig

http://www.w3.org/2001/XMLSchema#string

Paul D Ling

http://www.w3.org/2001/XMLSchema#string

Peijian Zou

http://www.w3.org/2001/XMLSchema#string

Sybille Thumann

http://www.w3.org/2001/XMLSchema#string

P2860

The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE

The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Studies on the propagation in vitro of poliomyelitis viruses. IV. Viral multiplication in a stable strain of human malignant epithelial cells (strain HeLa) derived from an epidermoid carcinoma of the cervix

Epstein-Barr virus lymphoproliferative disease after hematopoietic stem cell transplant

Epstein-barr virus sequence variation-biology and disease

Structural and Functional Characterization of a Complex between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 Subunit of TFIIH

Inference of macromolecular assemblies from crystalline state

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

Main-chain bond lengths and bond angles in protein structures

P304

e1004910

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1371/JOURNAL.PPAT.1004910

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Michael Sattler

Anders Friberg

P577

2015-05-29T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

277406859

http://www.w3.org/2001/XMLSchema#string

P698

26024477

http://www.w3.org/2001/XMLSchema#string

P932

4449002

http://www.w3.org/2001/XMLSchema#string

The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation.

about

P2860

P2860

The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932