The EBNA-2 arginine-glycine domain is critical but not essential for B-lymphocyte growth transformation; the rest of region 3 lacks essential interactive domains.
about
The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIEBinding of the heterogeneous ribonucleoprotein K (hnRNP K) to the Epstein-Barr virus nuclear antigen 2 (EBNA2) enhances viral LMP2A expressionModulation of Epstein-Barr virus nuclear antigen 2-dependent transcription by protein arginine methyltransferase 5.Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting.Residues 231 to 280 of the Epstein-Barr virus nuclear protein 2 are not essential for primary B-lymphocyte growth transformation.EBNA-LP associates with cellular proteins including DNA-PK and HA95.The genetic approach to the Epstein-Barr virus: from basic virology to gene therapy.C-terminal region of EBNA-2 determines the superior transforming ability of type 1 Epstein-Barr virus by enhanced gene regulation of LMP-1 and CXCR7.Molecular virology of Epstein-Barr virus.The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein.Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappaThe N-terminal half of EBNA2, except for seven prolines, is not essential for primary B-lymphocyte growth transformation.Ribosome Protein L4 is essential for Epstein-Barr Virus Nuclear Antigen 1 functionEpstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter.Epstein-Barr virus super-enhancer eRNAs are essential for MYC oncogene expression and lymphoblast proliferationFour EBNA2 domains are important for EBNALP coactivationFunctional cooperation of Epstein-Barr virus nuclear antigen 2 and the survival motor neuron protein in transactivation of the viral LMP1 promoter.Mapping EBNA-1 domains involved in binding to metaphase chromosomes.The 131-amino-acid repeat region of the essential 39-kilodalton core protein of fowlpox virus FP9, equivalent to vaccinia virus A4L protein, is nonessential and highly immunogenic.Epstein-Barr virus nuclear antigen 2 binds via its methylated arginine-glycine repeat to the survival motor neuron protein.Species-specific functions of Epstein-Barr virus nuclear antigen 2 (EBNA2) reveal dual roles for initiation and maintenance of B cell immortalization.
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The EBNA-2 arginine-glycine domain is critical but not essential for B-lymphocyte growth transformation; the rest of region 3 lacks essential interactive domains.
description
1994 nî lūn-bûn
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1994年の論文
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name
The EBNA-2 arginine-glycine do ...... essential interactive domains.
@ast
The EBNA-2 arginine-glycine do ...... essential interactive domains.
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The EBNA-2 arginine-glycine do ...... essential interactive domains.
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The EBNA-2 arginine-glycine do ...... essential interactive domains.
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The EBNA-2 arginine-glycine do ...... essential interactive domains.
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The EBNA-2 arginine-glycine do ...... essential interactive domains.
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The EBNA-2 arginine-glycine do ...... essential interactive domains
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1994-10-01T00:00:00Z