Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins.
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Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3CAssociation of chromatin proteins high mobility group box (HMGB) 1 and HMGB2 with mitotic chromosomesEBP2, a human protein that interacts with sequences of the Epstein-Barr virus nuclear antigen 1 important for plasmid maintenance.EBP2 plays a key role in Epstein-Barr virus mitotic segregation and is regulated by aurora family kinases.EBNA1 partitions Epstein-Barr virus plasmids in yeast cells by attaching to human EBNA1-binding protein 2 on mitotic chromosomesEpstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1The budding yeast homolog of the human EBNA1-binding protein 2 (Ebp2p) is an essential nucleolar protein required for pre-rRNA processing.Protein kinase A associates with HA95 and affects transcriptional coactivation by Epstein-Barr virus nuclear proteins.Interaction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: implication of cytoplasmic function of EBNA-LP.In vivo dynamics of EBNA1-oriP interaction during latent and lytic replication of Epstein-Barr virus.Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting.Hyperphosphorylation of EBNA2 by Epstein-Barr virus protein kinase suppresses transactivation of the LMP1 promoter.Functional analyses of the EBNA1 origin DNA binding protein of Epstein-Barr virus.Sequence and functional analysis of EBNA-LP and EBNA2 proteins from nonhuman primate lymphocryptovirusesEBNA-LP associates with cellular proteins including DNA-PK and HA95.Identification of major phosphorylation sites of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP): ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylationEBNA-1: a protein pivotal to latent infection by Epstein-Barr virus.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.Separation of the DNA replication, segregation, and transcriptional activation functions of Epstein-Barr nuclear antigen 1.Nuclear import of Epstein-Barr virus nuclear antigen 1 mediated by NPI-1 (Importin alpha5) is up- and down-regulated by phosphorylation of the nuclear localization signal for which Lys379 and Arg380 are essential.EBNA3C coactivation with EBNA2 requires a SUMO homology domain.Epstein-Barr virus (EBV) nuclear antigen 1 colocalizes with cellular replication foci in the absence of EBV plasmids.Epstein-Barr nuclear antigen leader protein coactivates transcription through interaction with histone deacetylase 4.The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation.Direct interactions between Epstein-Barr virus leader protein LP and the EBNA2 acidic domain underlie coordinate transcriptional regulation.Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappaThe Epstein-Barr virus-encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies.EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJkappa in Epstein-Barr virus-transformed B lymphocytes.Epstein-Barr virus nuclear protein LP stimulates EBNA-2 acidic domain-mediated transcriptional activationEpstein-Barr virus leader protein enhances EBNA-2-mediated transactivation of latent membrane protein 1 expression: a role for the W1W2 repeat domainRetention of plasmid DNA in mammalian cells is enhanced by binding of the Epstein-Barr virus replication protein EBNA1.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.Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation.Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation.Use of second-site homologous recombination to demonstrate that Epstein-Barr virus nuclear protein 3B is not important for lymphocyte infection or growth transformation in vitroAn Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator.The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation.Mitosis-specific hyperphosphorylation of Epstein-Barr virus nuclear antigen 2 suppresses its function.The Epstein-Barr Virus EBNA1 Protein.Regulatory network analysis of Epstein-Barr virus identifies functional modules and hub genes involved in infectious mononucleosis.
P2860
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P2860
Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
1990年學術文章
@zh-hant
name
Subnuclear localization and ph ...... nt infection nuclear proteins.
@en
Subnuclear localization and ph ...... nt infection nuclear proteins.
@nl
type
label
Subnuclear localization and ph ...... nt infection nuclear proteins.
@en
Subnuclear localization and ph ...... nt infection nuclear proteins.
@nl
prefLabel
Subnuclear localization and ph ...... nt infection nuclear proteins.
@en
Subnuclear localization and ph ...... nt infection nuclear proteins.
@nl
P2093
P1433
P1476
Subnuclear localization and ph ...... nt infection nuclear proteins.
@en
P2093
P304
P356
10.1016/0042-6822(90)90027-O
P407
P577
1990-06-01T00:00:00Z