P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
about
EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replicationThe splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylationProtein kinase C [micro] is regulated by the multifunctional chaperon protein p32Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitroSplicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particlesBinding of cellular p32 protein to the rubella virus P150 replicase protein via PxxPxR motifsThe autophagic inducer smARF interacts with and is stabilized by the mitochondrial p32 proteinEBP2, a human protein that interacts with sequences of the Epstein-Barr virus nuclear antigen 1 important for plasmid maintenance.Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1Interactions between rubella virus capsid and host protein p32 are important for virus replication.Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix proteinEpstein-Barr virus and virus human protein interaction mapsThe EBV nuclear antigen 1 (EBNA1) enhances B cell immortalization several thousandfoldSOCS1 and SOCS3 are targeted by hepatitis C virus core/gC1qR ligation to inhibit T-cell functionStructure of the T. brucei p22 protein, a cytochrome oxidase subunit II (COII) specific RNA editing accessory factorMam33 promotes cytochrome c oxidase subunit I translation in Saccharomyces cerevisiae mitochondria.Epstein-Barr virus latent genesThe human gC1qR/p32 gene, C1qBP. Genomic organization and promoter analysisThe hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qRDifferential isoform expression and interaction with the P32 regulatory protein controls the subcellular localization of the splicing factor U2AF26Epstein-Barr virus nuclear antigen 1 does not cause lymphoma in C57BL/6J miceDirect binding of hepatitis C virus core to gC1qR on CD4+ and CD8+ T cells leads to impaired activation of Lck and Akt.Mta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA.Interaction between basic residues of Epstein-Barr virus EBNA1 protein and cellular chromatin mediates viral plasmid maintenance.Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7.Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32.Identification of human cytomegalovirus UL84 virus- and cell-encoded binding partners by using proteomics analysisZinc coordination is required for and regulates transcription activation by Epstein-Barr nuclear antigen 1Epstein-Barr virus nuclear antigen 1 does not induce lymphoma in transgenic FVB mice.Disruption of PML subnuclear domains by the acidic IE1 protein of human cytomegalovirus is mediated through interaction with PML and may modulate a RING finger-dependent cryptic transactivator function of PMLRoscovitine inhibits EBNA1 serine 393 phosphorylation, nuclear localization, transcription, and episome maintenanceFunctional analyses of the EBNA1 origin DNA binding protein of Epstein-Barr virus.The replicator of the Epstein-Barr virus latent cycle origin of DNA replication, oriP, is composed of multiple functional elements.EBNA-1: a protein pivotal to latent infection by Epstein-Barr virus.Episomal vectors for gene expression in mammalian cells.Epstein-Barr virus nuclear antigen 1 activates transcription from episomal but not integrated DNA and does not alter lymphocyte growthHuman origin recognition complex binds to the region of the latent origin of DNA replication of Epstein-Barr virus.Maintenance of Epstein-Barr virus (EBV) oriP-based episomes requires EBV-encoded nuclear antigen-1 chromosome-binding domains, which can be replaced by high-mobility group-I or histone H1.Development of a novel helper-dependent adenovirus-Epstein-Barr virus hybrid system for the stable transformation of mammalian cells.Drosophila TAP/p32 is a core histone chaperone that cooperates with NAP-1, NLP, and nucleophosmin in sperm chromatin remodeling during fertilization.
P2860
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P2860
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
description
1997 nî lūn-bûn
@nan
1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
@ast
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
@en
type
label
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
@ast
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
@en
prefLabel
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
@ast
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.
@en
P2093
P356
P1433
P1476
P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus
@en
P2093
P356
10.1006/VIRO.1997.8739
P407
P577
1997-09-01T00:00:00Z