The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessential.
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Epstein-Barr virus LMP2A-induced B-cell survival in two unique classes of EmuLMP2A transgenic miceEpstein-Barr virus LMP2A reduces hyperactivation induced by LMP1 to restore normal B cell phenotype in transgenic miceThe EBNA3 family of Epstein-Barr virus nuclear proteins associates with the USP46/USP12 deubiquitination complexes to regulate lymphoblastoid cell line growthEpstein-Barr virus-encoded LMP2A induces an epithelial-mesenchymal transition and increases the number of side population stem-like cancer cells in nasopharyngeal carcinoma.The LMP2A ITAM is essential for providing B cells with development and survival signals in vivoMechanisms that regulate Epstein-Barr virus EBNA-1 gene transcription during restricted latency are conserved among lymphocryptoviruses of Old World primates.Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latencySignaling activities of gammaherpesvirus membrane proteinsPY motifs of Epstein-Barr virus LMP2A regulate protein stability and phosphorylation of LMP2A-associated proteins.EBNA-LP associates with cellular proteins including DNA-PK and HA95.An Epstein-Barr virus isolated from a lymphoblastoid cell line has a 16-kilobase-pair deletion which includes gp350 and the Epstein-Barr virus nuclear antigen 3AThe genetic approach to the Epstein-Barr virus: from basic virology to gene therapy.The (YXXL/I)2 signalling motif found in the cytoplasmic segments of the bovine leukaemia virus envelope protein and Epstein-Barr virus latent membrane protein 2A can elicit early and late lymphocyte activation events.Molecular virology of Epstein-Barr virus.Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell fusion.An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking.Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: protein 1 binds to the cytoskeleton through TNF receptor cytoplasmic factors.Latent Membrane Protein LMP2A Impairs Recognition of EBV-Infected Cells by CD8+ T Cells.The Epstein-Barr virus LMP1 cytoplasmic carboxy terminus is essential for B-lymphocyte transformation; fibroblast cocultivation complements a critical function within the terminal 155 residues.Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappa5' Coding and regulatory region sequence divergence with conserved function of the Epstein-Barr virus LMP2A homolog in herpesvirus papio.Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo.Identification of latent membrane protein 2A (LMP2A) domains essential for the LMP2A dominant-negative effect on B-lymphocyte surface immunoglobulin signal transductionEpstein-Barr virus latent membrane protein 2 associates with and is a substrate for mitogen-activated protein kinase.Epstein-Barr virus latent membrane protein 2A mediates transformation through constitutive activation of the Ras/PI3-K/Akt Pathway.EBV LMP2A affects LMP1-mediated NF-kappaB signaling and survival of lymphoma cells by regulating TRAF2 expression.Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation.n-Butyrate, a cell cycle blocker, inhibits the replication of polyomaviruses and papillomaviruses but not that of adenoviruses and herpesviruses.An Epstein-Barr virus with a 58-kilobase-pair deletion that includes BARF0 transforms B lymphocytes in vitroEpstein-Barr virus latent membrane protein 2A blocks calcium mobilization in B lymphocytes.Deletion of DNA encoding the first five transmembrane domains of Epstein-Barr virus latent membrane proteins 2A and 2B.Mutants of Epstein-Barr virus with a selective marker disrupting the TP gene transform B cells and replicate normally in culture.The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro.Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation.Identification of a novel protein encoded by the BamHI A region of the Epstein-Barr virus.Epstein-Barr virus latent membrane protein 2A activates beta-catenin signaling in epithelial cells.EBNA2 amino acids 3 to 30 are required for induction of LMP-1 and immortalization maintenance.Dynamic Epstein-Barr virus gene expression on the path to B-cell transformation.Epstein-Barr virus LMP2A increases IL-10 production in mitogen-stimulated primary B-cells and B-cell lymphomas.Epstein-Barr virus EBNA-3C is targeted to and regulates expression from the bidirectional LMP-1/2B promoter.
P2860
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P2860
The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessential.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The only domain which distingu ...... P2A is therefore nonessential.
@ast
The only domain which distingu ...... P2A is therefore nonessential.
@en
type
label
The only domain which distingu ...... P2A is therefore nonessential.
@ast
The only domain which distingu ...... P2A is therefore nonessential.
@en
prefLabel
The only domain which distingu ...... P2A is therefore nonessential.
@ast
The only domain which distingu ...... P2A is therefore nonessential.
@en
P2093
P2860
P1433
P1476
The only domain which distingu ...... MP2A is therefore nonessential
@en
P2093
P2860
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1992-11-01T00:00:00Z