A spliced Epstein-Barr virus gene expressed in immortalized lymphocytes is created by circularization of the linear viral genome.Laux G., Perricaudet M., Farrell P.J.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 7:769-774 (1988)Cited in123
Two related Epstein-Barr virus membrane proteins are encoded by separate genes.Sample J., Liebowitz D., Kieff E.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LMP2A AND LMP2B)CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Virol. 63:933-937 (1989)Cited in13
DNA sequence and expression of the B95-8 Epstein-Barr virus genome.Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C.[...], Barrell B.G.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM LMP2A)CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 310:207-211 (1984)Cited in7743
Updated Epstein-Barr virus (EBV) DNA sequence and analysis of a promoter for the BART (CST, BARF0) RNAs of EBV.de Jesus O., Smith P.R., Spender L.C., Elgueta Karstegl C., Niller H.H., Huang D., Farrell P.J.View abstractCited forGENOME REANNOTATIONCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 84:1443-1450 (2003)Cited in786
An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase.Longnecker R., Druker B., Roberts T.M., Kieff E.View abstractCited forPHOSPHORYLATION (ISOFORM LMP2A)CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Virol. 65:3681-3692 (1991)Cited in1
An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking.Miller C.L., Lee J.H., Kieff E., Longnecker R.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 91:772-776 (1994)Cited in1
Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases.Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., Kieff E.View abstractCited forINTERACTION WITH HUMAN SYK AND LYN (ISOFORM LMP2A)CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCImmunity 2:155-166 (1995)Cited in3
Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latency.Fruehling S., Swart R., Dolwick K.M., Kremmer E., Longnecker R.View abstractCited forMUTAGENESIS OF TYR-74; TYR-85 AND TYR-112CategoriesPhenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Virol. 72:7796-7806 (1998)Cited in1
Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signals.Caldwell R.G., Wilson J.B., Anderson S.J., Longnecker R.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCImmunity 9:405-411 (1998)Cited in1
Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases.Winberg G., Matskova L., Chen F., Plant P., Rotin D., Gish G., Ingham R., Ernberg I., Pawson T.View abstractCited forINTERACTION WITH HUMAN ITCH AND NEDD4L (ISOFORM LMP2A)CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 20:8526-8535 (2000)Cited in3
Epstein-Barr virus coopts lipid rafts to block the signaling and antigen transport functions of the BCR.Dykstra M.L., Longnecker R., Pierce S.K.View abstractCited forSUBCELLULAR LOCATIONCategoriesSubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCImmunity 14:57-67 (2001)Cited in1
Epstein-Barr virus latent membrane protein 2B (LMP2B) co-localizes with LMP2A in perinuclear regions in transiently transfected cells.Lynch D.T., Zimmerman J.S., Rowe D.T.View abstractCited forSUBCELLULAR LOCATIONCategoriesSubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Gen. Virol. 83:1025-1035 (2002)Cited in1
Lysine-independent ubiquitination of Epstein-Barr virus LMP2A.Ikeda M., Ikeda A., Longnecker R.View abstractCited forUBIQUITINATIONCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 300:153-159 (2002)Cited in1
Allele-dependent similarity between viral and self-peptide presentation by HLA-B27 subtypes.Fiorillo M.T., Ruckert C., Hulsmeyer M., Sorrentino R., Saenger W., Ziegler A., Uchanska-Ziegler B.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 236-244CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 280:2962-2971 (2005)Cited in1Mapped to2
Dual non-contiguous peptide occupancy of HLA class I evoke antiviral human CD8 T cell response and form neo-epitopes with self-antigens.Xiao Z., Ye Z., Tadwal V.S., Shen M., Ren E.C.View abstractCategoriesStructureSourcePDB: 5GRD, PDB: 5GSDPubMedEurope PMCSci Rep 7:5072-5072 (2017)Mapped to3
Structural and energetic evidence for highly peptide-specific tumor antigen targeting via allo-MHC restriction.Simpson A.A., Mohammed F., Salim M., Tranter A., Rickinson A.B., Stauss H.J., Moss P.A., Steven N.M., Willcox B.E.View abstractCategoriesStructureSourcePDB: 3REWPubMedEurope PMCProc Natl Acad Sci U S A 108:21176-21181 (2011)Mapped to3
LMP1 association with CD63 in endosomes and secretion via exosomes limits constitutive NF-kappaB activation.Verweij F.J., van Eijndhoven M.A., Hopmans E.S., Vendrig T., Wurdinger T., Cahir-McFarland E., Kieff E., Geerts D., van der Kant R.[...], Pegtel D.M.View abstractCategoriesInteractionSourceIntAct: P13285PubMedEurope PMCEMBO J 30:2115-2129 (2011)Mapped to5
Structural basis for T cell alloreactivity among three HLA-B14 and HLA-B27 antigens.Kumar P., Vahedi-Faridi A., Saenger W., Merino E., Lopez de Castro J.A., Uchanska-Ziegler B., Ziegler A.View abstractCategoriesStructureSourcePDB: 3BVNPubMedEurope PMCJ Biol Chem 284:29784-29797 (2009)Cited in1Mapped to4
Expression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral peptide and with a self-peptide.Kumar P., Vahedi-Faridi A., Merino E., Lopez de Castro J.A., Volz A., Ziegler A., Saenger W., Uchanska-Ziegler B.View abstractCategoriesStructureSourcePDB: 3BVNPubMedEurope PMCActa Crystallogr Sect F Struct Biol Cryst Commun 63:631-634 (2007)Mapped to3
NMR structural studies of the ItchWW3 domain reveal that phosphorylation at T30 inhibits the interaction with PPxY-containing ligands.Morales B., Ramirez-Espain X., Shaw A.Z., Martin-Malpartida P., Yraola F., Sanchez-Tillo E., Farrera C., Celada A., Royo M., Macias M.J.View abstractCategoriesStructureSourcePDB: 2JO9PubMedEurope PMCStructure 15:473-483 (2007)Cited in1Mapped to1
Identification of the WW domain-interaction sites in the unstructured N- terminal domain of EBV LMP 2A.Seo M.D., Park S.J., Kim H.J., Lee B.J.View abstractCategoriesInteractionSourceIntAct: P13285PubMedEurope PMCFEBS Lett 581:65-70 (2007)Mapped to2
Dual, HLA-B27 subtype-dependent conformation of a self-peptide.Hulsmeyer M., Fiorillo M.T., Bettosini F., Sorrentino R., Saenger W., Ziegler A., Uchanska-Ziegler B.View abstractCategoriesStructureSourcePDB: 1UXS, PDB: 1UXWPubMedEurope PMCJ. Exp. Med. 199:271-281 (2004)Cited in1Mapped to4