Cleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes.
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Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexAssembly and architecture of the EBV B cell entry triggering complexCharacteristics of Epstein-Barr virus envelope protein gp42.Mapping the N-terminal residues of Epstein-Barr virus gp42 that bind gH/gL by using fluorescence polarization and cell-based fusion assaysThe Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Herpes virus fusion and entry: a story with many characters.Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacersFusing structure and function: a structural view of the herpesvirus entry machinery.The KGD motif of Epstein-Barr virus gH/gL is bifunctional, orchestrating infection of B cells and epithelial cells.A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Epstein-Barr virus transcytosis through polarized oral epithelial cellsGlobal Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus.The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.Ovarian cancer molecular pathology.Epstein-Barr virus infection mechanismsThe Ig-like v-type domain of paired Ig-like type 2 receptor alpha is critical for herpes simplex virus type 1-mediated membrane fusion.Human MHC-II with Shared Epitope Motifs Are Optimal Epstein-Barr Virus Glycoprotein 42 Ligands-Relation to Rheumatoid Arthritis.Electrofusion of single cells in picoliter droplets.On chip electrofusion of single human B cells and mouse myeloma cells for efficient hybridoma generation.
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Cleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 15 April 2009
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
@en
Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
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type
label
Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
@en
Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
@nl
prefLabel
Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
@en
Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
@nl
P2093
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Cleavage and secretion of Epst ...... ane fusion with B lymphocytes.
@en
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Jessica Sorem
Richard Longnecker
Theodore S Jardetzky
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P304
P356
10.1128/JVI.00195-09
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P577
2009-04-15T00:00:00Z