Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1
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Analysis of a neutralizing antibody for human herpesvirus 6B reveals a role for glycoprotein Q1 in viral entryStructure of a trimeric variant of the Epstein-Barr virus glycoprotein BAntigen-specific T cells: analyses of the needles in the haystackStructural and Mechanistic Insights into the Tropism of Epstein-Barr VirusHerpesvirus gB: A Finely Tuned Fusion MachineStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryExploration of the P6/P7 region of the peptide-binding site of the human class II major histocompatability complex protein HLA-DR1Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease associationStructure of Epstein-Barr Virus Glycoprotein 42 Suggests a Mechanism for Triggering Receptor-Activated Virus EntryThe Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like DomainsCrystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexCrystal Structure of Reovirus Attachment Protein σ1 in Complex with Sialylated OligosaccharidesAssembly and architecture of the EBV B cell entry triggering complexCharacteristics of Epstein-Barr virus envelope protein gp42.The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.Biophysical investigations of complement receptor 2 (CD21 and CR2)-ligand interactions reveal amino acid contacts unique to each receptor-ligand pairMapping the N-terminal residues of Epstein-Barr virus gp42 that bind gH/gL by using fluorescence polarization and cell-based fusion assaysMutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusionThe 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.Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cellsInvestigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).A gammaherpesvirus uses alternative splicing to regulate its tropism and its sensitivity to neutralization.Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacersαvβ6- and αvβ8-integrins serve as interchangeable receptors for HSV gH/gL to promote endocytosis and activation of membrane fusion.Soluble Epstein-Barr virus glycoproteins gH, gL, and gp42 form a 1:1:1 stable complex that acts like soluble gp42 in B-cell fusion but not in epithelial cell fusion.Neuropilin 1 is an entry factor that promotes EBV infection of nasopharyngeal epithelial cellsMutational analysis of the HLA class II interaction with Epstein-Barr virus glycoprotein 42.Herpesvirus entry: an updateFusion of Epstein-Barr virus with epithelial cells can be triggered by αvβ5 in addition to αvβ6 and αvβ8, and integrin binding triggers a conformational change in glycoproteins gHgL.Fusing 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.Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry.Epstein-Barr virus entry.Binding-site interactions between Epstein-Barr virus fusion proteins gp42 and gH/gL reveal a peptide that inhibits both epithelial and B-cell membrane fusion.Nonmuscle myosin heavy chain IIA mediates Epstein-Barr virus infection of nasopharyngeal epithelial cells.Interference with T cell receptor-HLA-DR interactions by Epstein-Barr virus gp42 results in reduced T helper cell recognition.A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.HLAMatchmaker: a molecularly based algorithm for histocompatibility determination. V. Eplet matching for HLA-DR, HLA-DQ, and HLA-DP.
P2860
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P2860
Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@ast
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@en
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@nl
type
label
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@ast
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@en
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@nl
prefLabel
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@ast
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@en
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@nl
P2093
P3181
P1433
P1476
Structure of the Epstein-Barr ...... MHC class II receptor HLA-DR1
@en
P2093
Keith M Haan
Maureen M Mullen
Richard Longnecker
Theodore S Jardetzky
P304
P3181
P356
10.1016/S1097-2765(02)00465-3
P577
2002-02-01T00:00:00Z