Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex
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Structural and Mechanistic Insights into the Tropism of Epstein-Barr VirusEmerging Vaccine TechnologiesStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryStructure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibodyMechanism for neutralizing activity by the anti-CMV gH/gL monoclonal antibody MSL-109Viral membrane fusion.The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's sarcoma–associated herpesvirusAssembly and architecture of the EBV B cell entry triggering complexInsertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.A wide extent of inter-strain diversity in virulent and vaccine strains of alphaherpesviruses.Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.Herpes virus fusion and entry: a story with many characters.Epstein-Barr virus glycoprotein gB and gHgL can mediate fusion and entry in trans, and heat can act as a partial surrogate for gHgL and trigger a conformational change in gB.The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cellsThe viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex.Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacersStructural and biochemical studies of HCMV gH/gL/gO and Pentamer reveal mutually exclusive cell entry complexes.Comparative analysis of glycoprotein B (gB) of equine herpesvirus type 1 and type 4 (EHV-1 and EHV-4) in cellular tropism and cell-to-cell transmissionStructure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.Fusion 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.A site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex 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.Important but differential roles for actin in trafficking of Epstein-Barr virus in B cells and epithelial cells.Bovine herpesvirus type 4 glycoprotein L is nonessential for infectivity but triggers virion endocytosis during entry.Scanning Mutagenesis of Human Cytomegalovirus Glycoprotein gH/gL.Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry.Human Cytomegalovirus gH/gL/gO Promotes the Fusion Step of Entry into All Cell Types, whereas gH/gL/UL128-131 Broadens Virus Tropism through a Distinct Mechanism.Patient-Specific Neutralizing Antibody Responses to Herpes Simplex Virus Are Attributed to Epitopes on gD, gB, or Both and Can Be Type Specific.Human Cytomegalovirus gH/gL Forms a Stable Complex with the Fusion Protein gB in Virions.Nonmuscle myosin heavy chain IIA mediates Epstein-Barr virus infection of nasopharyngeal epithelial cells.Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Complementation of the function of glycoprotein H of human herpesvirus 6 variant A by glycoprotein H of variant B in the virus life cycle.Features of Human Herpesvirus-6A and -6B EntryRegulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors.Alphaherpesvirinae and Gammaherpesvirinae glycoprotein L and CMV UL130 originate from chemokinesThe large groove found in the gH/gL structure is an important functional domain for Epstein-Barr virus fusion.Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.
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P2860
Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex
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2010 nî lūn-bûn
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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
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2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
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name
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@ast
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@en
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@nl
type
label
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@ast
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@en
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@nl
prefLabel
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@ast
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@en
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@nl
P2093
P2860
P3181
P356
P1476
Crystal structure of the Epste ...... glycoprotein L (gH/gL) complex
@en
P2093
Austin N Kirschner
Hisae Matsuura
Richard Longnecker
Theodore S Jardetzky
P2860
P304
P3181
P356
10.1073/PNAS.1011806108
P407
P577
2010-12-28T00:00:00Z