Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.
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Abalone Hemocyanin Blocks the Entry of Herpes Simplex Virus 1 into Cells: a Potential New Antiviral StrategyEmerging Vaccine TechnologiesThe Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein InteractionCathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH.Herpes virus fusion and entry: a story with many characters.PDGF receptor-α does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway.Dissection of the antibody response against herpes simplex virus glycoproteins in naturally infected humansCrystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.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.Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Polyethylene glycol-mediated fusion of herpes simplex type 1 virions with the plasma membrane of cells that support endocytic entry.The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes.Glycoprotein targeted therapeutics: a new era of anti-herpes simplex virus-1 therapeuticsHuman cytomegalovirus (HCMV) glycoprotein gB promotes virus entry in trans acting as the viral fusion protein rather than as a receptor-binding protein.Dual split protein-based fusion assay reveals that mutations to herpes simplex virus (HSV) glycoprotein gB alter the kinetics of cell-cell fusion induced by HSV entry glycoproteinsContributions of herpes simplex virus 1 envelope proteins to entry by endocytosis.Regulation of HSV glycoprotein induced cascade of events governing cell-cell fusion.Human cytomegalovirus entry into cells.Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B.Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein B ectodomain contribute to its refolding during the fusion step of virus entry.Herpes simplex virus Membrane Fusion.Mildly Acidic pH Triggers an Irreversible Conformational Change in the Fusion Domain of Herpes Simplex Virus 1 Glycoprotein B and Inactivation of Viral Entry.A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD Is Defined by Using Alphaherpesvirus gH and gL Chimeras.
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P2860
Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.
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2011 nî lūn-bûn
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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2011 թվականի ապրիլին հրատարակված գիտական հոդված
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2011年の論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年論文
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2011年论文
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name
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@ast
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@en
Capturing the herpes simplex virus core fusion complex
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type
label
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@ast
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@en
Capturing the herpes simplex virus core fusion complex
@nl
prefLabel
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@ast
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@en
Capturing the herpes simplex virus core fusion complex
@nl
P2093
P2860
P356
P1433
P1476
Capturing the herpes simplex v ...... /gL) in an acidic environment.
@en
P2093
Ekaterina E Heldwein
Gary H Cohen
J Charles Whitbeck
Tina M Cairns
Tirumala K Chowdary
P2860
P304
P356
10.1128/JVI.00119-11
P407
P577
2011-04-20T00:00:00Z