Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B
about
PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein BBimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusionViral and developmental cell fusion mechanisms: conservation and divergenceHerpes simplex virus glycoprotein B associates with target membranes via its fusion loopsStructure of a trimeric variant of the Epstein-Barr virus glycoprotein BViral entry mechanisms: cellular and viral mediators of herpes simplex virus entryRandom linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein BStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStructure of Epstein-Barr Virus Glycoprotein 42 Suggests a Mechanism for Triggering Receptor-Activated Virus EntryCrystal structure of the conserved herpesvirus fusion regulator complex gH–gLStructure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibodyCrystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexThe Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein InteractionMolecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complexRole of Abl kinase and the Wave2 signaling complex in HIV-1 entry at a post-hemifusion stepInteraction domain of glycoproteins gB and gH of Marek's disease virus and identification of an antiviral peptide with dual functionsAssembly and architecture of the EBV B cell entry triggering complexReevaluating herpes simplex virus hemifusion.Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry.The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infectionAnti-glycoprotein H antibody impairs the pathogenicity of varicella-zoster virus in skin xenografts in the SCID mouse model.Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry.Insulin degrading enzyme induces a conformational change in varicella-zoster virus gE, and enhances virus infectivity and stabilityGlycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entryLow pH-induced conformational change in herpes simplex virus glycoprotein B.Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infectionCharacteristics of Epstein-Barr virus envelope protein gp42.Negative potentials across biological membranes promote fusion by class II and class III viral proteinsCholesterol dependence of varicella-zoster virion entry into target cellsCapturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Herpes virus fusion and entry: a story with many characters.The calcitonin receptor gene is a candidate for regulation of susceptibility to herpes simplex type 1 neuronal infection leading to encephalitis in ratImpact of valency of a glycoprotein B-specific monoclonal antibody on neutralization of herpes simplex virusBimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.Rhesus and human cytomegalovirus glycoprotein L are required for infection and cell-to-cell spread of virus but cannot complement each other.Class III viral membrane fusion proteins.Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor alpha.Differential effects on cell fusion activity of mutations in herpes simplex virus 1 glycoprotein B (gB) dependent on whether a gD receptor or a gB receptor is overexpressedDirect and specific binding of the UL16 tegument protein of herpes simplex virus to the cytoplasmic tail of glycoprotein E.
P2860
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P2860
Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@ast
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@en
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@nl
type
label
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@ast
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@en
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@nl
prefLabel
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@ast
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@en
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@nl
P2860
P356
P1476
Herpes simplex virus type 1 me ...... f glycoproteins D, H, L, and B
@en
P2093
Ravi P Subramanian
P2860
P304
P356
10.1073/PNAS.0608374104
P407
P577
2007-02-20T00:00:00Z