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.
about
Herpesvirus gB: A Finely Tuned Fusion MachineStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryThe cytoplasmic domain of varicella-zoster virus glycoprotein H regulates syncytia formation and skin pathogenesisReevaluating herpes simplex virus hemifusion.ZP2 and ZP3 cytoplasmic tails prevent premature interactions and ensure incorporation into the zona pellucida.Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.Fusing structure and function: a structural view of the herpesvirus entry machinery.Using a split luciferase assay (SLA) to measure the kinetics of cell-cell fusion mediated by herpes simplex virus glycoproteins.A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Exploiting herpes simplex virus entry for novel therapeutics.The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB.Herpes simplex virus Membrane Fusion.Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.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.Susceptibility of fish and turtles to three ranaviruses isolated from different ectothermic vertebrate classes.Mutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells.Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.
P2860
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P2860
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.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Insertion mutations in herpes ...... n cell fusion and viral entry.
@ast
Insertion mutations in herpes ...... n cell fusion and viral entry.
@en
type
label
Insertion mutations in herpes ...... n cell fusion and viral entry.
@ast
Insertion mutations in herpes ...... n cell fusion and viral entry.
@en
prefLabel
Insertion mutations in herpes ...... n cell fusion and viral entry.
@ast
Insertion mutations in herpes ...... n cell fusion and viral entry.
@en
P2093
P2860
P356
P1433
P1476
Insertion mutations in herpes ...... n cell fusion and viral entry.
@en
P2093
Julia O Jackson
Patricia G Spear
Richard Longnecker
P2860
P304
P356
10.1128/JVI.02215-09
P577
2009-12-09T00:00:00Z