Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions.
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Herpesvirus gB: A Finely Tuned Fusion MachineExtensive Mutagenesis of the HSV-1 gB Ectodomain Reveals Remarkable Stability of Its Postfusion FormReevaluating herpes simplex virus hemifusion.The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Modulation of Epstein-Barr virus glycoprotein B (gB) fusion activity by the gB cytoplasmic tail domainFusing structure and function: a structural view of the herpesvirus entry machinery.An immunoreceptor tyrosine-based inhibition motif in varicella-zoster virus glycoprotein B regulates cell fusion and skin pathogenesis.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 glycoproteinsThe Glycoprotein B Cytoplasmic Domain Lysine Cluster Is Critical for Varicella-Zoster Virus Cell-Cell Fusion Regulation and InfectionMutations in Pseudorabies Virus Glycoproteins gB, gD, and gH Functionally Compensate for the Absence of gL.Functional Characterization of Glycoprotein H Chimeras Composed of Conserved Domains of the Pseudorabies Virus and Herpes Simplex Virus 1 Homologs.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.Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype.Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.Epstein-Barr virus fusion with epithelial cells triggered by gB is restricted by a gL glycosylation site.Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation.Mutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells.Self-assembly of α-helices to form rare two-dimensional square P4mm symmetry via silica mineralization.
P2860
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P2860
Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Syncytial phenotype of C-termi ...... inished membrane interactions.
@ast
Syncytial phenotype of C-termi ...... inished membrane interactions.
@en
type
label
Syncytial phenotype of C-termi ...... inished membrane interactions.
@ast
Syncytial phenotype of C-termi ...... inished membrane interactions.
@en
prefLabel
Syncytial phenotype of C-termi ...... inished membrane interactions.
@ast
Syncytial phenotype of C-termi ...... inished membrane interactions.
@en
P2860
P356
P1433
P1476
Syncytial phenotype of C-termi ...... inished membrane interactions.
@en
P2093
Ekaterina E Heldwein
Tirumala Kumar Chowdary
P2860
P304
P356
10.1128/JVI.00206-10
P577
2010-03-03T00:00:00Z