Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a functional alphaherpesvirus receptor
about
Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infectionMolecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry.Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).Herpes simplex virus glycoprotein B associates with target membranes via its fusion loopsRandom mutagenesis of the gene encoding a viral ligand for multiple cell entry receptors to obtain viral mutants altered for receptor usage.Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein DNeuron-to-cell spread of pseudorabies virus in a compartmented neuronal culture systemHerpes B virus gD interaction with its human receptor--an in silico analysis approach.Herpes virus fusion and entry: a story with many characters.Amino acid substitutions in the V domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for Pseudorabies virus or bovine herpesvirus 1.The domains of glycoprotein D required to block apoptosis induced by herpes simplex virus 1 are largely distinct from those involved in cell-cell fusion and binding to nectin1Effects of herpes simplex virus on structure and function of nectin-1/HveC.Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasProteomic characterization of pseudorabies virus extracellular virionsStructure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface.Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusionHerpesvirus entry: an updateMutational evidence of internal fusion loops in herpes simplex virus glycoprotein BAlpha-herpesvirus glycoprotein D interaction with sensory neurons triggers formation of varicosities that serve as virus exit sitesDual 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 glycoproteinsA sugar binding protein cyanovirin-N blocks herpes simplex virus type-1 entry and cell fusion.Infection of neurons and encephalitis after intracranial inoculation of herpes simplex virus requires the entry receptor nectin-1Regulation of HSV glycoprotein induced cascade of events governing cell-cell fusion.Transgenic mice expressing a soluble form of porcine nectin-1/herpesvirus entry mediator C as a model for pseudorabies-resistant livestock.Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion.Potential nectin-1 binding site on herpes simplex virus glycoprotein d.Role for 3-O-sulfated heparan sulfate as the receptor for herpes simplex virus type 1 entry into primary human corneal fibroblasts.Substitution in the murine nectin1 receptor of a single conserved amino acid at a position distal from the herpes simplex virus gD binding site confers high-affinity binding to gD.Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry.Substitution of herpes simplex virus 1 entry glycoproteins with those of saimiriine herpesvirus 1 reveals a gD-gH/gL functional interaction and a region within the gD profusion domain that is critical for fusion.In vitro antiviral activity of neem (Azardirachta indica L.) bark extract against herpes simplex virus type-1 infection.Receptor-determined susceptibility of preimplantation embryos to pseudorabies virus and porcine reproductive and respiratory syndrome virus.Implication of Soluble Forms of Cell Adhesion Molecules in Infectious Disease and Tumor: Insights from Transgenic Animal Models.
P2860
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P2860
Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a functional alphaherpesvirus receptor
description
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2001
@ast
im März 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/03/15)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/03/15)
@nl
наукова стаття, опублікована в березні 2001
@uk
مقالة علمية (نشرت في 15-3-2001)
@ar
name
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@ast
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@en
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@nl
type
label
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@ast
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@en
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@nl
prefLabel
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@ast
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@en
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@nl
P2093
P356
P1433
P1476
Porcine HveC, a member of the ...... onal alphaherpesvirus receptor
@en
P2093
C. Krummenacher
G. H. Cohen
R. J. Eisenberg
R. S. Milne
S. A. Connolly
P304
P356
10.1006/VIRO.2000.0798
P407
P577
2001-03-15T00:00:00Z