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 nectin1
about
A new class of receptor for herpes simplex virus has heptad repeat motifs that are common to membrane fusion proteins.Discovery of mammalian genes that participate in virus infectionStructure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1Necroptosis: The Trojan horse in cell autonomous antiviral host defenseThe suppression of apoptosis by α-herpesvirus.The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entryStructure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.Baculovirus as versatile vectors for protein expression in insect and mammalian cells.Construction and properties of a herpes simplex virus 1 designed to enter cells solely via the IL-13alpha2 receptorA herpes simplex virus recombinant that exhibits a single-chain antibody to HER2/neu enters cells through the mammary tumor receptor, independently of the gD receptors.Herpes simplex virus infection and apoptosis.Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins.Apoptosis and antigen receptor function in T and B cells following exposure to herpes simplex virusEfficient replication by herpes simplex virus type 1 involves activation of the IkappaB kinase-IkappaB-p65 pathway.Potential nectin-1 binding site on herpes simplex virus glycoprotein d.Manipulation of apoptosis and necroptosis signaling by herpesvirusesHerpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL.Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein.Entry of herpes simplex virus mediated by chimeric forms of nectin1 retargeted to endosomes or to lipid rafts occurs through acidic endosomes.Herpes simplex virus type 1 immediate-early gene expression is required for the induction of apoptosis in human epithelial HEp-2 cellsCoexpression of UL20p and gK inhibits cell-cell fusion mediated by herpes simplex virus glycoproteins gD, gH-gL, and wild-type gB or an endocytosis-defective gB mutant and downmodulates their cell surface expression.The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2.Varicella-zoster virus ORF63 inhibits apoptosis of primary human neurons.
P2860
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P2860
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 nectin1
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The domains of glycoprotein D ...... fusion and binding to nectin1
@ast
The domains of glycoprotein D ...... fusion and binding to nectin1
@en
The domains of glycoprotein D ...... fusion and binding to nectin1
@nl
type
label
The domains of glycoprotein D ...... fusion and binding to nectin1
@ast
The domains of glycoprotein D ...... fusion and binding to nectin1
@en
The domains of glycoprotein D ...... fusion and binding to nectin1
@nl
prefLabel
The domains of glycoprotein D ...... fusion and binding to nectin1
@ast
The domains of glycoprotein D ...... fusion and binding to nectin1
@en
The domains of glycoprotein D ...... fusion and binding to nectin1
@nl
P2860
P50
P1433
P1476
The domains of glycoprotein D ...... fusion and binding to nectin1
@en
P2093
Elisa Avitabile
P2860
P304
P356
10.1128/JVI.77.6.3759-3767.2003
P407
P577
2003-03-01T00:00:00Z