Herpes simplex virus glycoprotein K is known to influence fusion of infected cells, yet is not on the cell surface.
about
N-terminal domain of Borna disease virus G (p56) protein is sufficient for virus receptor recognition and cell entryFunctional role of hepatitis C virus chimeric glycoproteins in the infectivity of pseudotyped virusElectrorotation studies of baby hamster kidney fibroblasts infected with herpes simplex virus type 1.Exacerbation of corneal scarring in HSV-1 gK-immunized mice correlates with elevation of CD8+CD25+ T cells in corneas of ocularly infected mice.Inhibitors of signal peptide peptidase (SPP) affect HSV-1 infectivity in vitro and in vivo.Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event.Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection.Glycoprotein K specified by herpes simplex virus type 1 is expressed on virions as a Golgi complex-dependent glycosylated species and functions in virion entryAmino acid differences in glycoproteins B (gB), C (gC), H (gH) and L (gL) are associated with enhanced herpes simplex virus type-1 (McKrae) entry via the paired immunoglobulin-like type-2 receptor α.Identification, localization, and regulation of expression of the UL24 protein of herpes simplex virus type 1.Plasma membrane topology of syncytial domains of herpes simplex virus type 1 glycoprotein K (gK): the UL20 protein enables cell surface localization of gK but not gK-mediated cell-to-cell fusionMutations within the pathogenic region of herpes simplex virus 1 gK signal sequences alter cell surface expression and neurovirulenceHerpes simplex virus glycoprotein K promotes egress of virus particles.Epitope mapping of HSV-1 glycoprotein K (gK) reveals a T cell epitope located within the signal domain of gKA herpes simplex virus 1 (McKrae) mutant lacking the glycoprotein K gene is unable to infect via neuronal axons and egress from neuronal cell bodies.A recombinant herpes simplex virus type 1 expressing two additional copies of gK is more pathogenic than wild-type virus in two different strains of mice.Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB.Overexpression of herpes simplex virus glycoprotein K (gK) alters expression of HSV receptors in ocularly-infected miceTime-resolved Global and Chromatin Proteomics during Herpes Simplex Virus Type 1 (HSV-1) Infection.Characterization of Varicella-Zoster virus glycoprotein K (open reading frame 5) and its role in virus growthPseudorabies virus glycoprotein gK is a virion structural component involved in virus release but is not required for entry.Pseudorabies virus glycoprotein K requires the UL20 gene product for processing.Insertions in the gG gene of pseudorabies virus reduce expression of the upstream Us3 protein and inhibit cell-to-cell spread of virus infection.Deletion of a Predicted β-Sheet Domain within the Amino Terminus of Herpes Simplex Virus Glycoprotein K Conserved among Alphaherpesviruses Prevents Virus Entry into Neuronal Axons.Human herpesvirus 6 variant A but not variant B induces fusion from without in a variety of human cells through a human herpesvirus 6 entry receptor, CD46.Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL.Herpes simplex virus type 1 glycoprotein K is not essential for infectious virus production in actively replicating cells but is required for efficient envelopment and translocation of infectious virions from the cytoplasm to the extracellular spaceComprehensive characterization of extracellular herpes simplex virus type 1 virions.Binding of Herpes Simplex Virus 1 UL20 to GODZ (DHHC3) Affects Its Palmitoylation and Is Essential for Infectivity and Proper Targeting and Localization of UL20 and Glycoprotein K.Coexpression 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.HSV-1 gM and the gK/pUL20 complex are important for the localization of gD and gH/L to viral assembly sites.Binding of HSV-1 glycoprotein K (gK) to signal peptide peptidase (SPP) is required for virus infectivityHerpes simplex virus 1 envelopment follows two diverse pathways.The absence of DHHC3 affects primary and latent HSV-1 infection.The Amino-terminus of HSV-1 Glycoprotein K (gK) is Required for gB Binding to Akt, Release of Intracellular Calcium and Fusion of the Viral Envelope with Plasma Membranes.
P2860
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P2860
Herpes simplex virus glycoprotein K is known to influence fusion of infected cells, yet is not on the cell surface.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Herpes simplex virus glycoprot ...... et is not on the cell surface.
@ast
Herpes simplex virus glycoprot ...... et is not on the cell surface.
@en
type
label
Herpes simplex virus glycoprot ...... et is not on the cell surface.
@ast
Herpes simplex virus glycoprot ...... et is not on the cell surface.
@en
prefLabel
Herpes simplex virus glycoprot ...... et is not on the cell surface.
@ast
Herpes simplex virus glycoprot ...... et is not on the cell surface.
@en
P2093
P2860
P1433
P1476
Herpes simplex virus glycoprot ...... yet is not on the cell surface
@en
P2093
Hutchinson L
Johnson DC
Roop-Beauchamp C
P2860
P304
P407
P577
1995-07-01T00:00:00Z