Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1.
about
Cell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB)Herpes simplex virus glycoprotein B associates with target membranes via its fusion loopsConstruction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deletedHerpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BRandom linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein BGenital Herpes: Insights into Sexually Transmitted Infectious DiseaseIdentification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis.The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA.Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins.A role for heparan sulfate in viral surfing.Effects of truncation of the carboxy terminus of pseudorabies virus glycoprotein B on infectivity.Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infectionHerpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles.Heparan sulfate proteoglycan binding by herpes simplex virus type 1 glycoproteins B and C, which differ in their contributions to virus attachment, penetration, and cell-to-cell spread.The extracellular domain of herpes simplex virus gE is sufficient for accumulation at cell junctions but not for cell-to-cell spread.A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells.Herpes simplex virus triggers and then disarms a host antiviral response.Mathematical modeling of herpes simplex virus distribution in solid tumors: implications for cancer gene therapy.A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH.A cell-free recombination system for site-specific integration of multigenic shuttle plasmids into the herpes simplex virus type 1 genome.Identification and characterization of a novel herpes simplex virus glycoprotein, gK, involved in cell fusionThe extracellular domain of herpes simplex virus gE is indispensable for efficient cell-to-cell spread: evidence for gE/gI receptorsHerpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entryDirected selection of recombinant human monoclonal antibodies to herpes simplex virus glycoproteins from phage display librariesHerpes virus fusion and entry: a story with many characters.Directed egress of animal viruses promotes cell-to-cell spreadTruncation of herpes simplex virus type 2 glycoprotein B increases its cell surface expression and activity in cell-cell fusion, but these properties are unrelated.Truncated forms of glycoprotein D of herpes simplex virus 1 capable of blocking apoptosis and of low-efficiency entry into cells form a heterodimer dependent on the presence of a cysteine located in the shared transmembrane domains.Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at early times and then redistribute to cell junctions to promote cell-cell spread.Identification of functional domains in herpes simplex virus 2 glycoprotein B.Herpes simplex virus glycoproteins gB and gD function in a redundant fashion to promote secondary envelopmentFunction of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusionVirus receptors: implications for pathogenesis and the design of antiviral agents.Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane.Herpes simplex virus glycoprotein K is known to influence fusion of infected cells, yet is not on the cell surface.Herpes simplex virus glycoprotein K promotes egress of virus particles.Glycoprotein B of herpes simplex virus type 1 oligomerizes through the intermolecular interaction of a 28-amino-acid domainGlycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo.Cross-linking of glycoprotein oligomers during herpes simplex virus type 1 entry.The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication.
P2860
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P2860
Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Linker-insertion nonsense and ...... f herpes simplex virus type 1.
@en
type
label
Linker-insertion nonsense and ...... f herpes simplex virus type 1.
@en
prefLabel
Linker-insertion nonsense and ...... f herpes simplex virus type 1.
@en
P2093
P2860
P1433
P1476
Linker-insertion nonsense and ...... f herpes simplex virus type 1.
@en
P2093
P2860
P304
P407
P577
1987-03-01T00:00:00Z