Oligomeric structure of glycoproteins in herpes simplex virus type 1.
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Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infectionStructure-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 loopsBlocking antibody access to neutralizing domains on glycoproteins involved in entry as a novel mechanism of immune evasion by herpes simplex virus type 1 glycoproteins C and EAntigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regionsSpecific association of glycoprotein B with lipid rafts during herpes simplex virus entryAbalone Hemocyanin Blocks the Entry of Herpes Simplex Virus 1 into Cells: a Potential New Antiviral StrategyTargeting of pseudorabies virus structural proteins to axons requires association of the viral Us9 protein with lipid raftsGenital Herpes: Insights into Sexually Transmitted Infectious DiseaseInternal catalase protects herpes simplex virus from inactivation by hydrogen peroxide.Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26.Fibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans.Three-dimensional structure of herpes simplex virus type 1 glycoprotein D at 2.4-nanometer resolutionThe gH-gL complex of herpes simplex virus (HSV) stimulates neutralizing antibody and protects mice against HSV type 1 challengeMonoclonal antibodies to distinct sites on herpes simplex virus (HSV) glycoprotein D block HSV binding to HVEMHerpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry.Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonanceStructural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex.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 first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.Localization of a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies.The domains of glycoprotein D required to block apoptosis depend on whether glycoprotein D is present in the virions carrying herpes simplex virus 1 genome lacking the gene encoding the glycoprotein.Glycoprotein K specified by herpes simplex virus type 1 is expressed on virions as a Golgi complex-dependent glycosylated species and functions in virion entryHerpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entryHerpes simplex virus type 1 glycoprotein e is required for axonal localization of capsid, tegument, and membrane glycoproteins.Better neutralization of herpes simplex virus type 1 (HSV-1) than HSV-2 by antibody from recipients of GlaxoSmithKline HSV-2 glycoprotein D2 subunit vaccine.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.Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system.Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEMBimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.Effects of herpes simplex virus on structure and function of nectin-1/HveC.Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).Development of a glycoprotein D-expressing dominant-negative and replication-defective herpes simplex virus 2 (HSV-2) recombinant viral vaccine against HSV-2 infection in miceFunction of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusionDirect and specific binding of the UL16 tegument protein of herpes simplex virus to the cytoplasmic tail of glycoprotein E.The shear stress of host cell invasion: exploring the role of biomolecular complexesCross-linking of glycoprotein oligomers during herpes simplex virus type 1 entry.Evidence for a multiprotein gamma-2 herpesvirus entry complex.The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes.Differential protein partitioning within the herpesvirus tegument and envelope underlies a complex and variable virion architecture.
P2860
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P2860
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
@en
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
@nl
type
label
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
@en
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
@nl
prefLabel
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
@en
Oligomeric structure of glycoproteins in herpes simplex virus type 1.
@nl
P2093
P2860
P1433
P1476
Oligomeric structure of glycoproteins in herpes simplex virus type 1
@en
P2093
C G Handler
R J Eisenberg
P2860
P304
P407
P577
1996-09-01T00:00:00Z