A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH.
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Differences in the N termini of herpes simplex virus type 1 and 2 gDs that influence functional interactions with the human entry receptor Nectin-2 and an entry receptor expressed in Chinese hamster ovary cellsAnalysis of a neutralizing antibody for human herpesvirus 6B reveals a role for glycoprotein Q1 in viral entryDetermination and analysis of the complete nucleotide sequence of human herpesvirusHerpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryCrystal structure of the conserved herpesvirus fusion regulator complex gH–gLArms Race between Enveloped Viruses and the Host ERAD MachineryGenital Herpes: Insights into Sexually Transmitted Infectious DiseaseCharacterization of Vesicular Stomatitis Virus Pseudotypes Bearing Essential Entry Glycoproteins gB, gD, gH, and gL of Herpes Simplex Virus 1.Reevaluating herpes simplex virus hemifusion.Fast screening procedures for random transposon libraries of cloned herpesvirus genomes: mutational analysis of human cytomegalovirus envelope glycoprotein genesThe murid herpesvirus-4 gH/gL binds to glycosaminoglycans.The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry.Trafficking to the plasma membrane of the seven-transmembrane protein encoded by human herpesvirus 6 U51 gene involves a cell-specific function present in T lymphocytes.Intracellular formation and processing of the heterotrimeric gH-gL-gO (gCIII) glycoprotein envelope complex of human cytomegalovirus.Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infectionThe gH-gL complex of herpes simplex virus (HSV) stimulates neutralizing antibody and protects mice against HSV type 1 challengeEpstein-Barr virus lacking glycoprotein gp42 can bind to B cells but is not able to infectHerpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles.Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells.HveA (herpesvirus entry mediator A), a coreceptor for herpes simplex virus entry, also participates in virus-induced cell fusion.Structural 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.Pseudotyping of glycoprotein D-deficient herpes simplex virus type 1 with vesicular stomatitis virus glycoprotein G enables mutant virus attachment and entry.Identification and characterization of a novel herpes simplex virus glycoprotein, gK, involved in cell fusionHSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Soluble V domain of Nectin-1/HveC enables entry of herpes simplex virus type 1 (HSV-1) into HSV-resistant cells by binding to viral glycoprotein DHerpes virus fusion and entry: a story with many characters.The nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.Gammaherpesvirus lytic gene expression as characterized by DNA array.Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function.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.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 fusionA subpopulation of tegument protein vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells.Comparative analysis of the genes UL1 through UL7 of the duck enteritis virus and other herpesviruses of the subfamily AlphaherpesvirinaeGlycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H.The herpes simplex virus type 1 UL3 transcript starts within the UL3 open reading frame and encodes a 224-amino-acid proteinBimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.
P2860
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P2860
A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH.
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
A novel herpes simplex virus g ...... and surface expression of gH.
@ast
A novel herpes simplex virus g ...... and surface expression of gH.
@en
type
label
A novel herpes simplex virus g ...... and surface expression of gH.
@ast
A novel herpes simplex virus g ...... and surface expression of gH.
@en
prefLabel
A novel herpes simplex virus g ...... and surface expression of gH.
@ast
A novel herpes simplex virus g ...... and surface expression of gH.
@en
P2093
P2860
P1433
P1476
A novel herpes simplex virus g ...... and surface expression of gH.
@en
P2093
A C Minson
D C Johnson
K Goldsmith
L Hutchinson
N Davis-Poynter
S Primorac
P2860
P304
P407
P577
1992-04-01T00:00:00Z