Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion.
about
Herpes simplex virus glycoprotein B associates with target membranes via its fusion loopsHerpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BInteraction domain of glycoproteins gB and gH of Marek's disease virus and identification of an antiviral peptide with dual functionsReevaluating herpes simplex virus hemifusion.Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry.Anti-glycoprotein H antibody impairs the pathogenicity of varicella-zoster virus in skin xenografts in the SCID mouse model.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.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 infectionCapturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Herpes virus fusion and entry: a story with many characters.Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD.The herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry.Molecular gymnastics at the herpesvirus surface.Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.Fusing structure and function: a structural view of the herpesvirus entry machinery.N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for functionInsertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.Peptide inhibitors against herpes simplex virus infections.Cell entry mechanisms of HSV: what we have learned in recent years.Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies.Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein.Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain.Structure-function dissection of the Pseudorabies virus glycoprotein B fusion loops.
P2860
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P2860
Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@en
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@nl
type
label
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@en
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@nl
prefLabel
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@en
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@nl
P2093
P2860
P356
P1433
P1476
Hydrophobic alpha-helices 1 an ...... ce virus infection and fusion.
@en
P2093
Christian Bergamini
Giorgio Lenaz
Romana Fato
Tatiana Gianni
P2860
P304
P356
10.1128/JVI.00504-06
P407
P577
2006-08-01T00:00:00Z