Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function.
about
Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusionHerpes simplex virus glycoprotein B associates with target membranes via its fusion loopsAntigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regionsStuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entryStructure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibodyAntigenic Characterization of the HCMV gH/gL/gO and Pentamer Cell Entry Complexes Reveals Binding Sites for Potently Neutralizing Human AntibodiesGlobal sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.Blocking herpes simplex virus 2 glycoprotein E immune evasion as an approach to enhance efficacy of a trivalent subunit antigen vaccine for genital herpes.Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.Herpes virus fusion and entry: a story with many characters.Dissection of the antibody response against herpes simplex virus glycoproteins in naturally infected humansA site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex gHgL.Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein BN-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for functionPatient-Specific Neutralizing Antibody Responses to Herpes Simplex Virus Are Attributed to Epitopes on gD, gB, or Both and Can Be Type Specific.Regulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors.Regulation of HSV glycoprotein induced cascade of events governing cell-cell fusion.Mutations in the amino terminus of herpes simplex virus type 1 gL can reduce cell-cell fusion without affecting gH/gL trafficking.Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B.Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion.Role of microvesicles in the spread of Herpes simplex virus type 1 in oligodendrocytic cells.
P2860
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P2860
Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function.
description
2006 nî lūn-bûn
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2006 թուականի Մարտին հրատարակուած գիտական յօդուած
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2006 թվականի մարտին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
Epitope mapping of herpes simp ...... ated with biological function.
@ast
Epitope mapping of herpes simp ...... ated with biological function.
@en
Epitope mapping of herpes simp ...... ated with biological function.
@nl
type
label
Epitope mapping of herpes simp ...... ated with biological function.
@ast
Epitope mapping of herpes simp ...... ated with biological function.
@en
Epitope mapping of herpes simp ...... ated with biological function.
@nl
prefLabel
Epitope mapping of herpes simp ...... ated with biological function.
@ast
Epitope mapping of herpes simp ...... ated with biological function.
@en
Epitope mapping of herpes simp ...... ated with biological function.
@nl
P2093
P2860
P1433
P1476
Epitope mapping of herpes simp ...... ated with biological function.
@en
P2093
Gary H Cohen
Isabelle Baribaud
J Charles Whitbeck
Manuel Ponce-de-Leon
Marie S Shaner
Tina M Cairns
P2860
P304
P356
10.1128/JVI.80.6.2596-2608.2006
P407
P577
2006-03-01T00:00:00Z