Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H.
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Structural and Mechanistic Insights into the Tropism of Epstein-Barr VirusStuck 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–gLStructure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibodyMechanism for neutralizing activity by the anti-CMV gH/gL monoclonal antibody MSL-109Reevaluating herpes simplex virus hemifusion.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.The gH-gL complex of herpes simplex virus (HSV) stimulates neutralizing antibody and protects mice against HSV type 1 challengeStructural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex.An adenovirus vector with genetically modified fibers demonstrates expanded tropism via utilization of a coxsackievirus and adenovirus receptor-independent cell entry mechanism.Mutations of Epstein-Barr virus gH that are differentially able to support fusion with B cells or epithelial cells.The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.Herpes simplex virus type 2 glycoprotein H interacts with integrin αvβ3 to facilitate viral entry and calcium signaling in human genital tract epithelial cells.Herpes virus fusion and entry: a story with many characters.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.Identification of functional domains in herpes simplex virus 2 glycoprotein B.Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasStructure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.Fusion of Epstein-Barr virus with epithelial cells can be triggered by αvβ5 in addition to αvβ6 and αvβ8, and integrin binding triggers a conformational change in glycoproteins gHgL.A site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex gHgL.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 functionMultiple receptor interactions trigger release of membrane and intracellular calcium stores critical for herpes simplex virus entry.Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion.Drosophila Schneider 2 (S2) cells: a novel tool for studying HSV-induced membrane fusionHuman cytomegalovirus glycoproteins gB and gH/gL mediate epithelial cell-cell fusion when expressed either in cis or in transInsertional mutations in herpes simplex virus type 1 gL identify functional domains for association with gH and for membrane fusion.Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8.Epidermal growth factor receptor-PI3K signaling controls cofilin activity to facilitate herpes simplex virus 1 entry into neuronal cells.Cellular integrins function as entry receptors for human cytomegalovirus via a highly conserved disintegrin-like domain.Herpes simplex virus infects most cell types in vitro: clues to its successNonmuscle myosin heavy chain IIb mediates herpes simplex virus 1 entryNovel mutations in gB and gH circumvent the requirement for known gD Receptors in herpes simplex virus 1 entry and cell-to-cell spread.Structure-based mutational analysis of the highly conserved domain IV of glycoprotein H of pseudorabies virus.Glycoproteins D of equine herpesvirus type 1 (EHV-1) and EHV-4 determine cellular tropism independently of integrins.The transmembrane domain and cytoplasmic tail of herpes simplex virus type 1 glycoprotein H play a role in membrane fusion.Pseudorabies virus glycoprotein L is necessary for virus infectivity but dispensable for virion localization of glycoprotein H.Herpes simplex virus Membrane Fusion.A heptad repeat in herpes simplex virus 1 gH, located downstream of the alpha-helix with attributes of a fusion peptide, is critical for virus entry and fusion.
P2860
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P2860
Site-directed and linker insertion mutagenesis of herpes simplex virus type 1 glycoprotein H.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Site-directed and linker inser ...... x virus type 1 glycoprotein H.
@en
Site-directed and linker inser ...... x virus type 1 glycoprotein H.
@nl
type
label
Site-directed and linker inser ...... x virus type 1 glycoprotein H.
@en
Site-directed and linker inser ...... x virus type 1 glycoprotein H.
@nl
prefLabel
Site-directed and linker inser ...... x virus type 1 glycoprotein H.
@en
Site-directed and linker inser ...... x virus type 1 glycoprotein H.
@nl
P2093
P2860
P1433
P1476
Site-directed and linker inser ...... ex virus type 1 glycoprotein H
@en
P2093
P2860
P304
P407
P577
1997-03-01T00:00:00Z