Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion.
about
Human herpesvirus 6 glycoprotein complex formation is required for folding and trafficking of the gH/gL/gQ1/gQ2 complex and its cellular receptor bindingStuck 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 antibodyCrystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complexAssembly and architecture of the EBV B cell entry triggering complexCharacteristics of Epstein-Barr virus envelope protein gp42.The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Epstein-Barr virus glycoprotein gB and gHgL can mediate fusion and entry in trans, and heat can act as a partial surrogate for gHgL and trigger a conformational change in gB.The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cellsStructure-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.Fusing structure and function: a structural view of the herpesvirus entry machinery.Epstein-Barr virus entry.Binding-site interactions between Epstein-Barr virus fusion proteins gp42 and gH/gL reveal a peptide that inhibits both epithelial and B-cell membrane fusion.Nonmuscle myosin heavy chain IIA mediates Epstein-Barr virus infection of nasopharyngeal epithelial cells.A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Compatibility of the gH homologues of Epstein-Barr virus and related lymphocryptovirusesThe large groove found in the gH/gL structure is an important functional domain for Epstein-Barr virus fusion.The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope protein whose processing is dependent on coexpression with the BMRF2 protein.Functional homology of gHs and gLs from EBV-related gamma-herpesviruses for EBV-induced membrane fusionThe Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8.Integrins as triggers of Epstein-Barr virus fusion and epithelial cell infection.Epstein-Barr Virus (EBV)-associated gastric carcinoma.Epstein-Barr virus infection mechanismsEBV glycoproteins: where are we now?Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies.
P2860
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P2860
Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@ast
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@en
type
label
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@ast
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@en
prefLabel
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@ast
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@en
P2860
P1433
P1476
Point mutations in EBV gH that ...... ll and epithelial cell fusion.
@en
P2093
Lindsey M Hutt-Fletcher
P2860
P304
P356
10.1016/J.VIROL.2007.01.025
P407
P577
2007-02-20T00:00:00Z