The transmembrane domain and cytoplasmic tail of herpes simplex virus type 1 glycoprotein H play a role in membrane fusion.
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Structural and Mechanistic Insights into the Tropism of Epstein-Barr VirusHerpesvirus gB: A Finely Tuned Fusion MachineStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeA Rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNAThe cytoplasmic domain of varicella-zoster virus glycoprotein H regulates syncytia formation and skin pathogenesisCharacterization of Vesicular Stomatitis Virus Pseudotypes Bearing Essential Entry Glycoproteins gB, gD, gH, and gL of Herpes Simplex Virus 1.Reevaluating herpes simplex virus hemifusion.Specific inhibition of human cytomegalovirus glycoprotein B-mediated fusion by a novel thiourea small molecule.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.Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion.The amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.Identification of proteins associated with murine gammaherpesvirus 68 virions.Herpes virus fusion and entry: a story with many characters.PDGF receptor-α does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway.Individual influenza A virus mRNAs show differential dependence on cellular NXF1/TAP for their nuclear export.Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimerasFunction of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusionN-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for functionA soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Nucleozin targets cytoplasmic trafficking of viral ribonucleoprotein-Rab11 complexes in influenza A virus infection.Human cytomegalovirus glycoproteins gB and gH/gL mediate epithelial cell-cell fusion when expressed either in cis or in transThe Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.The major determinant of attenuation in mice of the Candid1 vaccine for Argentine hemorrhagic fever is located in the G2 glycoprotein transmembrane domain.Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL.Kaposi's sarcoma-associated herpesvirus gH/gL: glycoprotein export and interaction with cellular receptors.Herpes simplex virus Membrane Fusion.Influence of acylation sites of influenza B virus hemagglutinin on fusion pore formation and dilation.The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2.Regulation of varicella-zoster virus-induced cell-to-cell fusion by the endocytosis-competent glycoproteins gH and gE.The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD Is Defined by Using Alphaherpesvirus gH and gL Chimeras.A single gD glycoprotein can mediate infection by Herpes simplex virus.Mutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells.Structural basis for the physiological temperature dependence of the association of VP16 with the cytoplasmic tail of herpes simplex virus glycoprotein H.Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.Structural rearrangement within an enveloped virus upon binding to the host cell.Fusogenic domains in herpes simplex virus type 1 glycoprotein H.Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.
P2860
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P2860
The transmembrane domain and cytoplasmic tail of herpes simplex virus type 1 glycoprotein H play a role in membrane fusion.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
The transmembrane domain and c ...... lay a role in membrane fusion.
@en
The transmembrane domain and c ...... lay a role in membrane fusion.
@nl
type
label
The transmembrane domain and c ...... lay a role in membrane fusion.
@en
The transmembrane domain and c ...... lay a role in membrane fusion.
@nl
prefLabel
The transmembrane domain and c ...... lay a role in membrane fusion.
@en
The transmembrane domain and c ...... lay a role in membrane fusion.
@nl
P2093
P2860
P1433
P1476
The transmembrane domain and c ...... lay a role in membrane fusion.
@en
P2093
Andrew Harman
Helena Browne
Tony Minson
P2860
P304
10708-10716
P356
10.1128/JVI.76.21.10708-10716.2002
P407
P577
2002-11-01T00:00:00Z