Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail
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Measles Virus Fusion Protein: Structure, Function and InhibitionStructural and Mechanistic Insights into the Tropism of Epstein-Barr VirusHerpesvirus gB: A Finely Tuned Fusion MachineFunctional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane FusionRecombinant influenza A H3N2 viruses with mutations of HA transmembrane cysteines exhibited altered virological characteristics.The cytoplasmic tail of the human respiratory syncytial virus F protein plays critical roles in cellular localization of the F protein and infectious progeny production.Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy.Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions.Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein.Activity of the Mason-Pfizer monkey virus fusion protein is modulated by single amino acids in the cytoplasmic tail.Characterization of an alternate form of Newcastle disease virus fusion protein.The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Analysis of the pH requirement for membrane fusion of different isolates of the paramyxovirus parainfluenza virus 5.Modulation of Epstein-Barr virus glycoprotein B (gB) fusion activity by the gB cytoplasmic tail domainThe transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Effects of stabilization of the gp41 cytoplasmic domain on fusion activity and infectivity of SIVmac239.The paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Paramyxovirus fusion and entry: multiple paths to a common endMaturation cleavage of the murine leukemia virus Env precursor separates the transmembrane subunits to prime it for receptor triggeringSignal peptide and helical bundle domains of virulent canine distemper virus fusion protein restrict fusogenicityThe respiratory syncytial virus fusion protein and neutrophils mediate the airway mucin response to pathogenic respiratory syncytial virus infection.Mutations in the cytoplasmic domain of the Newcastle disease virus fusion protein confer hyperfusogenic phenotypes modulating viral replication and pathogenicityMutagenesis of Paramyxovirus Hemagglutinin-Neuraminidase Membrane-Proximal Stalk Region Influences Stability, Receptor Binding, and Neuraminidase Activity.Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virusConserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins.Assembly of the Marburg virus envelope."Cytoplasmic domain effects on exposure of co-receptor-binding sites of HIV-1 Env".Efficient reovirus- and measles virus-mediated pore expansion during syncytium formation is dependent on annexin A1 and intracellular calcium.Point mutations in the paramyxovirus F protein that enhance fusion activity shift the mechanism of complement-mediated virus neutralization.Functional role of the cytoplasmic tail domain of the major envelope fusion protein of group II baculoviruses.Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein B ectodomain contribute to its refolding during the fusion step of virus entry.C-terminal tyrosine residues modulate the fusion activity of the Hendra virus fusion protein.The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection.The measles virus fusion protein transmembrane region modulates availability of an active glycoprotein complex and fusion efficiency.Altered interaction of the matrix protein with the cytoplasmic tail of hemagglutinin modulates measles virus growth by affecting virus assembly and cell-cell fusion.Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.The respiratory syncytial virus fusion protein targets to the perimeter of inclusion bodies and facilitates filament formation by a cytoplasmic tail-dependent mechanism.Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation.
P2860
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P2860
Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail
description
2004 nî lūn-bûn
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2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
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2004年論文
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2004年論文
@zh-hant
2004年論文
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2004年論文
@zh-mo
2004年論文
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2004年论文
@wuu
name
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@ast
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@en
type
label
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@ast
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@en
prefLabel
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@ast
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@en
P2093
P2860
P356
P1476
Activation of a paramyxovirus ...... ling from the cytoplasmic tail
@en
P2093
Charles J Russell
David L Waning
Robert A Lamb
Theodore S Jardetzky
P2860
P304
P356
10.1073/PNAS.0403339101
P407
P577
2004-06-14T00:00:00Z