Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein.
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Mutational Evidence for an Internal Fusion Peptide in Flavivirus Envelope Protein EMolecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.Mutagenesis of the La Crosse Virus glycoprotein supports a role for Gc (1066–1087) as the fusion peptideStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStructure of the Ebola virus glycoprotein bound to an antibody from a human survivorStructure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformationThe avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH.Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoproteinStudies of the "chain reversal regions" of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry.A charged second-site mutation in the fusion peptide rescues replication of a mutant avian sarcoma and leukosis virus lacking critical cysteine residues flanking the internal fusion domain.The single ligand-binding repeat of Tva, a low density lipoprotein receptor-related protein, contains two ligand-binding surfaces.Cysteines flanking the internal fusion peptide are required for the avian sarcoma/leukosis virus glycoprotein to mediate the lipid mixing stage of fusion with high efficiency.Atypical fusion peptide of Nelson Bay virus fusion-associated small transmembrane proteinAn antibody directed against the fusion peptide of Junin virus envelope glycoprotein GPC inhibits pH-induced membrane fusion.Features of a spatially constrained cystine loop in the p10 FAST protein ectodomain define a new class of viral fusion peptides.Covalent modifications of the ebola virus glycoprotein.The curious case of arenavirus entry, and its inhibition.Development of treatment strategies to combat Ebola and Marburg viruses.Structural and functional properties of an unusual internal fusion peptide in a nonenveloped virus membrane fusion protein.SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.A conserved sequence within the H2 subunit of the vaccinia virus entry/fusion complex is important for interaction with the A28 subunit and infectivity.Expression and characterization of a soluble, active form of the jaagsiekte sheep retrovirus receptor, Hyal2.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.The hr1 and fusion peptide regions of the subgroup B avian sarcoma and leukosis virus envelope glycoprotein influence low pH-dependent membrane fusion.Expanded tropism and altered activation of a retroviral glycoprotein resistant to an entry inhibitor peptide.Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion.
P2860
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P2860
Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leukosis virus envelope glycoprotein.
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2000 nî lūn-bûn
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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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name
Critical role for the cysteine ...... s virus envelope glycoprotein.
@ast
Critical role for the cysteine ...... s virus envelope glycoprotein.
@en
type
label
Critical role for the cysteine ...... s virus envelope glycoprotein.
@ast
Critical role for the cysteine ...... s virus envelope glycoprotein.
@en
prefLabel
Critical role for the cysteine ...... s virus envelope glycoprotein.
@ast
Critical role for the cysteine ...... s virus envelope glycoprotein.
@en
P2860
P1433
P1476
Critical role for the cysteine ...... s virus envelope glycoprotein.
@en
P2093
P2860
P304
P356
10.1128/JVI.74.20.9738-9741.2000
P577
2000-10-01T00:00:00Z