Interacting domains of the HN and F proteins of newcastle disease virus.
about
Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionStructure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkEvidence of independent evolution of genotype XIII Newcastle disease viruses in India.Newcastle disease virus in Madagascar: identification of an original genotype possibly deriving from a died out ancestor of genotype IV.Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.Different regions of the newcastle disease virus fusion protein modulate pathogenicity.Roles of the fusion and hemagglutinin-neuraminidase proteins in replication, tropism, and pathogenicity of avian paramyxoviruses.Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.Two single amino acid substitutions in the intervening region of Newcastle disease virus HN protein attenuate viral replication and pathogenicity.Individual N-glycans added at intervals along the stalk of the Nipah virus G protein prevent fusion but do not block the interaction with the homologous F protein.Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor bindingRole of thiol/disulfide exchange in newcastle disease virus entryThe hemagglutinin-neuraminidase protein of Newcastle disease virus determines tropism and virulence.Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein.Viral entry mechanisms: the increasing diversity of paramyxovirus entry.Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion.Paramyxovirus Glycoproteins and the Membrane Fusion Process.Nipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering.Functional interaction between paramyxovirus fusion and attachment proteins.Acidic amino acids increase fusion activity in the specific fusion domain of Newcastle disease virus fusion protein.Newcastle disease virus fusion and haemagglutinin-neuraminidase proteins contribute to its macrophage host range'a'-Position-mutated and G4-mutated hemagglutinin-neuraminidase proteins of Newcastle disease virus impair fusion and hemagglutinin-neuraminidase-fusion interaction by different mechanisms.Glycoprotein interactions in paramyxovirus fusion.Effects of heptad repeat regions of f protein on the specific membrane fusion in paramyxoviruses.Canine distemper virus and measles virus fusion glycoprotein trimers: partial membrane-proximal ectodomain cleavage enhances function.Probing the spatial organization of measles virus fusion complexesA histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusionPolybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein.
P2860
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P2860
Interacting domains of the HN and F proteins of newcastle disease virus.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
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2003年學術文章
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2003年學術文章
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2003年學術文章
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name
Interacting domains of the HN and F proteins of newcastle disease virus.
@ast
Interacting domains of the HN and F proteins of newcastle disease virus.
@en
type
label
Interacting domains of the HN and F proteins of newcastle disease virus.
@ast
Interacting domains of the HN and F proteins of newcastle disease virus.
@en
prefLabel
Interacting domains of the HN and F proteins of newcastle disease virus.
@ast
Interacting domains of the HN and F proteins of newcastle disease virus.
@en
P2860
P1433
P1476
Interacting domains of the HN and F proteins of newcastle disease virus.
@en
P2093
Kathryn A Gravel
Trudy G Morrison
P2860
P304
11040-11049
P356
10.1128/JVI.77.20.11040-11049.2003
P407
P577
2003-10-01T00:00:00Z