Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor binding
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Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionModes of paramyxovirus fusion: a Henipavirus perspectiveInfluence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein.Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site.Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptorsMutation at residue 523 creates a second receptor binding site on human parainfluenza virus type 1 hemagglutinin-neuraminidase proteinRole of the two sialic acid binding sites on the newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusionMutations in the DI-DII Linker of Human Parainfluenza Virus Type 3 Fusion Protein Result in Diminished Fusion Activity.Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.A second receptor binding site on human parainfluenza virus type 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism.Paramyxovirus fusion and entry: multiple paths to a common endMutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein.A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusionInteracting domains of the HN and F proteins of newcastle disease virus.Mechanism for active membrane fusion triggering by morbillivirus attachment protein.Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.Paramyxoviruses: different receptors - different mechanisms of fusion.Human parainfluenza virus infection of the airway epithelium: viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity.Kinetic dependence of paramyxovirus entry inhibition.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.Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein.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.Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational changeMultiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins.'a'-Position-mutated and G4-mutated hemagglutinin-neuraminidase proteins of Newcastle disease virus impair fusion and hemagglutinin-neuraminidase-fusion interaction by different mechanisms.The second receptor binding site of the globular head of the Newcastle disease virus hemagglutinin-neuraminidase activates the stalk of multiple paramyxovirus receptor binding proteins to trigger fusion.Glycoprotein interactions in paramyxovirus fusion.Selectively receptor-blind measles viruses: Identification of residues necessary for SLAM- or CD46-induced fusion and their localization on a new hemagglutinin structural model.Canine distemper virus and measles virus fusion glycoprotein trimers: partial membrane-proximal ectodomain cleavage enhances function.A histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusionGenomic characterisation of a lentogenic Newcastle disease virus strain HX01 isolated from sick pigs in China.
P2860
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P2860
Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor binding
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Fusion deficiency induced by m ...... ent defect in receptor binding
@ast
Fusion deficiency induced by m ...... ent defect in receptor binding
@en
type
label
Fusion deficiency induced by m ...... ent defect in receptor binding
@ast
Fusion deficiency induced by m ...... ent defect in receptor binding
@en
prefLabel
Fusion deficiency induced by m ...... ent defect in receptor binding
@ast
Fusion deficiency induced by m ...... ent defect in receptor binding
@en
P2093
P2860
P1433
P1476
Fusion deficiency induced by m ...... ent defect in receptor binding
@en
P2093
Anne M Mirza
Elizabeth A Corey
Elizabeth Levandowsky
Ronald M Iorio
P2860
P304
P356
10.1128/JVI.77.12.6913-6922.2003
P407
P577
2003-06-01T00:00:00Z