Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein.
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Unity in diversity: shared mechanism of entry among paramyxovirusesStructure of the Ulster Strain Newcastle Disease Virus Hemagglutinin-Neuraminidase Reveals Auto-Inhibitory Interactions Associated with Low VirulenceStructure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkFunctional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses.N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site.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.Mutation 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 fusionTiming is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein.Paramyxovirus fusion and entry: multiple paths to a common endLoss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site.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 bindingContribution of HN protein length diversity to Newcastle disease virus virulence, replication and biological activities.Newcastle Disease Virus Establishes Persistent Infection in Tumor Cells In Vitro: Contribution of the Cleavage Site of Fusion Protein and Second Sialic Acid Binding Site of Hemagglutinin-Neuraminidase.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.Chicken galectin-1B inhibits Newcastle disease virus adsorption and replication through binding to HN glycoprotein.Effects of the HN gene C-terminal extensions on the Newcastle disease virus virulence.Genomic characterisation of a lentogenic Newcastle disease virus strain HX01 isolated from sick pigs in China.Identification of genetic mutations associated with attenuation and changes in tropism of Urabe mumps virus.
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Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on December 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Biological significance of the ...... lutinin-neuraminidase protein.
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Biological significance of the ...... lutinin-neuraminidase protein.
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Biological significance of the ...... lutinin-neuraminidase protein.
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Biological significance of the ...... lutinin-neuraminidase protein.
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Biological significance of the ...... lutinin-neuraminidase protein.
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Biological significance of the ...... lutinin-neuraminidase protein.
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P2093
P2860
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Biological significance of the ...... lutinin-neuraminidase protein.
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Allen Portner
Garry Taylor
Sateesh Krishnamurthy
Siba K Samal
Tatiana L Bousse
Toru Takimoto
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P304
13351-13355
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10.1128/JVI.78.23.13351-13355.2004
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2004-12-01T00:00:00Z