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.
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Modes of paramyxovirus fusion: a Henipavirus perspectiveBimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringUnity in diversity: shared mechanism of entry among paramyxovirusesHenipavirus mediated membrane fusion, virus entry and targeted therapeuticsStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStructure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkStructure and Mutagenesis of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Stalk Domain Reveals a Four-Helix Bundle and the Role of the Stalk in Fusion PromotionStructure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomainEvidence of independent evolution of genotype XIII Newcastle disease viruses in India.Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Activation of paramyxovirus membrane fusion and virus entryStructural and mechanistic studies of measles virus illuminate paramyxovirus entry.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry.Replication, neurotropism, and pathogenicity of avian paramyxovirus serotypes 1-9 in chickens and ducksProbing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptorsNewcastle disease virus fusion protein is the major contributor to protective immunity of genotype-matched vaccine.Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.Roles of the fusion and hemagglutinin-neuraminidase proteins in replication, tropism, and pathogenicity of avian paramyxoviruses.Role 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.Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entryEmerging paramyxoviruses: molecular mechanisms and antiviral strategiesComprehensive Analysis and Characterization of Linear Antigenic Domains on HN Protein from Genotype VII Newcastle Disease Virus Using Yeast Surface Display System.Mutations in the DI-DII Linker of Human Parainfluenza Virus Type 3 Fusion Protein Result in Diminished Fusion Activity.Paramyxovirus fusion and entry: multiple paths to a common endTwo single amino acid substitutions in the intervening region of Newcastle disease virus HN protein attenuate viral replication and pathogenicity.Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein.Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.Mechanism for active membrane fusion triggering by morbillivirus attachment protein.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 bindingParamyxoviruses: different receptors - different mechanisms of fusion.A mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation.A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)Immobilization of the N-terminal helix stabilizes prefusion paramyxovirus fusion proteins.Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein
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P2860
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.
description
article científic
@ca
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
Amino acid substitutions in th ...... nteraction with the F protein.
@en
Amino acid substitutions in th ...... nteraction with the F protein.
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type
label
Amino acid substitutions in th ...... nteraction with the F protein.
@en
Amino acid substitutions in th ...... nteraction with the F protein.
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Amino acid substitutions in th ...... nteraction with the F protein.
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Amino acid substitutions in th ...... nteraction with the F protein.
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P2860
P1433
P1476
Amino acid substitutions in th ...... nteraction with the F protein.
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P2093
Ronald M Iorio
Vanessa R Melanson
P2860
P304
13053-13061
P356
10.1128/JVI.78.23.13053-13061.2004
P407
P577
2004-12-01T00:00:00Z