about
Modes of paramyxovirus fusion: a Henipavirus perspectiveUnity in diversity: shared mechanism of entry among paramyxovirusesStructure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkActivation of paramyxovirus membrane fusion and virus entryInhibition of Nipah virus infection in vivo: targeting an early stage of paramyxovirus fusion activation during viral entryThe measles virus hemagglutinin stalk: structures and functions of the central fusion activation and membrane-proximal segmentsStructural and mechanistic studies of measles virus illuminate paramyxovirus entry.Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptorsCanine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry.Electron tomography imaging of surface glycoproteins on human parainfluenza virus 3: association of receptor binding and fusion proteins before receptor engagementRole 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 fusionMechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entryComprehensive Analysis and Characterization of Linear Antigenic Domains on HN Protein from Genotype VII Newcastle Disease Virus Using Yeast Surface Display System.Targeted entry of enveloped viruses: measles and herpes simplex virus I.Multiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus FamilyTwo single amino acid substitutions in the intervening region of Newcastle disease virus HN protein attenuate viral replication and pathogenicity.Cysteines in the stalk of the nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation.Base of the measles virus fusion trimer head receives the signal that triggers membrane fusion.Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.N-Glycans on the Nipah virus attachment glycoprotein modulate fusion and viral entry as they protect against antibody neutralizationMembrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.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.The receptor attachment function of measles virus hemagglutinin can be replaced with an autonomous protein that binds Her2/neu while maintaining its fusion-helper function.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.Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.Inhibition of Rho-associated coiled-coil-forming kinase increases efficacy of measles virotherapy.Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virusFusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cellsMultiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins.Paramyxovirus Glycoproteins and the Membrane Fusion Process.The Fusion Protein Specificity of the Parainfluenza Virus Hemagglutinin-Neuraminidase Protein Is Not Solely Defined by the Primary Structure of Its Stalk Domain.Nipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering.Measles virus fusion machinery activated by sialic acid binding globular domain.Full conversion of the hemagglutinin-neuraminidase specificity of the parainfluenza virus 5 fusion protein by replacement of 21 amino acids in its head region with those of the simian virus 41 fusion protein.Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.Localization of a region in the fusion protein of avian metapneumovirus that modulates cell-cell fusionThe 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.Spring-loaded model revisited: paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein.Different Origins of Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein Modulate the Replication Efficiency and Pathogenicity of the Virus.
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description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
Glycoprotein interactions in paramyxovirus fusion.
@en
Glycoprotein interactions in paramyxovirus fusion.
@nl
type
label
Glycoprotein interactions in paramyxovirus fusion.
@en
Glycoprotein interactions in paramyxovirus fusion.
@nl
prefLabel
Glycoprotein interactions in paramyxovirus fusion.
@en
Glycoprotein interactions in paramyxovirus fusion.
@nl
P2093
P2860
P356
P1433
P1476
Glycoprotein interactions in paramyxovirus fusion.
@en
P2093
Paul J Mahon
Ronald M Iorio
Vanessa R Melanson
P2860
P304
P356
10.2217/FVL.09.17
P577
2009-07-01T00:00:00Z