Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion.
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Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionBimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringReplacement of the ectodomains of the hemagglutinin-neuraminidase and fusion glycoproteins of recombinant parainfluenza virus type 3 (PIV3) with their counterparts from PIV2 yields attenuated PIV2 vaccine candidatesMembrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins.Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkStructure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion proteinStructure 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) ectodomainRefolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy.Activation of paramyxovirus membrane fusion and virus entryInfluence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein.Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface.Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity.Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Probing 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.Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: an HN mutation diminishes the rate of F activation and fusionFusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor bindingTiming is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.A second receptor binding site on human parainfluenza virus type 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism.The paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Avian paramyxovirus serotype-1: a review of disease distribution, clinical symptoms, and laboratory diagnosticsParamyxovirus fusion and entry: multiple paths to a common endFusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and IIStructural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion.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.Incorporation of functional HN-F glycoprotein-containing complexes into newcastle disease virus is dependent on cholesterol and membrane lipid raft integrityType II integral membrane protein, TM of J paramyxovirus promotes cell-to-cell fusion.Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.Interacting domains of the HN and F proteins of newcastle disease virus.Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.The hemagglutinin-neuraminidase protein of Newcastle disease virus determines tropism and virulence.Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion proteinHuman parainfluenza virus infection of the airway epithelium: viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity.Kinetic dependence of paramyxovirus entry inhibition.Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.
P2860
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P2860
Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Mutations in the Newcastle dis ...... in in the promotion of fusion.
@en
type
label
Mutations in the Newcastle dis ...... in in the promotion of fusion.
@en
prefLabel
Mutations in the Newcastle dis ...... in in the promotion of fusion.
@en
P2093
P356
P1433
P1476
Mutations in the Newcastle dis ...... in in the promotion of fusion.
@en
P2093
P356
10.1006/VIRO.1998.9501
P407
P577
1999-01-01T00:00:00Z