Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein.
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Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringStructure 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) ectodomainInteraction between the Hemagglutinin-Neuraminidase and Fusion Glycoproteins of Human Parainfluenza Virus Type III Regulates Viral Growth In VivoActivation 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.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.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.Newcastle disease virus HN protein alters the conformation of the F protein at cell surfacesInhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.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 fusionVariable sensitivity to substitutions in the N-terminal heptad repeat of Mason-Pfizer monkey virus transmembrane protein.Roles of the fusion and hemagglutinin-neuraminidase proteins in replication, tropism, and pathogenicity of avian paramyxoviruses.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Comprehensive Analysis and Characterization of Linear Antigenic Domains on HN Protein from Genotype VII Newcastle Disease Virus Using Yeast Surface Display System.Ephrin-B2 and ephrin-B3 as functional henipavirus receptorsTwo single amino acid substitutions in the intervening region of Newcastle disease virus HN protein attenuate viral replication and pathogenicity.Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and IIMutations 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.New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2Interacting domains of the HN and F proteins of newcastle disease virus.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.Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor bindingRole of thiol/disulfide exchange in newcastle disease virus entryA 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)A Y526Q mutation in the Newcastle disease virus HN protein reduces its functional activities and attenuates virus replication and pathogenicity.Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.Contribution of HN protein length diversity to Newcastle disease virus virulence, replication and biological activities.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.Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cellsMutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion.Nipah virus attachment glycoprotein stalk C-terminal region links receptor binding to fusion triggering.Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.Glycoprotein interactions in paramyxovirus fusion.
P2860
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P2860
Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Mutational analysis of heptad ...... stle disease virus HN protein.
@ast
Mutational analysis of heptad ...... stle disease virus HN protein.
@en
type
label
Mutational analysis of heptad ...... stle disease virus HN protein.
@ast
Mutational analysis of heptad ...... stle disease virus HN protein.
@en
prefLabel
Mutational analysis of heptad ...... stle disease virus HN protein.
@ast
Mutational analysis of heptad ...... stle disease virus HN protein.
@en
P2860
P1433
P1476
Mutational analysis of heptad ...... astle disease virus HN protein
@en
P2093
J Stone-Hulslander
T G Morrison
P2860
P304
P577
1999-05-01T00:00:00Z