Probing the spatial organization of measles virus fusion complexes
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Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic StabilityMeasles Virus Fusion Protein: Structure, Function and InhibitionStructure of the measles virus hemagglutinin bound to its cellular receptor SLAMStructure 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) ectodomainSequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion processEGFR Interacts with the Fusion Protein of Respiratory Syncytial Virus Strain 2-20 and Mediates Infection and Mucin ExpressionStructural basis of efficient contagion: measles variations on a theme by parainfluenza viruses.Functional and structural characterization of neutralizing epitopes of measles virus hemagglutinin protein.Activation of paramyxovirus membrane fusion and virus entryPeste des petits ruminants virus infection of small ruminants: a comprehensive review.The 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.Measles virus-induced suppression of immune responses.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.Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.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.Canine distemper virus infects canine keratinocytes and immune cells by using overlapping and distinct regions located on one side of the attachment proteinTiming is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesDual Mutation Events in the Haemagglutinin-Esterase and Fusion Protein from an Infectious Salmon Anaemia Virus HPR0 Genotype Promote Viral Fusion and Activation by an Ubiquitous Host Protease.Ephrin-B2 and ephrin-B3 as functional henipavirus receptorsMultiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus FamilyStructural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion.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.New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.Triggering the measles virus membrane fusion machinery.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.Envelope protein dynamics in paramyxovirus entry.The measles virus nucleocapsid protein tail domain is dispensable for viral polymerase recruitment and activity.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.Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virus
P2860
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P2860
Probing the spatial organization of measles virus fusion complexes
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Probing the spatial organization of measles virus fusion complexes
@en
type
label
Probing the spatial organization of measles virus fusion complexes
@en
prefLabel
Probing the spatial organization of measles virus fusion complexes
@en
P2093
P2860
P356
P1433
P1476
Probing the spatial organization of measles virus fusion complexes
@en
P2093
Courtney St Clair
Dominika Gaus
James P Snyder
Richard K Plemper
Stefanie A Krumm
Tanja Paal
P2860
P304
10480-10493
P356
10.1128/JVI.01195-09
P407
P577
2009-08-05T00:00:00Z