Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.
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Measles Virus Fusion Protein: Structure, Function and InhibitionUnity in diversity: shared mechanism of entry among paramyxovirusesStructure 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 VivoViral membrane fusion.Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion processHuman Metapneumovirus Is Capable of Entering Cells by Fusion with Endosomal MembranesStructural basis of efficient contagion: measles variations on a theme by parainfluenza viruses.Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Activation of paramyxovirus membrane fusion and virus entryThe measles virus hemagglutinin stalk: structures and functions of the central fusion activation and membrane-proximal segmentsIdentification of amino acid substitutions with compensational effects in the attachment protein of canine distemper virus.Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Unraveling a three-step spatiotemporal mechanism of triggering of receptor-induced Nipah virus fusion and cell entry.On the stability of parainfluenza virus 5 F proteins.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Multiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus FamilyType II integral membrane protein, TM of J paramyxovirus promotes cell-to-cell fusion.Membrane 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.Envelope protein dynamics in paramyxovirus entry.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.Immobilization of the N-terminal helix stabilizes prefusion paramyxovirus fusion proteins.Mutagenesis of Paramyxovirus Hemagglutinin-Neuraminidase Membrane-Proximal Stalk Region Influences Stability, Receptor Binding, and Neuraminidase Activity.Flexibility of the Head-Stalk Linker Domain of Paramyxovirus HN Glycoprotein Is Essential for Triggering Virus Fusion.Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.Minimal features of efficient incorporation of the hemagglutinin-neuraminidase protein into sendai virus particles.Fusion 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.Site-specific glycosylation of the Newcastle disease virus haemagglutinin-neuraminidase.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 glycoprotein complexes preassemble intracellularly and relax during transport to the cell surface in preparation for fusionA stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.Characterization of a key residue for hyperfusogenic phenotype in human parainfluenza virus type 2 (hPIV-2) fusion glycoprotein.Structure and organization of paramyxovirus particles.Mutations in the Fusion Protein of Measles Virus That Confer Resistance to the Membrane Fusion Inhibitors Carbobenzoxy-d-Phe-l-Phe-Gly and 4-Nitro-2-Phenylacetyl Amino-Benzamide.Different Origins of Newcastle Disease Virus Hemagglutinin-Neuraminidase Protein Modulate the Replication Efficiency and Pathogenicity of the Virus.Chicken galectin-1B inhibits Newcastle disease virus adsorption and replication through binding to HN glycoprotein.
P2860
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P2860
Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.
description
2012 nî lūn-bûn
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2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
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2012年學術文章
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name
Fusion activation by a headles ...... ular mechanism for triggering.
@ast
Fusion activation by a headles ...... ular mechanism for triggering.
@en
type
label
Fusion activation by a headles ...... ular mechanism for triggering.
@ast
Fusion activation by a headles ...... ular mechanism for triggering.
@en
prefLabel
Fusion activation by a headles ...... ular mechanism for triggering.
@ast
Fusion activation by a headles ...... ular mechanism for triggering.
@en
P2093
P2860
P356
P1476
Fusion activation by a headles ...... ular mechanism for triggering.
@en
P2093
Aarohi Zokarkar
Brett D Welch
George P Leser
Robert A Lamb
Theodore S Jardetzky
P2860
P304
P356
10.1073/PNAS.1213813109
P407
P577
2012-09-04T00:00:00Z