Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
about
Cell entry of enveloped virusesHenipavirus mediated membrane fusion, virus entry and targeted therapeuticsParamyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Epitope dampening monotypic measles virus hemagglutinin glycoprotein results in resistance to cocktail of monoclonal antibodies.Prevention of measles virus infection by intranasal delivery of fusion inhibitor peptidesUnraveling 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 engagementTiming is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entryPlasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.Electrostatic Architecture of the Infectious Salmon Anemia Virus (ISAV) Core Fusion Protein Illustrates a Carboxyl-Carboxylate pH Sensor.Paramyxovirus fusion and entry: multiple paths to a common endCysteines in the stalk of the nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation.Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.Structure of the primed paramyxovirus fusion protein.Triggering the measles virus membrane fusion machinery.Mechanism for active membrane fusion triggering by morbillivirus attachment protein.Nipah virus envelope-pseudotyped lentiviruses efficiently target ephrinB2-positive stem cell populations in vitro and bypass the liver sink when administered in vivoTransmembrane Domain Lengths Serve as Signatures of Organismal Complexity and Viral Transport Mechanisms.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.Mutagenesis of Paramyxovirus Hemagglutinin-Neuraminidase Membrane-Proximal Stalk Region Influences Stability, Receptor Binding, and Neuraminidase Activity.In Vivo Efficacy of Measles Virus Fusion Protein-Derived Peptides Is Modulated by the Properties of Self-Assembly and Membrane Residence.Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virusParamyxovirus Glycoproteins and the Membrane Fusion Process.A Structurally Unresolved Head Segment of Defined Length Favors Proper Measles Virus Hemagglutinin Tetramerization and Efficient Membrane Fusion Triggering.Measles virus fusion machinery activated by sialic acid binding globular domain.A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.Mutant fusion proteins with enhanced fusion activity promote measles virus spread in human neuronal cells and brains of suckling hamsters.Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.Heparan sulfate is an attachment factor for foamy virus entry.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.Structure of the infectious salmon anemia virus receptor complex illustrates a unique binding strategy for attachment.Measles virus hemagglutinin: structural insights into cell entry and measles vaccine.Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins.Measles virus mutants possessing the fusion protein with enhanced fusion activity spread effectively in neuronal cells, but not in other cells, without causing strong cytopathology.Intramolecular complementation of measles virus fusion protein stability confers cell-cell fusion activity at 37 °C.Mutations in the putative dimer-dimer interfaces of the measles virus hemagglutinin head domain affect membrane fusion triggering.Measles Vaccine.
P2860
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P2860
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@ast
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@en
type
label
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@ast
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@en
prefLabel
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@ast
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@en
P2860
P921
P1433
P1476
Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.
@en
P2093
Richard K Plemper
Ronald M Iorio
P2860
P304
P356
10.1371/JOURNAL.PPAT.1002058
P5008
P577
2011-06-01T00:00:00Z
2011-06-02T00:00:00Z