A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion. - Wikidata - awgldk - TriplyDB

A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.

A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.

http://www.wikidata.org/entity/Q39106872

about

Measles Virus Fusion Protein: Structure, Function and Inhibition Unity in diversity: shared mechanism of entry among paramyxoviruses The Host Cell Receptors for Measles Virus and Their Interaction with the Viral Hemagglutinin (H) Protein Viral membrane fusion.Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses.Activation of paramyxovirus membrane fusion and virus entry The measles virus hemagglutinin stalk: structures and functions of the central fusion activation and membrane-proximal segments Cross-resistance mechanism of respiratory syncytial virus against structurally diverse entry inhibitors.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.Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.Unraveling 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 engagement 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 Family Tunable and reversible drug control of protein production via a self-excising degron.Canine Distemper Virus Fusion Activation: Critical Role of Residue E123 of CD150/SLAM.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.Molecular determinants defining the triggering range of prefusion F complexes of canine distemper virus Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cells Multiple 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 fusion Measles virus fusion machinery activated by sialic acid binding globular domain.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.Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation.Promotion of virus assembly and organization by the measles virus matrix protein.Evolution of New Variants/Mutants of JE Virus, Its Effect on Neurovirulence, Antigenicity, Host Immune Responses and Disease Transmission in Endemic Areas

P2860

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P2860

A stabilized headless measles virus attachment protein stalk efficiently triggers membrane fusion.

http://www.wikidata.org/entity/Q39106872

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

A stabilized headless measles ...... ntly triggers membrane fusion.

@en

A stabilized headless measles ...... ntly triggers membrane fusion.

@nl

type

label

A stabilized headless measles ...... ntly triggers membrane fusion.

@en

A stabilized headless measles ...... ntly triggers membrane fusion.

@nl

prefLabel

A stabilized headless measles ...... ntly triggers membrane fusion.

@en

A stabilized headless measles ...... ntly triggers membrane fusion.

@nl

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P1433

Journal of Virology

P1476

A stabilized headless measles ...... ntly triggers membrane fusion.

@en

P2093

Elizabeth R Wright

http://www.w3.org/2001/XMLSchema#string

Gabriella Kiss

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Isabel Schestak

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Richard K Plemper

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Rolf Suter

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P2860

Modeling of the bacterial growth curve

Cell entry of enveloped viruses

Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III

Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2

Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3

Structure of the measles virus hemagglutinin bound to the CD46 receptor

Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM

Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk

Structure and Mutagenesis of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Stalk Domain Reveals a Four-Helix Bundle and the Role of the Stalk in Fusion Promotion

Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4

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11693-11703

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scholarly article

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10.1128/JVI.01945-13

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21

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87

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Melinda A. Brindley

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2013-08-21T00:00:00Z

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256072920

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23966411

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P921

membrane fusion involved in viral entry into host cell

P932

3807326

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