N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry. - Wikidata - wikimedia - TriplyDB

N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry.

N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry.

http://www.wikidata.org/entity/Q40287207

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A mechanistic paradigm for broad-spectrum antivirals that target virus-cell fusion Modes of paramyxovirus fusion: a Henipavirus perspective Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering Determinants of the Bovine Leukemia Virus Envelope Glycoproteins Involved in Infectivity, Replication and Pathogenesis Measles Virus Fusion Protein: Structure, Function and Inhibition Unity in diversity: shared mechanism of entry among paramyxoviruses Henipavirus mediated membrane fusion, virus entry and targeted therapeutics Co-assembly of viral envelope glycoproteins regulates their polarized sorting in neurons The Neutralizing Activity of Anti-Hepatitis C Virus Antibodies Is Modulated by Specific Glycans on the E2 Envelope Protein Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme 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 Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Activation of paramyxovirus membrane fusion and virus entry Endothelial galectin-1 binds to specific glycans on nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation.Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.Antibody evasion by a gammaherpesvirus O-glycan shield Evidence for henipavirus spillover into human populations in Africa.The secret life of viral entry glycoproteins: moonlighting in immune evasion.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors 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.Timing of galectin-1 exposure differentially modulates Nipah virus entry and syncytium formation in endothelial cells.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein.Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry Hendra and nipah infection: pathology, models and potential therapies.Emerging paramyxoviruses: molecular mechanisms and antiviral strategies Coordinate deletion of N-glycans from the heptad repeats of the fusion F protein of Newcastle disease virus yields a hyperfusogenic virus with increased replication, virulence, and immunogenicity Mutation of a Single Envelope N-Linked Glycosylation Site Enhances the Pathogenicity of Bovine Leukemia Virus.Multiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus Family Paramyxovirus fusion and entry: multiple paths to a common end N-linked glycosylation attenuates H3N2 influenza viruses.The Role of Conserved N-Linked Glycans on Ebola Virus Glycoprotein 2.Molecular determinants of antiviral potency of paramyxovirus entry inhibitors.Incorporation of functional HN-F glycoprotein-containing complexes into newcastle disease virus is dependent on cholesterol and membrane lipid raft integrity Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.N-Glycans on the Nipah virus attachment glycoprotein modulate fusion and viral entry as they protect against antibody neutralization

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N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry.

http://www.wikidata.org/entity/Q40287207

description

2006 nî lūn-bûn

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2006年论文

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2006年论文

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2006年论文

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name

N-glycans on Nipah virus fusio ...... mbrane fusion and viral entry.

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type

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N-glycans on Nipah virus fusio ...... mbrane fusion and viral entry.

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N-glycans on Nipah virus fusio ...... embrane fusion and viral entry

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N-glycans on Nipah virus fusio ...... mbrane fusion and viral entry.

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JVI.80.10.4878-4889.2006

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Journal of Virology

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N-glycans on Nipah virus fusio ...... mbrane fusion and viral entry.

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Andrea Bertolotti-Ciarlet

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Daniel Y Choi

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Ernest L Levroney

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Hector C Aguilar

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Jennifer A Fulcher

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Linda G Baum

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Luciana Kohatsu

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Mike C Wolf

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

Oscar A Negrete

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

Sara T Hashimi

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P2860

Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus

Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses

Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.

Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion

Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein.

Nipah Virus Infection

The HIV Env-mediated fusion reaction

Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection

HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process

Antibody neutralization and escape by HIV-1

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4878-4889

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10.1128/JVI.80.10.4878-4889.2006

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10

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80

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Claire Marie Filone

Kenneth A Matreyek

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2006-05-01T00:00:00Z

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16641279

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