Identification of specific histidines as pH sensors in flavivirus membrane fusion - Wikidata - wikimedia - TriplyDB

Identification of specific histidines as pH sensors in flavivirus membrane fusion

Identification of specific histidines as pH sensors in flavivirus membrane fusion

http://www.wikidata.org/entity/Q27487066

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Small-molecule inhibitors of dengue-virus entry Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1 Crystal structure of glycoprotein C from Rift Valley fever virus Antibody Binding Modulates Conformational Exchange in Domain III of Dengue Virus E Protein Flavivirus cell entry and membrane fusion Viral membrane fusion and nucleocapsid delivery into the cytoplasm are distinct events in some flaviviruses The pH sensor for flavivirus membrane fusion Flavivirus reveals its access code Crystal Structure of Dengue Virus Type 1 Envelope Protein in the Postfusion Conformation and Its Implications for Membrane Fusion Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion Protein Human Monoclonal Antibodies against West Nile Virus Induced by Natural Infection Neutralize at a Postattachment Step Diversification of West Nile virus in a subtropical region Impact of Quaternary Organization on the Antigenic Structure of the Tick-Borne Encephalitis Virus Envelope Glycoprotein E E1 Mutants Identify a Critical Region in the Trimer Interface of the Semliki Forest Virus Fusion Protein Dealing with low pH: entry and exit of alphaviruses and flaviviruses Protonation of Individual Histidine Residues Is Not Required for the pH-Dependent Entry of West Nile Virus: Evaluation of the "Histidine Switch" Hypothesis Peptide Inhibitors of Dengue-Virus Entry Target a Late-Stage Fusion Intermediate Cryo-EM structure of the mature dengue virus at 3.5-Å resolution Crystal Structure of the Japanese Encephalitis Virus Envelope Protein Crystal structure of glycoprotein E2 from bovine viral diarrhea virus Analysis of worldwide sequence mutations in Zika virus proteins E, NS1, NS3 and NS5 from a structural point of view Fusion of Enveloped Viruses in Endosomes.Dengue virus ensures its fusion in late endosomes using compartment-specific lipids.Mechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidol The pH dependence of flavivirus envelope protein structure: insights from molecular dynamics simulations.Probing the mechanism of pH-induced large-scale conformational changes in dengue virus envelope protein using atomistic simulations.Studies of the "chain reversal regions" of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry.Identification and Characterization of a Novel Broad-Spectrum Virus Entry Inhibitor.Structural, antigenic, and evolutionary characterizations of the envelope protein of newly emerging Duck Tembusu Virus.Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion.Near-atomic structure of Japanese encephalitis virus reveals critical determinants of virulence and stability.In vitro and in vivo studies identify important features of dengue virus pr-E protein interactions Japanese encephalitis virus vaccine candidates generated by chimerization with dengue virus type 4 In vitro reconstitution reveals key intermediate states of trimer formation by the dengue virus membrane fusion protein Progress in the identification of dengue virus entry/fusion inhibitors The structural dynamics of the flavivirus fusion peptide-membrane interaction Sequential conformational rearrangements in flavivirus membrane fusion.Atomic-level functional model of dengue virus Envelope protein infectivity.Structure-based mutational analysis of several sites in the E protein: implications for understanding the entry mechanism of Japanese encephalitis virus Critical role of leucine-valine change in distinct low pH requirements for membrane fusion between two related retrovirus envelopes.

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P2860

Identification of specific histidines as pH sensors in flavivirus membrane fusion

http://www.wikidata.org/entity/Q27487066

description

2008 nî lūn-bûn

@nan

2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

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2008年论文

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name

Identification of specific histidines as pH sensors in flavivirus membrane fusion

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Identification of specific histidines as pH sensors in flavivirus membrane fusion

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Identification of specific histidines as pH sensors in flavivirus membrane fusion

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type

label

Identification of specific histidines as pH sensors in flavivirus membrane fusion

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Identification of specific histidines as pH sensors in flavivirus membrane fusion

@en

Identification of specific histidines as pH sensors in flavivirus membrane fusion

@nl

prefLabel

Identification of specific histidines as pH sensors in flavivirus membrane fusion

@ast

Identification of specific histidines as pH sensors in flavivirus membrane fusion

@en

Identification of specific histidines as pH sensors in flavivirus membrane fusion

@nl

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Journal of Cell Biology

P1476

Identification of specific histidines as pH sensors in flavivirus membrane fusion

@en

P2093

Franz X Heinz

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Richard Fritz

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P2860

Structure of dengue virus: implications for flavivirus organization, maturation, and fusion

Differences in the postfusion conformations of full-length and truncated class II fusion protein E of tick-borne encephalitis virus.

Mutational Evidence for an Internal Fusion Peptide in Flavivirus Envelope Protein E

Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH.

Second-Site Revertants of a Semliki Forest Virus Fusion-Block Mutation Reveal the Dynamics of a Class II Membrane Fusion Protein

Involvement of Lipids in Different Steps of the Flavivirus Fusion Mechanism

Crystal Structure of West Nile Virus Envelope Glycoprotein Reveals Viral Surface Epitopes

Crystal Structure of the West Nile Virus Envelope Glycoprotein

A ligand-binding pocket in the dengue virus envelope glycoprotein

Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH

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353-61

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scholarly article

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10.1083/JCB.200806081

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2

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183

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18936253

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2568029

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