Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes - Wikidata - awgldk - TriplyDB

Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump Biophysical EPR Studies Applied to Membrane Proteins.Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties.Influenza M2 Transmembrane Domain Senses Membrane Heterogeneity and Enhances Membrane Curvature.Slow but Steady Wins the Race: Dissimilarities among New Dual Inhibitors of the Wild-Type and the V27A Mutant M2 Channels of Influenza A Virus.Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5).Signature of an aggregation-prone conformation of tau.Influenza A Virus M2 Protein: Roles from Ingress to Egress.A New Wavelet Denoising Method for Experimental Time-Domain Signals: Pulsed Dipolar Electron Spin Resonance.The role of conformational heterogeneity in regulating the apoptotic activity of BAX protein.Site-Directed Spin Labeling EPR for Studying Membrane Proteins.A facile approach for the in vitro assembly of multimeric membrane transport proteins.

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P2860

Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

http://www.wikidata.org/entity/Q35865367

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

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Scientific Reports

P1476

Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes

@en

P2093

Haley D Norman

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

Jack H Freed

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

Peter P Borbat

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

P2860

Structure and mechanism of the M2 proton channel of influenza A virus

The closed state of a H+ channel helical bundle combining precise orientational and distance restraints from solid state NMR

Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus

Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger

Structural basis for the function and inhibition of an influenza virus proton channel

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus

Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer

Assembly and budding of influenza virus.

The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue

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11757

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scholarly article

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10.1038/SREP11757

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5

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Elka R Georgieva

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2015-07-20T00:00:00Z

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280300968

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26190831

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transmembrane protein

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4507135

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