Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.

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Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.

P2860

Q47554176-49144CE7-42D8-426A-94FF-BF6339BA6F12

P2860

Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.

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http://www.wikidata.org/entity/Q40046703

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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2017年论文

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2017年论文

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name

Protonation equilibria and por ...... channel from solid-state NMR.

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type

Item

label

Protonation equilibria and por ...... channel from solid-state NMR.

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prefLabel

Protonation equilibria and por ...... channel from solid-state NMR.

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P1476

Protonation equilibria and por ...... channel from solid-state NMR.

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P2093

Alexander A Shcherbakov

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

Jonathan K Williams

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

Jun Wang

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

Mei Hong

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

P2860

Thermodynamic Quantities for the Ionization Reactions of Buffers

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

Solution structure and functional analysis of the influenza B 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

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

High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction

Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel

Structural basis for proton conduction and inhibition by the influenza M2 protein.

P304

17876-17884

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scholarly article

P356

10.1074/JBC.M117.813998

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English

P433

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P478

292

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P50

Jun Wang

Jonathan K. Williams

Alexander A Shcherbakov

Mei Hong

P577

2017-09-11T00:00:00Z

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P698

28893910

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P921

transmembrane protein

P932

5663885

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Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.

about

P2860

P2860

Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932