Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.

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Functional characterization of a melittin analog containing a non-natural tryptophan analog Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.

P2860

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P2860

Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.

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http://www.wikidata.org/entity/Q39308524

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2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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2013年学术文章

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2013年学术文章

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2013年学术文章

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Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

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Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

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Item

label

Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

@en

Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

@nl

prefLabel

Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

@en

Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

@nl

P1476

Nanosecond Dynamics of Influen ...... Shifts of a Native Tryptophan.

@en

P2093

Dmitri Toptygin

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

Lidia Cristian

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

Ludwig Brand

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

William F Degrado

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

P2860

Mechanisms of tryptophan fluorescence shifts in proteins

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

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

Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: The Role of Ser31 in Amantadine Binding

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

pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus

Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values.

P31

scholarly article

P356

10.1016/J.CHEMPHYS.2012.12.018

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

P478

422

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P50

Vikas Nanda

P577

2013-08-01T00:00:00Z

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P698

24273370

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P932

3833813

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Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.

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P2860

P2860

Nanosecond Dynamics of InfluenzaA/M2TM and an Amantadine Resistant Mutant Probed by Time-Dependent Red Shifts of a Native Tryptophan.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P31

P356

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P31

P356

P478

P50

P577

P698

P932