(Q42718364)

English

Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy

scientific article published on 7 March 2011

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

5 November 2017

Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy (English)

1 reference

Europe PubMed Central

PMC publication ID

5 November 2017

transmembrane protein

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1

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Europe PubMed Central

PMC publication ID

5 November 2017

2

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Europe PubMed Central

PMC publication ID

5 November 2017

William DeGrado

4

object named as

William F DeGrado

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Europe PubMed Central

5 November 2017

PMC publication ID

author name string

Yibing Wu

3

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Europe PubMed Central

PMC publication ID

5 November 2017

Mei Hong

5

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Europe PubMed Central

PMC publication ID

5 November 2017

language of work or name

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publication date

7 March 2011

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Europe PubMed Central

PMC publication ID

5 November 2017

Journal of the American Chemical Society

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Europe PubMed Central

PMC publication ID

5 November 2017

133

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Europe PubMed Central

PMC publication ID

5 November 2017

12

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Europe PubMed Central

PMC publication ID

5 November 2017

4274-4284

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Europe PubMed Central

PMC publication ID

5 November 2017

describes a project that uses

NMR spectroscopy

1 reference

based on heuristic

inferred from title

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

1 reference

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Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR

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Influenza virus M2 protein mediates ESCRT-independent membrane scission

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Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibition

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

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Coexistence of two adamantane binding sites in the influenza A M2 ion channel

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

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Binding hot spots and amantadine orientation in the influenza a virus M2 proton channel

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Effects of amantadine on the dynamics of membrane-bound influenza A M2 transmembrane peptide studied by NMR relaxation.

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Structure and function of the influenza A M2 proton channel

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Identification of the functional core of the influenza A virus A/M2 proton-selective ion channel

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Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation

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Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus

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Mechanism of drug inhibition and drug resistance of influenza A M2 channel

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Molecular dynamics calculations suggest a conduction mechanism for the M2 proton channel from influenza A virus

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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

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pH-induced conformational change of the influenza M2 protein C-terminal domain

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Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel

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Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

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Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel.

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Identifiers

10.1021/JA102581N

1 reference

Europe PubMed Central

PMC publication ID

5 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

5 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

5 November 2017

ResearchGate publication ID

0 references

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