Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy [Biophysics and Computational Biology]
Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy
Yuki Toyama, Hanaho Kano, Yoko Mase, Mariko Yokogawa, Masanori Osawa, Ichio Shimada...
Date: 2018-04-10
Ethanol consumption leads to a wide range of pharmacological effects by acting on the signaling proteins in the human nervous system, such as ion channels. Despite its familiarity and biological importance, very little is known about the molecular mechanisms underlying the ethanol action, due to extremely weak binding affinity and... Read More
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04-11-2018 12:49 AM
[NMR paper] Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.
Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.
Related Articles Structural basis for the ethanol action on G-protein-activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2018 Mar 26;:
Authors: Toyama Y, Kano H, Mase Y, Yokogawa M, Osawa M, Shimada I
Abstract
Ethanol consumption leads to a wide range of pharmacological effects by acting on the signaling proteins in the human nervous system,...
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03-28-2018 02:16 PM
[NMR paper] Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
Related Articles Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.
J Mol Biol. 2017 May 20;:
Authors: Mandala VS, Liao SY, Kwon B, Hong M
Abstract
The influenza M2 protein forms an acid-activated proton channel that is essential for virus replication. The transmembrane H37 selects for protons under low external pH (pHout) while W41...
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05-26-2017 08:36 PM
[NMR paper] Probing the Interaction of the Potassium Channel Modulating KCNE1 in Lipid Bilayers via Solid-State NMR Spectroscopy.
Probing the Interaction of the Potassium Channel Modulating KCNE1 in Lipid Bilayers via Solid-State NMR Spectroscopy.
Related Articles Probing the Interaction of the Potassium Channel Modulating KCNE1 in Lipid Bilayers via Solid-State NMR Spectroscopy.
Magn Reson Chem. 2017 Feb 23;:
Authors: Zhang R, Sahu ID, Comer RG, Maltsev S, Dabney-Smith C, Lorigan GA
Abstract
KCNE1 is known to modulate the voltage-gated potassium channel ? subunit KCNQ1 to generate slowly activating potassium currents. This potassium channel is essential...
Structural basis for the ethanol action on G-protein–activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy - pnas.org
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