Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
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Structural studies of ion permeation and Ca2+ blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel poreVoltage-dependent gating in a "voltage sensor-less" ion channel.Intrinsic versus extrinsic voltage sensitivity of blocker interaction with an ion channel poreAlveolar epithelial CNGA1 channels mediate cGMP-stimulated, amiloride-insensitive, lung liquid absorption.Extracellular protons titrate voltage gating of a ligand-gated ion channel.Position and motions of the S4 helix during opening of the Shaker potassium channel.cAMP control of HCN2 channel Mg2+ block reveals loose coupling between the cyclic nucleotide-gating ring and the pore.Gating at the selectivity filter of ion channels that conduct Na+ and K+ ions.Multiple mechanisms underlying rectification in retinal cyclic nucleotide-gated (CNGA1) channels.Proton transfer unlocks inactivation in cyclic nucleotide-gated A1 channels.
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Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on August 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
@en
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
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type
label
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
@en
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
@nl
prefLabel
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
@en
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
@nl
P2093
P2860
P356
P1476
Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.
@en
P2093
Juan Ramón Martínez-François
Yanping Xu
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P304
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10.1085/JGP.200910240
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2009-08-01T00:00:00Z