Coupled ion movement underlies rectification in an inward-rectifier K+ channel.
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Crystal Structure of the Eukaryotic Strong Inward-Rectifier K+ Channel Kir2.2 at 3.1 A ResolutionPhysical determinants of strong voltage sensitivity of K+ channel blockMechanism of potassium-channel selectivity revealed by Na+ and Li+ binding sites within the KcsA poreCrystal Structure of the Mammalian GIRK2 K+ Channel and Gating Regulation by G Proteins, PIP2, and SodiumThe voltage-dependent gate in MthK potassium channels is located at the selectivity filterMechanism underlying slow kinetics of the OFF gating current in Shaker potassium channel.Intrinsic versus extrinsic voltage sensitivity of blocker interaction with an ion channel poreMolecular diversity and regulation of renal potassium channels.Polyamines as gating molecules of inward-rectifier K+ channels.Dequalinium: a novel, high-affinity blocker of CNGA1 channelsPore- and state-dependent cadmium block of I(Ks) channels formed with MinK-55C and wild-type KCNQ1 subunitsRevisiting voltage-dependent relief of block in ion channels: a mechanism independent of punchthrough.Rapid intracellular TEA block of the KcsA potassium channel.A shaker K+ channel with a miniature engineered voltage sensor.K+ channel selectivity depends on kinetic as well as thermodynamic factors.K⁺-dependent selectivity and external Ca²⁺ block of Shab K⁺ channels.Selectivity filter gating in large-conductance Ca(2+)-activated K+ channels.Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1.The polyamine binding site in inward rectifier K+ channels.Ring of negative charge in BK channels facilitates block by intracellular Mg2+ and polyamines through electrostatics.A cation-pi interaction between extracellular TEA and an aromatic residue in potassium channels.The role of the cytoplasmic pore in inward rectification of Kir2.1 channelsInteractions of external K+ and internal blockers in a weak inward-rectifier K+ channel.Blocker state dependence and trapping in hyperpolarization-activated cation channels: evidence for an intracellular activation gateTuning the voltage dependence of tetraethylammonium block with permeant ions in an inward-rectifier K+ channel.Na+ block and permeation in a K+ channel of known structureIRK1 inward rectifier K(+) channels exhibit no intrinsic rectification.Probing an open CFTR pore with organic anion blockersInteraction mechanisms between polyamines and IRK1 inward rectifier K+ channels.Pore block versus intrinsic gating in the mechanism of inward rectification in strongly rectifying IRK1 channels.Mechanism of IRK1 channel block by intracellular polyamines.Kinetics of inward-rectifier K+ channel block by quaternary alkylammonium ions. dimension and properties of the inner porePermeation properties of inward-rectifier potassium channels and their molecular determinantsMolecular basis of inward rectification: polyamine interaction sites located by combined channel and ligand mutagenesis.Investigating the putative glycine hinge in Shaker potassium channel.Blocker protection by short spermine analogs: refined mapping of the spermine binding site in a Kir channelProperties of the inner pore region of TRPV1 channels revealed by block with quaternary ammoniums.Blocking pore-open mutants of CLC-0 by amphiphilic blockers.KirBac1.1: it's an inward rectifying potassium channel.Energetic role of the paddle motif in voltage gating of Shaker K(+) channels.
P2860
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P2860
Coupled ion movement underlies rectification in an inward-rectifier K+ channel.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Coupled ion movement underlies rectification in an inward-rectifier K+ channel.
@en
type
label
Coupled ion movement underlies rectification in an inward-rectifier K+ channel.
@en
prefLabel
Coupled ion movement underlies rectification in an inward-rectifier K+ channel.
@en
P2860
P356
P1476
Coupled ion movement underlies rectification in an inward-rectifier K+ channel.
@en
P2860
P304
P356
10.1085/JGP.112.2.211
P577
1998-08-01T00:00:00Z