ArticleThe Journal of general physiology2002
IRK1 inward rectifier K(+) channels exhibit no intrinsic rectification.
Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 35 citations in OpenAlex.
- Unconventional voltage sensing in an inwardly rectifying potassium channel.The Journal of general physiology · 2021Article
- Kir4.1/Kir5.1 channels possess strong intrinsic inward rectification determined by a voltage-dependent K+-flux gating mechanism.The Journal of general physiology · 2021Article
- A small viral potassium ion channel with an inherent inward rectification.Channels (Austin, Tex.) · 2019Article
- New Insights on Astrocyte Ion Channels: Critical for Homeostasis and Neuron-Glia Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Review
- Multi-ion versus single-ion conduction mechanisms can yield current rectification in biological ion channels.Journal of biological physics · 2014Article
- KCNE1-KCNQ1 osmoregulation by interaction of phosphatidylinositol-4,5-bisphosphate with Mg2+ and polyamines.The Journal of physiology · 2010Article
- Extracellular protons titrate voltage gating of a ligand-gated ion channel.The Journal of general physiology · 2010Article
- Cardiac strong inward rectifier potassium channels.Journal of molecular and cellular cardiology · 2010Review
- Physical determinants of strong voltage sensitivity of K(+) channel block.Nature structural & molecular biology · 2009Article
- Low-affinity spermine block mediating outward currents through Kir2.1 and Kir2.2 inward rectifier potassium channels.The Journal of physiology · 2007Article
- Charges in the cytoplasmic pore control intrinsic inward rectification and single-channel properties in Kir1.1 and Kir2.1 channels.The Journal of membrane biology · 2007Article
- Block by internal Mg2+ causes voltage-dependent inactivation of Kv1.5.European biophysics journal : EBJ · 2006Article
- Ring of negative charge in BK channels facilitates block by intracellular Mg2+ and polyamines through electrostatics.The Journal of general physiology · 2006Article
- The polyamine binding site in inward rectifier K+ channels.The Journal of general physiology · 2006Article
- Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1.The Journal of general physiology · 2006Article
- Differential polyamine sensitivity in inwardly rectifying Kir2 potassium channels.The Journal of physiology · 2006Article
- Evidence for sequential ion-binding loci along the inner pore of the IRK1 inward-rectifier K+ channel.The Journal of general physiology · 2005Article
- Mechanism of the voltage sensitivity of IRK1 inward-rectifier K+ channel block by the polyamine spermine.The Journal of general physiology · 2005Article
- Different intracellular polyamine concentrations underlie the difference in the inward rectifier K(+) currents in atria and ventricles of the guinea-pig heart.The Journal of physiology · 2005Article
- A ring of negative charges in the intracellular vestibule of Kir2.1 channel modulates K+ permeation.Biophysical journal · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In intact cells the depolarization-induced outward IRK1 currents undergo profound relaxation so that the steady-state macroscopic I-V curve exhibits strong inward rectification. A modest degree of rectification persists after the membrane patches were perfused with artificial solutions devoid of Mg(2+) and polyamines, which has been interpreted as a reflection of intrinsic channel gating and led to the view that inward rectification results from enhancement of the intrinsic gating by intracellular cations rather than simple pore block. Furthermore, IRK1 exhibits significant extracellular K(+)-sensitive relaxation of its inward current, a feature that has been likened to the C-type inactivation observed in the voltage-activated Shaker K(+) channels. We found that both these current relaxations can be accounted for by impurities in some common constituents of recording solutions, such as residual hydroxyethylpiperazine in HEPES and ethylenediamine in EDTA. Therefore, inherently, IRK1 channels are essentially ohmic at the macroscopic level, and the voltage jump-induced current relaxations do not reflect IRK1 gating but the unusually high affinity of its pore for cations. Furthermore, our study helps define the optimal experimental conditions for studying IRK1.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.