ArticleThe Journal of physiology2001
Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues.
Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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
63 citing papers in PubMed, 102 citations in OpenAlex.
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Conserved Kir channel mechanisms governing intrinsic excitability in human and rodent parvalbumin neurons.Communications biology · 2026Article
- Postnatal reduction of eIF4E overexpression in D1-SPNs ameliorates KCNQ channel dysfunction, hyperexcitability and ASD-like behaviours.Cellular and molecular life sciences : CMLS · 2026Article
- WONOEP XVII appraisal: Targeting network excitability beyond the synapse -Neurotransmitter, ionic, and electro -diffusions.Epilepsia · 2025Review
- Dopaminergic Inhibition of the Inwardly Rectifying Potassium Current in Direct Pathway Medium Spiny Neurons in Normal and Parkinsonian Striatum.Brain sciences · 2025Article
- Regulation of input excitability in human and mouse parvalbumin interneurons by Kir potassium channels.bioRxiv : the preprint server for biology · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Article
- Barium and psoriasis: a mini-review and hypothesis linking environmental exposures to ion channel modulation.Frontiers in medicine · 2025Review
- CD146Cell communication and signaling : CCS · 2024Article
- Article
- An affordable Three-Dimensional (3D) Printed Recording Chamber for Two-Electrode Voltage Clamp Electrophysiology.Journal of undergraduate neuroscience education : JUNE : a publication of FUN, Faculty for Undergraduate Neuroscience · 2023Article
- The origins of the full-field flash electroretinogram b-wave.Frontiers in molecular neuroscience · 2023Review
- The hyperpolarization-activated, cyclic nucleotide-gated channel resides on myocytes in mouse bladders and contributes to adrenergic-induced detrusor relaxation.American journal of physiology. Regulatory, integrative and comparative physiology · 2022Article
- Inwardly rectifying potassium channels mediate polymyxin-induced nephrotoxicity.Cellular and molecular life sciences : CMLS · 2022Article
- A selectivity filter mutation provides insights into gating regulation of a KCommunications biology · 2022Article
- KPhysiological reports · 2022Article
- Differential effects of obesity on visceral versus subcutaneous adipose arteries: role of shear-activated Kir2.1 and alterations to the glycocalyx.American journal of physiology. Heart and circulatory physiology · 2022Article
- Weak Cation Selectivity in HCN Channels Results From KFunction (Oxford, England) · 2022Article
- Combination of Sildenafil and BaFrontiers in pharmacology · 2022Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. The block of the IRK1/Kir2.1 inwardly rectifying K+ channel by a Ba(2+) ion is highly voltage dependent, where the ion binds approximately half-way within the membrane electrical field. The mechanism by which two distinct mutations, E125N and T141A, affect Ba(2+) block of Kir2.1 was investigated using heterologous expression in Xenopus oocytes. 2. Analysis of the blocking kinetics showed that E125 and T141 affect the entry and binding of Ba(2+) to the channel, respectively. Replacing the glutamate at position 125 with an asparagine greatly decreased the rate at which the Ba(2+) ions enter and leave the pore. In contrast, replacing the polar threonine at position 141 with an alanine affected the entry rate of the Ba(2+) ions while leaving the exit rate unchanged. 3. Acidification of the extracellular solution slowed the exit rate of the Ba(2+) from the wild-type channel, but had no such effect on the Kir2.1(E125N) mutant. 4. These results thus reveal two unique roles for the amino acids at positions 125 and 141 in aiding the interaction of Ba(2+) with the channel. Their possible roles in K+ permeation are discussed.
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.