ArticlePflugers Archiv : European journal of physiology2010
Functional consequences of Kir2.1/Kir2.2 subunit heteromerization.
Article in Pflugers Archiv : European journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 19 citations in OpenAlex.
- The network of cardiac KNaunyn-Schmiedeberg's archives of pharmacology · 2024Review
- Subunit gating resulting from individual protonation events in Kir2 channels.Nature communications · 2023Article
- Subunit gating resulting from individual protonation events in Kir2 channels.Research square · 2023Article
- Gating and modulation of an inward-rectifier potassium channel.The Journal of general physiology · 2023Article
- Sildenafil affects the human Kir2.1 and Kir2.2 channels at clinically relevant concentrations: Inhibition potentiated by low BaFrontiers in pharmacology · 2023Article
- Article
- Kir2.2 p.Thr140Met: a genetic susceptibility to sporadic periodic paralysis.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2018Article
- Regional variation of the inwardly rectifying potassium current in the canine heart and the contributions to differences in action potential repolarization.Journal of molecular and cellular cardiology · 2015Article
- The inward rectifier potassium channel Kir2.1 is expressed in mouse neutrophils from bone marrow and liver.American journal of physiology. Cell physiology · 2015Article
- CaMKII regulation of cardiac K channels.Frontiers in pharmacology · 2014Review
- The function and molecular identity of inward rectifier channels in vestibular hair cells of the mouse inner ear.Journal of neurophysiology · 2012Article
- Kir2.6 regulates the surface expression of Kir2.x inward rectifier potassium channels.The Journal of biological chemistry · 2011Article
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 2 countries.
Funding
Abstract
Kir2 subunits form channels that underlie classical strongly inwardly rectifying potassium currents. While homomeric Kir2 channels display a number of distinct and physiologically important properties, the functional properties of heteromeric Kir2 assemblies, as well as the stoichiometries and the arrangements of Kir2 subunits in native channels, remain largely unknown. Therefore, we have implemented a concatemeric approach, whereby all four cloned Kir2 subunits were linked in tandem, in order to study the effects of Kir2.1 and Kir2.2 heteromerization on properties of the resulting channels. Kir2.2 subunits contributed stronger to single-channel conductance than Kir2.1 subunits, and channels containing two or more Kir2.2 subunits displayed conductances indistinguishable from that of a Kir2.2 homomeric channel. In contrast, single-channel kinetics was a more discriminating property. The open times were significantly shorter in Kir2.2 channels compared with Kir2.1 channels and decreased nearly proportionally to the number of Kir2.2 subunits in the heteromeric channel. Similarly, the sensitivity to block by barium also depended on the proportions of Kir2.1 to Kir2.2 subunits. Overall, the results showed that Kir2.1 and Kir2.2 subunits exert neither a dominant nor an anomalous effect on any of the properties of heteromeric channels. The data highlight opportunities and challenges of using differential properties of Kir2 channels in deciphering the subunit composition of native inwardly rectifying potassium currents.
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.