Evidence map›Paper›PMID 42591064›Full record

ReviewBiochemical Society transactions2026

Molecular mechanisms of Kir channel gating.

Arpan Bysack, Hariharasundaram Raghuraman

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Arpan BysackBiophysical Sciences Division, Saha Institute of Nuclear Physics, Kolkata, India.
Hariharasundaram RaghuramanBiophysical Sciences Division, Saha Institute of Nuclear Physics, Kolkata, India.ORCID 0000-0001-9106-8278

Funding

Department of Atomic Energy, Government of India (DAE) BARBS/RSI-4008
6 · The paper itself

Abstract

Inward-rectifying K+ (Kir) channels are ubiquitously present in variety of cells and play an important role in maintaining resting membrane potential and supporting K+ homeostasis. They are an important family of K+ channels that connects cellular metabolism to membrane excitability, and exhibit complex lipid-protein interaction landscape. Dysfunction of Kir channels is, therefore, associated with multi-factorial diseases and are important drug targets. Recent high-resolution structural dynamics and functional studies of several Kir channels have significantly advanced our understanding of the mechanisms of voltage-dependent pore block and channel gating regulation mediated by lipids, and other modulators. In the present minireview, based on recent knowledge derived from prokaryotic and eukaryotic Kir channels, we highlight the binding sites of the channel for various ligands/modulators, and also provide an emerging model focusing on the structural rearrangements associated with the transition of the channel from the closed/deactivated to open/activated conformation during lipid-dependent gating, which should be broadly applicable to all Kir channels.

Indexed as

Ion Channel GatingPotassium Channels, Inwardly RectifyingAnimalsBinding SitesHumansLigandsModels, MolecularProtein ConformationLigandsPotassium Channels, Inwardly RectifyingInward-rectifying K+ channellipid-dependent gatingsmall-molecule modulatorsstructural dynamicsvoltage-dependent pore block

Identifiers

PMID42591064
PMCPMC13488966

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.