Evidence map›Paper›PMID 41672996›Full record

ArticleNature communications2026

Bioactive lipid-mediated structural and functional regulation of the essential human potassium channel Kir7.1.

Qingwei Niu, Simon Vu, Yuanjian Xu, Mingxing Qian, Anastasiia Rudenko, Jin Ye, Jianwei Zeng, Wei Huang, Douglas F Covey, Rui Zhang and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026
    Review
  2. Review
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

12 authors.

Qingwei Niu *Department of Cell Biology and Physiology, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-7657-1462
Simon Vu *Center for Investigation of Membrane Excitability Diseases (CIMED), WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.
Yuanjian XuDepartment of Developmental Biology and Taylor Family Institute for Innovative Psychiatric Research, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0009-0003-1108-3286
Mingxing QianDepartment of Developmental Biology and Taylor Family Institute for Innovative Psychiatric Research, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-2106-2855
Anastasiia RudenkoDepartment of Cell Biology and Physiology, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.
Jin YeDepartment of Biochemistry and Molecular Biophysics, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0003-1004-5344
Jianwei ZengDepartment of Biochemistry and Molecular Biophysics, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-6880-3366
Wei HuangDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH, USA.ORCID http://orcid.org/0000-0003-2097-8148
Douglas F CoveyDepartment of Developmental Biology and Taylor Family Institute for Innovative Psychiatric Research, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-9316-8683
Rui ZhangDepartment of Biochemistry and Molecular Biophysics, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA. zhangrui@wustl.edu.ORCID http://orcid.org/0000-0003-3159-9565
Ziao FuDepartment of Cell Biology and Physiology, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA. ziao@wustl.edu.ORCID http://orcid.org/0000-0001-5036-1945
Polina V LishkoDepartment of Cell Biology and Physiology, WashU Medicine; Washington University School of Medicine, St. Louis, MO, USA. lishko@wustl.edu.ORCID http://orcid.org/0000-0003-3140-2769

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inwardly rectifying potassium channel Kir7.1 is essential for the physiological function of diverse tissues, including the retinal pigment epithelium and the gestational myometrium. Loss-of-function mutations in KCNJ13, which encodes Kir7.1, or conditional ablation of Kir7.1 in the retinal pigment epithelium, lead to early-onset vision loss. Despite strong genetic evidence supporting Kir7.1 as a therapeutic target, its regulation by endogenous ligands-beyond phosphoinositides-remains poorly understood. Here, we report cryo-electron microscopy structures of human Kir7.1 in multiple functional states at resolutions ranging from 2.8 Å to 4.0 Å. These structures uncover the molecular basis of Kir7.1 modulation by PI

Indexed as

Potassium Channels, Inwardly RectifyingAnimalsBinding SitesCholesterolCryoelectron MicroscopyHEK293 CellsHumansIon Channel GatingLigandsPhosphatidylinositol 4,5-DiphosphateCholesterolKir7.1 channelLigandsPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Inwardly Rectifying

Identifiers

PMID41672996
PMCPMC13018574

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.