Evidence map›Paper›PMID 25558901›Full record

ReviewChannels (Austin, Tex.)2014

Focus on Kir7.1: physiology and channelopathy.

Mohit Kumar, Bikash R Pattnaik

Open access · goldAbstract readReview
In one paragraph

Review in Channels (Austin, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.3field-weighted citation impact, top 42% of its field
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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Precision therapeutic tRNA rescue of nonsense mutation R166X inJournal of precision medicine (Amsterdam, Netherlands) · 2025
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. KAmerican journal of physiology. Renal physiology · 2023
    Article
  9. Article
  10. Inward rectifier potassium (Kir) channels in the retina: living our vision.American journal of physiology. Cell physiology · 2022
    Review
  11. Kir7.1 disease mutant T153I within the inner pore affects KAmerican journal of physiology. Cell physiology · 2022
    Article
  12. Sensing through Non-Sensing Ocular Ion Channels.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Article
  15. Expression, localization, and functional properties of inwardly rectifying KAmerican journal of physiology. Renal physiology · 2020
    Review
  16. KFrontiers in cellular neuroscience · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Article
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 at 2 institutions in 2 countries.

Mohit Kumara Departments of Biotechnology and Bioinformatics ; NIIT University ; Neemrana , Rajasthan , India.
Bikash R Pattnaik
McPherson College · USNIIT University · IN

Funding

Institutional Clinical and Translational Science AwardUL1TR000427 · NCATS · UNIVERSITY OF WISCONSIN-MADISON · PI DREZNER, MARC KENNETH · 2012 to 2016
$32.2M
NCATS NIH HHS UL1 TR000427NCATS NIH HHS UL1TR000427
6 · The paper itself

Abstract

Genetic studies have linked alterations in Kir7.1 channel to diverse pathologies. We summarize functional relevance of Kir7.1 channel in retinal pigment epithelium (RPE), regulation of channel function by various cytoplasmic metabolites, and mutations that cause channelopathies. At the apical membrane of RPE, K(+) channels contribute to subretinal K(+) homeostasis and support Na(+)/K(+) pump and Na(+)-K(+)-2Cl(-) cotransporter function by providing a pathway for K(+) secretion. Electrophysiological studies have established that barium- and cesium-sensitive inwardly rectifying K(+) (Kir) channels make up a major component of the RPE apical membrane K(+) conductance. Native human RPE expresses transcripts for Kir1.1, Kir2.1, Kir2.2, Kir3.1, Kir3.4, Kir4.2, and Kir6.1, albeit at levels at least 50-fold lower than Kir7.1. Kir7.1 is structurally similar to other Kir channels, consisting of 2 trans-membrane domains, a pore-forming loop that contains the selectivity filter, and 2 cytoplasmic polar tails. Within the cytoplasmic structure, clusters of amino acid sequences form regulatory domains that interact with cellular metabolites and control the opening and closing of the channel. Recent evidence indicated that intrinsic sequence motifs present in Kir7.1 control surface expression. Mutant Kir7.1 channels are associated with inherited eye pathologies such as Snowflake Vitreoretinal Degeneration (SVD) and Lebers Congenital Amaurosis (LCA16). Based on the current evidence, mutations implicated in channelopathies have the potential to be used for genetic testing to diagnose blindness due to Kir7.1.

Indexed as

Amino Acid SequenceAnimalsChannelopathiesHumansMolecular Sequence DataPotassium Channels, Inwardly RectifyingProtein TransportRetinal Pigment EpitheliumKir7.1 channelPotassium Channels, Inwardly RectifyingchannelopathyLCApotassium channelretinal degenerationretinal pigment epitheliumSVD

Identifiers

PMID25558901
PMCPMC4594557
OpenAlexW1974853045

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.