Evidence map›Paper›PMID 22079268›Full record

ReviewMolecular genetics and metabolism2012

Genetic defects in the hotspot of inwardly rectifying K(+) (Kir) channels and their metabolic consequences: a review.

Bikash R Pattnaik, Matti P Asuma, Ryan Spott, De-Ann M Pillers

Open access · greenAbstract readReview
In one paragraph

Review in Molecular genetics and metabolism, 2012. 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
1.3field-weighted citation impact, top 21% 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, 41 citations in OpenAlex.

  1. Review
  2. The role of polyamine metabolism in cellular function and physiology.American journal of physiology. Cell physiology · 2024
    Review
  3. Inward rectifier potassium (Kir) channels in the retina: living our vision.American journal of physiology. Cell physiology · 2022
    Review
  4. Evolution of inwardly rectifying potassium channels and their gene expression in zebrafish embryos.Developmental dynamics : an official publication of the American Association of Anatomists · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Electric organ discharge diversification in mormyrid weakly electric fish is associated with differential expression of voltage-gated ion channel genes.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2017
    Article
  12. Caveolin-1 regulates corneal wound healing by modulating Kir4.1 activity.American journal of physiology. Cell physiology · 2016
    Article
  13. Article
  14. Article
  15. A Critical Gating Switch at a Modulatory Site in Neuronal Kir3 Channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  16. Article
  17. Article
  18. Focus on Kir7.1: physiology and channelopathy.Channels (Austin, Tex.) · 2014
    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

4 authors at 2 institutions in 1 country.

Bikash R PattnaikDepartment of Pediatrics, University of Wisconsin, Madison, USA. bikashp@pediatrics.wisc.edu
Matti P Asuma
Ryan Spott
De-Ann M Pillers
University of Wisconsin–Madison · USSmith-Kettlewell Eye Research Institute · US

Funding

INSTITUTIONAL CTSA (UW-MADISON): CLINICAL TRIALSUL1RR025011 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI DREZNER, MARC KENNETH · 2007 to 2011
$29.5M
NCRR NIH HHS 1UL1RR025011NCRR NIH HHS UL1 RR025011
6 · The paper itself

Abstract

Inwardly rectifying potassium (Kir) channels are essential for maintaining normal potassium homeostasis and the resting membrane potential. As a consequence, mutations in Kir channels cause debilitating diseases ranging from cardiac failure to renal, ocular, pancreatic, and neurological abnormalities. Structurally, Kir channels consist of two trans-membrane domains, a pore-forming loop that contains the selectivity filter and two cytoplasmic polar tails. Within the cytoplasmic structure, clusters of amino acid sequences form regulatory domains that interact with cellular metabolites to control the opening and closing of the channel. In this review, we present an overview of Kir channel function and recent progress in the characterization of selected Kir channel mutations that lie in and near a C-terminal cytoplasmic 'hotspot' domain. The resultant molecular mechanisms by which the loss or gain of channel function leads to organ failure provide potential opportunities for targeted therapeutic interventions for this important group of channelopathies.

Indexed as

Amino Acid SequenceHumansIon Channel GatingMolecular Sequence DataMutationPotassium Channels, Inwardly RectifyingPotassium Channels, Inwardly Rectifying

Identifiers

PMID22079268
PMCPMC3253982
OpenAlexW2007029779

What OpenQuestion holds

Textmetadata
LicenceTDM
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.