Evidence map›Paper›PMID 21958666›Full record

ReviewBiochimica et biophysica acta2012

Structural correlates of selectivity and inactivation in potassium channels.

Jason G McCoy, Crina M Nimigean

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 1 pooled it
–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

48 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. KFrontiers in pharmacology · 2026
    Pooled it
  2. Review
  3. Structure of the human TWIK-2 potassium channel and its inhibition by pimozide.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024
    Article
  6. Article
  7. Structures of Gating Intermediates in a KJournal of molecular biology · 2021
    Article
  8. Article
  9. Article
  10. Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020
    Article
  12. Article
  13. Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Conformational ensembles of non-peptide ω-conotoxin mimetics and CaComputational and structural biotechnology journal · 2020
    Article
  17. Article
  18. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  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.

Jason G McCoyDepartment of Anesthesiology, Weill Cornell Medical College, 1300 York Avenue, New York, NY 10021, USA.
Crina M Nimigean

Funding

Molecular Mechanisms of Potassium Channel Permeation and GatingR01GM088352 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI NIMIGEAN, CRINA M · 2010 to 2025
$5.6M
NIGMS NIH HHS R01 GM088352
6 · The paper itself

Abstract

Potassium channels are involved in a tremendously diverse range of physiological applications requiring distinctly different functional properties. Not surprisingly, the amino acid sequences for these proteins are diverse as well, except for the region that has been ordained the "selectivity filter". The goal of this review is to examine our current understanding of the role of the selectivity filter and regions adjacent to it in specifying selectivity as well as its role in gating/inactivation and possible mechanisms by which these processes are coupled. Our working hypothesis is that an amino acid network behind the filter modulates selectivity in channels with the same signature sequence while at the same time affecting channel inactivation properties. This article is part of a Special Issue entitled: Membrane protein structure and function.

Indexed as

Amino Acid SequenceAnimalsHumansModels, MolecularMolecular Sequence DataPotassium ChannelsProtein Structure, SecondarySequence AlignmentPotassium Channels

Identifiers

PMID21958666
PMCPMC3253935

What OpenQuestion holds

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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.