Evidence map›Paper›PMID 24082096›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Heme impairs the ball-and-chain inactivation of potassium channels.

Nirakar Sahoo, Nishit Goradia, Oliver Ohlenschläger, Roland Schönherr, Manfred Friedrich, Winfried Plass, Reinhard Kappl, Toshinori Hoshi, Stefan H Heinemann

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Review
  2. Article
  3. Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. A new world of heme function.Pflugers Archiv : European journal of physiology · 2020
    Article
  18. Impact of intracellular hemin on N-type inactivation of voltage-gated KPflugers Archiv : European journal of physiology · 2020
    Article
  19. Altered gating of KeLife · 2019
    Article
  20. Modulation of KPflugers Archiv : European journal of physiology · 2019
    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

9 authors.

Nirakar SahooCenter for Molecular Biomedicine, Department of Biophysics, Friedrich Schiller University Jena and Jena University Hospital, D-07745 Jena, Germany.
Nishit Goradia
Oliver Ohlenschläger
Roland Schönherr
Manfred Friedrich
Winfried Plass
Reinhard Kappl
Toshinori Hoshi
Stefan H Heinemann

Funding

REGULATION OF ION CHANNELS BY METHIONINE OXIDATIONR01GM057654 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOSHI, TOSHINORI, OLCESE, RICCARDO · 1998 to 2014
$5.0M
6 · The paper itself

Abstract

Fine-tuned regulation of K(+) channel inactivation enables excitable cells to adjust action potential firing. Fast inactivation present in some K(+) channels is mediated by the distal N-terminal structure (ball) occluding the ion permeation pathway. Here we show that Kv1.4 K(+) channels are potently regulated by intracellular free heme; heme binds to the N-terminal inactivation domain and thereby impairs the inactivation process, thus enhancing the K(+) current with an apparent EC50 value of ∼20 nM. Functional studies on channel mutants and structural investigations on recombinant inactivation ball domain peptides encompassing the first 61 residues of Kv1.4 revealed a heme-responsive binding motif involving Cys13:His16 and a secondary histidine at position 35. Heme binding to the N-terminal inactivation domain induces a conformational constraint that prevents it from reaching its receptor site at the vestibule of the channel pore.

Indexed as

HemeKv1.4 Potassium ChannelAnimalsCrystallography, X-RayIon TransportProtein BindingProtein Structure, TertiaryRatsXenopus laevisHemeKv1.4 Potassium ChannelA-type channelcysteineintrinsically disordered domainNMRN-type inactivation

Identifiers

PMID24082096
PMCPMC3801010

What OpenQuestion holds

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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.