Evidence map›Paper›PMID 21997217›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain.

Victor P T Pau, Frank J Smith, Alexander B Taylor, Liubov V Parfenova, Elsie Samakai, Matthew M Callaghan, Karin Abarca-Heidemann, P John Hart, Brad S Rothberg

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Redox Regulation of KAntioxidants & redox signaling · 2024
    Review
  5. Article
  6. Certain, but Not All, Tetraether Lipids from the Thermoacidophilic ArchaeonInternational journal of molecular sciences · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Polyamine block of MthK potassium channels.The Journal of general physiology · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017
    Review
  19. Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015
    Review
  20. Ethanol Effect on BK Channels is Modulated by Magnesium.Alcoholism, clinical and experimental research · 2015
    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.

Victor P T PauDepartment of Biochemistry, Temple University School of Medicine, 3400 North Broad Street, Philadelphia, PA 19140, USA.
Frank J Smith
Alexander B Taylor
Liubov V Parfenova
Elsie Samakai
Matthew M Callaghan
Karin Abarca-Heidemann
P John Hart
Brad S Rothberg

Funding

Structure and Function of Potassium ChannelsR01GM068523 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI ROTHBERG, BRAD S. · 2004 to 2010
$1.9M
NIGMS NIH HHS GM068523NIGMS NIH HHS R01 GM068523
6 · The paper itself

Abstract

Regulator of K(+) conductance (RCK) domains control the activity of a variety of K(+) transporters and channels, including the human large conductance Ca(2+)-activated K(+) channel that is important for blood pressure regulation and control of neuronal firing, and MthK, a prokaryotic Ca(2+)-gated K(+) channel that has yielded structural insight toward mechanisms of RCK domain-controlled channel gating. In MthK, a gating ring of eight RCK domains regulates channel activation by Ca(2+). Here, using electrophysiology and X-ray crystallography, we show that each RCK domain contributes to three different regulatory Ca(2+)-binding sites, two of which are located at the interfaces between adjacent RCK domains. The additional Ca(2+)-binding sites, resulting in a stoichiometry of 24 Ca(2+) ions per channel, is consistent with the steep relation between [Ca(2+)] and MthK channel activity. Comparison of Ca(2+)-bound and unliganded RCK domains suggests a physical mechanism for Ca(2+)-dependent conformational changes that underlie gating in this class of channels.

Indexed as

Models, MolecularProtein Structure, TertiaryBinding SitesCalciumCrystallography, X-RayElectrophysiologyIon Channel GatingLipid BilayersPotassium Channels, Calcium-ActivatedCalciumLipid BilayersPotassium Channels, Calcium-Activated

Identifiers

PMID21997217
PMCPMC3203816

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.