Evidence map›Paper›PMID 12149279›Full record

ArticleThe Journal of general physiology2002

Elimination of the BK(Ca) channel's high-affinity Ca(2+) sensitivity.

Lin Bao, Anne M Rapin, Ericka C Holmstrand, Daniel H Cox

Abstract read
In one paragraph

Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing 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

81 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. CaInternational journal of molecular sciences · 2023
    Review
  5. Article
  6. FeACS chemical biology · 2020
    Article
  7. Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Interactions of divalent cations with calcium binding sites of BK channels reveal independent motions within the gating ring.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Review
  19. Review
  20. Article

21 more citing papers are in PubMed but not listed here.

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.

Lin BaoMolecular Cardiology Research Institute, New England Medical Center, and the Department of Neuroscience, Tufts University School of Medicine, Boston, MA 02111, USA.
Anne M Rapin
Ericka C Holmstrand
Daniel H Cox

Funding

Regulation of BK Channel Gating by its Beta SubunitR01HL064831 · NHLBI · TUFTS UNIVERSITY BOSTON · PI COX, DANIEL HENRY · 2001 to 2010
$1.6M
NHLBI NIH HHS R01 HL064831NHLBI NIH HHS R01HL64831
6 · The paper itself

Abstract

We report here a combination of site-directed mutations that eliminate the high-affinity Ca(2+) response of the large-conductance Ca(2+)-activated K(+) channel (BK(Ca)), leaving only a low-affinity response blocked by high concentrations of Mg(2+). Mutations at two sites are required, the "Ca(2+) bowl," which has been implicated previously in Ca(2+) binding, and M513, at the end of the channel's seventh hydrophobic segment. Energetic analyses of mutations at these positions, alone and in combination, argue that the BK(Ca) channel contains three types of Ca(2+) binding sites, one of low affinity that is Mg(2+) sensitive (as has been suggested previously) and two of higher affinity that have similar binding characteristics and contribute approximately equally to the power of Ca(2+) to influence channel opening. Estimates of the binding characteristics of the BK(Ca) channel's high-affinity Ca(2+)-binding sites are provided.

Indexed as

AnimalsBinding, CompetitiveBinding SitesCalciumLarge-Conductance Calcium-Activated Potassium ChannelsMagnesiumModels, BiologicalMutationOocytesPotassium Channels, Calcium-ActivatedXenopus laevisCalciumLarge-Conductance Calcium-Activated Potassium ChannelsMagnesiumPotassium Channels, Calcium-Activated

Identifiers

PMID12149279
PMCPMC2234461

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.