Evidence map›Paper›PMID 16344323›Full record

ArticleThe Journal of general physiology2006

Effects of multiple metal binding sites on calcium and magnesium-dependent activation of BK channels.

Lei Hu, Huanghe Yang, Jingyi Shi, Jianmin Cui

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. 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
  4. Ethanol Effect on BK Channels is Modulated by Magnesium.Alcoholism, clinical and experimental research · 2015
    Article
  5. Review
  6. State-dependent FRET reports calcium- and voltage-dependent gating-ring motions in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mg2+ enhances voltage sensor/gate coupling in BK channels.The Journal of general physiology · 2008
    Article
  13. Mg2+ mediates interaction between the voltage sensor and cytosolic domain to activate BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  14. 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.

Lei HuDepartment of Biomedical Engineering and Cardiac Bioelectricity and Arrhythmia Center, Washington University, St. Louis, MO 63130, USA.
Huanghe Yang
Jingyi Shi
Jianmin Cui

Funding

Ca2+ Dependent K+ Channels: Allosteric GatingR01HL070393 · NHLBI · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2002 to 2015
$4.9M
NHLBI NIH HHS R01 HL070393NHLBI NIH HHS R01-HL70393
6 · The paper itself

Abstract

BK channels are activated by physiological concentrations of intracellular Ca2+ and Mg2+ in a variety of cells. Previous studies have identified two sites important for high-affinity Ca2+ sensing between [Ca2+]i of 0.1-100 microM and a site important for Mg2+ sensing between [Mg2+]i of 0.1-10 mM. BK channels can be also activated by Ca2+ and Mg2+ at concentrations>10 mM so that the steady-state conductance and voltage (G-V) relation continuously shifts to more negative voltage ranges when [Mg2+]i increases from 0.1-100 mM. We demonstrate that a novel site is responsible for metal sensing at concentrations>=10 mM, and all four sites affect channel activation independently. As a result, the contributions of these sites to channel activation are complex, depending on the combination of Ca2+ and Mg2+ concentrations. Here we examined the effects of each of these sites on Ca2+ and Mg2+-dependent activation and the data are consistent with the suggestion that these sites are responsible for metal binding. We provide an allosteric model for quantitative estimation of the contributions that each of these putative binding sites makes to channel activation at any [Ca2+]i and [Mg2+]i.

Indexed as

Allosteric SiteAnimalsBinding SitesCalciumFemaleIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsMagnesiumMathematicsMembrane PotentialsModels, BiologicalMutationOocytesXenopus laevisCalciumLarge-Conductance Calcium-Activated Potassium ChannelsMagnesium

Identifiers

PMID16344323
PMCPMC2151482
OpenAlexW2130815833

What OpenQuestion holds

Textmetadata
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.