Evidence map›Paper›PMID 23183698›Full record

ArticleThe Journal of general physiology2012

Perspectives on: conformational coupling in ion channels: conformational coupling in BK potassium channels.

Frank T Horrigan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. An Additional CaCell reports · 2020
    Article
  8. Article
  9. 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
  10. Review
  11. Article
  12. Modeling ion channels: past, present, and future.The Journal of general physiology · 2014
    Review
  13. Single-channel kinetics of BK (Slo1) channels.Frontiers in physiology · 2014
    Review
  14. Review
  15. Article
  16. Properties of Slo1 K+ channels with and without the gating ring.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Article
  18. Review
  19. 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

1 author at 1 institution in 1 country.

Frank T HorriganDepartment of Molecular Physiology and Biophysics, Baylor College of Medicine Houston, TX 77030, USA. Horrigan@bcm.edu
Baylor College of Medicine · US

Funding

Allosteric mechanisms of CA-activated K channel gatingR01NS042901 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI HORRIGAN, FRANK T · 2001 to 2011
$3.0M
NINDS NIH HHS NS42901NINDS NIH HHS R01 NS042901
6 · The paper itself

Abstract

Large conductance calcium- and voltage-dependent BK potassium channels (aka BK(Ca), MaxiK, Slo1, KCa1.1, and KCNMA1) are expressed in a wide variety of tissues throughout the body and are activated by both intracellular Ca(2+) and membrane depolarization. Owing to these properties, BK channels participate in diverse physiological processes from electrical excitability in neurons and secretory cells, and regulation of smooth muscle tone to tuning of auditory hair cells (Vergara et al., 1998; Ghatta et al., 2006). The response to voltage and Ca(2+) allows BK channels to integrate electrical and calcium signaling, which is central to their physiological role. Understanding how BK and other multimodal channels are regulated by and integrate diverse stimuli is not only physiologically important but also relevant to the topic of conformational coupling. As a voltage- and ligand-dependent channel, BK channels contain both voltage-sensor and ligand-binding domains as well as a gate to regulate the flow of K(+) through the pore. Coupling of conformational changes in one domain to another provides the basis for transducing voltage and ligand binding into channel opening and, therefore, defines, together with the functional properties of the gate and sensors, the signal transduction properties of the channel. The goal of this perspective is to provide an overview on the role and molecular basis of conformational coupling between functional domains in BK channels and outline some of the questions that remain to be answered.

Indexed as

CalciumCalcium SignalingIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsProtein ConformationCalciumLarge-Conductance Calcium-Activated Potassium Channels

Identifiers

PMID23183698
PMCPMC3514727
OpenAlexW2021295065

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.