Evidence map›Paper›PMID 18474637›Full record

ArticleThe Journal of general physiology2008

Position and role of the BK channel alpha subunit S0 helix inferred from disulfide crosslinking.

Guoxia Liu, Sergey I Zakharov, Lin Yang, Shi-Xian Deng, Donald W Landry, Arthur Karlin, Steven O Marx

Abstract read
In one paragraph

Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  2. Review
  3. Review
  4. β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  5. Article
  6. Article
  7. Review
  8. Oxidative modulation of voltage-gated potassium channels.Antioxidants & redox signaling · 2014
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Cysteine scanning and modification reveal major differences between BK channels and Kv channels in the inner pore region.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Guoxia Liu1 Division of Cardiology, Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Sergey I Zakharov
Lin Yang
Shi-Xian Deng
Donald W Landry
Arthur Karlin
Steven O Marx

Funding

CTSA INFRASTRUCTURE FOR PEDIATRIC RESEARCHUL1RR024156 · NCRR · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GINSBERG, HENRY N · 2006 to 2011
$53.0M
REGULATION OF RYANODINE RECEPTORS BY ALLOSTERIC MODULATIONP01HL081172 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KARLIN, ARTHUR · 2007 to 2011
$7.3M
BK CHANNEL MODULATION BY BETA SUBUNITSR01NS054946 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KARLIN, ARTHUR, MARX, STEVEN O · 2007 to 2014
$2.8M
NCRR NIH HHS UL1 RR024156NHLBI NIH HHS P01 HL081172NINDS NIH HHS R01 NS054946
6 · The paper itself

Abstract

The position and role of the unique N-terminal transmembrane (TM) helix, S0, in large-conductance, voltage- and calcium-activated potassium (BK) channels are undetermined. From the extents of intra-subunit, endogenous disulfide bond formation between cysteines substituted for the residues just outside the membrane domain, we infer that the extracellular flank of S0 is surrounded on three sides by the extracellular flanks of TM helices S1 and S2 and the four-residue extracellular loop between S3 and S4. Eight different double cysteine-substituted alphas, each with one cysteine in the S0 flank and one in the S3-S4 loop, were at least 90% disulfide cross-linked. Two of these alphas formed channels in which 90% cross-linking had no effect on the V(50) or on the activation and deactivation rate constants. This implies that the extracellular ends of S0, S3, and S4 are close in the resting state and move in concert during voltage sensor activation. The association of S0 with the gating charge bearing S3 and S4 could contribute to the considerably larger electrostatic energy required to activate the BK channel compared with typical voltage-gated potassium channels with six TM helices.

Indexed as

Allosteric RegulationAmino Acid SequenceAmino Acid SubstitutionCalciumCell Line, TransformedConserved SequenceCysteineDisulfidesElectrophysiologyHelix-Loop-Helix MotifsHumansIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMembrane PotentialsMolecular Sequence DataProtein EngineeringCalciumCysteineDisulfidesLarge-Conductance Calcium-Activated Potassium Channel alpha Subunits

Identifiers

PMID18474637
PMCPMC2391248

What OpenQuestion holds

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LicenceCC BY-NC-SA
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Registered trials

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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.