Evidence map›Paper›PMID 21746846›Full record

ArticleThe Journal of general physiology2011

Charge substitution for a deep-pore residue reveals structural dynamics during BK channel gating.

Xixi Chen, Richard W Aldrich

Open access · greenAbstract read
In one paragraph

Article in The Journal of general physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  5. The functionally relevant site for paxilline inhibition of BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Review
  7. Molecular mechanisms of Slo2 KThe Journal of physiology · 2017
    Article
  8. Atomic determinants of BK channel activation by polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. BK channel opening involves side-chain reorientation of multiple deep-pore residues.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Xixi ChenSection of Neurobiology and Center for Learning and Memory, The University of Texas at Austin, Austin, TX 78712, USA.
Richard W Aldrich
The University of Texas at Austin · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pore-lining amino acids of ion channel proteins reside on the interface between a polar (the pore) and a nonpolar environment (the rest of the protein). The structural dynamics of this region, which physically controls ionic flow, are essential components of channel gating. Using large-conductance, Ca(2+)-dependent K(+) (BK) channels, we devised a systematic charge-substitution method to probe conformational changes in the pore region during channel gating. We identified a deep-pore residue (314 in hSlo1) as a marker of structural dynamics. We manipulated the charge states of this residue by substituting amino acids with different valence and pKa, and by adjusting intracellular pH. We found that the charged states of the 314 residues stabilized an open state of the BK channel. With models based on known structures of related channels, we postulate a dynamic rearrangement of the deep-pore region during BK channel opening/closing, which involves a change of the degree of pore exposure for 314.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionArginineCells, CulturedHEK293 CellsHumansHydrogen-Ion ConcentrationIon Channel GatingLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMethionineModels, MolecularProtein Structure, TertiaryStructure-Activity RelationshipArginineLarge-Conductance Calcium-Activated Potassium ChannelsMethionine

Identifiers

PMID21746846
PMCPMC3149437
OpenAlexW2150807393

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.