Evidence map›Paper›PMID 12843404›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification.

Tinatin I Brelidze, Xiaowei Niu, Karl L Magleby

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

92 citing papers in PubMed, 144 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Pathogenic variants in the polycystin pore helix cause distinct forms of channel dysfunction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. BK Channelopathies andAnnual review of physiology · 2024
    Review
  8. eLife · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Calcium-Activated KHandbook of experimental pharmacology · 2021
    Article
  15. Article
  16. Article
  17. Molecular Structure of the Hair Cell Mechanoelectrical Transduction Complex.Cold Spring Harbor perspectives in medicine · 2019
    Review
  18. Article
  19. Article
  20. Article

32 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

3 authors at 1 institution in 1 country.

Tinatin I BrelidzeDepartment of Physiology and Biophysics, University of Miami School of Medicine, 1600 N.W. 10th Avenue, Miami, FL 33136, USA.
Xiaowei Niu
Karl L Magleby
University of Miami · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Large-conductance Ca2+-voltage-activated K+ channels (BK channels) control many key physiological processes, such as neurotransmitter release and muscle contraction. A signature feature of BK channels is that they have the largest single channel conductance of all K+ channels. Here we examine the mechanism of this large conductance. Comparison of the sequence of BK channels to lower-conductance K+ channels and to a crystallized bacterial K+ channel (MthK) revealed that BK channels have a ring of eight negatively charged glutamate residues at the entrance to the intracellular vestibule. This ring of charge, which is absent in lower-conductance K+ channels, is shown to double the conductance of BK channels for outward currents by increasing the concentration of K+ in the vestibule through an electrostatic mechanism. Removing the ring of charge converts BK channels to inwardly rectifying channels. Thus, a simple electrostatic mechanism contributes to the large conductance of BK channels.

Indexed as

Amino Acids, AcidicAmino Acid SequenceAnimalsConserved SequenceElectric ConductivityFemaleHumansIn Vitro TechniquesLarge-Conductance Calcium-Activated Potassium ChannelsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOocytesPotassium Channels, Calcium-ActivatedProtein ConformationRecombinant ProteinsAmino Acids, AcidicLarge-Conductance Calcium-Activated Potassium ChannelsPotassium Channels, Calcium-ActivatedRecombinant Proteins

Identifiers

PMID12843404
PMCPMC166430
OpenAlexW1977221331

What OpenQuestion holds

Textmetadata
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.