Evidence map›Paper›PMID 20038524›Full record

ArticleThe Journal of general physiology2010

Inactivation of the KcsA potassium channel explored with heterotetramers.

Dvir Rotem, Amy Mason, Hagan Bayley

Open access · greenAbstract read
In one paragraph

Article in The Journal of general physiology, 2010. 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
1.2field-weighted citation impact, top 21% 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, 27 citations in OpenAlex.

  1. Article
  2. A Multi-Scale Approach to Model KFrontiers in molecular biosciences · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Tetrameric assembly of KvLm K+ channels with defined numbers of voltage sensors.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  10. Article
  11. Mechanism for selectivity-inactivation coupling in KcsA potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  12. Review
  13. 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

3 authors at 1 institution in 1 country.

Dvir RotemDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, England, UK.
Amy Mason
Hagan Bayley
University of Oxford · GB

Funding

Medical Research Council G0300122
6 · The paper itself

Abstract

The tetrameric prokaryotic potassium channel KcsA is activated by protons acting on the intracellular aspect of the protein and inactivated through conformational changes in the selectivity filter. Inactivation is modulated by a network of interactions within each protomer between the pore helix and residues at the external entrance of the channel. Inactivation is suppressed by the E71A mutation, which perturbs the stability of this network. Here, cell-free protein synthesis followed by protein purification by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to produce heterotetramers of KcsA that contain different combinations of wild-type and E71A subunits. Single-channel recordings from these heterotetramers reveal how the network of interactions in individual protomers affects ionic conduction and channel inactivation, suggesting that the latter is a cooperative process.

Indexed as

Ion Channel GatingBacterial ProteinsLipid BilayersPotassium ChannelsStructure-Activity RelationshipBacterial ProteinsLipid BilayersPotassium Channelsprokaryotic potassium channel

Identifiers

PMID20038524
PMCPMC2806417
OpenAlexW2143013070

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.