Evidence map›Paper›PMID 20637420›Full record

ArticleStructure (London, England : 1993)2010

Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry.

Sayan Gupta, Vassiliy N Bavro, Rhijuta D'Mello, Stephen J Tucker, Catherine Vénien-Bryan, Mark R Chance

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Cholesterol regulation of mechanosensitive ion channels.Frontiers in cell and developmental biology · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Therapeutic Antibodies Targeting Potassium Ion Channels.Handbook of experimental pharmacology · 2021
    Article
  16. Review
  17. Article
  18. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  19. Article
  20. Review
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

6 authors.

Sayan GuptaCenter for Synchrotron Biosciences, Case Western Reserve University, Cleveland, OH 44022, USA.
Vassiliy N Bavro
Rhijuta D'Mello
Stephen J Tucker
Catherine Vénien-Bryan
Mark R Chance

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Center for Synchrotron BiosciencesP41EB001979 · NIBIB · YESHIVA UNIVERSITY · PI CHANCE, MARK R · 2003 to 2008
$5.6M
Radiolytic Footprinting Methods for Structural Mass SpectrometryR01EB009688 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2010 to 2013
$1.1M
Biotechnology and Biological Sciences Research Council BB/F013035/1British Heart Foundation PG/09/016/26992NIBIB NIH HHS P30 EB009998NIBIB NIH HHS P41 EB001979NIBIB NIH HHS R01 EB009688Wellcome Trust 084655
6 · The paper itself

Abstract

Potassium channels are dynamic proteins that undergo large conformational changes to regulate the flow of K(+) ions across the cell membrane. Understanding the gating mechanism of these channels therefore requires methods for probing channel structure in both their open and closed conformations. Radiolytic footprinting is used to study the gating mechanism of the inwardly-rectifying potassium channel KirBac3.1. The purified protein stabilized in either open or closed conformations was exposed to focused synchrotron X-ray beams on millisecond timescales to modify solvent accessible amino acid side chains. These modifications were identified and quantified using high-resolution mass spectrometry. The differences observed between the closed and open states were then used to reveal local conformational changes that occur during channel gating. The results provide support for a proposed gating mechanism of the Kir channel and demonstrate a method of probing the dynamic gating mechanism of other integral membrane proteins and ion channels.

Indexed as

Models, MolecularProtein ConformationIon Channel GatingMass SpectrometryPotassium Channels, Inwardly RectifyingPulse RadiolysisSynchrotronsPotassium Channels, Inwardly Rectifying

Identifiers

PMID20637420
PMCPMC3124773

What OpenQuestion holds

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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.