Evidence map›Paper›PMID 24287615›Full record

ArticleNature communications2013

Hysteresis of ligand binding in CNGA2 ion channels.

Vasilica Nache, Thomas Eick, Eckhard Schulz, Ralf Schmauder, Klaus Benndorf

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.8field-weighted citation impact, top 34% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  8. Review
  9. Redefining the role of CaCell death & disease · 2022
    Article
  10. Thermodynamic profile of mutual subunit control in a heteromeric receptor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Hysteretic Behavior in Voltage-Gated Channels.Frontiers in pharmacology · 2020
    Review
  16. Article
  17. Stepwise activation of a class C GPCR begins with millisecond dimer rearrangement.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Vasilica NacheInstitut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, 07743 Jena, Germany.
Thomas Eick
Eckhard Schulz
Ralf Schmauder
Klaus Benndorf
Jena University Hospital · DEFriedrich Schiller University Jena · DESchmalkalden University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetrameric cyclic nucleotide-gated (CNG) channels mediate receptor potentials in olfaction and vision. The channels are activated by the binding of cyclic nucleotides to a binding domain embedded in the C terminus of each subunit. Here using a fluorescent cGMP derivative (fcGMP), we show for homotetrameric CNGA2 channels that ligand unbinding is ~50 times faster at saturating than at subsaturating fcGMP. Analysis with complex Markovian models reveals two pathways for ligand unbinding; the partially liganded open channel unbinds its ligands from closed states only, whereas the fully liganded channel reaches a different open state from which it unbinds all four ligands rapidly. Consequently, the transition pathways for ligand binding and activation of a fully liganded CNGA2 channel differ from that of ligand unbinding and deactivation, resulting in pronounced hysteresis of the gating mechanism. This concentration-dependent gating mechanism allows the channels to respond to changes in the cyclic nucleotide concentration with different kinetics.

Indexed as

AnimalsCyclic GMPCyclic Nucleotide-Gated Cation ChannelsDimerizationFemaleKineticsLigandsOocytesPatch-Clamp TechniquesProtein BindingXenopus laevisXenopus ProteinsCyclic GMPCyclic Nucleotide-Gated Cation ChannelsLigandsXenopus Proteins

Identifiers

PMID24287615
PMCPMC3868267
OpenAlexW2021815653

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.