Evidence map›Paper›PMID 16081488›Full record

ArticleThe Journal of physiology2005

Activation of olfactory-type cyclic nucleotide-gated channels is highly cooperative.

Vasilica Nache, Eckhard Schulz, Thomas Zimmer, Jana Kusch, Christoph Biskup, Rolf Koopmann, Volker Hagen, Klaus Benndorf

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.3field-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

31 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Ion Channel-Based Reporters for cAMP Detection.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. 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
  10. Review
  11. Article
  12. Article
  13. The long tale of the calcium activated ClChannels (Austin, Tex.) · 2017
    Review
  14. Article
  15. Article
  16. Review
  17. Family of prokaryote cyclic nucleotide-modulated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Article
  19. Article
  20. Insulin receptor regulates photoreceptor CNG channel activity.American journal of physiology. Endocrinology and metabolism · 2012
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Vasilica NacheInstitut für Physiologie II, Friedrich-Schiller-Universität Jena, Germany.
Eckhard Schulz
Thomas Zimmer
Jana Kusch
Christoph Biskup
Rolf Koopmann
Volker Hagen
Klaus Benndorf
Friedrich Schiller University Jena · DELeibniz-Forschungsinstitut für Molekulare Pharmakologie · DESchmalkalden University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) ion channels play a key role in the sensory transduction of vision and olfaction. The channels are opened by the binding of cyclic nucleotides. Native olfactory CNG channels are heterotetramers of CNGA2, CNGA4, and CNGB1b subunits. Upon heterologous expression, only CNGA2 subunits can form functional homotetrameric channels. It is presently not known how the binding of the ligands to the four subunits is translated to channel opening. We studied activation of olfactory CNG channels by photolysis-induced jumps of cGMP or cAMP, two cyclic nucleotides with markedly different apparent affinity. It is shown that at equal degree of activation, the activation time course of homotetrameric channels is similar with cGMP and cAMP and it is also similar in homo- and heterotetrameric channels with the same cyclic nucleotide. Kinetic models were globally fitted to activation time courses of homotetrameric channels. While all models containing equivalent binding sites failed, a model containing three binding sites with a ligand affinity high-low-high described the data adequately. Only the second binding step switches from a very low to a very high open probability. We propose a unique gating mechanism for homotetrameric and heterotetrameric channels that involves only three highly cooperative binding steps.

Indexed as

Models, BiologicalAnimalsCell MembraneCells, CulturedComputer SimulationCyclic Nucleotide-Gated Cation ChannelsIon Channel GatingIon ChannelsMembrane PotentialsNucleotides, CyclicOocytesSmellXenopus laevisCyclic Nucleotide-Gated Cation ChannelsIon ChannelsNucleotides, Cyclicolfactory cyclic-nucleotide-gated channel 2

Identifiers

PMID16081488
PMCPMC1464204
OpenAlexW2169799159

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.