Evidence map›Paper›PMID 8744304›Full record

ArticleBiophysical journal1996

Subunit interactions in the activation of cyclic nucleotide-gated ion channels.

M D Varnum, W N Zagotta

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1996. 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
2.5field-weighted citation impact, top 10% 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, 75 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Article
  8. Distribution, amplification, and summation of cyclic nucleotide sensitivities within single olfactory sensory cilia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Tyrosine phosphorylation of rod cyclic nucleotide-gated channels switches off Ca2+/calmodulin inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  14. Article
  15. Stepwise contribution of each subunit to the cooperative activation of BK channels by Ca2+.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  16. Mechanism of calcium/calmodulin inhibition of rod cyclic nucleotide-gated channels.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  17. Molecular regions controlling the activity of CNG channels.The Journal of general physiology · 2001
    Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

M D VarnumDepartment of Physiology and Biophysics, Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
W N Zagotta
Howard Hughes Medical Institute · US

Funding

GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
NEI NIH HHS EY 10329NEI NIH HHS R01 EY010329
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) ion channels of retinal photoreceptors and olfactory neurons are multimeric proteins of unknown stoichiometry. To investigate the subunit interactions that occur during CNG channel activation, we have used tandem cDNA constructs of the rod CNG channel to generate heteromultimeric channels composed of wild-type and mutant subunits. We introduced point mutations that affect channel activation: 1) D604M, which alters the relative ability of agonists to promote the allosteric conformational change(s) associated with channel opening, and 2) T560A, which primarily affects the initial binding affinity for cGMP, and to a lesser extent, the allosteric transition. At saturating concentrations of agonist, heteromultimeric channels were intermediate between wild-type and mutant homomultimers in agonist efficacy and apparent affinity for cGMP, cIMP, and cAMP, consistent with a model for the allosteric transition involving a concerted conformational change in all of the channel subunits. Results were also consistent with a model involving independent transitions in two or three, but not one or four, of the channel subunits. The behavior of the heterodimers implies that the channel stoichiometry is some multiple of 2 and is consistent with a tetrameric quaternary structure for the functional channel complex. Steady-state dose-response relations for homomultimeric and heteromultimeric channels were well fit by a Monod, Wyman, and Changeux model with a concerted allosteric opening transition stabilized by binding of agonist.

Indexed as

Allosteric SiteAnimalsBiophysical PhenomenaBiophysicsCattleDimerizationIn Vitro TechniquesIon Channel GatingIon ChannelsModels, BiologicalMutagenesis, Site-DirectedNucleotides, CyclicProtein ConformationRecombinant ProteinsRetinal Rod Photoreceptor CellsIon ChannelsNucleotides, CyclicRecombinant Proteins

Identifiers

PMID8744304
PMCPMC1225246
OpenAlexW1993910833

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.