Evidence map›Paper›PMID 18287006›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Gating at the selectivity filter in cyclic nucleotide-gated channels.

Jorge E Contreras, Deepa Srikumar, Miguel Holmgren

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

56 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Mechanism of use-dependent Kv2 channel inhibition by RY785.The Journal of general physiology · 2022
    Article
  5. Article
  6. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Closed state-coupled C-type inactivation in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Article
  19. Review
  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

3 authors at 2 institutions in 1 country.

Jorge E ContrerasPorter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892-3701, USA.
Deepa Srikumar
Miguel Holmgren
National Institute of Neurological Disorders and Stroke · USNational Institutes of Health · US

Funding

Structure and Function of Membrane ProteinsZIANS002993 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2009 to 2025
$24.0M
Structure and Function of Membrane ProteinsZ01NS002993 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2002 to 2008
$1.1M
Intramural NIH HHS
6 · The paper itself

Abstract

By opening and closing the permeation pathway (gating) in response to cGMP binding, cyclic nucleotide-gated (CNG) channels serve key roles in the transduction of visual and olfactory signals. Compiling evidence suggests that the activation gate in CNG channels is not located at the intracellular end of pore, as it has been established for voltage-activated potassium (K(V)) channels. Here, we show that ion permeation in CNG channels is tightly regulated at the selectivity filter. By scanning the entire selectivity filter using small cysteine reagents, like cadmium and silver, we observed a state-dependent accessibility pattern consistent with gated access at the middle of the selectivity filter, likely at the corresponding position known to regulate structural changes in KcsA channels in response to low concentrations of permeant ions.

Indexed as

Amino Acid SubstitutionAnimalsCadmiumCell LineCyclic GMPCyclic Nucleotide-Gated Cation ChannelsCysteineIon Channel GatingProtein ConformationSilverSubstrate SpecificityTransfectionCadmiumCyclic GMPCyclic Nucleotide-Gated Cation ChannelsCysteineSilver

Identifiers

PMID18287006
PMCPMC2265121
OpenAlexW2057073947

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.