Evidence map›Paper›PMID 29311674›Full record

ArticleScientific reports2018

The gating mechanism in cyclic nucleotide-gated ion channels.

Monica Mazzolini, Manuel Arcangeletti, Arin Marchesi, Luisa M R Napolitano, Debora Grosa, Sourav Maity, Claudio Anselmi, Vincent Torre

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  12. Review
  13. Sensing through Non-Sensing Ocular Ion Channels.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Retinal Cyclic Nucleotide-Gated Channels: From Pathophysiology to Therapy.International journal of molecular sciences · 2018
    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

8 authors at 3 institutions in 3 countries.

Monica MazzoliniInternational School for Advanced Studies, Trieste, 34136, Italy. mazzolin@sissa.it.
Manuel ArcangelettiInternational School for Advanced Studies, Trieste, 34136, Italy.
Arin MarchesiINSERM U1006, Aix-Marseille Université, Parc Scientifique et Technologique de Luminy, Marseille, 13009, France.
Luisa M R NapolitanoInternational School for Advanced Studies, Trieste, 34136, Italy.
Debora GrosaInternational School for Advanced Studies, Trieste, 34136, Italy.
Sourav MaityInternational School for Advanced Studies, Trieste, 34136, Italy.
Claudio AnselmiNational Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA.ORCID http://orcid.org/0000-0002-3017-5085
Vincent TorreInternational School for Advanced Studies, Trieste, 34136, Italy. torre@sissa.it.
Scuola Internazionale Superiore di Studi Avanzati · ITInserm · FRNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels mediate transduction in several sensory neurons. These channels use the free energy of CNs' binding to open the pore, a process referred to as gating. CNG channels belong to the superfamily of voltage-gated channels, where the motion of the α-helix S6 controls gating in most of its members. To date, only the open, cGMP-bound, structure of a CNG channel has been determined at atomic resolution, which is inadequate to determine the molecular events underlying gating. By using electrophysiology, site-directed mutagenesis, chemical modification, and Single Molecule Force Spectroscopy, we demonstrate that opening of CNGA1 channels is initiated by the formation of salt bridges between residues in the C-linker and S5 helix. These events trigger conformational changes of the α-helix S5, transmitted to the P-helix and leading to channel opening. Therefore, the superfamily of voltage-gated channels shares a similar molecular architecture but has evolved divergent gating mechanisms.

Indexed as

Ion Channel GatingAmino Acid MotifsBinding SitesCyclic Nucleotide-Gated Cation ChannelsModels, MolecularMutationPosition-Specific Scoring MatricesProtein BindingProtein ConformationProtein FoldingStructure-Activity RelationshipCyclic Nucleotide-Gated Cation Channels

Identifiers

PMID29311674
PMCPMC5758780
OpenAlexW2781981101

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.