Evidence map›Paper›PMID 21187429›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structural studies of ion permeation and Ca2+ blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel pore.

Mehabaw G Derebe, Weizhong Zeng, Yang Li, Amer Alam, Youxing Jiang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

30 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  3. The open gate of the AMPA receptor forms a CaNature structural & molecular biology · 2024
    Article
  4. Article
  5. Mechanism of Calcium Permeation in a Glutamate Receptor Ion Channel.Journal of chemical information and modeling · 2023
    Article
  6. Interrogating the gating motions of the NaK channel.The Journal of general physiology · 2022
    Article
  7. Article
  8. High-Resolution Structures of KHandbook of experimental pharmacology · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 2 countries.

Mehabaw G DerebeDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9040, USA.
Weizhong Zeng
Yang Li
Amer Alam
Youxing Jiang
Chinese Academy of Sciences · CNHoward Hughes Medical Institute · USSouthwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

Structural mechanisms of ion selectivity and gating in tetrameric cation channelsR01GM079179 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, YOUXING · 2007 to 2019
$3.5M
Howard Hughes Medical InstituteNIGMS NIH HHS 5 F31 GM07703NIGMS NIH HHS GM079179NIGMS NIH HHS R01 GM079179
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels play an essential role in the visual and olfactory sensory systems and are ubiquitous in eukaryotes. Details of their underlying ion selectivity properties are still not fully understood and are a matter of debate in the absence of high-resolution structures. To reveal the structural mechanism of ion selectivity in CNG channels, particularly their Ca(2+) blockage property, we engineered a set of mimics of CNG channel pores for both structural and functional analysis. The mimics faithfully represent the CNG channels they are modeled after, permeate Na(+) and K(+) equally well, and exhibit the same Ca(2+) blockage and permeation properties. Their high-resolution structures reveal a hitherto unseen selectivity filter architecture comprising three contiguous ion binding sites in which Na(+) and K(+) bind with different ion-ligand geometries. Our structural analysis reveals that the conserved acidic residue in the filter is essential for Ca(2+) binding but not through direct ion chelation as in the currently accepted view. Furthermore, structural insight from our CNG mimics allows us to pinpoint equivalent interactions in CNG channels through structure-based mutagenesis that have previously not been predicted using NaK or K(+) channel models.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsBacillus cereusBacterial ProteinsCalciumCattleHumansIonsLigandsMolecular Sequence DataMutagenesisPotassiumProtein ConformationRecombinant ProteinsSequence Homology, Amino AcidBacterial ProteinsCalciumIonsLigandsPotassiumRecombinant ProteinsSodium

Identifiers

PMID21187429
PMCPMC3021057
OpenAlexW2027788236

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.