Evidence map›Paper›PMID 34699778›Full record

ArticleNeuron2022

Structural mechanisms of assembly, permeation, gating, and pharmacology of native human rod CNG channel.

Jing Xue, Yan Han, Weizhong Zeng, Youxing Jiang

Open access · greenAbstract read
In one paragraph

Article in Neuron, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  11. The open gate of the AMPA receptor forms a CaNature structural & molecular biology · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Development of a translatable gene augmentation therapy for CNGB1-retinitis pigmentosa.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  18. Article
  19. Article
  20. Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

4 authors at 1 institution in 1 country.

Jing XueHoward Hughes Medical Institute and Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Yan HanHoward Hughes Medical Institute and Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Weizhong ZengHoward Hughes Medical Institute and Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Youxing JiangHoward Hughes Medical Institute and Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA. Electronic address: youxing.jiang@utsouthwestern.edu.
Howard Hughes Medical Institute · US

Funding

Structural and Functional Studies of Organellar Ion ChannelsR35GM140892 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, YOUXING · 2021 to 2025
$1.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM140892
6 · The paper itself

Abstract

Mammalian cyclic nucleotide-gated (CNG) channels are nonselective cation channels activated by cGMP or cAMP and play essential roles in the signal transduction of the visual and olfactory sensory systems. CNGA1, the principal component of the CNG channel from rod photoreceptors, can by itself form a functional homotetrameric channel and has been used as the model system in the majority of rod CNG studies. However, the native rod CNG functions as a heterotetramer consisting of three A1 and one B1 subunits and exhibits different functional properties than the CNGA1 homomer. Here we present the functional analysis of human rod CNGA1/B1 heterotetramer and its cryo-EM structures in apo, cGMP-bound, cAMP-bound, and L-cis-Diltiazem-blocked states. These structures, with resolution ranging from 2.6 to 3.3 Å, elucidate the structural mechanisms underlying the 3:1 subunit stoichiometry, the asymmetrical gating upon cGMP activation, and the unique pharmacological property of the native rod CNG channel.

Indexed as

Cyclic GMPCyclic Nucleotide-Gated Cation ChannelsAnimalsHumansMammalsCyclic GMPCyclic Nucleotide-Gated Cation ChannelscGMP and cAMP activationCNGA1 and CNGB1 heterotetramercyclic nucleotide-gatednative rod CNG channelsignal transductionvisual and olfactory sensory system

Identifiers

PMID34699778
PMCPMC8738139
OpenAlexW3209047196

What OpenQuestion holds

Textmetadata
LicenceTDM
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.