Evidence map›Paper›PMID 33651975›Full record

ArticleNeuron2021

Structural mechanisms of gating and selectivity of human rod CNGA1 channel.

Jing Xue, Yan Han, Weizhong Zeng, Yan Wang, Youxing Jiang

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 88 citations in OpenAlex.

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  12. Identification ofMolecules (Basel, Switzerland) · 2025
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  13. GORK KNature communications · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 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.
Yan WangHoward 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 mechanisms of ion selectivity and gating in tetrameric cation channelsR01GM079179 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, YOUXING · 2007 to 2019
$3.5M
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 R01 GM079179NIGMS NIH HHS R35 GM140892
6 · The paper itself

Abstract

Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand gating in human rod CNGA1 channel by determining its cryo-EM structures in both the apo closed and cGMP-bound open states. Distinct from most other members of voltage-gated tetrameric cation channels, CNGA1 forms a central channel gate in the middle of the membrane, occluding the central cavity. Structural analyses of ion binding profiles in the selectivity filters of the wild-type channel and the E365Q filter mutant allow us to unambiguously define the two Ca

Indexed as

Binding SitesCalciumCyclic GMPCyclic Nucleotide-Gated Cation ChannelsHEK293 CellsHumansIon Channel GatingProtein ConformationCalciumCNGA1 protein, humanCyclic GMPCyclic Nucleotide-Gated Cation ChannelsCa(2+) blockage and permeationcGMP activationCNG channelcyclic nucleotide-gatedsignal transductionvisual and olfactory sensory system

Identifiers

PMID33651975
PMCPMC8068614
OpenAlexW3133659278

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.