Evidence map›Paper›PMID 30158696›Full record

ArticleNature2018

Crystal structure of the natural anion-conducting channelrhodopsin GtACR1.

Yoon Seok Kim, Hideaki E Kato, Keitaro Yamashita, Shota Ito, Keiichi Inoue, Charu Ramakrishnan, Lief E Fenno, Kathryn E Evans, Joseph M Paggi, Ron O Dror and 3 more

Abstract read
In one paragraph

Article in Nature, 2018. 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
5.7field-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

56 citing papers in PubMed, 119 citations in OpenAlex.

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  8. Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 2 countries.

Yoon Seok KimDepartment of Bioengineering, Department of Psychiatry and Behavioral Sciences, and Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Hideaki E KatoDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA. hekato@stanford.edu.
Keitaro YamashitaRIKEN SPring-8 Center, Hyogo, Japan.
Shota ItoDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, Japan.
Keiichi InouePRESTO, Japan Science and Technology Agency, Honcho, Kawaguchi, Japan.
Charu RamakrishnanDepartment of Bioengineering, Department of Psychiatry and Behavioral Sciences, and Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Lief E FennoDepartment of Bioengineering, Department of Psychiatry and Behavioral Sciences, and Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Kathryn E EvansDepartment of Bioengineering, Department of Psychiatry and Behavioral Sciences, and Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA.
Joseph M PaggiDepartment of Computer Science, Stanford University, Stanford, CA, USA.
Ron O DrorDepartment of Computer Science, Stanford University, Stanford, CA, USA.
Hideki KandoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, Japan.
Brian K KobilkaDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Karl DeisserothDepartment of Bioengineering, Department of Psychiatry and Behavioral Sciences, and Howard Hughes Medical Institute, Stanford University, Stanford, CA, USA. deissero@stanford.edu.
Stanford University · USHoward Hughes Medical Institute · USNagoya Institute of Technology · JPJapan Science and Technology Agency · JPSPring-8 · JP

Funding

Channel Structure-Based Tools for Precise Interrogation of Circuitry and BehaviorR37MH075957 · NIMH · STANFORD UNIVERSITY · PI DEISSEROTH, KARL A. · 2013 to 2022
$7.3M
Technology development for fast optical interrogation of living neural circuitryR01MH075957 · NIMH · STANFORD UNIVERSITY · PI DEISSEROTH, KARL A. · 2008 to 2012
$2.6M
Howard Hughes Medical InstituteNIMH NIH HHS R01 MH075957NIMH NIH HHS R37 MH075957
6 · The paper itself

Abstract

The naturally occurring channelrhodopsin variant anion channelrhodopsin-1 (ACR1), discovered in the cryptophyte algae Guillardia theta, exhibits large light-gated anion conductance and high anion selectivity when expressed in heterologous settings, properties that support its use as an optogenetic tool to inhibit neuronal firing with light. However, molecular insight into ACR1 is lacking owing to the absence of structural information underlying light-gated anion conductance. Here we present the crystal structure of G. theta ACR1 at 2.9 Å resolution. The structure reveals unusual architectural features that span the extracellular domain, retinal-binding pocket, Schiff-base region, and anion-conduction pathway. Together with electrophysiological and spectroscopic analyses, these findings reveal the fundamental molecular basis of naturally occurring light-gated anion conductance, and provide a framework for designing the next generation of optogenetic tools.

Indexed as

AnionsBacteriorhodopsinsBinding SitesChannelrhodopsinsCryptophytaCrystallography, X-RayElectric ConductivityIon Channel GatingIon TransportModels, MolecularOptogeneticsRetinaldehydeSchiff BasesAnionsBacteriorhodopsinsChannelrhodopsinsRetinaldehydeSchiff Bases

Identifiers

PMID30158696
PMCPMC6340299
OpenAlexW2888978497

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.