Evidence map›Paper›PMID 22266941›Full record

ArticleNature2012

Crystal structure of the channelrhodopsin light-gated cation channel.

Hideaki E Kato, Feng Zhang, Ofer Yizhar, Charu Ramakrishnan, Tomohiro Nishizawa, Kunio Hirata, Jumpei Ito, Yusuke Aita, Tomoya Tsukazaki, Shigehiko Hayashi and 5 more

Open access · greenAbstract read
In one paragraph

Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 231 papers.

0numbers the graph read from it
0cells of the map it votes in
231citing papers in PubMed
22.1field-weighted citation impact, top 1% 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

231 citing papers in PubMed, 542 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  6. Article
  7. Article
  8. Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Transcendent Aspects of Proton Channels.Annual review of physiology · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

171 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 7 institutions in 3 countries.

Hideaki E KatoDepartment of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
Feng Zhang
Ofer Yizhar
Charu Ramakrishnan
Tomohiro Nishizawa
Kunio Hirata
Jumpei Ito
Yusuke Aita
Tomoya Tsukazaki
Shigehiko Hayashi
Peter Hegemann
Andrés D Maturana
Ryuichiro Ishitani
Karl Deisseroth
Osamu Nureki
The University of Tokyo · JPHoward Hughes Medical Institute · USNagaoka University of Technology · JPHumboldt-Universität zu Berlin · DEKyoto University · JPSPring-8 · JPStanford University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Channelrhodopsins (ChRs) are light-gated cation channels derived from algae that have shown experimental utility in optogenetics; for example, neurons expressing ChRs can be optically controlled with high temporal precision within systems as complex as freely moving mammals. Although ChRs have been broadly applied to neuroscience research, little is known about the molecular mechanisms by which these unusual and powerful proteins operate. Here we present the crystal structure of a ChR (a C1C2 chimaera between ChR1 and ChR2 from Chlamydomonas reinhardtii) at 2.3 Å resolution. The structure reveals the essential molecular architecture of ChRs, including the retinal-binding pocket and cation conduction pathway. This integration of structural and electrophysiological analyses provides insight into the molecular basis for the remarkable function of ChRs, and paves the way for the precise and principled design of ChR variants with novel properties.

Indexed as

LightAnimalsBacteriorhodopsinsBinding SitesCationsCattleChlamydomonas reinhardtiiCrystallography, X-RayIon Channel GatingIon ChannelsModels, MolecularMutationProtein ConformationRecombinant Fusion ProteinsRetinaldehydeRhodopsinBacteriorhodopsinsCationsIon ChannelsRecombinant Fusion ProteinsRetinaldehydeRhodopsinSchiff Bases

Identifiers

PMID22266941
PMCPMC4160518
OpenAlexW2062594525

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.