Evidence map›Paper›PMID 14615590›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Channelrhodopsin-2, a directly light-gated cation-selective membrane channel.

Georg Nagel, Tanjef Szellas, Wolfram Huhn, Suneel Kateriya, Nona Adeishvili, Peter Berthold, Doris Ollig, Peter Hegemann, Ernst Bamberg

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,247 papers.

0numbers the graph read from it
0cells of the map it votes in
1,247citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

1,247 citing papers in PubMed, 2,682 citations in OpenAlex.

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  4. Nobels oblige.Nature plants · 2026
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1,187 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 1 country.

Georg NagelMax-Planck-Institut für Biophysik, Marie-Curie-Strasse 15, 60439 Frankfurt, Germany. georg.nagel@mpibp-frankfurt.mpg.de
Tanjef Szellas
Wolfram Huhn
Suneel Kateriya
Nona Adeishvili
Peter Berthold
Doris Ollig
Peter Hegemann
Ernst Bamberg
University of Regensburg · DEGoethe University Frankfurt · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial-type rhodopsins are found in archaea, prokaryotes, and eukaryotes. Some of them represent membrane ion transport proteins such as bacteriorhodopsin, a light-driven proton pump, or channelrhodopsin-1 (ChR1), a recently identified light-gated proton channel from the green alga Chlamydomonas reinhardtii. ChR1 and ChR2, a related microbial-type rhodopsin from C. reinhardtii, were shown to be involved in generation of photocurrents of this green alga. We demonstrate by functional expression, both in oocytes of Xenopus laevis and mammalian cells, that ChR2 is a directly light-switched cation-selective ion channel. This channel opens rapidly after absorption of a photon to generate a large permeability for monovalent and divalent cations. ChR2 desensitizes in continuous light to a smaller steady-state conductance. Recovery from desensitization is accelerated by extracellular H+ and negative membrane potential, whereas closing of the ChR2 ion channel is decelerated by intracellular H+. ChR2 is expressed mainly in C. reinhardtii under low-light conditions, suggesting involvement in photoreception in dark-adapted cells. The predicted seven-transmembrane alpha helices of ChR2 are characteristic for G protein-coupled receptors but reflect a different motif for a cation-selective ion channel. Finally, we demonstrate that ChR2 may be used to depolarize small or large cells, simply by illumination.

Indexed as

Algal ProteinsAnimalsCationsCell LineChlamydomonas reinhardtiiCricetinaeFemaleHumansHydrogen-Ion ConcentrationIn Vitro TechniquesIon Channel GatingIon ChannelsLightMembrane PotentialsOocytesPhotobiologyAlgal ProteinsCationsIon ChannelsProtozoan ProteinsRecombinant ProteinsRhodopsin

Identifiers

PMID14615590
PMCPMC283525
OpenAlexW2159423248

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.