Evidence map›Paper›PMID 31004059›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Unifying photocycle model for light adaptation and temporal evolution of cation conductance in channelrhodopsin-2.

Jens Kuhne, Johannes Vierock, Stefan Alexander Tennigkeit, Max-Aylmer Dreier, Jonas Wietek, Dennis Petersen, Konstantin Gavriljuk, Samir F El-Mashtoly, Peter Hegemann, Klaus Gerwert

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Article
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  5. Multicolor photoreactions of the red light-activated channelrhodopsin Chrimson.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
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  11. Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025
    Article
  12. Article
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  18. Multiple retinal isomerizations during the early phase of the bestrhodopsin photoreaction.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
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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

10 authors.

Jens KuhneDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Johannes VierockInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
Stefan Alexander TennigkeitDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Max-Aylmer DreierDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany.ORCID 0000-0003-0056-014X
Jonas WietekInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.ORCID 0000-0002-8079-7042
Dennis PetersenDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Konstantin GavriljukDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Samir F El-MashtolyDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Peter HegemannInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, 10115 Berlin, Germany hegemann@rz.hu-berlin.de klaus.gerwert@bph.rub.de.
Klaus GerwertDepartment of Biophysics, Ruhr-Universität Bochum, 44780 Bochum, Germany; hegemann@rz.hu-berlin.de klaus.gerwert@bph.rub.de.ORCID 0000-0001-8759-5964

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although channelrhodopsin (ChR) is a widely applied light-activated ion channel, important properties such as light adaptation, photocurrent inactivation, and alteration of the ion selectivity during continuous illumination are not well understood from a molecular perspective. Herein, we address these open questions using single-turnover electrophysiology, time-resolved step-scan FTIR, and Raman spectroscopy of fully dark-adapted ChR2. This yields a unifying parallel photocycle model integrating now all so far controversial discussed data. In dark-adapted ChR2, the protonated retinal Schiff base chromophore (RSBH

Indexed as

CationsChannelrhodopsinsChlamydomonas reinhardtiiHEK293 CellsHumansIsomerismLightProtein ConformationProtonsRetinaldehydeCationsChannelrhodopsinsProtonsRetinaldehydechannelrhodopsin-2electrophysiologyoptogeneticsphotoisomerizationtime-resolved FTIR

Identifiers

PMID31004059
PMCPMC6510988

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.