Evidence map›Paper›PMID 28775289›Full record

ArticleScientific reports2017

Reaction dynamics of the chimeric channelrhodopsin C1C2.

Yusaku Hontani, Marco Marazzi, Katja Stehfest, Tilo Mathes, Ivo H M van Stokkum, Marcus Elstner, Peter Hegemann, John T M Kennis

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Multicolor photoreactions of the red light-activated channelrhodopsin Chrimson.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Multistep 11-Journal of the American Chemical Society · 2025
    Article
  5. Article
  6. Article
  7. Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025
    Article
  8. Article
  9. 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
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

8 authors.

Yusaku HontaniDepartment of Physics and Astronomy, Vrije Universiteit Amsterdam, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands.
Marco MarazziInstitute of Physical Chemistry, Karlsruhe Institute of Technology, Karlstrasse 12, D-76131, Karlsruhe, Germany.ORCID 0000-0001-7158-7994
Katja StehfestInstitute of Biology, Experimental Biophysics, Humboldt-Universität, Invalidenstraße 42, D-10115, Berlin, Germany.
Tilo MathesDepartment of Physics and Astronomy, Vrije Universiteit Amsterdam, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands.
Ivo H M van StokkumDepartment of Physics and Astronomy, Vrije Universiteit Amsterdam, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands.ORCID 0000-0002-6143-2021
Marcus ElstnerInstitute of Physical Chemistry, Karlsruhe Institute of Technology, Karlstrasse 12, D-76131, Karlsruhe, Germany.
Peter HegemannInstitute of Biology, Experimental Biophysics, Humboldt-Universität, Invalidenstraße 42, D-10115, Berlin, Germany.
John T M KennisDepartment of Physics and Astronomy, Vrije Universiteit Amsterdam, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands. j.t.m.kennis@vu.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Channelrhodopsin (ChR) is a key protein of the optogenetic toolkit. C1C2, a functional chimeric protein of Chlamydomonas reinhardtii ChR1 and ChR2, is the only ChR whose crystal structure has been solved, and thus uniquely suitable for structure-based analysis. We report C1C2 photoreaction dynamics with ultrafast transient absorption and multi-pulse spectroscopy combined with target analysis and structure-based hybrid quantum mechanics/molecular mechanics calculations. Two relaxation pathways exist on the excited (S

Indexed as

Amino AcidsBinding SitesChannelrhodopsinsIsomerismMolecular Dynamics SimulationProtein BindingProtein ConformationQuantum TheorySpectrum AnalysisStructure-Activity RelationshipAmino AcidsChannelrhodopsins

Identifiers

PMID28775289
PMCPMC5543136

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Registered trials

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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.