Evidence map›Paper›PMID 22773746›Full record

ArticleThe Plant cell2012

A flavin binding cryptochrome photoreceptor responds to both blue and red light in Chlamydomonas reinhardtii.

Benedikt Beel, Katja Prager, Meike Spexard, Severin Sasso, Daniel Weiss, Nico Müller, Mark Heinnickel, David Dewez, Danielle Ikoma, Arthur R Grossman and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
14.9field-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

73 citing papers in PubMed, 175 citations in OpenAlex.

  1. Review
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  8. Article
  9. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  10. Dynamics and mechanism of DNA repair by a bifunctional cryptochrome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
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  19. Article
  20. A Single-Component Blue Light-Induced System Based on EL222 inInternational journal of molecular sciences · 2022
    Article

13 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

12 authors at 6 institutions in 3 countries.

Benedikt BeelInstitute of General Botany and Plant Physiology, Friedrich Schiller University, 07743 Jena, Germany.
Katja Prager
Meike Spexard
Severin Sasso
Daniel Weiss
Nico Müller
Mark Heinnickel
David Dewez
Danielle Ikoma
Arthur R Grossman
Tilman Kottke
Maria Mittag
Carnegie Institution for Science · USFriedrich Schiller University Jena · DEBielefeld University · DESchiller International University · FRDepartment of Plant Biology · USLeibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryptochromes are flavoproteins that act as sensory blue light receptors in insects, plants, fungi, and bacteria. We have investigated a cryptochrome from the green alga Chlamydomonas reinhardtii with sequence homology to animal cryptochromes and (6-4) photolyases. In response to blue and red light exposure, this animal-like cryptochrome (aCRY) alters the light-dependent expression of various genes encoding proteins involved in chlorophyll and carotenoid biosynthesis, light-harvesting complexes, nitrogen metabolism, cell cycle control, and the circadian clock. Additionally, exposure to yellow but not far-red light leads to comparable increases in the expression of specific genes; this expression is significantly reduced in an acry insertional mutant. These in vivo effects are congruent with in vitro data showing that blue, yellow, and red light, but not far-red light, are absorbed by the neutral radical state of flavin in aCRY. The aCRY neutral radical is formed following blue light absorption of the oxidized flavin. Red illumination leads to conversion to the fully reduced state. Our data suggest that aCRY is a functionally important blue and red light-activated flavoprotein. The broad spectral response implies that the neutral radical state functions as a dark form in aCRY and expands the paradigm of flavoproteins and cryptochromes as blue light sensors to include other light qualities.

Indexed as

LightCell CycleChlamydomonas reinhardtiiChlorophyllCircadian ClocksCircadian RhythmCryptochromesEscherichia coliFlavinsGenetic Complementation TestMutagenesis, InsertionalOxidation-ReductionPhotoreceptors, PlantPhylogenyPlants, Genetically ModifiedTransgenesChlorophyllCryptochromesFlavinsPhotoreceptors, Plant

Identifiers

PMID22773746
PMCPMC3426128
OpenAlexW2125826919

What Socratic 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 Socratic graph.