Evidence map›Paper›PMID 32169020›Full record

ArticleAnnual review of plant biology2020

Mechanisms of Cryptochrome-Mediated Photoresponses in Plants.

Qin Wang, Chentao Lin

Open access · bronzeAbstract read
In one paragraph

Article in Annual review of plant biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
38.5field-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

128 citing papers in PubMed, 272 citations in OpenAlex.

  1. Review
  2. Key residues Tyr293, Val360, and Tyr399 regulate flavin stability in the plant cryptochrome from Chlamydomonas reinhardtii.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
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  15. Antarctic MicroalgaMarine drugs · 2026
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68 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

2 authors at 2 institutions in 2 countries.

Qin WangBasic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Chentao LinDepartment of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, California 90095, USA; email: clin@mcdb.ucla.edu.
Fujian Agriculture and Forestry University · CNUniversity of California, Los Angeles · US

Funding

The signaling mechanisms of Arabidopsis CRY2R01GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 2001 to 2021
$9.5M
PLANT PHOTOSENSORY RECEPTOR CRY2--SIGNALING MECHANISMR29GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 1997 to 2001
$204k
NIGMS NIH HHS R01 GM056265NIGMS NIH HHS R29 GM056265
6 · The paper itself

Abstract

Cryptochromes are blue-light receptors that mediate photoresponses in plants. The genomes of most land plants encode two clades of cryptochromes, CRY1 and CRY2, which mediate distinct and overlapping photoresponses within the same species and between different plant species. Photoresponsive protein-protein interaction is the primary mode of signal transduction of cryptochromes. Cryptochromes exist as physiologically inactive monomers in the dark; the absorption of photons leads to conformational change and cryptochrome homooligomerization, which alters the affinity of cryptochromes interacting with cryptochrome-interacting proteins to form various cryptochrome complexes. These cryptochrome complexes, collectively referred to as the cryptochrome complexome, regulate transcription or stability of photoresponsive proteins to modulate plant growth and development. The activity of cryptochromes is regulated by photooligomerization; dark monomerization; cryptochrome regulatory proteins; and cryptochrome phosphorylation, ubiquitination, and degradation. Most of the more than 30 presently known cryptochrome-interacting proteins are either regulated by other photoreceptors or physically interactingwith the protein complexes of other photoreceptors. Some cryptochrome-interacting proteins are also hormonal signaling or regulatory proteins. These two mechanisms enable cryptochromes to integrate blue-light signals with other internal and external signals to optimize plant growth and development.

Indexed as

ArabidopsisArabidopsis ProteinsCryptochromesLightTranscription FactorsArabidopsis ProteinsCryptochromesTranscription FactorsArabidopsisblue lightCRY1CRY2cryptochromephotomorphogenesisphotoreceptorprotein–protein interactionsproteolysistranscription

Identifiers

PMID32169020
PMCPMC7428154
OpenAlexW3011051107

What OpenQuestion holds

Textmetadata
LicenceTDM
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.