Evidence map›Paper›PMID 42644644›Full record

ArticleChembiochem : a European journal of chemical biology2026

Functional Characterization of Conserved Positively Charged Residues Surrounding the Ligand-Binding Pocket in Plant Cryptochromes.

Mengqi Wan, Hao Liu, Jiaying Zhang, Xiaoyu Feng, Xin Guang, Shuchang Hu, Xiaoran Li, Min Wei, Wenxin Yin, Jun Lv and 1 more

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

11 authors.

Mengqi WanDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Hao LiuDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Jiaying ZhangDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Xiaoyu FengDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Xin GuangDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Shuchang HuDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Xiaoran LiDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Min WeiDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Wenxin YinDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Jun LvDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.
Bin WenDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Wannan Medical College, Wuhu, Anhui, China.ORCID https://orcid.org/0000-0003-1459-7998

Funding

Research Fund for the Doctoral Program of Wannan Medical College WYRCQD2023041the Key Project of Education Department of Anhui Province 2024AH051900
6 · The paper itself

Abstract

Plant cryptochromes are blue light-responsive photoreceptor proteins that regulate various photoresponses throughout plant growth and development. Compared with their homologous CPD I/III photolyases, plant cryptochromes have lost DNA repair activity but evolved signal transduction functions. The structurally conserved ligand-binding pocket, which corresponds to the photolyase active site, exhibits distinctive features in plant cryptochromes, with key binding residues being altered relative to photolyases. Notably, the distribution of charged amino acids around this pocket differs markedly between the two protein families. In this study, we identified two conserved positively charged residues (Arg237 and Arg357) flanking this pocket in Chlamydomonas reinhardtii cryptochrome (pCRY) and its Arabidopsis homologs. Biochemical and physiological analyses demonstrated that these residues effectively modulate photoreduction kinetics and oxidative stability of the flavin adenine dinucleotide (FAD) cofactor, participate in ATP binding, and ultimately influence flowering time in transgenic Arabidopsis plants. Our findings reveal that these conserved positively charged sites play critical roles in regulating the photosensitivity and functional stability of plant cryptochromes.

Indexed as

ArabidopsisChlamydomonas reinhardtiiCryptochromesAdenosine TriphosphateAmino Acid SequenceArabidopsis ProteinsBinding SitesConserved SequenceFlavin-Adenine DinucleotideLigandsModels, MolecularOxidation-ReductionAdenosine TriphosphateArabidopsis ProteinsCryptochromesFlavin-Adenine DinucleotideLigandsadenosine triphosphateoxidationphotoreductionplant cryptochromesubstrate‐binding pocket

Identifiers

PMID42644644
PMCPMC13509081

What OpenQuestion holds

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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.