ArticleNature communications2023
A marine cryptochrome with an inverse photo-oligomerization mechanism.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Functional Characterization of Conserved Positively Charged Residues Surrounding the Ligand-Binding Pocket in Plant Cryptochromes.Chembiochem : a European journal of chemical biology · 2026Article
- Decoding darkness by seeking photoreceptor functions with and without light.Nature plants · 2026Review
- The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026Article
- A Simple Modification of a Commercial Plunge-Freezer to Allow Time-Resolved Vitrification for Cryo-EM Analyses of Light-Activated Proteins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- All Light, Everywhere? Photoreceptors at Nonconventional Sites.Physiology (Bethesda, Md.) · 2024Review
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptochromes (CRYs) are a structurally conserved but functionally diverse family of proteins that can confer unique sensory properties to organisms. In the marine bristle worm Platynereis dumerilii, its light receptive cryptochrome L-CRY (PdLCry) allows the animal to discriminate between sunlight and moonlight, an important requirement for synchronizing its lunar cycle-dependent mass spawning. Using cryo-electron microscopy, we show that in the dark, PdLCry adopts a dimer arrangement observed neither in plant nor insect CRYs. Intense illumination disassembles the dimer into monomers. Structural and functional data suggest a mechanistic coupling between the light-sensing flavin adenine dinucleotide chromophore, the dimer interface, and the C-terminal tail helix, with a likely involvement of the phosphate binding loop. Taken together, our work establishes PdLCry as a CRY protein with inverse photo-oligomerization with respect to plant CRYs, and provides molecular insights into how this protein might help discriminating the different light intensities associated with sunlight and moonlight.
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Registered trials
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.