ArticleCommunications biology2021
Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 48 citations in OpenAlex.
- The Human Circadian Clock Protein Cryptochrome-1 Responds to Photochemistry by Conformational Changes.Journal of the American Chemical Society · 2026Article
- The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026Article
- Chemical biology approaches to study and target circadian clocks and their components.FEBS letters · 2026Review
- Sortase-mediated ligation of cytochrome c peroxidase and cytochrome c highlights the roles of dynamics and conformational specificity for interprotein electron transfer.Journal of inorganic biochemistry · 2026Article
- Structure of European robin cryptochrome 1 reveals a role in circadian rhythms, not magnetoreception.iScience · 2025Article
- Cryptochrome interaction networks across different tissues in Drosophila melanogaster.Biology direct · 2025Article
- The ionic and protonation states of flavin control the activation and recovery of Drosophila cryptochrome.Communications chemistry · 2025Article
- Linear free energy relationship between reduction potential and photoreduction rate: studies on Drosophila cryptochrome.The FEBS journal · 2025Article
- Flavoproteins as native and genetically encoded spin probes for in cell ESR spectroscopy.Nature communications · 2025Article
- Mitochondrial inhibitors reveal roles of specific respiratory chain complexes in CRY-dependent degradation of TIM.Scientific reports · 2024Article
- Article
- Dissecting the Interaction between Cryptochrome and Timeless Reveals Underpinnings of Light-Dependent Recognition.Biochemistry · 2024Article
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- A marine cryptochrome with an inverse photo-oligomerization mechanism.Nature communications · 2023Article
- Dimerization of European Robin Cryptochrome 4a.The journal of physical chemistry. B · 2023Article
- Article
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy.Bioconjugate chemistry · 2023Article
- The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments.Nature communications · 2023Article
- Direct experimental observation of blue-light-induced conformational change and intermolecular interactions of cryptochrome.Communications biology · 2022Article
- Room-temperature serial synchrotron crystallography of Drosophila cryptochrome.Acta crystallographica. Section D, Structural biology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Light-induction of an anionic semiquinone (SQ) flavin radical in Drosophila cryptochrome (dCRY) alters the dCRY conformation to promote binding and degradation of the circadian clock protein Timeless (TIM). Specific peptide ligation with sortase A attaches a nitroxide spin-probe to the dCRY C-terminal tail (CTT) while avoiding deleterious side reactions. Pulse dipolar electron-spin resonance spectroscopy from the CTT nitroxide to the SQ shows that flavin photoreduction shifts the CTT ~1 nm and increases its motion, without causing full displacement from the protein. dCRY engineered to form the neutral SQ serves as a dark-state proxy to reveal that the CTT remains docked when the flavin ring is reduced but uncharged. Substitutions of flavin-proximal His378 promote CTT undocking in the dark or diminish undocking in the light, consistent with molecular dynamics simulations and TIM degradation activity. The His378 variants inform on recognition motifs for dCRY cellular turnover and strategies for developing optogenetic tools.
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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 OpenQuestion graph.