ReviewAntioxidants & redox signaling2011
Flavin redox switching of protein functions.
Review in Antioxidants & redox signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
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.
Who cites it
34 citing papers in PubMed, 58 citations in OpenAlex.
- Protein Electrostatics Tune the Singlet-Triplet Energy Gap in Natural and Engineered Phototropin Light-Oxygen-Voltage (LOV) Domains.Journal of the American Chemical Society · 2026Article
- Article
- Quadruple parametric optical mapping to measure cardiac metabolism-excitation-contraction coupling.Communications biology · 2025Article
- Sensing the Reducing Power to Determine the Cell Fate: Flavin Redox-Switches in Signal Transduction.Current microbiology · 2025Review
- Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222.Nucleic acids research · 2025Article
- Insights into the cellular function and mechanism of action of quinone reductase 2 (NQO2).The Biochemical journal · 2025Review
- Adaptive Laboratory Evolution of Flavin Functionality Identifies Dihydrolipoyl Dehydrogenase as One of the Critical Points for the Activity of 7,8-Didemethyl-Riboflavin as a Surrogate for Riboflavin inMolecules (Basel, Switzerland) · 2024Article
- Evolutionary analysis of Quinone Reductases 1 and 2 suggests that NQO2 evolved to function as a pseudoenzyme.Protein science : a publication of the Protein Society · 2024Article
- A c-di-GMP signaling module controls responses to iron in Pseudomonas aeruginosa.Nature communications · 2024Article
- Aging and neuronal death.Aging · 2023Article
- Zika virus remodelled ER membranes contain proviral factors involved in redox and methylation pathways.Nature communications · 2023Article
- Biofilm formation and cell plasticity drive diazotrophy in an anoxygenic phototrophic bacterium.Applied and environmental microbiology · 2023Article
- Redox status of the plant cell determines epigenetic modifications under abiotic stress conditions and during developmental processes.Journal of advanced research · 2022Review
- The Unusual Cosubstrate Specificity of NQO2: Conservation Throughout the Amniotes and Implications for Cellular Function.Frontiers in pharmacology · 2022Article
- The diverse functionality of NQO1 and its roles in redox control.Redox biology · 2021Review
- Modulating Enzyme FunctionFrontiers in molecular biosciences · 2021Article
- Trapping conformational states of a flavin-dependentThe Journal of biological chemistry · 2020Article
- Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019Review
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Redox Modulation of Oligomeric State in Proline Utilization A.Biophysical journal · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Flavin cofactors impart remarkable catalytic diversity to enzymes, enabling them to participate in a broad array of biological processes. The properties of flavins also provide proteins with a versatile redox sensor that can be utilized for converting physiological signals such as cellular metabolism, light, and redox status into a unique functional output. The control of protein functions by the flavin redox state is important for transcriptional regulation, cell signaling pathways, and environmental adaptation. A significant number of proteins that have flavin redox switches are found in the Per-Arnt-Sim (PAS) domain family and include flavoproteins that act as photosensors and respond to changes in cellular redox conditions. Biochemical and structural studies of PAS domain flavoproteins have revealed key insights into how flavin redox changes are propagated to the surface of the protein and translated into a new functional output such as the binding of a target protein in a signaling pathway. Mechanistic details of proteins unrelated to the PAS domain are also emerging and provide novel examples of how the flavin redox state governs protein-membrane interactions in response to appropriate stimuli. Analysis of different flavin switch proteins reveals shared mechanistic themes for the regulation of protein structure and function by flavins.
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What OpenQuestion holds
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.