ArticleNature chemical biology2025
Quantitative chemoproteomics reveals dopamine's protective modification of Tau.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
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Who cites it
8 citing papers in PubMed.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
- The Association Between Alzheimer's Disease-Related Biomarkers And Parkinson's Disease Based On Single-Cell Sequencing Analysis Combined With Mendelian Randomization.Journal of molecular neuroscience : MN · 2026Article
- Histaminylation alters collagen matrix mechanics and attenuates cardiac fibrosis post-myocardial infarction via mechanotransduction signaling axis.Signal transduction and targeted therapy · 2026Article
- Monoaminylation in Human Health and Disease: State of the Field, Challenges, and Emerging Directions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Global profiling of arginine reactivity and ligandability in the human proteome.Nature chemistry · 2026Article
- From seeds to symptoms: the molecular landscape of tau seeding in Alzheimer's disease.Frontiers in neuroscience · 2026Review
- Reimagining biogenic amine signaling in the brain and beyond.Trends in neurosciences · 2026Review
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Dopamine (DA) is one of the most important neurotransmitters. Its oxidation leads to electrophilic quinone, which covalently modifies nucleophilic residues in proteins, resulting in 'dopamination'. Individual dopaminated proteins have been studied, most of which were functionally damaged by dopamination. Here, we developed a quantitative chemoproteomic strategy to site-specifically measure proteins' dopamination. More than 6,000 dopamination sites were quantified. Half-maximal inhibitory concentration values for 63 hypersensitive sites were measured. Among them, hypersensitive dopamination of two cysteines in microtubule-associated protein Tau was biochemically validated and functionally characterized to prevent Tau's amyloid fibrillation and promote Tau-mediated assembly of microtubules. In addition, endogenous dopamination of Tau in mouse brain was detected through targeted mass spectrometry analysis. Our study not only provides a global portrait of dopamination but also discovers a protective role of DA in regulating the function of Tau, which will enhance our understanding of the physiological and pathological functions of DA in human brain.
Indexed as
Identifiers
39979588What 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.