ArticleNeurotoxicology2021
In vitro inhibition of glutathione-S-transferase by dopamine and its metabolites, 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetic acid.
Article in Neurotoxicology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Oxidative stress and dysregulated long noncoding RNAs in the pathogenesis of Parkinson's disease.Biological research · 2025Review
- Selective dopaminergic neurotoxicity modulated by inherent cell-type specific neurobiology.Neurotoxicology · 2024Review
- Disruption of Dopamine Homeostasis Associated with Alteration of Proteins in Synaptic Vesicles: A Putative Central Mechanism of Parkinson's Disease Pathogenesis.Aging and disease · 2024Review
- Role of Protein Damage Inflicted by Dopamine Metabolites in Parkinson's Disease: Evidence, Tools, and Outlook.Chemical research in toxicology · 2022Review
- Characterization of Catecholaldehyde Adducts with Carnosine and l-Cysteine Reveals Their Potential as Biomarkers of Catecholaminergic Stress.Chemical research in toxicology · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Parkinson's disease is characterized by dopamine dyshomeostasis and oxidative stress. The aldehyde metabolite of dopamine, 3,4-dihydroxyphenylacetaldehyde (DOPAL), has been reported to be cytotoxic and capable of protein modification. Protein modification by DOPAL has been implicated in the pathogenesis of Parkinson's disease, but the complete pathology is unknown. Our findings show that DOPAL modifies glutathione S-transferase (GST), an important enzyme in the antioxidant defense system. DOPAL, dopamine, and the metabolite 3,4-dihydroxyphenylacetic acid (DOPAC), inhibited the activity of GST isolated from N27 dopaminergic cells at an IC
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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.