ArticleBioorganic & medicinal chemistry2010
Inactivation of protein tyrosine phosphatases by oltipraz and other cancer chemopreventive 1,2-dithiole-3-thiones.
Article in Bioorganic & medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- ECM1 expression in chronic liver disease: Regulation by EGF/STAT1 and IFNγ/NRF2 signalling.JHEP reports : innovation in hepatology · 2025Article
- Filtering through the role of NRF2 in kidney disease.Archives of pharmacal research · 2020Review
- Covalent inhibition of protein tyrosine phosphatases.Molecular bioSystems · 2017Review
- Anticancer activity and chemoprevention of xenobiotic organosulfurs in preclinical model systems.Oncology discovery · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dithiolethiones upregulate the expression of cancer-preventive proteins via modification of thiol residues in the Keap1-Nrf2 transcription factor complex. In addition to Keap1-Nrf2, dithiolethiones have the potential to modify a variety of cysteine-containing proteins in the cell. Such 'off target' reactions could contribute to either side effects or cancer-preventive efficacy. Evidence is presented here that cancer chemopreventive dithiolethiones inactivate protein tyrosine phosphatases via covalent, but thiol-labile, modification of active site residues. This observation may explain a number of previously reported cellular responses to dithiolethiones.
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Registered trials
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