ArticleChemical research in toxicology2022
Chemoproteomic Approach for the Quantitative Identification of Arsenic-Binding Proteins.
Article in Chemical research in toxicology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Arsenic binds to nuclear transport factors and disrupts nucleocytoplasmic transport.Journal of cell science · 2025Article
- Direct binding of arsenicals to nuclear transport factors disrupts nucleocytoplasmic transport.bioRxiv : the preprint server for biology · 2025Article
- Chemoproteomic Approach for Identifying Nuclear Arsenite-Binding Proteins.Chemical research in toxicology · 2025Article
- PRDX1 protects ATM from arsenite-induced proteotoxicity and maintains its stability during DNA damage signaling.Oncotarget · 2025Article
- Defining high confidence targets of differential CpG methylation in response to in utero arsenic exposure and implications for cancer risk.Toxicology and applied pharmacology · 2024Article
- Recent progress in analytical strategies of arsenic-binding proteomes in living systems.Analytical and bioanalytical chemistry · 2023Review
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Authors and funding
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Abstract
Arsenic is a widespread environmental contaminant, and long-term exposure to arsenic in drinking water is known to be associated with the development of many human diseases. Identification of arsenic-binding proteins is important for understanding the mechanisms underlying the toxic effects of arsenic species. Here, we developed a chemoproteomic strategy, relying on the use of a biotin-As(III) probe, stable isotope labeling by amino acids in cell culture, and liquid chromatography-tandem mass spectrometry analysis, to identify quantitatively As(III)-binding proteins. Over 400 proteins were enriched from the lysate of HEK293T cells with streptavidin beads immobilized with the biotin-As(III) probe. Competitive labeling experiments in the presence or absence of
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