ArticleRedox biology2019
Monitoring structural modulation of redox-sensitive proteins in cells with MS-CETSA.
Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Article
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- Unresolved questions regarding cellular cysteine sources and their possible relationships to ferroptosis.Advances in cancer research · 2024Review
- Adverse effect of Tamarindus indica and tamoxifen combination on redox balance and genotoxicity of breast cancer cell.Journal, genetic engineering & biotechnology · 2023Article
- Redox signaling in impaired cascades of wound healing: promising approach.Molecular biology reports · 2023Review
- Rewiring of the protein-protein-metabolite interactome during the diauxic shift in yeast.Cellular and molecular life sciences : CMLS · 2022Article
- Thiol-disulphide independent in-cell trapping for the identification of peroxiredoxin 2 interactors.Redox biology · 2021Article
- Chemoproteomics for Plasmodium Parasite Drug Target Discovery.Chembiochem : a European journal of chemical biology · 2021Review
- Celastrol exerts a neuroprotective effect by directly binding to HMGB1 protein in cerebral ischemia-reperfusion.Journal of neuroinflammation · 2021Article
- Characterization of the Heat-Stable Proteome during Seed Germination in Arabidopsis with Special Focus on LEA Proteins.International journal of molecular sciences · 2021Article
- Mutant p53-reactivating compound APR-246 synergizes with asparaginase in inducing growth suppression in acute lymphoblastic leukemia cells.Cell death & disease · 2021Article
- Prdx1 Interacts with ASK1 upon Exposure to HAntioxidants (Basel, Switzerland) · 2021Article
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- The right tools for the job: the central role for next generation chemical probes and chemistry-based target deconvolution methods in phenotypic drug discovery.RSC medicinal chemistry · 2021Review
- System-wide identification and prioritization of enzyme substrates by thermal analysis.Nature communications · 2021Article
- Mutant thermal proteome profiling for characterization of missense protein variants and their associated phenotypes within the proteome.The Journal of biological chemistry · 2020Article
- Cellular thermal shift assay for the identification of drug-target interactions in the Plasmodium falciparum proteome.Nature protocols · 2020Article
- Comprehensive chemical proteomics for target deconvolution of the redox active drug auranofin.Redox biology · 2020Article
- Thermal proteome profiling for interrogating protein interactions.Molecular systems biology · 2020Review
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Authors and funding
13 authors at 6 institutions in 3 countries.
Funding
Abstract
Reactive oxygen species (ROS) induce different cellular stress responses but can also mediate cellular signaling. Augmented levels of ROS are associated with aging, cancer as well as various metabolic and neurological disorders. ROS can also affect the efficacy and adverse effects of drugs. Although proteins are key mediators of most ROS effects, direct studies of ROS-modulated-protein function in the cellular context are very challenging. Therefore the understanding of specific roles of different proteins in cellular ROS responses is still relatively rudimentary. In the present work we show that Mass Spectrometry-Cellular Thermal Shift Assay (MS-CETSA) can directly monitor ROS and redox modulations of protein structure at the proteome level. By altering ROS levels in cultured human hepatocellular carcinoma cell lysates and intact cells, we detected CETSA responses in many proteins known to be redox sensitive, and also revealed novel candidate ROS sensitive proteins. Studies in intact cells treated with hydrogen peroxide and sulfasalazine, a ROS modulating drug, identified not only proteins that are directly modified, but also proteins reporting on downstream cellular effects. Comprehensive changes are seen on rate-limiting proteins regulating key cellular processes, including known redox control systems, protein degradation, epigenetic control and protein translational processes. Interestingly, concerted shifts on ATP-binding proteins revealed redox-induced modulation of ATP levels, which likely control many cellular processes. Collectively, these studies establish CETSA as a novel method for cellular studies of redox modulations of proteins, which implicated in a wide range of processes and for the discovery of CETSA-based biomarkers reporting on the efficacy as well as adverse effects of drugs.
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