ArticlePloS one2010
Purification of reversibly oxidized proteins (PROP) reveals a redox switch controlling p38 MAP kinase activity.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 44 citations in OpenAlex.
- Reactive oxygen species (ROS) in cancer: from redox signaling and metabolic plasticity to therapeutic vulnerabilities.Exploration of targeted anti-tumor therapy · 2026Review
- Cystine/glutamate antiporter xCT controls skeletal muscle glutathione redox, bioenergetics and differentiation.Redox biology · 2024Article
- Structural basis of a redox-dependent conformational switch that regulates the stress kinase p38α.Nature communications · 2023Article
- Hydrogen peroxide-dependent oxidation of ERK2 within its D-recruitment site alters its substrate selection.iScience · 2023Article
- Cysteine modifications (oxPTM) and protein sulphenylation-mediated sulfenome expression in plants: evolutionary conserved signaling networks?Plant signaling & behavior · 2021Article
- Activated Thiol Sepharose-based proteomic approach to quantify reversible protein oxidation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- HThe Journal of biological chemistry · 2018Article
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- Redox Imbalance in the Development of Colorectal Cancer.Journal of Cancer · 2017Review
- Deciphering fact from artifact when using reporter assays to investigate the roles of host factors on L1 retrotransposition.Mobile DNA · 2016Article
- Redox regulation of Rac1 by thiol oxidation.Free radical biology & medicine · 2015Article
- Sulfenome mining in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Redox homeostasis: the linchpin in stem cell self-renewal and differentiation.Cell death & disease · 2013Review
- Systemic redox regulation of cellular information processing.Antioxidants & redox signaling · 2012Article
- Fluorescent coumarin thiols measure biological redox couples.Organic letters · 2012Article
- Proteomic profile of reversible protein oxidation using PROP, purification of reversibly oxidized proteins.PloS one · 2012Article
- Reversible and irreversible protein glutathionylation: biological and clinical aspects.Expert opinion on drug metabolism & toxicology · 2011Review
- Redox regulation of protein kinases.Critical reviews in biochemistry and molecular biologyReview
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Oxidation of cysteine residues of proteins is emerging as an important means of regulation of signal transduction, particularly of protein kinase function. Tools to detect and quantify cysteine oxidation of proteins have been a limiting factor in understanding the role of cysteine oxidation in signal transduction. As an example, the p38 MAP kinase is activated by several stress-related stimuli that are often accompanied by in vitro generation of hydrogen peroxide. We noted that hydrogen peroxide inhibited p38 activity despite paradoxically increasing the activating phosphorylation of p38. To address the possibility that cysteine oxidation may provide a negative regulatory effect on p38 activity, we developed a biochemical assay to detect reversible cysteine oxidation in intact cells. This procedure, PROP, demonstrated in vivo oxidation of p38 in response to hydrogen peroxide and also to the natural inflammatory lipid prostaglandin J2. Mutagenesis of the potential target cysteines showed that oxidation occurred preferentially on residues near the surface of the p38 molecule. Cysteine oxidation thus controls a functional redox switch regulating the intensity or duration of p38 activity that would not be revealed by immunodetection of phosphoprotein commonly interpreted as reflective of p38 activity.
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