ArticleFree radical biology & medicine2013
Glutathiolated Ras: characterization and implications for Ras activation.
Article in Free radical biology & medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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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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
20 citing papers in PubMed, 35 citations in OpenAlex.
- ARHGEF7 S-glutathionylation promotes cancer cell migration through Rac1 activation.bioRxiv : the preprint server for biology · 2026Article
- Oncogenic mutant KRAS inhibition through oxidation at cysteine 118.Molecular oncology · 2025Article
- Histone oxidation as a new mechanism of metabolic control over gene expression.Trends in genetics : TIG · 2024Review
- K128 ubiquitination constrains RAS activity by expanding its binding interface with GAP proteins.The EMBO journal · 2024Article
- Regulation of Ras Signaling by S-Nitrosylation.Antioxidants (Basel, Switzerland) · 2023Review
- The ribosome assembly GTPase EngA is involved in redox signaling in cyanobacteria.Frontiers in microbiology · 2023Article
- The molecular basis for immune dysregulation by the hyperactivated E62K mutant of the GTPase RAC2.The Journal of biological chemistry · 2020Article
- Biology, pathology, and therapeutic targeting of RAS.Advances in cancer research · 2020Review
- Structural basis of the atypical activation mechanism of KRASThe Journal of biological chemistry · 2019Article
- Cysteine-based regulation of redox-sensitive Ras small GTPases.Redox biology · 2019Review
- Molecular Mechanisms of Nitric Oxide in Cancer Progression, Signal Transduction, and Metabolism.Antioxidants & redox signaling · 2019Review
- Precise characterization of KRAS4b proteoforms in human colorectal cells and tumors reveals mutation/modification cross-talk.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Redox regulation of Rac1 by thiol oxidation.Free radical biology & medicine · 2015Article
- Article
- Decreased tumorigenesis in mice with a Kras point mutation at C118.Nature communications · 2014Article
- Biophysical and proteomic characterization strategies for cysteine modifications in Ras GTPases.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Rho GTPases, oxidation, and cell redox control.Small GTPases · 2014Review
- Causes and consequences of cysteine S-glutathionylation.The Journal of biological chemistry · 2013Review
- S-glutathionylation in monocyte and macrophage (dys)function.International journal of molecular sciences · 2013Review
- Site-specific monoubiquitination activates Ras by impeding GTPase-activating protein function.Small GTPasesArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ras GTPases cycle between active GTP-bound and inactive GDP-bound forms to regulate a multitude of cellular processes, including cell growth, differentiation, and apoptosis. The activation state of Ras is regulated by protein modulatory agents that accelerate the slow intrinsic rates of GDP dissociation and GTP hydrolysis. Similar to the action of guanine-nucleotide exchange factors, the rate of GDP dissociation can be greatly enhanced by the reaction of Ras with small-molecule redox agents, such as nitrogen dioxide, which can promote Ras activation. Nitrogen dioxide is an autoxidation product of nitric oxide and can react with an accessible cysteine of Ras to cause oxidation of the bound guanine nucleotide to facilitate Ras guanine nucleotide dissociation. Glutathione has also been reported to modify Ras and alter its activity. To elucidate the mechanism by which glutathione alters Ras guanine nucleotide binding properties, we performed NMR, top-down and bottom-up mass spectrometry, and biochemical analyses of glutathiolated Ras. We determined that treatment of H-Ras, lacking the nonconserved hypervariable region, with oxidized glutathione results in glutathiolation specifically at cysteine 118. However, glutathiolation does not alter Ras structure or biochemical properties. Rather, changes in guanine nucleotide binding properties and Ras activity occur upon exposure of Ras to free radicals, presumably through the generation of a cysteine 118 thiyl radical. Interestingly, Ras glutathiolation protects Ras from further free radical-mediated activation events. Therefore, glutathiolation does not affect Ras activity unless Ras is modified by glutathione through a radical-mediated mechanism.
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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.