ArticleNature communications2021
Global profiling of distinct cysteine redox forms reveals wide-ranging redox regulation in C. elegans.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 109 citations in OpenAlex.
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- Defining and refining the cysteine redoxome through sulfur chemical biology.Nature chemical biology · 2026Review
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- ROMO1 overexpression protects the mitochondrial cysteinome from oxidations in aging.Nature communications · 2025Article
- More questions than answers: insights into potential cysteine-rich receptor-like kinases redox signalling in Arabidopsis.The Plant journal : for cell and molecular biology · 2025Review
- Low-input redoxomics facilitates global identification of metabolic regulators of oxidative stress in the gut.Signal transduction and targeted therapy · 2025Article
- Activity-Based Protein Profiling for Functional Cysteines and Protein Target Identification.Methods in molecular biology (Clifton, N.J.) · 2025Article
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- Regulation of Caenorhabditis elegans HLH-30 subcellular localization dynamics: Evidence for a redox-dependent mechanism.Free radical biology & medicine · 2024Article
- Histone oxidation as a new mechanism of metabolic control over gene expression.Trends in genetics : TIG · 2024Review
- Superoxide-responsive quinone methide precursors (QMP-SOs) to study superoxide biology by proximity labeling and chemoproteomics.RSC chemical biology · 2024Article
- ROS-mediated regulation of β2AR function: Does oxidation play a meaningful role towards β2-agonist tachyphylaxis in airway obstructive diseases?Biochemical pharmacology · 2024Review
- Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions.Life science alliance · 2024Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Post-translational changes in the redox state of cysteine residues can rapidly and reversibly alter protein functions, thereby modulating biological processes. The nematode C. elegans is an ideal model organism for studying cysteine-mediated redox signaling at a network level. Here we present a comprehensive, quantitative, and site-specific profile of the intrinsic reactivity of the cysteinome in wild-type C. elegans. We also describe a global characterization of the C. elegans redoxome in which we measured changes in three major cysteine redox forms after H
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