ReviewChemical research in toxicology2010
Formation, reactivity, and detection of protein sulfenic acids.
Review in Chemical research in toxicology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 108 citations in OpenAlex.
- Use of Human Serum Albumin CysAntioxidants (Basel, Switzerland) · 2026Review
- Radiation-response inFEMS microbes · 2026Article
- The antioxidant and oxidant properties of hydropersulfides (RSSH) and polysulfide species.Redox biology · 2022Article
- Peroxisome-Derived Hydrogen Peroxide Modulates the Sulfenylation Profiles of Key Redox Signaling Proteins in Flp-In T-REx 293 Cells.Frontiers in cell and developmental biology · 2022Article
- PRDX4 and Its Roles in Various Cancers.Technology in cancer research & treatment · 2019Review
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- De Novo Design of an Allosteric Metalloprotein Assembly with Strained Disulfide Bonds.Journal of the American Chemical Society · 2016Article
- Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.Nature communications · 2016Article
- Formation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative Stress.The Journal of biological chemistry · 2016Article
- Redox homeostasis, T cells and kidney diseases: three faces in the dark.Clinical kidney journal · 2016Article
- Protein Sulfenylation: A Novel Readout of Environmental Oxidant Stress.Chemical research in toxicology · 2015Article
- Global, in situ, site-specific analysis of protein S-sulfenylation.Nature protocols · 2015Article
- Oxidation as an important factor of protein damage: Implications for Maillard reaction.Journal of biosciences · 2015Review
- Reactive oxygen and nitrogen species in steatotic hepatocytes: a molecular perspective on the pathophysiology of ischemia-reperfusion injury in the fatty liver.Antioxidants & redox signaling · 2014Review
- Thiol-based redox switches.Biochimica et biophysica acta · 2014Review
- Controlled free radical attack in the apoplast: a hypothesis for roles of O, N and S species in regulatory and polysaccharide cleavage events during rapid abscission by Azolla.Plant science : an international journal of experimental plant biology · 2014Review
- Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Biochemistry · 2014Article
- Chemical biology approaches to study protein cysteine sulfenylation.Biopolymers · 2014Review
- Positive oxidative stress in aging and aging-related disease tolerance.Redox biology · 2014Review
- Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling.Antioxidants & redox signaling · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
It has become clear in recent decades that the post-translational modification of protein cysteine residues is a crucial regulatory event in biology. Evidence supports the reversible oxidation of cysteine thiol groups as a mechanism of redox-based signal transduction, while the accumulation of proteins with irreversible thiol oxidations is a hallmark of stress-induced cellular damage. The initial formation of cysteine-sulfenic acid (SOH) derivatives, along with the reactive properties of this functional group, serves as a crossroads whereby the local redox environment may dictate the progression of either regulatory or pathological outcomes. Protein-SOH are established as transient intermediates in the formation of more stable cysteine oxidation products both under basal conditions and in response to several redox-active extrinsic compounds. This review details both direct and multistep chemical routes proposed to generate protein-SOH, the spectrum of secondary reactions that may follow their initial formation and the arsenal of experimental tools available for their detection. Pioneering studies that have provided a framework for our current understanding of protein-SOH as well as state-of-the-art proteomic strategies designed for global assessments of this post-translational modification are highlighted.
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What OpenQuestion holds
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.