ReviewFree radical biology & medicine2015
Protein thiyl radical reactions and product formation: a kinetic simulation.
Review in Free radical biology & medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
15 citing papers in PubMed, 51 citations in OpenAlex.
- Oxygen Depletion and the Role of Cellular Antioxidants in FLASH Radiotherapy: Mechanistic Insights from Monte Carlo Radiation-Chemical Modeling.Antioxidants (Basel, Switzerland) · 2025Article
- HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The Chemical Reactivity of Membrane Lipids.Chemical reviews · 2024Review
- Cysteine Is the Only Universally Affected and Disfavored Proteomic Amino Acid under Oxidative Conditions in Animals.Antioxidants (Basel, Switzerland) · 2024Article
- Biomarkers of Postpartum Depression: A Narrative Review.Journal of clinical medicine · 2023Review
- Actions of Thiols, Persulfides, and Polysulfides as Free Radical Scavenging Antioxidants.Antioxidants & redox signaling · 2023Review
- Radical Mediated RapidBiomolecules · 2022Article
- Probing the Role of Cysteine Thiyl Radicals in Biology: Eminently Dangerous, Difficult to Scavenge.Antioxidants (Basel, Switzerland) · 2022Review
- Chemistry and Biochemistry of Sulfur Natural Compounds: Key Intermediates of Metabolism and Redox Biology.Oxidative medicine and cellular longevity · 2020Review
- The teleos of metallo-reduction and metallo-oxidation in eukaryotic iron and copper trafficking.Metallomics : integrated biometal science · 2018Article
- Light-Induced Covalent Buffer Adducts to Histidine in a Model Protein.Pharmaceutical research · 2018Article
- Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria.Redox biology · 2016Review
- Protein oxidation and peroxidation.The Biochemical journal · 2016Review
- Thiyl radicals and induction of protein degradation.Free radical research · 2016Review
- Introduction: What we do and do not know regarding redox processes of thiols in signaling pathways.Free radical biology & medicine · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein thiyl radicals are important intermediates generated in redox processes of thiols and disulfides. Thiyl radicals efficiently react with glutathione and ascorbate, and the common notion is that these reactions serve to eliminate thiyl radicals before they can enter potentially hazardous processes. However, over the past years increasing evidence has been provided for rather efficient intramolecular hydrogen transfer processes of thiyl radicals in proteins and peptides. Based on rate constants published for these processes, we have performed kinetic simulations of protein thiyl radical reactivity. Our simulations suggest that protein thiyl radicals enter intramolecular hydrogen transfer reactions to a significant extent even under physiologic conditions, i.e., in the presence of 30 µM oxygen, 1 mM ascorbate, and 10 mM glutathione. At lower concentrations of ascorbate and glutathione, frequently observed when tissue is exposed to oxidative stress, the extent of irreversible protein thiyl radical-dependent protein modification increases.
Indexed as
Identifiers
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.