ReviewBiophysical reviews2014
Thiol redox biochemistry: insights from computer simulations.
Review in Biophysical reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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Who cites it
10 citing papers in PubMed, 42 citations in OpenAlex.
- Discovery of a Potent Triazole-Based Reversible Targeted Covalent Inhibitor of Cruzipain.ACS medicinal chemistry letters · 2025Article
- Analytical Methods for Assessing Thiol Antioxidants in Biological Fluids: A Review.Molecules (Basel, Switzerland) · 2024Review
- Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility.Nature communications · 2023Article
- Probing the Role of Cysteine Thiyl Radicals in Biology: Eminently Dangerous, Difficult to Scavenge.Antioxidants (Basel, Switzerland) · 2022Review
- Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.Antioxidants (Basel, Switzerland) · 2021Review
- 3D interaction homology: Hydropathic interaction environments of serine and cysteine are strikingly different and their roles adapt in membrane proteins.Current research in structural biology · 2021Article
- Reaction Pathway and Selectivity Control of Tetraethyl Thiuram Disulfide Synthesis with NaHCOACS omega · 2020Article
- A dual attack on the peroxide bond. The common principle of peroxidatic cysteine or selenocysteine residues.Redox biology · 2020Article
- Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modifications.International journal of molecular sciences · 2019Review
- Residue Adjacency Matrix Based Feature Engineering for Predicting Cysteine Reactivity in Proteins.Computational and structural biotechnology journal · 2019Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thiol redox chemical reactions play a key role in a variety of physiological processes, mainly due to the presence of low-molecular-weight thiols and cysteine residues in proteins involved in catalysis and regulation. Specifically, the subtle sensitivity of thiol reactivity to the environment makes the use of simulation techniques extremely valuable for obtaining microscopic insights. In this work we review the application of classical and quantum-mechanical atomistic simulation tools to the investigation of selected relevant issues in thiol redox biochemistry, such as investigations on (1) the protonation state of cysteine in protein, (2) two-electron oxidation of thiols by hydroperoxides, chloramines, and hypochlorous acid, (3) mechanistic and kinetics aspects of the de novo formation of disulfide bonds and thiol-disulfide exchange, (4) formation of sulfenamides, (5) formation of nitrosothiols and transnitrosation reactions, and (6) one-electron oxidation pathways.
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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.