ReviewFree radical biology & medicine2015
Tripping up Trp: Modification of protein tryptophan residues by reactive oxygen species, modes of detection, and biological consequences.
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 47 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
47 citing papers in PubMed, 144 citations in OpenAlex.
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- A Novel Indigoidine-like NRPS Gene fromAntioxidants (Basel, Switzerland) · 2026Article
- Quantum Information Flow in Microtubule Tryptophan Networks.Entropy (Basel, Switzerland) · 2026Article
- Micellar Solvent Accessibility of Esterified Polyoxyethylene Chains as Crucial Element of Polysorbate Oxidation: A Density Functional Theory, Molecular Dynamics Simulation and Liquid Chromatography/Mass Spectrometry Investigation.Molecular pharmaceutics · 2025Article
- Trp31 Residue of Trx-1 Is Essential for Maintaining Antioxidant Activity and Cellular Redox Defense Against Oxidative Stress.Antioxidants (Basel, Switzerland) · 2025Article
- Reactivity of amino acids and short peptide sequences: identifying bioactive compounds via DFT calculations.Molecular diversity · 2025Article
- Luminescent Lanthanide Infinite Coordination Polymers for Ratiometric Sensing Applications.Molecules (Basel, Switzerland) · 2025Review
- Effect of Boiling Treatment on Linoleic Acid-Induced Oxidation of Myofibrillar Protein in Grass Carp.Foods (Basel, Switzerland) · 2024Article
- Functionality of Reactive Oxygen Species (ROS) in Plants: Toxicity and Control inPlants (Basel, Switzerland) · 2024Review
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- An artificial metalloenzyme that can oxidize water photocatalytically: design, synthesis, and characterization.Chemical science · 2024Article
- Article
- Oxidative Post-translational Protein Modifications upon Ischemia/Reperfusion Injury.Antioxidants (Basel, Switzerland) · 2024Article
- Oxidation of polysorbates - An underestimated degradation pathway?International journal of pharmaceutics: X · 2023Review
- Oxidation Products of Tryptophan and Proline in Adipokinetic Hormones-Artifacts or Post-Translational Modifications?Life (Basel, Switzerland) · 2023Article
- Antioxidant Capacity of Free and Peptide Tryptophan Residues Determined by the ORAC (Oxygen Radical Absorbance Capacity) Assay Is Modulated by Radical-Radical Reactions and Oxidation Products.Foods (Basel, Switzerland) · 2023Article
- Article
- Mitochondrial Dysfunction, Altered Mitochondrial Oxygen, and Energy Metabolism Associated with the Pathogenesis of Schizophrenia.International journal of molecular sciences · 2023Review
- Superoxide Anion Chemistry-Its Role at the Core of the Innate Immunity.International journal of molecular sciences · 2023Review
- LITE-1 mediates behavioral responses to X-rays inFrontiers in neuroscience · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proteins comprise a majority of the dry weight of a cell, rendering them a major target for oxidative modification. Oxidation of proteins can result in significant alterations in protein molecular mass such as breakage of the polypeptide backbone and/or polymerization of monomers into dimers, multimers, and sometimes insoluble aggregates. Protein oxidation can also result in structural changes to amino acid residue side chains, conversions that have only a modest effect on protein size but can have widespread consequences for protein function. There are a wide range of rate constants for amino acid reactivity, with cysteine, methionine, tyrosine, phenylalanine, and tryptophan having the highest rate constants with commonly encountered biological oxidants. Free tryptophan and tryptophan protein residues react at a diffusion-limited rate with hydroxyl radical and also have high rate constants for reactions with singlet oxygen and ozone. Although oxidation of proteins in general and tryptophan residues specifically can have effects detrimental to the health of cells and organisms, some modifications are neutral, whereas others contribute to the function of the protein in question or may act as a signal that damaged proteins need to be replaced. This review provides a brief overview of the chemical mechanisms by which tryptophan residues become oxidized, presents both the strengths and the weaknesses of some of the techniques used to detect these oxidative interactions, and discusses selected examples of the biological consequences of tryptophan oxidation in proteins from animals, plants, and microbes.
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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.