ReviewAntioxidants & redox signaling2012
Tyrosine modifications in aging.
Review in Antioxidants & redox signaling, 2012. 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.
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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.
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Who cites it
34 citing papers in PubMed, 77 citations in OpenAlex.
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- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- Nitric Oxide in Plant Functioning: Metabolism, Signaling, and Responses to Infestation with Ecdysozoa Parasites.Biology · 2023Review
- Identification and validation of aging-related gene signatures and their immune landscape in diabetic nephropathy.Frontiers in medicine · 2023Article
- Crosstalk of ferroptosis and oxidative stress in infectious diseases.Frontiers in molecular biosciences · 2023Review
- Disease-Gene Networks of Skin Pigmentation Disorders and Reconstruction of Protein-Protein Interaction Networks.Bioengineering (Basel, Switzerland) · 2022Article
- Separation and Detection of Tyrosine and Phenylalanine-derived Oxidative Stress Biomarkers Using Microchip Electrophoresis with Electrochemical Detection.Electroanalysis · 2022Article
- Current Insights on Neurodegeneration by the Italian Proteomics Community.Biomedicines · 2022Review
- Halogenation of tyrosine perturbs large-scale protein self-organization.Nature communications · 2022Article
- Plasma Metabolite Profiles Following Consumption of Animal Protein and Soybean-Based Diet in Hypercholesterolemic Postmenopausal Women.Metabolites · 2022Article
- Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress.Redox biology · 2021Article
- Higher susceptibility to heme oxidation and lower protein stability of the rare αBiochemical pharmacology · 2021Article
- Influence of spatial structure on protein damage susceptibility: a bioinformatics approach.Scientific reports · 2021Article
- Oxidative cross-linking of fibronectin confers protease resistance and inhibits cellular migration.Science signaling · 2020Article
- Efficient Site-Specific Prokaryotic and Eukaryotic Incorporation of Halotyrosine Amino Acids into Proteins.ACS chemical biology · 2020Article
- Design of a Protein Motif Responsive to Tyrosine Nitration and an Encoded Turn-Off Sensor of Tyrosine Nitration.Biochemistry · 2019Article
- Age-Dependent Oxidative Stress Elevates Arginase 1 and Uncoupled Nitric Oxide Synthesis in Skeletal Muscle of Aged Mice.Oxidative medicine and cellular longevity · 2019Article
- A longitudinal study of neurotrophic, oxidative, and inflammatory markers in first-onset depression in midlife women.European archives of psychiatry and clinical neuroscience · 2018Article
- Biological Activities, Health Benefits, and Therapeutic Properties of Avenanthramides: From Skin Protection to Prevention and Treatment of Cerebrovascular Diseases.Oxidative medicine and cellular longevity · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
significanceThe understanding of physiological and pathological processes involving protein oxidation, particularly under conditions of aging and oxidative stress, can be aided by proteomic identification of proteins that accumulate oxidative post-translational modifications only if these detected modifications are connected to functional consequences. The modification of tyrosine (Tyr) residues can elicit significant changes in protein structure and function, which, in some cases, may contribute to biological aging and age-related pathologies, such as atherosclerosis, neurodegeneration, and cataracts. RECENT ADVANCES: Studies characterizing proteins in which Tyr has been modified to 3-nitrotyrosine, 3,4-dihydroxyphenylalanine, 3,3'-dityrosine and other cross-links, or 3-chlorotyrosine are reviewed, with an emphasis on structural and functional consequences. CRITICAL ISSUES: Distinguishing between inconsequential modifications and functionally significant ones requires careful biochemical and biophysical analysis of target proteins, as well as innovative methods for isolating the effects of the multiple modifications that often occur under oxidizing conditions. FUTURE DIRECTIONS: The labor-intensive task of isolating and characterizing individual modified proteins must continue, especially given the expanding list of known modifications. Emerging approaches, such as genetic and metabolic incorporation of unnatural amino acids, hold promise for additional focused studies of this kind.
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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.