ArticleACS chemical biology2019
Genetically Encoded Protein Tyrosine Nitration in Mammalian Cells.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Selecting aminoacyl-tRNA synthetase/tRNA pairs for efficient genetic encoding of noncanonical amino acids into proteins.Nature protocols · 2026Review
- Strategies to Expand the Genetic Code of Mammalian Cells.Chemical reviews · 2025Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Salivary metabolomics in patients with oral lichen planus: a preliminary study based on NMR spectroscopy.Clinical oral investigations · 2024Article
- Functional analysis of protein post-translational modifications using genetic codon expansion.Protein science : a publication of the Protein Society · 2023Review
- Generating EfficientACS chemical biology · 2022Article
- Halogenation of tyrosine perturbs large-scale protein self-organization.Nature communications · 2022Article
- Engineered bacterial host for genetic encoding of physiologically stable protein nitration.Frontiers in molecular biosciences · 2022Article
- Creating a Selective Nanobody Against 3-Nitrotyrosine Containing Proteins.Frontiers in chemistry · 2022Article
- Photosynthetic reaction center variants made via genetic code expansion show Tyr at M210 tunes the initial electron transfer mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Genetic encoding of a highly photostable, long lifetime fluorescent amino acid for imaging in mammalian cells.Chemical science · 2021Article
- Chemogenetic and optogenetic control of post-translational modifications through genetic code expansion.Current opinion in chemical biology · 2021Review
- Synthesis and Evaluation of Novel Ring-Strained Noncanonical Amino Acids for Residue-Specific Bioorthogonal Reactions in Living Cells.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
- Overcoming Near-Cognate Suppression in a Release Factor 1-Deficient Host with an Improved Nitro-Tyrosine tRNA Synthetase.Journal of molecular biology · 2020Article
- Efficient Site-Specific Prokaryotic and Eukaryotic Incorporation of Halotyrosine Amino Acids into Proteins.ACS chemical biology · 2020Article
- The Relationship between the Concentration of Salivary Tyrosine and Antioxidants in Patients with Oral Lichen Planus.Oxidative medicine and cellular longevity · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Tyrosine nitration has served as a major biomarker for oxidative stress and is present in high abundance in over 50 disease pathologies in humans. While data mounts on specific disease pathways from specific sites of tyrosine nitration, the role of these modifications is still largely unclear. Strategies for installing site-specific tyrosine nitration in target proteins in eukaryotic cells, through routes not dependent on oxidative stress, would provide a powerful method to address the consequences of tyrosine nitration. Developed here is a Methanosarcina barkeri aminoacyl-tRNA synthetase/tRNA pair that efficiently incorporates nitrotyrosine site-specifically into proteins in mammalian cells. We demonstrate the utility of this approach to produce nitrated proteins identified in disease conditions by producing site-specific nitroTyr-containing manganese superoxide dismutase and 14-3-3 proteins in eukaryotic cells.
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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.