ReviewAdvances in nutrition (Bethesda, Md.)2016
Stress Response and Adaptation Mediated by Amino Acid Misincorporation during Protein Synthesis.
Review in Advances in nutrition (Bethesda, Md.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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
21 citing papers in PubMed, 36 citations in OpenAlex.
- Adaptive laboratory evolution with ethionine identifies novel genetic determinants for enhanced protein and methionine accumulation in Saccharomyces cerevisiae.Journal of biological engineering · 2026Article
- Ribosome-associated quality control of aberrant protein production during amino acid limitation.bioRxiv : the preprint server for biology · 2026Article
- Antioxidant evolution of fibrinogen: a crucial role of methionines.Biophysical reviews · 2025Review
- Connecting tRNA Charging and Decoding through the Axis of Nucleotide Modifications at Position 37.Journal of molecular biology · 2025Review
- A narrow range of transcript-error rates across the Tree of Life.Science advances · 2025Article
- Natural human tRNARNA (New York, N.Y.) · 2025Article
- The central role of translation elongation in response to stress.Biochemical Society transactions · 2023Article
- Global translational control by the transcriptional repressor TrcR in the filamentous cyanobacterium Anabaena sp. PCC 7120.Communications biology · 2023Article
- Proteogenomics analysis of CUG codon translation in the human pathogen Candida albicans.BMC biology · 2021Article
- Formation and persistence of polyglutamine aggregates in mistranslating cells.Nucleic acids research · 2021Article
- Mitochondrial mistranslation modulated by metabolic stress causes cardiovascular disease and reduced lifespan.Aging cell · 2021Article
- tRNA Biology in the Pathogenesis of Diabetes: Role of Genetic and Environmental Factors.International journal of molecular sciences · 2021Review
- Chemical-Genetic Interactions with the Proline Analog L-Azetidine-2-Carboxylic Acid inG3 (Bethesda, Md.) · 2020Article
- Duplication of leucyl-tRNA synthetase in an archaeal extremophile may play a role in adaptation to variable environmental conditions.The Journal of biological chemistry · 2020Article
- Article
- Modulating Mistranslation Potential of tRNAGenetics · 2019Article
- Methionine in proteins: The Cinderella of the proteinogenic amino acids.Protein science : a publication of the Protein Society · 2019Review
- Methionine in Proteins: It's Not Just for Protein Initiation Anymore.Neurochemical research · 2019Review
- Myristoylated methionine sulfoxide reductase A is a late endosomal protein.The Journal of biological chemistry · 2018Article
- Codon misreading tRNAs promote tumor growth in mice.RNA biology · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Translation of genetic information into functional proteins is critical for all cellular life. Accurate protein synthesis relies on proper aminoacylation of transfer RNAs (tRNAs) and decoding of mRNAs by the ribosome with the use of aminoacyl-tRNAs. Mistranslation can lead to pathologic consequences. All cells contain elaborate quality control mechanisms in translation, although translational fidelity may be regulated by various factors such as nutrient limitation or reactive oxygen species. Translation fidelity is maintained via the accuracy of tRNA aminoacylation by the aminoacyl-tRNA synthetases and matching of the mRNA codon with the tRNA anticodon by the ribosome. Stringent substrate discrimination and proofreading are critical in aminoacylating tRNAs with their cognate amino acid to maintain high accuracy of translation. Although the composition of the cellular proteome generally adheres to the genetic code, accumulating evidence indicates that cells can also deliberately mistranslate; they synthesize mutant proteins that deviate from the genetic code in response to stress or environmental changes. Mistranslation with tRNA charged with noncognate amino acids can expand the proteome to enhance stress response and help adaptation. Here, we review current knowledge on mistranslation through tRNA misacylation and describe advances in our understanding of translational control in the regulation of stress response and human diseases.
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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.