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- W2971134501 endingPage "593" @default.
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- W2971134501 abstract "Here we highlight the role of epitranscriptomic systems in post-transcriptional regulation, with a specific focus on RNA modifying writers required for the incorporation of the 21st amino acid selenocysteine during translation, and the pathologies linked to epitranscriptomic and selenoprotein defects. Epitranscriptomic marks in the form of enzyme-catalyzed modifications to RNA have been shown to be important signals regulating translation, with defects linked to altered development, intellectual impairment, and cancer. Modifications to rRNA, mRNA and tRNA can affect their structure and function, while the levels of these dynamic tRNA-specific epitranscriptomic marks are stress-regulated to control translation. The tRNA for selenocysteine contains five distinct epitranscriptomic marks and the ALKBH8 writer for the wobble uridine (U) has been shown to be vital for the translation of the glutathione peroxidase (GPX) and thioredoxin reductase (TRXR) family of selenoproteins. The reactive oxygen species (ROS) detoxifying selenocysteine containing proteins are a prime examples of how specialized translation can be regulated by specific tRNA modifications working in conjunction with distinct codon usage patterns, RNA binding proteins and specific 3’ untranslated region (UTR) signals. We highlight the important role of selenoproteins in detoxifying ROS and provide details on how epitranscriptomic marks and selenoproteins can play key roles in and maintaining mitochondrial function and preventing disease." @default.
- W2971134501 created "2019-09-05" @default.
- W2971134501 creator A5035478404 @default.
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- W2971134501 creator A5082344202 @default.
- W2971134501 creator A5082562666 @default.
- W2971134501 creator A5084886148 @default.
- W2971134501 date "2019-11-01" @default.
- W2971134501 modified "2023-10-16" @default.
- W2971134501 title "Epitranscriptomic systems regulate the translation of reactive oxygen species detoxifying and disease linked selenoproteins" @default.
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