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• W3013325882 abstract "Abstract Amino acid hydroxylation is a common post-translational modification, which generally regulates protein interactions or adds a functional group that can be further modified. Such hydroxylation is currently considered irreversible, necessitating the degradation and re-synthesis of the entire protein to reset the modification. Here we present evidence that the cellular machinery can reverse FIH-mediated asparagine hydroxylation on intact proteins. These data suggest that asparagine hydroxylation is a flexible and dynamic post-translational modification akin to modifications involved in regulating signalling networks, such as phosphorylation, methylation and ubiquitylation." @default.
• W3013325882 created "2020-04-03" @default.
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• W3013325882 date "2020-03-25" @default.
• W3013325882 modified "2023-10-01" @default.
• W3013325882 title "Asparagine hydroxylation is likely to be a reversible post-translational modification" @default.
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• W3013325882 doi "https://doi.org/10.1101/2020.03.22.002436" @default.
• W3013325882 hasPublicationYear "2020" @default.
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