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- W3048346310 endingPage "1789" @default.
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- W3048346310 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 signaling networks, such as phosphorylation, methylation and ubiquitylation." @default.
- W3048346310 created "2020-08-13" @default.
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- W3048346310 date "2020-11-01" @default.
- W3048346310 modified "2023-10-06" @default.
- W3048346310 title "Asparagine Hydroxylation is a Reversible Post-translational Modification" @default.
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- W3048346310 doi "https://doi.org/10.1074/mcp.ra120.002189" @default.
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