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- W4220699331 endingPage "102352" @default.
- W4220699331 startingPage "102352" @default.
- W4220699331 abstract "In living systems, the chemical space and functional repertoire of proteins are dramatically expanded through the post-translational modification (PTM) of various amino acid residues. These modifications frequently trigger unique protein–protein interactions (PPIs) – for example with reader proteins that directly bind the modified amino acid residue – which leads to downstream functional outcomes. The modification of a protein can also perturb its PPI network indirectly, for example, through altering its conformation or subcellular localization. Uncovering the network of unique PTM-triggered PPIs is essential to fully understand the roles of an ever-expanding list of PTMs in our biology. In this review, we discuss established strategies and current challenges associated with this endeavor." @default.
- W4220699331 created "2022-04-03" @default.
- W4220699331 creator A5003864328 @default.
- W4220699331 creator A5020333513 @default.
- W4220699331 creator A5023139047 @default.
- W4220699331 date "2022-06-01" @default.
- W4220699331 modified "2023-10-09" @default.
- W4220699331 title "Uncovering post-translational modification-associated protein–protein interactions" @default.
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- W4220699331 doi "https://doi.org/10.1016/j.sbi.2022.102352" @default.
- W4220699331 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35334254" @default.
- W4220699331 hasPublicationYear "2022" @default.