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- W2192299058 abstract "Protein prenylation is a posttranslational modification catalyzed by prenyltransferases involving the attachment of farnesyl or geranylgeranyl groups to residues near the C-termini of proteins. This irreversible covalent modification is important for membrane localization and proper signal transduction. Here, the use of isoprenoid analogues for studying prenylated proteins is reviewed. First, experiments with analogues containing small fluorophores that are alternative substrates for prenyltransferases are described. Those analogues have been useful for quantifying binding affinity and for the production of fluorescently labeled proteins. Next, the use of analogues that incorporate biotin, bioorthogonal groups or antigenic moieties is described. Such probes have been particularly useful for identifying proteins that are naturally prenylated within mammalian cells. Overall, the use of isoprenoid analogues has contributed significantly to the understanding of protein prenlation." @default.
- W2192299058 created "2016-06-24" @default.
- W2192299058 creator A5004120095 @default.
- W2192299058 creator A5048332389 @default.
- W2192299058 date "2016-02-01" @default.
- W2192299058 modified "2023-10-14" @default.
- W2192299058 title "Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications" @default.
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- W2192299058 doi "https://doi.org/10.1016/j.bioorg.2015.12.003" @default.
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