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• W2896411544 endingPage "1570.e19" @default.
• W2896411544 startingPage "1562" @default.
• W2896411544 abstract "The post-translational modification (PTM) and signaling molecule poly(ADP-ribose) (PAR) has an impact on diverse biological processes. This PTM is regulated by a series of ADP-ribosyl glycohydrolases (PARG enzymes) that cleave polymers and/or liberate monomers from their protein targets. Existing methods for monitoring these hydrolases rely on detection of the natural substrate, PAR, commonly achieved via radioisotopic labeling. Here we disclose a general substrate for monitoring PARG activity, TFMU-ADPr, which directly reports on total PAR hydrolase activity via release of a fluorophore; this substrate has excellent reactivity, generality (processed by the major PARG enzymes), stability, and usability. A second substrate, TFMU-IDPr, selectively reports on PARG activity only from the enzyme ARH3. Use of these probes in whole-cell lysate experiments has revealed a mechanism by which ARH3 is inhibited by cholera toxin. TFMU-ADPr and TFMU-IDPr are versatile tools for assessing small-molecule inhibitors in vitro and probing the regulation of ADP-ribosyl catabolic enzymes." @default.
• W2896411544 created "2018-10-26" @default.
• W2896411544 creator A5021767059 @default.
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• W2896411544 date "2018-12-01" @default.
• W2896411544 modified "2023-09-30" @default.
• W2896411544 title "Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate" @default.
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• W2896411544 doi "https://doi.org/10.1016/j.chembiol.2018.09.008" @default.
• W2896411544 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6309520" @default.
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• W2896411544 hasPublicationYear "2018" @default.
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