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Updated: Mar 20, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
Sirtuin1 (SIRT1) in the Acetylation of Downstream Target Proteins
Ana R Gomes1, Jay Sze Yong1, Khai Cheng Kiew1
1Department of Surgery and Cancer, Imperial College London, Hammersmith Hospital Campus, London Du Cane Road, London, W12 0NN, UK.
Abstract:
Acetylation has been shown to be an important posttranslational modification (PTM) of both histone and nonhistone proteins with particular implications in cell signaling and transcriptional regulation of gene expression. Many studies have already demonstrated that SIRT1 is able to deacetylate histones and lead to gene silencing. It can also regulate the function of tumor suppressors including FOXO proteins and p53 by deacetylation. Here, we describe three experimental approaches for studying the modulation of the acetylation status of some of the known downstream targets of SIRT1.
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