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SIRT1 was originally identified as a histone deacetylase [ 55, 56], leading to large changes in overall gene expression, but SIRT1 also has been found to deacetylate a number of other protein targets [ 57, 58], including transcription factors that may directly affect expression of specific genes.
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HDAC3 has also been found to deacetylate acetyltransferases PCAF and p300/CBP and inhibit their function [ 45, 46].
SIRT1 increases survival in response to stress such as DNA damage by deacetylating a number of substrates including pro-apoptotic protein p53.
SIRT1 deacetylates a number of protein substrates, including histones, FOXOs, PGC-1α, and p53, leading to cellular protection.
SIRT1 is the most widely studied sirtuin, which deacetylates a number of substrates such as PGC-1α.
SIRT1 deacetylates a number of cellular proteins including p53, FOXO, PGC-1α, and LXR [ 15- 22].
We examined the capability of SIRT6 to deacetylate a set of five fluorogenic substrates based on p53 and histone H3 sequences.
"We found out a number of things.
The literature suggests that SIRT1 is a NAD+-dependent deacetylase, which has the ability to regulate a number of processes by deacetylating key proteins such as p53 (at K382), Foxo, Ku70 and provoke an inhibitory effect on apoptosis.
I found a number of attractive plays.
However, SIRT1 can deacetylate histones and a number of non-histone substrates.
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