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- W2044897645 endingPage "e963452" @default.
- W2044897645 startingPage "e963452" @default.
- W2044897645 abstract "Acetylation of protein lysine residues is a reversible and dynamic process that is controlled by histone acetyltransferases (HATs) and deacetylases (HDACs and SIRTs). Recent studies have revealed that acetylation modulates not only nuclear proteins but also cytoplasmic or mitochondrial proteins, including many metabolic enzymes. In tumors, cellular metabolism is reprogrammed to provide intermediates for biosynthesis such as nucleotides, fatty acids, and amino acids, and thereby favor the rapid proliferation of cancer cells and tumor development. An increasing number of investigations have indicated that acetylation plays an important role in tumor metabolism. Here, we summarize the substrates that are modified by acetylation, especially oncogenes, tumor suppressor genes, and enzymes that are implicated in tumor metabolism." @default.
- W2044897645 created "2016-06-24" @default.
- W2044897645 creator A5013530010 @default.
- W2044897645 creator A5047200703 @default.
- W2044897645 creator A5048529643 @default.
- W2044897645 creator A5086236254 @default.
- W2044897645 date "2014-09-15" @default.
- W2044897645 modified "2023-10-16" @default.
- W2044897645 title "Impact of acetylation on tumor metabolism" @default.
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