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N-acetyltransferase 10 refers to a family of highly conserved enzymes with two prominent, though distinct, human members: NAA10 and NAT10. NAA10 is the catalytic subunit of the NatA complex, responsible for the N-terminal acetylation of 40–50% of the human proteome, and implicated in processes such as cell cycle regulation, apoptosis, DNA damage response, and cancer progression[1][4][9][10]. NAT10 is a nucleolar GCN5-related acetyltransferase, functioning as the primary “writer” of N4-acetylcytidine (ac4C) modifications on multiple RNAs and also acetylates proteins such as p53 and α-tubulin[5][6][7][8]. Both enzymes are implicated in tumorigenesis, developmental syndromes, and other major diseases. While drug inhibitors are under investigation, no therapies are yet approved. NAT10 and NAA10 are distinct in structure and substrate preference, but both are essential for cellular homeostasis and are emerging as high-value targets in cancer and disease therapy[2][3][8][9]. Note: Be aware of nomenclature ambiguity—NAA10 and NAT10 are separate enzymes that have both been referred to as "N-acetyltransferase 10" in literature. Ensure future structured extraction clarifies which target (NAA10 vs. NAT10) is of interest in the specific drug discovery context.
Acetylation inhibition: blocks protein or RNA acetylation, impacting protein stability, RNA function, cell proliferation, and DNA repair. Remodeling chromatin or modulating RNA modification to alter gene expression and protein synthesis.
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