期刊
CURRENT MEDICINAL CHEMISTRY
卷 28, 期 20, 页码 3892-3912出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929867327666200810135039
关键词
SUMO; cancer; ubiquitin-like; post-translational modifications; natural products; small-molecules; enzyme inhibitors
资金
- NCI NIH HHS [R01 CA213566] Funding Source: Medline
SUMOylation is an important post-translational modification involving the attachment of SUMO polypeptide to target proteins. Dysregulation of SUMOylation pathway is observed in cancer and neurological diseases, with upregulated SUMO enzymes correlated with prognosis and disease progression. Inhibitors of SUMOylation are being actively researched, including natural products, peptidomimetics, and synthetic derivatives identified via virtual screens.
SUMOylation has emerged as an important post-translational modification that involves the covalent attachment of the Small Ubiquitin-like Modifier (SUMO) polypeptide to a lysine residue of a target protein. The enzymatic pathway of SUMOylation is very similar to ubiquitinylation and involves an activating enzyme, a conjugating enzyme, ligases, and deconjugating enzymes. SUMOylation modulates the function of a number of proteins associated with various pathways, and in fact, dysregulation of the SUMOylation pathway is observed in both cancer and neurological diseases. In many cancers, the SUMO enzymes are upregulated, and SUMO levels correlate directly with prognosis and disease progression. As a result, there has been an emphasis on the discovery and development of inhibitors of SUMOylation. In this review, the latest advances in SUMOylation inhibitors are described alongside the methods used to discover small molecule SUMOylation inhibitors, which include natural products, peptidomimetics, as well as synthetic derivatives identified via virtual screens.
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