PT - JOURNAL ARTICLE AU - Yanfang Yang AU - Zijing Xia AU - Xixi Wang AU - Xinyu Zhao AU - Zenghua Sheng AU - Yang Ye AU - Gu He AU - Liangxue Zhou AU - Hongxia Zhu AU - Ningzhi Xu AU - Shufang Liang TI - Small-Molecule Inhibitors Targeting Protein SUMOylation as Novel Anticancer Compounds AID - 10.1124/mol.118.112300 DP - 2018 Aug 01 TA - Molecular Pharmacology PG - 885--894 VI - 94 IP - 2 4099 - http://molpharm.aspetjournals.org/content/94/2/885.short 4100 - http://molpharm.aspetjournals.org/content/94/2/885.full SO - Mol Pharmacol2018 Aug 01; 94 AB - SUMOylation, one of post-translational modifications, is covalently modified on lysine residues of a target protein through an enzymatic cascade reaction similar to protein ubiquitination. Along with identification of many SUMOylated proteins, protein SUMOylation has been proven to regulate multiple biologic activities including transcription, cell cycle, DNA repair, and innate immunity. The dysregulation of protein SUMOylation and deSUMOylation modification is linked with carcinogenesis and tumor progression. The SUMOylation-associated enzymes are usually elevated in various cancers, which function as cancer biomarkers to relate to poor outcomes for patients. Considering the significance of protein SUMOylation in regulating diverse biologic functions in cancer progression, numerous small-molecule inhibitors targeting protein SUMOylation pathway are developed as potentially clinical anticancer therapeutics. Here, we systematically summarize the latest progresses of associations of small ubiquitin-like modifier (SUMO) enzymes with cancers and small-molecular inhibitors against human cancers by targeting SUMOylation enzymes. We also compared the pros and cons of several special anticancer inhibitors targeting SUMO pathway. As more efforts are invested in this field, small-molecule inhibitors targeting the SUMOylation modification pathway are promising for development into novel anticancer drugs.