Lee, In-Gyun Lee, Bong-Jin 2024-01-19T10:03:43Z 2024-01-19T10:03:43Z 2023-03-16 2023-02 2076-3921 https://pubs.kist.re.kr/handle/201004/114012 Aurora kinase A (AURKA), which is a member of serine/threonine kinase family, plays a critical role in regulating mitosis. AURKA has drawn much attention as its dysregulation is critically associated with various cancers, leading to the development of AURKA inhibitors, a new class of anticancer drugs. As the spatiotemporal activity of AURKA critically depends on diverse intra- and inter-molecular factors, including its interaction with various protein cofactors and post-translational modifications, each of these pathways should be exploited for the development of a novel class of AURKA inhibitors other than ATP-competitive inhibitors. Several lines of evidence have recently shown that redox-active molecules can modify the cysteine residues located on the kinase domain of AURKA, thereby regulating its activity. In this review, we present the current understanding of how oxidative modifications of cysteine residues of AURKA, induced by redox-active molecules, structurally and functionally regulate AURKA and discuss their implications in the discovery of novel AURKA inhibitors. English MDPI AG Aurora Kinase A Regulation by Cysteine Oxidative Modification Article 10.3390/antiox12020531 1 Antioxidants, v.12, no.2 Antioxidants 12 2 Y scie scopus 000938281300001 2-s2.0-85149196938 Biochemistry & Molecular Biology Chemistry, Medicinal Food Science & Technology Biochemistry & Molecular Biology Pharmacology & Pharmacy Food Science & Technology Review SMALL-MOLECULE INHIBITORS PROTEIN PHOSPHATASE 2A REACTIVE CYSTEINE A KINASE N-MYC REDOX REGULATION STRUCTURAL BASIS PK(A) VALUES ACTIVATION PHOSPHORYLATION Aurora kinase A (AURKA) redox-active molecules cysteine oxidative modification