Aurora-A mediated phosphorylation of LDHB promotes glycolysis and tumor progression by relieving the substrate-inhibition effect - Cheng, Aoxing; Zhang, Peng; Wang, Bo; Yang, Dongdong; Duan, Xiaotao; Jiang, Yongliang; Xu, Tian; Jiang, Ya; Shi, Jiahui; Ding, Chengtao; Wu, Gao; Sang, Zhihong; et al. (Nature communications, 2019)
Keywords: 13/1; 14/33; 631/67/2327; 631/67/395; 82/16; 82/58; 82/80; 96/10; Animals; Aurora Kinase A - antagonists & inhibitors; Aurora Kinase A - metabolism; Azepines - pharmacology; Cancer; Cell culture; Cell Line, Tumor; Glycolysis; HEK293 Cells; HeLa Cells; Humanities and Social Sciences; Humans; Intermediates; Isoenzymes - genetics; Isoenzymes - metabolism; Kinases; L-Lactate dehydrogenase; L-Lactate Dehydrogenase - genetics; L-Lactate Dehydrogenase - metabolism; Lactate dehydrogenase; Lactic acid; Lactic Acid - metabolism; Male; Mice, Inbred BALB C; Mice, Nude; multidisciplinary; Mutation; NAD; NADH; Neoplasms - drug therapy; Neoplasms - genetics; Neoplasms - metabolism; Nicotinamide adenine dinucleotide; Phosphorylation; Pyrimidines - pharmacology; Pyruvic acid; Pyruvic Acid - metabolism; Pyruvic Acid - pharmacology; Regeneration; Science; Science (multidisciplinary); Serine; Serine - genetics; Serine - metabolism; Substrate inhibition; Substrate Specificity - drug effects; Tumor Burden - drug effects; Tumors; Xenograft Model Antitumor Assays; Xenografts; Xenotransplantation