Fatty acid synthase mediates EGFR palmitoylation in EGFR mutated non-small cell lung cancer

• Main Authors: Ali, A, Levantini, E, Teo, J.T, Goggi, J, Clohessy, J.G, Wu, C.S, Chen, L, Yang, H, Krishnan, I, Kocher, O, Zhang, J, Soo, R.A, Bhakoo, K, Chin, T.M, Tenen, D.G
• Other Authors: CANCER SCIENCE INSTITUTE OF SINGAPORE
• Format: Article
• Published: 2020
• Subjects: epidermal growth factor receptor; fatty acid synthase; gefitinib; protein tyrosine kinase inhibitor; tetrahydrolipstatin; EGFR protein, human; fatty acid; protein kinase B; protein kinase inhibitor; animal cell; animal experiment; animal model; antineoplastic activity; Article; cancer inhibition; cell cycle; cell proliferation; cell viability; controlled study; enzyme inhibition; fatty acid metabolism; female; human; human cell; in vivo study; male; mouse; non small cell lung cancer; nonhuman; palmitoylation; priority journal; signal transduction; transgenic mouse; tumor resistance; tumor volume; tumor xenograft; ubiquitination; animal; antagonists and inhibitors; biological model; drug effect; drug resistance; drug screening; gene expression regulation; gene silencing; genetics; lipoylation; lung tumor; metabolism; mutation; pathology; tumor cell line; upregulation; Animals; Carcinoma, Non-Small-Cell Lung; Cell Line, Tumor; Cell Proliferation; Drug Resistance, Neoplasm; ErbB Receptors; Fatty Acid Synthases; Fatty Acids; Gene Expression Regulation, Neoplastic; Gene Silencing; Lipoylation; Lung Neoplasms; Male; Mice, Transgenic; Models, Biological; Mutation; Orlistat; Protein Kinase Inhibitors; Proto-Oncogene Proteins c-akt; Signal Transduction; Ubiquitination; Up-Regulation; Xenograft Model Antitumor Assays
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/173737
• Institution: National University of Singapore

10.15252/emmm.201708313