A Systematic Review of Histone Lysine-Specific Demethylase 1 and Its Inhibitors

• Published in: Medicinal research reviews Vol. 35; no. 5; pp. 1032 - 1071
• Main Authors: Zheng, Yi-Chao, Ma, Jinlian, Wang, Zhiru, Li, Jinfeng, Jiang, Bailing, Zhou, Wenjuan, Shi, Xiaojing, Wang, Xixin, Zhao, Wen, Liu, Hong-Min
• Format: Journal Article
• Language: English
• Published: United States Blackwell Publishing Ltd 01.09.2015; Wiley Subscription Services, Inc
• Subjects: Antineoplastic Agents - therapeutic use; Breast Neoplasms - metabolism; Cancer; Catalysis; Cell Nucleus - metabolism; Epigenesis, Genetic; Epithelial-Mesenchymal Transition; Female; Genes; Histone Demethylases - antagonists & inhibitors; Histone Demethylases - chemistry; histone modification; Histones - chemistry; Humans; inhibitors; Inhibitory Concentration 50; LSD1; Molecular Dynamics Simulation; Neoplasm Metastasis; Neoplasms - metabolism; Oxygen - chemistry; Peptides - chemistry; Protein Interaction Mapping; Protein Structure, Tertiary; Receptors, Estrogen - metabolism; Stem Cells - metabolism; Transcription, Genetic; inhibitors; cancer; histone modification; LSD1

Histone lysine‐specific demethylase 1 (LSD1) is the first discovered and reported histone demethylase by Dr. Shi Yang's group in 2004. It is classified as a member of amine oxidase superfamily, the common feature of which is using the flavin adenine dinucleotide (FAD) as its cofactor. Since it...