title: G9a - An Appealing Antineoplastic Target.
abstract: BACKGROUND
  G9a is the primary enzyme for mono- and dimethylation at Lys 9 of histone H3 and forms predominantly the heteromeric complex as a G9a-GLP (G9a-like protein) that is a functional histone lysine methltransferase in vivo. Mounting evidence suggests that G9a catalyzes methylation of histone and nonhistone proteins, which plays a crucial role in diverse biological processes and human diseases.
  
  
  METHODS
  In this study, the current knowledge on biological functions of G9a and inhibitors were summarized.
  
  
  RESULTS
  we review the current knowledge on biological functions of G9a, with particular emphasis on regulating gene expression and cell processes, and involvement in human diseases. We outline a perspective on various classes of G9a inhibitors to date from both articles and patents with an emphasis on their discovery, activity and the current research status.
  
  
  CONCLUSIONS
  We highlight the key knowledge on potential biological functions and various human diseases. We also reviewed the discovery and characterization of the reported G9a inhibitors. However, we also propose the challenges and future opportunities in study of G9a. This review could make a crucial contribution to the long journey to develop drug-like molecules targeting G9a.
authors.affiliation: State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
authors.forename: Wei-Lin
authors.initials: WL
authors.lastname: Chen
authors.affiliation: Department of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University, Nanjing, 210009, China.
authors.forename: Hao-Peng
authors.initials: HP
authors.lastname: Sun
authors.affiliation: Jiangsu Key Laboratory of Drug Design and Optimization, China Pharmaceutical University, Nanjing, 210009, China.
authors.forename: Dong-Dong
authors.initials: DD
authors.lastname: Li
authors.affiliation: Jiangsu Key Laboratory of Drug Design and Optimization, China Pharmaceutical University, Nanjing, 210009, China.
authors.forename: Zhi-Hui
authors.initials: ZH
authors.lastname: Wang
authors.affiliation: Jiangsu Key Laboratory of Drug Design and Optimization, China Pharmaceutical University, Nanjing, 210009, China.
authors.forename: Qi-Dong
authors.initials: QD
authors.lastname: You
authors.affiliation: State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.
authors.forename: Xiao-Ke
authors.initials: XK
authors.lastname: Guo
mesh_terms: D000241:Adenosine / Q000031:analogs & derivatives / Q000494:pharmacology; D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology*; D001381:Azepines / Q000494:pharmacology; D001562:Benzimidazoles / Q000737:chemistry / Q000494:pharmacology; D019175:DNA Methylation; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D006649:Histocompatibility Antigens / Q000737:chemistry / Q000378:metabolism*; D011495:Histone-Lysine N-Methyltransferase / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D058990:Molecular Targeted Therapy; D011799:Quinazolines / Q000494:pharmacology
chemical_list: C551961:7-(2-(2-(dimethylamino)ethoxy)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine; D000970:Antineoplastic Agents; D001381:Azepines; C518299:BIX 01294; D001562:Benzimidazoles; D004791:Enzyme Inhibitors; D006649:Histocompatibility Antigens; D011799:Quinazolines; C445405:EHMT2 protein, human; D011495:Histone-Lysine N-Methyltransferase; D000241:Adenosine; C006235:sinefungin
keywords: Biological functions; G9a; Histone Lysine Methltransferase; antineoplastic target; diseases; inhibitors