In silico probing and biological evaluation of SETDB1/ESET-targeted novel compounds that reduce tri-methylated histone H3K9 (H3K9me3) level

ERG-associated protein with the SET domain (ESET/SET domain bifurcated 1/SETDB1/KMT1E) is a histone lysine methyltransferase (HKMT) and it preferentially tri-methylates lysine 9 of histone H3 (H3K9me3). SETDB1/ESET leads to heterochromatin condensation and epigenetic gene silencing. These functional...

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Veröffentlicht in:	Journal of computer-aided molecular design 2017-10, Vol.31 (10), p.877-889
Hauptverfasser:	Park, Insun, Hwang, Yu Jin, Kim, TaeHun, Viswanath, Ambily Nath Indu, Londhe, Ashwini M., Jung, Seo Yun, Sim, Kyoung Mi, Min, Sun-Joon, Lee, Ji Eun, Seong, Jihye, Kim, Yun Kyung, No, Kyoung Tai, Ryu, Hoon, Pae, Ae Nim
Format:	Artikel
Sprache:	eng
Schlagworte:	Animal Anatomy Benzene Derivatives - chemistry Benzene Derivatives - pharmacology Bifurcations Binding Sites Cell Line Cell Survival Chemistry Chemistry and Materials Science Computer Applications in Chemistry Computer Simulation Cytotoxicity Databases, Pharmaceutical Disorders Epigenetics Histology Histone-Lysine N-Methyltransferase - metabolism Histones - metabolism Homology Humans Inhibitors Lead compounds Ligands Lysine Methylation Molecular Docking Simulation Molecular structure Morphology Neurons - cytology Neurons - drug effects Pharmaceutical sciences Pharmacology Physical Chemistry Protein Binding Protein Methyltransferases - antagonists & inhibitors Protein Methyltransferases - metabolism Structure-Activity Relationship Toxicity
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