title: Chemical probes of histone lysine methyltransferases.
abstract: Growing evidence suggests that histone methyltransferases (HMTs, also known as protein methyltransferases (PMTs)) play an important role in diverse biological processes and human diseases by regulating gene expression and the chromatin state. Therefore, HMTs have been increasingly recognized by the biomedical community as a class of potential therapeutic targets. High quality chemical probes of HMTs, as tools for deciphering their physiological functions and roles in human diseases and testing therapeutic hypotheses, are critical for advancing this promising field. In this review, we focus on the discovery, characterization, and biological applications of chemical probes for HMTs.
authors.affiliation: Department of Structural and Chemical Biology, ‡Department of Oncological Sciences, §Department of Pharmacology and Systems Therapeutics, Icahn School of Medicine at Mount Sinai , 1425 Madison Avenue, New York, New York 10029, United States.
authors.forename: H Ümit
authors.initials: HÜ
authors.lastname: Kaniskan
authors.forename: Jian
authors.initials: J
authors.lastname: Jin
mesh_terms: D000818:Animals; D015195:Drug Design; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D054852:Small Molecule Libraries / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D054852:Small Molecule Libraries; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine