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Targeting of proteins in the histone modification machinery has emerged as a promising new direction to fight disease. The search for compounds that inhibit proteins that readout histone modification has led to several new epigenetic drugs, mostly for proteins involved in recognition of acetylated lysines. However, this approach proved to be a challenging task for methyllysine readers, which typically feature shallow binding pockets. Moreover, reader proteins of trimethyllysine K36 on thedoi:10.3390/molecules25214951 pmid:33114657 pmcid:PMC7662849 fatcat:5oardfmtpbhwvc3j2zwpvdks5a