PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30622280-0 2019 Author Correction: Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR. N(2)-methyl-L-lysine 61-74 tumor protein p53 binding protein 1 Homo sapiens 95-100 28241136-0 2017 TIRR regulates 53BP1 by masking its histone methyl-lysine binding function. N(2)-methyl-L-lysine 44-57 tumor protein p53 binding protein 1 Homo sapiens 15-20 30002377-0 2018 Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR. N(2)-methyl-L-lysine 42-55 tumor protein p53 binding protein 1 Homo sapiens 76-81 29844495-8 2018 Our studies elucidate the mechanism by which TIRR recognizes 53BP1 Tudor and functions as a cellular inhibitor of the histone methyl-lysine readers. N(2)-methyl-L-lysine 126-139 tumor protein p53 binding protein 1 Homo sapiens 61-66 25590533-4 2015 Through a cross-screening approach, we identified UNC2170 (1) as a micromolar ligand of 53BP1, which demonstrates at least 17-fold selectivity for 53BP1 as compared to other methyl-lysine (Kme) binding proteins tested. N(2)-methyl-L-lysine 174-187 tumor protein p53 binding protein 1 Homo sapiens 88-93 25590533-5 2015 Structural studies revealed that the tert-butyl amine of UNC2170 anchors the compound in the methyl-lysine (Kme) binding pocket of 53BP1, making it competitive with endogenous Kme substrates. N(2)-methyl-L-lysine 93-106 tumor protein p53 binding protein 1 Homo sapiens 131-136