PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28442255-2 2017 When assessed with the commercially available HDAC8 peptide substrate Fluor-de-Lys -HDAC8 that harbors the unnatural 7-amino-4-methylcoumarin (AMC) residue immediately C-terminal to the Nepsilon-acetyl-lysine residue to be deacetylated, our compounds exhibited comparable activation potency to that of TM-2-51, the strongest HDAC8 activator reported in the current literature. N(alpha)-acetyllysine 195-208 histone deacetylase 8 Homo sapiens 46-51 33998791-0 2021 Comparative QM/MM Molecular Dynamics and Umbrella Sampling Simulations: Interaction of the Zinc-Bound Intermediate Gem-Diolate Trapoxin A Inhibitor and Acetyl-l-lysine Substrate with Histone Deacetylase 8. N(alpha)-acetyllysine 152-167 histone deacetylase 8 Homo sapiens 183-204 33998791-8 2021 The optimum binding to the active site of HDAC8 for structures of gem-diolate TA (intermediate state) and acetyl-l-lysine (intermediate state) was determined according to the corresponding energy profiles. N(alpha)-acetyllysine 106-121 histone deacetylase 8 Homo sapiens 42-47 28442255-2 2017 When assessed with the commercially available HDAC8 peptide substrate Fluor-de-Lys -HDAC8 that harbors the unnatural 7-amino-4-methylcoumarin (AMC) residue immediately C-terminal to the Nepsilon-acetyl-lysine residue to be deacetylated, our compounds exhibited comparable activation potency to that of TM-2-51, the strongest HDAC8 activator reported in the current literature. N(alpha)-acetyllysine 195-208 histone deacetylase 8 Homo sapiens 84-89 28442255-2 2017 When assessed with the commercially available HDAC8 peptide substrate Fluor-de-Lys -HDAC8 that harbors the unnatural 7-amino-4-methylcoumarin (AMC) residue immediately C-terminal to the Nepsilon-acetyl-lysine residue to be deacetylated, our compounds exhibited comparable activation potency to that of TM-2-51, the strongest HDAC8 activator reported in the current literature. N(alpha)-acetyllysine 195-208 histone deacetylase 8 Homo sapiens 84-89 27933794-1 2016 Histone deacetylase 8 (HDAC8) catalyzes the hydrolysis of acetyl-l-lysine to yield products l-lysine and acetate through a mechanism in which a nucleophilic water molecule is activated by a histidine general base and a catalytic metal ion (Zn2+ or Fe2+). N(alpha)-acetyllysine 58-73 histone deacetylase 8 Homo sapiens 0-21 27933794-1 2016 Histone deacetylase 8 (HDAC8) catalyzes the hydrolysis of acetyl-l-lysine to yield products l-lysine and acetate through a mechanism in which a nucleophilic water molecule is activated by a histidine general base and a catalytic metal ion (Zn2+ or Fe2+). N(alpha)-acetyllysine 58-73 histone deacetylase 8 Homo sapiens 23-28