PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	46-51	
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