PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30054507-8	2018	Suppression of DRP1 by HDAC8 was likely mediated by decreasing the level of acetylated histone H3 lysine 27 (a hallmark of active promoters) at the DRP1 promoter.	Lysine	98-104	histone deacetylase 8	Homo sapiens	23-28	
30358439-9	2019	Chromatin immunoprecipitation quantitative PCR using an antibody against H3K27ac (histone H3 acetylated at lysine 27; a known HDAC8 substrate and a marker for active enhancers) suggested that HDAC8 inhibition with NCC170 ameliorated TGFbeta1-induced loss of H3K27ac at the PPARgamma gene enhancer.	Lysine	107-113	histone deacetylase 8	Homo sapiens	192-197	
34917889-0	2021	Kinetic Characterization of Human Histone Deacetylase 8 With Medium-Chain Fatty Acyl Lysine.	Lysine	85-91	histone deacetylase 8	Homo sapiens	34-55	
34917889-5	2021	HDAC8 activity was analyzed with various peptides where the target lysine is modified with medium-chain fatty acyl group.	Lysine	67-73	histone deacetylase 8	Homo sapiens	0-5	
33998791-2	2021	Histone deacetylase 8 (HDAC8), which is proved to be involved in carcinogenesis, is an enzyme associated with the chromatin for post-translational deacetylation of acetylated lysine.	Lysine	175-181	histone deacetylase 8	Homo sapiens	0-21	
33998791-2	2021	Histone deacetylase 8 (HDAC8), which is proved to be involved in carcinogenesis, is an enzyme associated with the chromatin for post-translational deacetylation of acetylated lysine.	Lysine	175-181	histone deacetylase 8	Homo sapiens	23-28	
33827976-3	2021	Here, we showed that pharmacological inhibition of histone deacetylase 8 (HDAC8), a histone H3 lysine 27 (H3K27)-specific isozyme overexpressed in a variety of human cancers, thwarts HCC tumorigenicity in a T cell-dependent manner.	Lysine	95-101	histone deacetylase 8	Homo sapiens	51-72	
33827976-3	2021	Here, we showed that pharmacological inhibition of histone deacetylase 8 (HDAC8), a histone H3 lysine 27 (H3K27)-specific isozyme overexpressed in a variety of human cancers, thwarts HCC tumorigenicity in a T cell-dependent manner.	Lysine	95-101	histone deacetylase 8	Homo sapiens	74-79	
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+).	Lysine	65-73	histone deacetylase 8	Homo sapiens	0-21	
28509866-7	2017	Furthermore, HDAC8 induced tri-methylation of histone H3 lysine 27 (H3K27me3), which is known to suppress PTEN expression, through at least in part down-regulating the H3K27me3 eraser Jumonji Domain Containing (JMJD) 3.	Lysine	57-63	histone deacetylase 8	Homo sapiens	13-18	
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+).	Lysine	65-73	histone deacetylase 8	Homo sapiens	23-28	
27459069-7	2016	Screening a panel of peptides with different acyl lysine modifications, we found that HDAC8 can catalyze the removal of acyl groups with 2-16 carbons from lysine 9 of the histone H3 peptide (H3K9).	Lysine	50-56	histone deacetylase 8	Homo sapiens	86-91	
27459069-7	2016	Screening a panel of peptides with different acyl lysine modifications, we found that HDAC8 can catalyze the removal of acyl groups with 2-16 carbons from lysine 9 of the histone H3 peptide (H3K9).	Lysine	155-161	histone deacetylase 8	Homo sapiens	86-91	
27459069-12	2016	This is the first report of a zinc-dependent HDAC with de-fatty-acylation activity, and identification of HDAC8 de-fatty-acylation targets will help to further understand the function of HDAC8 and protein lysine fatty acylation.	Lysine	205-211	histone deacetylase 8	Homo sapiens	106-111	
20870437-1	2010	Zinc-dependent histone deacetylase 8 removes the epsilon-acetyl groups present in the N-terminal lysine residues of histone proteins, thereby restricting various transcription factors from being expressed.	Lysine	97-103	histone deacetylase 8	Homo sapiens	15-36	
26383163-8	2015	Mechanistically, HDAC8 physically interacted with the chromatin modifier EZH2 to concordantly repress Wnt antagonists via histone H4 deacetylation and H3 lysine 27 trimethylation.	Lysine	154-160	histone deacetylase 8	Homo sapiens	17-22	
22272142-1	2011	Histone deacetylase 8 (HDAC8) is an enzyme involved in deacetylating the amino groups of terminal lysine residues, thereby repressing the transcription of various genes including tumor suppressor gene.	Lysine	98-104	histone deacetylase 8	Homo sapiens	0-21	
22272142-1	2011	Histone deacetylase 8 (HDAC8) is an enzyme involved in deacetylating the amino groups of terminal lysine residues, thereby repressing the transcription of various genes including tumor suppressor gene.	Lysine	98-104	histone deacetylase 8	Homo sapiens	23-28	
14701748-0	2004	Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetyl groups from lysine residues of histone and nonhistone proteins.	Lysine	185-191	histone deacetylase 8	Homo sapiens	23-44