PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32428298-2	2020	PD-404,182 was shown to be a selective covalent inhibitor of HDAC8 that forms mixed disulfides with several cysteine residues and is also able to transform thiol groups to thiocyanates.	Sulfhydryl Compounds	156-161	histone deacetylase 8	Homo sapiens	61-66	
32428298-5	2020	Therefore, the inhibition mechanism of HDAC8 by PD-404,182 involves both, covalent modification of thiols as well as ligand mediated disulfide formation.	Sulfhydryl Compounds	99-105	histone deacetylase 8	Homo sapiens	39-44	
21215647-6	2011	This assumption is consistent with the molecular modelling of the complex of psammaplin A thiol with h-HDAC8.	Sulfhydryl Compounds	90-95	histone deacetylase 8	Homo sapiens	103-108	
30611847-10	2019	Further optimization of non-covalent interaction and thiol-reactivity provides opportunities to develop therapeutic useful covalent HDAC8 inhibitors.	Sulfhydryl Compounds	53-58	histone deacetylase 8	Homo sapiens	132-137	
25793284-3	2015	Each inhibitor contains a pendant side chain thiol that coordinates to the active site Zn(2+) ion, as observed in the X-ray crystal structure of the HDAC8-Largazole complex [Cole, K. E., Dowling, D. P., Boone, M. A., Phillips, A. J., and Christianson, D. W. (2011) J.	Sulfhydryl Compounds	45-50	histone deacetylase 8	Homo sapiens	149-154	
19956788-4	2008	In the light of the structural features of histone deacetylase 8, we propose that the enzyme interacts with the gold nanoparticles via the surface exposed thiol groups, and such interaction occurs in two alternative modes.	Sulfhydryl Compounds	155-160	histone deacetylase 8	Homo sapiens	43-64