PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29240439-2	2018	Although NSAIDs are known to impact multiple cellular signaling mechanisms, a recent finding is that the NSAID salicylate can disrupt histone acetylation, in part through direct inhibition of the lysine acetyltransferase (KAT) p300/CBP.	Salicylates	111-121	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	222-225	
28717171-4	2017	As the salicylate motif is necessary for the activity of the lysine acetyltransferase (KAT) inhibitor anacardic acid, we hypothesized these effects were associated with the inhibition of KAT activity.	Salicylates	7-17	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	87-90	
28717171-4	2017	As the salicylate motif is necessary for the activity of the lysine acetyltransferase (KAT) inhibitor anacardic acid, we hypothesized these effects were associated with the inhibition of KAT activity.	Salicylates	7-17	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	187-190	
28717171-6	2017	In vitro KAT assays confirmed that salicylate directly inhibited PCAF/Kat2b, Tip60/Kat5 and hMOF/Kat8, and this inhibition was likely involved in the reversal of EMT in the metastatic prostate cancer cell line PC-3.	Salicylates	35-45	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	9-12