PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30108796-2	2017	Herein, we report the first toxicological evaluation of imidazopyridine-based DGAT2 inhibitors and show that the arteriopathy associated with imidazopyridine 1 can be mitigated with small structural modifications, and is thus not mechanism related.	imidazopyridine	56-71	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	78-83	
30422629-5	2018	Herein, we describe imidazopyridines represented by PF-06424439 (1) and 2 as long residence time inhibitors of DGAT2.	imidazopyridine	20-36	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	111-116	
30422629-9	2018	A binding assay utilizing 125I-labeled imidazopyridine demonstrated that the level of imidazopyridine binding to DGAT2 mutant enzymes, H161A and H163A, dramatically decreased to 11-17% of that of the wild-type enzyme, indicating that these residues are critical for imidazopyridines to bind to DGAT2.	imidazopyridine	39-54	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	113-118	
30422629-9	2018	A binding assay utilizing 125I-labeled imidazopyridine demonstrated that the level of imidazopyridine binding to DGAT2 mutant enzymes, H161A and H163A, dramatically decreased to 11-17% of that of the wild-type enzyme, indicating that these residues are critical for imidazopyridines to bind to DGAT2.	imidazopyridine	86-101	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	113-118	
30422629-9	2018	A binding assay utilizing 125I-labeled imidazopyridine demonstrated that the level of imidazopyridine binding to DGAT2 mutant enzymes, H161A and H163A, dramatically decreased to 11-17% of that of the wild-type enzyme, indicating that these residues are critical for imidazopyridines to bind to DGAT2.	imidazopyridine	86-101	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	294-299	
30422629-9	2018	A binding assay utilizing 125I-labeled imidazopyridine demonstrated that the level of imidazopyridine binding to DGAT2 mutant enzymes, H161A and H163A, dramatically decreased to 11-17% of that of the wild-type enzyme, indicating that these residues are critical for imidazopyridines to bind to DGAT2.	imidazopyridine	266-282	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	113-118	
30422629-10	2018	Taken together, imidazopyridines may thus represent a promising lead series for the development of DGAT2 inhibitors that display an unprecedented combination of potency, selectivity, and in vivo efficacy.	imidazopyridine	16-32	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	99-104	
26349027-0	2015	Discovery and Optimization of Imidazopyridine-Based Inhibitors of Diacylglycerol Acyltransferase 2 (DGAT2).	imidazopyridine	30-45	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	66-98	
26349027-0	2015	Discovery and Optimization of Imidazopyridine-Based Inhibitors of Diacylglycerol Acyltransferase 2 (DGAT2).	imidazopyridine	30-45	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	100-105	
26349027-1	2015	The medicinal chemistry and preclinical biology of imidazopyridine-based inhibitors of diacylglycerol acyltransferase 2 (DGAT2) is described.	imidazopyridine	51-66	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	87-119	
26349027-1	2015	The medicinal chemistry and preclinical biology of imidazopyridine-based inhibitors of diacylglycerol acyltransferase 2 (DGAT2) is described.	imidazopyridine	51-66	acyl-CoA wax alcohol acyltransferase 1	Homo sapiens	121-126