PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35526488-2	2022	Usually, very-long chain fatty acids are first activated by acyl-CoA synthetase (ACS) to generate acyl-CoA for oxidation by acyl-CoA oxidase (ACOX) in peroxisomes, and the resultant shorter chain fatty acids will be further oxidized in mitochondria.	Acyl Coenzyme A	98-106	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	124-140	
35526488-2	2022	Usually, very-long chain fatty acids are first activated by acyl-CoA synthetase (ACS) to generate acyl-CoA for oxidation by acyl-CoA oxidase (ACOX) in peroxisomes, and the resultant shorter chain fatty acids will be further oxidized in mitochondria.	Acyl Coenzyme A	98-106	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	142-146	
9624157-3	1998	The first step of this system, catalyzed by acyl-CoA oxidase (AOX), converts fatty acyl-CoA to 2-trans-enoyl-CoA.	Acyl Coenzyme A	77-91	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	44-60	
9624157-3	1998	The first step of this system, catalyzed by acyl-CoA oxidase (AOX), converts fatty acyl-CoA to 2-trans-enoyl-CoA.	Acyl Coenzyme A	77-91	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	62-65	
9624157-7	1998	These observations implicate acyl-CoA and other putative substrates for AOX, as biological ligands for PPARalpha; thus, a normal AOX gene is indispensable for the physiological regulation of PPARalpha.	Acyl Coenzyme A	29-37	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	72-75	
9624157-7	1998	These observations implicate acyl-CoA and other putative substrates for AOX, as biological ligands for PPARalpha; thus, a normal AOX gene is indispensable for the physiological regulation of PPARalpha.	Acyl Coenzyme A	29-37	acyl-Coenzyme A oxidase 1, palmitoyl	Mus musculus	129-132