PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21527675-5	2011	There, viperin interacted with the mitochondrial trifunctional protein that mediates beta-oxidation of fatty acids to generate adenosine triphosphate (ATP).	Fatty Acids	103-114	radical S-adenosyl methionine domain containing 2	Homo sapiens	7-14	
31980458-3	2020	This process involves translocation of viperin to the mitochondrion, where it binds the beta-subunit (HADHB) of the mitochondrial trifunctional enzyme complex that catalyzes thiolysis of beta-ketoacyl-CoA esters as part of fatty acid beta-oxidation.	Fatty Acids	223-233	radical S-adenosyl methionine domain containing 2	Homo sapiens	39-46	
31980458-9	2020	Targeting viperin to mitochondria decreased cellular ATP levels by more than 50%, consistent with the enzyme disrupting fatty acid catabolism.	Fatty Acids	120-130	radical S-adenosyl methionine domain containing 2	Homo sapiens	10-17	
23935494-2	2013	We show here that this increase is a consequence of the virus-induced redistribution of the host protein viperin to mitochondria and its capacity to interact with and block the function of the mitochondrial trifunctional protein (TFP), the enzyme that mediates fatty acid-beta-oxidation.	Fatty Acids	261-271	radical S-adenosyl methionine domain containing 2	Homo sapiens	105-112