PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31980458-9	2020	Targeting viperin to mitochondria decreased cellular ATP levels by more than 50%, consistent with the enzyme disrupting fatty acid catabolism.	Adenosine Triphosphate	53-56	radical S-adenosyl methionine domain containing 2	Homo sapiens	10-17	
21527675-5	2011	There, viperin interacted with the mitochondrial trifunctional protein that mediates beta-oxidation of fatty acids to generate adenosine triphosphate (ATP).	Adenosine Triphosphate	127-149	radical S-adenosyl methionine domain containing 2	Homo sapiens	7-14	
21527675-5	2011	There, viperin interacted with the mitochondrial trifunctional protein that mediates beta-oxidation of fatty acids to generate adenosine triphosphate (ATP).	Adenosine Triphosphate	151-154	radical S-adenosyl methionine domain containing 2	Homo sapiens	7-14	
21527675-6	2011	This interaction with viperin, but not with a mutant lacking the viperin iron-sulfur cluster-binding motif, reduced cellular ATP generation, which resulted in actin cytoskeleton disruption and enhancement of infection.	Adenosine Triphosphate	125-128	radical S-adenosyl methionine domain containing 2	Homo sapiens	22-29