PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32203098-2	2020	While hepatic fructose-1,6-bisphosphatase is well known as a key enzyme for gluconeogenesis, the role of muscle fructose-1,6-bisphosphatase 2 (Fbp2) in glucose disposal and thermogenesis is unknown.	Glucose	152-159	fructose bisphosphatase 2	Mus musculus	112-141	
32203098-2	2020	While hepatic fructose-1,6-bisphosphatase is well known as a key enzyme for gluconeogenesis, the role of muscle fructose-1,6-bisphosphatase 2 (Fbp2) in glucose disposal and thermogenesis is unknown.	Glucose	152-159	fructose bisphosphatase 2	Mus musculus	143-147	
32203098-9	2020	Taken together, these data demonstrate that Fbp2 is essential for muscle thermogenesis by replenishing the intramuscular glycogen pool through glyconeogenesis when the exogenous glucose source is limited.	Glucose	178-185	fructose bisphosphatase 2	Mus musculus	44-48	
22532827-4	2012	In this study, we used a combination of live-cell imaging and mathematical modeling to examine the effects of inducibly-expressed PFK2/FBPase2 mutants on glucose-induced Ca(2+) pulsatility in mouse islets.	Glucose	154-161	fructose bisphosphatase 2	Mus musculus	135-142	
33139001-9	2021	The underlying mechanism might be explained by the dysregulation of Fbp2/Cpt1a/Pfkl/Scd1 axis, which promoted the overload of glucose and lipid through the AMPK signaling pathway.	Glucose	126-133	fructose bisphosphatase 2	Mus musculus	68-72