PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20009024-7	2010	Although protein-bound fructose-epsilon-lysines were more abundant in Fn3k(-/-) vs. WT islets, islet cell survival and function and their glucotoxic alterations were almost identical in both types of islets, except for a lower level of apoptosis in Fn3k(-/-) islets cultured for 3 wk in G30.	fructose-epsilon-lysines	23-47	fructosamine 3 kinase	Mus musculus	70-74	
16819943-2	2006	In the present paper, we have explored, through a targeted gene inactivation approach, the role of FN3K (fructosamine 3-kinase), an intracellular enzyme that phosphorylates free and protein-bound fructose-epsilon-lysines and which is potentially involved in protein repair.	fructose-epsilon-lysines	196-220	fructosamine 3 kinase	Mus musculus	99-103	
16819943-2	2006	In the present paper, we have explored, through a targeted gene inactivation approach, the role of FN3K (fructosamine 3-kinase), an intracellular enzyme that phosphorylates free and protein-bound fructose-epsilon-lysines and which is potentially involved in protein repair.	fructose-epsilon-lysines	196-220	fructosamine 3 kinase	Mus musculus	105-126