PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33562682-8	2021	We know that NRF2 functions depend on removal of sugar adducts by the frutosamine-3-kinase (FN3K).	Sugars	49-54	fructosamine 3 kinase	Homo sapiens	70-90	
33562682-8	2021	We know that NRF2 functions depend on removal of sugar adducts by the frutosamine-3-kinase (FN3K).	Sugars	49-54	fructosamine 3 kinase	Homo sapiens	92-96	
26352355-5	2015	FN3K phosphorylates fructosamines on the third carbon of their sugar moiety, making them unstable and causing them to detach from proteins, suggesting a protective role of this enzyme.	Sugars	63-68	fructosamine 3 kinase	Homo sapiens	0-4	
20967558-2	2012	Fructosamine-3-kinase (FN3K), an enzyme found in mammals and birds, phosphorylates fructosamines on the third carbon of their sugar moiety, making them unstable and causing them to detach from proteins.	Sugars	126-131	fructosamine 3 kinase	Homo sapiens	0-21	
20967558-2	2012	Fructosamine-3-kinase (FN3K), an enzyme found in mammals and birds, phosphorylates fructosamines on the third carbon of their sugar moiety, making them unstable and causing them to detach from proteins.	Sugars	126-131	fructosamine 3 kinase	Homo sapiens	23-27	
21613209-10	2011	FN3K and FN3K-RP are known to phosphorylate sugar moieties on glycosylated proteins, but this is the first report that these enzymes can phosphorylate hydrophobic xenobiotics.	Sugars	44-49	fructosamine 3 kinase	Homo sapiens	0-4	
16920277-3	2007	Because of these considerations, we have proposed that the intrinsic toxicity of glucose and other sugars is counteracted in vivo by active deglycation mechanisms including transglycation of Schiff"s bases and FN3K-dependent breakdown of fructosamines.	Sugars	99-105	fructosamine 3 kinase	Homo sapiens	210-214