PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
21924559-2	2011	As shown in several studies, most conclusively by data on the FN3K-KO mouse, this enzyme breaks down compounds produced by the non-enzymatic glycation of proteins by D-glucose.	Glucose	166-175	fructosamine 3 kinase	Mus musculus	62-66
20967558-4	2012	Mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo.	Fructosamine	48-61	fructosamine 3 kinase	Mus musculus	18-22
20967558-4	2012	Mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo.	fructosyl-lysine	71-85	fructosamine 3 kinase	Mus musculus	18-22
33917258-6	2021	AGE-type autofluorescence (AF) was measured to assess the time-dependent effects of FN3K on glycolaldehyde-induced AGE-modified porcine lens fragments and to evaluate its actions on intact lenses after in vivo intravitreal FN3K injection of murine eyes.	glycolaldehyde	92-106	fructosamine 3 kinase	Mus musculus	84-88
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
20009024-0	2010	Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations.	Ribose	139-145	fructosamine 3 kinase	Mus musculus	11-32
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
16987105-2	2006	The discovery that FN3K (fructosamine 3-kinase) results in protein deglycation upon phosphorylation of glucose-derived Amadori products suggests that intracellular glycation could be deleterious under certain circumstances.	Glucose	103-110	fructosamine 3 kinase	Mus musculus	19-23
16987105-2	2006	The discovery that FN3K (fructosamine 3-kinase) results in protein deglycation upon phosphorylation of glucose-derived Amadori products suggests that intracellular glycation could be deleterious under certain circumstances.	Glucose	103-110	fructosamine 3 kinase	Mus musculus	25-46
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
16819943-3	2006	Fn3k-/- mice looked healthy and had normal blood glucose and serum fructosamine levels.	Glucose	49-56	fructosamine 3 kinase	Mus musculus	0-4
16819943-3	2006	Fn3k-/- mice looked healthy and had normal blood glucose and serum fructosamine levels.	Fructosamine	67-79	fructosamine 3 kinase	Mus musculus	0-4
16819943-6	2006	Other intracellular proteins were also significantly more glycated in Fn3k-/- mice in erythrocytes (1.8-2.2-fold) and in brain, kidney, liver and skeletal muscle (1.2-1.8-fold), indicating that FN3K removes fructosamines from intracellular proteins in vivo.	Fructosamine	207-220	fructosamine 3 kinase	Mus musculus	70-74
16819943-7	2006	The urinary excretion of free fructose-epsilon-lysine was 10-20-fold higher in fed mice compared with mice starved for 36 h, and did not differ between fed Fn3k+/+ and Fn3k-/- mice, indicating that food is the main source of urinary fructose-epsilon-lysine in these mice and that FN3K does not participate in the metabolism of food-derived fructose-epsilon-lysine.	fructose-epsilon-lysine	30-53	fructosamine 3 kinase	Mus musculus	280-284
16819943-8	2006	However, in starved animals, the urinary excretion of fructose-epsilon-lysine was 2.5-fold higher in Fn3k-/- mice compared with Fn3k+/+ or Fn3k+/- mice.	fructose-epsilon-lysine	54-77	fructosamine 3 kinase	Mus musculus	101-105
16819943-9	2006	Furthermore, a marked increase (5-13-fold) was observed in the concentration of free fructose-epsilon-lysine in tissues of fed Fn3k-/- mice compared with control mice, indicating that FN3K participates in the metabolism of endogenously produced fructose-epsilon-lysine.	fructose-epsilon-lysine	85-108	fructosamine 3 kinase	Mus musculus	127-131
16819943-9	2006	Furthermore, a marked increase (5-13-fold) was observed in the concentration of free fructose-epsilon-lysine in tissues of fed Fn3k-/- mice compared with control mice, indicating that FN3K participates in the metabolism of endogenously produced fructose-epsilon-lysine.	fructose-epsilon-lysine	85-108	fructosamine 3 kinase	Mus musculus	184-188
16819943-9	2006	Furthermore, a marked increase (5-13-fold) was observed in the concentration of free fructose-epsilon-lysine in tissues of fed Fn3k-/- mice compared with control mice, indicating that FN3K participates in the metabolism of endogenously produced fructose-epsilon-lysine.	fructose-epsilon-lysine	245-268	fructosamine 3 kinase	Mus musculus	184-188
16819943-10	2006	Taken together, these data indicate that FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine.	fructose-epsilon-lysine	137-160	fructosamine 3 kinase	Mus musculus	41-45