PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
27394048-1	2017	BACKGROUND: Fructosamine 3 kinase (FN3K) is a deglycating enzyme, which may play a key role in reducing diabetes-induced organ damage by removing bound glucose from glycated proteins.	Glucose	152-159	fructosamine 3 kinase	Homo sapiens	12-33
27394048-4	2017	The dialyzed solution (containing +-1000 micromol/L fructosamine) was used as an FN3K substrate.	Fructosamine	52-64	fructosamine 3 kinase	Homo sapiens	81-85
27394048-1	2017	BACKGROUND: Fructosamine 3 kinase (FN3K) is a deglycating enzyme, which may play a key role in reducing diabetes-induced organ damage by removing bound glucose from glycated proteins.	Glucose	152-159	fructosamine 3 kinase	Homo sapiens	35-39
27394048-7	2017	The decrease in fructosamine concentration over time is a measure for the FN3K activity (1 U corresponding to 1 micromol/min).	Fructosamine	16-28	fructosamine 3 kinase	Homo sapiens	74-78
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.	Fructosamine	20-33	fructosamine 3 kinase	Homo sapiens	0-4
26850632-7	2016	An in vitro removal of fructosamine of the valve was initiated using ATP-dependent fructosamine 3-kinase (FN3K).	Fructosamine	23-35	fructosamine 3 kinase	Homo sapiens	83-104
26850632-7	2016	An in vitro removal of fructosamine of the valve was initiated using ATP-dependent fructosamine 3-kinase (FN3K).	Fructosamine	23-35	fructosamine 3 kinase	Homo sapiens	106-110
26850632-11	2016	In the in vitro deglycation study, a significant lower aortic valve fructosamine concentration was detected after treatment with FN3K.	Fructosamine	68-80	fructosamine 3 kinase	Homo sapiens	129-133
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.	Carbon	47-53	fructosamine 3 kinase	Homo sapiens	0-4
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.	Fructosamine	83-96	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.	Fructosamine	83-96	fructosamine 3 kinase	Homo sapiens	23-27
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.	Carbon	110-116	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.	Carbon	110-116	fructosamine 3 kinase	Homo sapiens	23-27
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
20967558-7	2012	As with FN3K, the third carbon is phosphorylated and this leads to destabilization of the ketoamines.	Carbon	24-30	fructosamine 3 kinase	Homo sapiens	8-12
20967558-7	2012	As with FN3K, the third carbon is phosphorylated and this leads to destabilization of the ketoamines.	ketoamines	90-100	fructosamine 3 kinase	Homo sapiens	8-12
20967558-11	2012	The specificity of FN3K homologues present in plants and bacteria is similar to that of mammalian FN3KRP, suggesting that deglycation of ribulosamines and/or erythrulosamines is an ancient mechanism.	ribulosamines	137-150	fructosamine 3 kinase	Homo sapiens	19-23
20967558-11	2012	The specificity of FN3K homologues present in plants and bacteria is similar to that of mammalian FN3KRP, suggesting that deglycation of ribulosamines and/or erythrulosamines is an ancient mechanism.	erythrulosamines	158-174	fructosamine 3 kinase	Homo sapiens	19-23
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
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	Fructosamine	76-89	fructosamine 3 kinase	Homo sapiens	0-21
21288167-2	2011	Fructosamine 3-kinase (FN3K), initially identified in erythrocytes, appears to be responsible for the removal of fructosamine from proteins, suggesting a protective role in nonenzymatic glycation.	Fructosamine	113-125	fructosamine 3 kinase	Homo sapiens	0-21
21288167-2	2011	Fructosamine 3-kinase (FN3K), initially identified in erythrocytes, appears to be responsible for the removal of fructosamine from proteins, suggesting a protective role in nonenzymatic glycation.	Fructosamine	113-125	fructosamine 3 kinase	Homo sapiens	23-27
21052529-1	2010	Fructosamine-3-Kinase (FN3K) is an enzyme phosphorilating fructoselysine (FL) residues on glycated proteins, resulting in the production of protein-bound FL-3-phosphate.	fructosyl-lysine	58-72	fructosamine 3 kinase	Homo sapiens	0-21
21052529-1	2010	Fructosamine-3-Kinase (FN3K) is an enzyme phosphorilating fructoselysine (FL) residues on glycated proteins, resulting in the production of protein-bound FL-3-phosphate.	fructosyl-lysine	58-72	fructosamine 3 kinase	Homo sapiens	23-27
21052529-1	2010	Fructosamine-3-Kinase (FN3K) is an enzyme phosphorilating fructoselysine (FL) residues on glycated proteins, resulting in the production of protein-bound FL-3-phosphate.	fructosyl-lysine	74-76	fructosamine 3 kinase	Homo sapiens	0-21
21052529-1	2010	Fructosamine-3-Kinase (FN3K) is an enzyme phosphorilating fructoselysine (FL) residues on glycated proteins, resulting in the production of protein-bound FL-3-phosphate.	fructosyl-lysine	74-76	fructosamine 3 kinase	Homo sapiens	23-27
21052529-1	2010	Fructosamine-3-Kinase (FN3K) is an enzyme phosphorilating fructoselysine (FL) residues on glycated proteins, resulting in the production of protein-bound FL-3-phosphate.	fl-3-phosphate	154-168	fructosamine 3 kinase	Homo sapiens	0-21
21052529-1	2010	Fructosamine-3-Kinase (FN3K) is an enzyme phosphorilating fructoselysine (FL) residues on glycated proteins, resulting in the production of protein-bound FL-3-phosphate.	fl-3-phosphate	154-168	fructosamine 3 kinase	Homo sapiens	23-27
21613209-7	2011	Incubation of human RBC lysates with 1-deoxy-1-morpholinofructose, a competitive inhibitor of FN3K, inhibited ~10% of the kinase activity, suggesting FN3K-RP is the principal kinase responsible for activation of CS-0777 in blood.	1-deoxy-1-morpholinofructose	37-65	fructosamine 3 kinase	Homo sapiens	94-98
21613209-8	2011	Lysates from HEK293 cells overexpressing FN3K or FN3K-RP resulted in phosphorylation of CS-0777 and structurally related molecules but showed little kinase activity for FTY720 and no kinase activity for sphingosine.	Cesium	88-90	fructosamine 3 kinase	Homo sapiens	41-45
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	Fructosamine	76-89	fructosamine 3 kinase	Homo sapiens	23-27
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	fructosamine-3-phosphate	103-127	fructosamine 3 kinase	Homo sapiens	0-21
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	fructosamine-3-phosphate	103-127	fructosamine 3 kinase	Homo sapiens	23-27
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	Phosphates	118-127	fructosamine 3 kinase	Homo sapiens	0-21
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	Phosphates	118-127	fructosamine 3 kinase	Homo sapiens	23-27
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	3-deoxyglucasone	183-199	fructosamine 3 kinase	Homo sapiens	0-21
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	3-deoxyglucasone	183-199	fructosamine 3 kinase	Homo sapiens	23-27
19834870-3	2010	Fructosamine-3-kinase (FN3K) is an intracellular enzyme that phosphorylates fructosamines resulting in fructosamine-3-phosphate, which subsequently decomposes to inorganic phosphate, 3-deoxyglucasone and the unmodified amine.	Amines	7-12	fructosamine 3 kinase	Homo sapiens	23-27
17686456-1	2007	Fructosamine-3-kinase (FN3K) phosphorylates fructosamines to fructosamine-3-phosphates.	Fructosamine	44-57	fructosamine 3 kinase	Homo sapiens	0-21
17686456-1	2007	Fructosamine-3-kinase (FN3K) phosphorylates fructosamines to fructosamine-3-phosphates.	Fructosamine	44-57	fructosamine 3 kinase	Homo sapiens	23-27
17686456-1	2007	Fructosamine-3-kinase (FN3K) phosphorylates fructosamines to fructosamine-3-phosphates.	fructosamine-3-phosphates	61-86	fructosamine 3 kinase	Homo sapiens	0-21
17686456-1	2007	Fructosamine-3-kinase (FN3K) phosphorylates fructosamines to fructosamine-3-phosphates.	fructosamine-3-phosphates	61-86	fructosamine 3 kinase	Homo sapiens	23-27
17686456-6	2007	One of these is meglumine-3-phosphate (Meg3P), an activity consistent with the known substrate specificity of FN3K.	meglumine-3-phosphate	16-37	fructosamine 3 kinase	Homo sapiens	110-114
17686456-6	2007	One of these is meglumine-3-phosphate (Meg3P), an activity consistent with the known substrate specificity of FN3K.	meg3p	39-44	fructosamine 3 kinase	Homo sapiens	110-114
17681011-1	2007	The purpose of this work was to identify the function of bacterial homologues of fructosamine 3-kinase (FN3K), a mammalian enzyme responsible for the removal of fructosamines from proteins.	Fructosamine	161-174	fructosamine 3 kinase	Homo sapiens	81-102
17681011-1	2007	The purpose of this work was to identify the function of bacterial homologues of fructosamine 3-kinase (FN3K), a mammalian enzyme responsible for the removal of fructosamines from proteins.	Fructosamine	161-174	fructosamine 3 kinase	Homo sapiens	104-108
17681011-6	2007	They also phosphorylated protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines, therefore having properties similar to those of mammalian FN3K-related protein.	ribulosamines	39-52	fructosamine 3 kinase	Homo sapiens	169-173
17681011-6	2007	They also phosphorylated protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines, therefore having properties similar to those of mammalian FN3K-related protein.	erythrulosamines	56-72	fructosamine 3 kinase	Homo sapiens	169-173
16523184-1	2006	BACKGROUND: Part of the fructosamines that are bound to intracellular proteins are repaired by fructosamine 3-kinase (FN3K).	Fructosamine	24-37	fructosamine 3 kinase	Homo sapiens	95-116
16920277-0	2007	Fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by fructosamine-3-kinase (FN3K) and/or fructosamine-3-kinase-related-protein (FN3KRP).	fructosamine-6-phosphates	0-25	fructosamine 3 kinase	Homo sapiens	107-128
16920277-0	2007	Fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by fructosamine-3-kinase (FN3K) and/or fructosamine-3-kinase-related-protein (FN3KRP).	fructosamine-6-phosphates	0-25	fructosamine 3 kinase	Homo sapiens	130-134
16920277-0	2007	Fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by fructosamine-3-kinase (FN3K) and/or fructosamine-3-kinase-related-protein (FN3KRP).	fructosamine-3,6-bisphosphates	63-93	fructosamine 3 kinase	Homo sapiens	107-128
16920277-0	2007	Fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by fructosamine-3-kinase (FN3K) and/or fructosamine-3-kinase-related-protein (FN3KRP).	fructosamine-3,6-bisphosphates	63-93	fructosamine 3 kinase	Homo sapiens	130-134
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
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.	Fructosamine	238-251	fructosamine 3 kinase	Homo sapiens	210-214
16920277-5	2007	Two such important questions are In this paper we propose a resolution of both these quandaries by proposing that fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by FN3KRP and/or possibly FN3K.	fructosamine-6-phosphates	114-139	fructosamine 3 kinase	Homo sapiens	221-225
16920277-5	2007	Two such important questions are In this paper we propose a resolution of both these quandaries by proposing that fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by FN3KRP and/or possibly FN3K.	fructosamine-3,6-bisphosphates	177-207	fructosamine 3 kinase	Homo sapiens	221-225
16670083-1	2006	Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines.	Fructosamine	106-119	fructosamine 3 kinase	Homo sapiens	0-21
16670083-1	2006	Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines.	Fructosamine	106-119	fructosamine 3 kinase	Homo sapiens	23-27
16670083-1	2006	Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines.	Glucose	173-180	fructosamine 3 kinase	Homo sapiens	0-21
16670083-1	2006	Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines.	Glucose	173-180	fructosamine 3 kinase	Homo sapiens	23-27
16670083-1	2006	Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines.	Amines	113-119	fructosamine 3 kinase	Homo sapiens	0-21
16670083-1	2006	Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines.	Amines	113-119	fructosamine 3 kinase	Homo sapiens	23-27
16670083-9	2006	Furthermore, lysozyme glycated with Glu-6-P was converted by MDP-1 to a substrate for FN3K.	Glucose-6-Phosphate	36-43	fructosamine 3 kinase	Homo sapiens	86-90
16670083-10	2006	We conclude that MDP-1 may act physiologically in conjunction with FN3K to free proteins from the glycation products derived from Glu-6-P.	Glucose-6-Phosphate	130-137	fructosamine 3 kinase	Homo sapiens	67-71
18334852-2	2007	Instead, recent identification of fructosamine 3 kinase (FN3K) has unveiled that fructosamines can be physiologically repaired, so that the FN3K enzyme could be considered a new form of protein repair.	Fructosamine	81-94	fructosamine 3 kinase	Homo sapiens	34-55
18334852-2	2007	Instead, recent identification of fructosamine 3 kinase (FN3K) has unveiled that fructosamines can be physiologically repaired, so that the FN3K enzyme could be considered a new form of protein repair.	Fructosamine	81-94	fructosamine 3 kinase	Homo sapiens	57-61
18334852-2	2007	Instead, recent identification of fructosamine 3 kinase (FN3K) has unveiled that fructosamines can be physiologically repaired, so that the FN3K enzyme could be considered a new form of protein repair.	Fructosamine	81-94	fructosamine 3 kinase	Homo sapiens	140-144
17072594-1	2006	Fructosamine-3-kinase (FN3K) mediates the regeneration of lysine from fructosamines formed on proteins as a result of the "early" Maillard reaction.	Lysine	58-64	fructosamine 3 kinase	Homo sapiens	0-21
17072594-1	2006	Fructosamine-3-kinase (FN3K) mediates the regeneration of lysine from fructosamines formed on proteins as a result of the "early" Maillard reaction.	Lysine	58-64	fructosamine 3 kinase	Homo sapiens	23-27
17072594-1	2006	Fructosamine-3-kinase (FN3K) mediates the regeneration of lysine from fructosamines formed on proteins as a result of the "early" Maillard reaction.	Fructosamine	70-83	fructosamine 3 kinase	Homo sapiens	0-21
17072594-1	2006	Fructosamine-3-kinase (FN3K) mediates the regeneration of lysine from fructosamines formed on proteins as a result of the "early" Maillard reaction.	Fructosamine	70-83	fructosamine 3 kinase	Homo sapiens	23-27
17072594-2	2006	As fructosamines and advanced glycation endproducts derived therefrom are supposed to play an adverse role in the development of diabetic complications, FN3K is discussed as a protein-repairing enzyme.	Fructosamine	3-16	fructosamine 3 kinase	Homo sapiens	153-157
17072594-4	2006	The assay is based on the FN3K-dependent conversion of the synthetic UV-active fructosamine Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine (BzGFruK) to Nalpha-hippuryl-Nepsilon-(phosphofructosyl)lysine (BzGpFruK).	Fructosamine	79-91	fructosamine 3 kinase	Homo sapiens	26-30
17072594-4	2006	The assay is based on the FN3K-dependent conversion of the synthetic UV-active fructosamine Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine (BzGFruK) to Nalpha-hippuryl-Nepsilon-(phosphofructosyl)lysine (BzGpFruK).	nalpha-hippuryl-nepsilon-(1-deoxy-d-fructosyl)lysine	92-144	fructosamine 3 kinase	Homo sapiens	26-30
17072594-4	2006	The assay is based on the FN3K-dependent conversion of the synthetic UV-active fructosamine Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine (BzGFruK) to Nalpha-hippuryl-Nepsilon-(phosphofructosyl)lysine (BzGpFruK).	bzgfruk	146-153	fructosamine 3 kinase	Homo sapiens	26-30
17072594-4	2006	The assay is based on the FN3K-dependent conversion of the synthetic UV-active fructosamine Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine (BzGFruK) to Nalpha-hippuryl-Nepsilon-(phosphofructosyl)lysine (BzGpFruK).	nalpha-hippuryl-nepsilon-(phosphofructosyl)lysine	158-207	fructosamine 3 kinase	Homo sapiens	26-30
17072594-4	2006	The assay is based on the FN3K-dependent conversion of the synthetic UV-active fructosamine Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine (BzGFruK) to Nalpha-hippuryl-Nepsilon-(phosphofructosyl)lysine (BzGpFruK).	bzgpfruk	209-217	fructosamine 3 kinase	Homo sapiens	26-30
16523184-1	2006	BACKGROUND: Part of the fructosamines that are bound to intracellular proteins are repaired by fructosamine 3-kinase (FN3K).	Fructosamine	24-37	fructosamine 3 kinase	Homo sapiens	118-122
15705060-1	2005	FN3K (fructosamine 3-kinase) is a mammalian enzyme that catalyses the phosphorylation of fructosamines, which thereby becomes unstable and detaches from proteins.	Fructosamine	89-102	fructosamine 3 kinase	Homo sapiens	0-4
16359826-2	2006	While this process has been viewed traditionally as entirely non-enzymatic and unidirectional, the discovery of fructosamine-3-phosphate (FN3K) and identification of FN3K-mediated deglycation mechanisms have made it apparent that non-enzymatic glycation is not unidirectional and that it can be reversed by deglycation reactions.	fructosamine-3-phosphate	112-136	fructosamine 3 kinase	Homo sapiens	138-142
16359826-3	2006	While FN3K operates on ketosamines, the second intermediate in the non-enzymatic glycation cascade, we recently identified another potential deglycation mechanism that can operate on Schiff bases, the first intermediates of the non-enzymatic glycation process.	ketosamines	23-34	fructosamine 3 kinase	Homo sapiens	6-10
16359826-3	2006	While FN3K operates on ketosamines, the second intermediate in the non-enzymatic glycation cascade, we recently identified another potential deglycation mechanism that can operate on Schiff bases, the first intermediates of the non-enzymatic glycation process.	Schiff Bases	183-195	fructosamine 3 kinase	Homo sapiens	6-10
15705060-1	2005	FN3K (fructosamine 3-kinase) is a mammalian enzyme that catalyses the phosphorylation of fructosamines, which thereby becomes unstable and detaches from proteins.	Fructosamine	89-102	fructosamine 3 kinase	Homo sapiens	6-27
15922110-0	2005	Intrinsic toxicity of glucose, due to non-enzymatic glycation, is controlled in-vivo by deglycation systems including: FN3K-mediated deglycation of fructosamines and transglycation of aldosamines.	Fructosamine	148-161	fructosamine 3 kinase	Homo sapiens	119-123
16037312-2	2005	Over the past several years we and others have shown that in cells this nonenzymatic process can be reversed by an ATP-dependent reaction catalyzed by fructosamine-3-kinase (FN3K) and possibly by its isozyme, fructosamine-3-kinase-related protein (FN3KRP).	Adenosine Triphosphate	115-118	fructosamine 3 kinase	Homo sapiens	151-172
16037312-2	2005	Over the past several years we and others have shown that in cells this nonenzymatic process can be reversed by an ATP-dependent reaction catalyzed by fructosamine-3-kinase (FN3K) and possibly by its isozyme, fructosamine-3-kinase-related protein (FN3KRP).	Adenosine Triphosphate	115-118	fructosamine 3 kinase	Homo sapiens	174-178
16037312-3	2005	In this study we provide the first evidence that this FN3K-dependent deglycation, acting on the Amadori products, is complemented by another deglycation process operating on the very first product of nonenzymatic glycation, glucosylamines (Schiff"s bases).	glucosylamines	224-238	fructosamine 3 kinase	Homo sapiens	54-58
16037312-3	2005	In this study we provide the first evidence that this FN3K-dependent deglycation, acting on the Amadori products, is complemented by another deglycation process operating on the very first product of nonenzymatic glycation, glucosylamines (Schiff"s bases).	schiff"s bases	240-254	fructosamine 3 kinase	Homo sapiens	54-58
15694695-5	2005	A mammalian fructosamine-3-kinase (FN-3-K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate has been isolated and cloned by two independent groups.	fructosyl-lysine	65-79	fructosamine 3 kinase	Homo sapiens	12-33
15694695-5	2005	A mammalian fructosamine-3-kinase (FN-3-K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate has been isolated and cloned by two independent groups.	fructosyl-lysine	65-79	fructosamine 3 kinase	Homo sapiens	35-41
15694695-5	2005	A mammalian fructosamine-3-kinase (FN-3-K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate has been isolated and cloned by two independent groups.	fructosyl-lysine	81-83	fructosamine 3 kinase	Homo sapiens	12-33
15694695-5	2005	A mammalian fructosamine-3-kinase (FN-3-K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate has been isolated and cloned by two independent groups.	fructosyl-lysine	81-83	fructosamine 3 kinase	Homo sapiens	35-41
15694695-5	2005	A mammalian fructosamine-3-kinase (FN-3-K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate has been isolated and cloned by two independent groups.	fl-3-phosphate	119-133	fructosamine 3 kinase	Homo sapiens	12-33
15694695-5	2005	A mammalian fructosamine-3-kinase (FN-3-K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate has been isolated and cloned by two independent groups.	fl-3-phosphate	119-133	fructosamine 3 kinase	Homo sapiens	35-41
15922110-7	2005	We propose that of the two pathways, the FN3K-independent mechanism is more important due to the fact that it breaks down the very first intermediate of the Maillard reaction, the Schiff base (a.k.a aldosamine).	Schiff Bases	180-191	fructosamine 3 kinase	Homo sapiens	41-45
15922110-7	2005	We propose that of the two pathways, the FN3K-independent mechanism is more important due to the fact that it breaks down the very first intermediate of the Maillard reaction, the Schiff base (a.k.a aldosamine).	aldosamine	199-209	fructosamine 3 kinase	Homo sapiens	41-45
15922110-8	2005	We postulate that this, FN3K-independent, deglycation occurs by transglycation, in which carbohydrate moieties of glycated amines, such as glucoselysines on proteins, are removed by intracellular nucleophiles including free amino acids and peptides such as glutathione, carnosine and anserine.	Carbohydrates	89-101	fructosamine 3 kinase	Homo sapiens	24-28
15922110-8	2005	We postulate that this, FN3K-independent, deglycation occurs by transglycation, in which carbohydrate moieties of glycated amines, such as glucoselysines on proteins, are removed by intracellular nucleophiles including free amino acids and peptides such as glutathione, carnosine and anserine.	Amines	123-129	fructosamine 3 kinase	Homo sapiens	24-28
15137908-1	2004	Fructosamine 3-kinase (FN3K), an enzyme initially identified in erythrocytes, catalyses the phosphorylation of fructosamines on their third carbon, leading to their destabilization and their removal from protein.	Fructosamine	111-124	fructosamine 3 kinase	Homo sapiens	0-21
15137908-1	2004	Fructosamine 3-kinase (FN3K), an enzyme initially identified in erythrocytes, catalyses the phosphorylation of fructosamines on their third carbon, leading to their destabilization and their removal from protein.	Fructosamine	111-124	fructosamine 3 kinase	Homo sapiens	23-27
15137908-4	2004	NMR analysis indicated that 1-deoxy-1-morpholinopsicose (DMP, a substrate for FN3K and FN3K-RP), like 1-deoxy-1-morpholinofructose (DMF, a substrate of FN3K), penetrated erythrocytes and was converted into the corresponding 3-phospho-derivative.	1-deoxy-1-morpholino-psicose	57-60	fructosamine 3 kinase	Homo sapiens	87-91
15137908-1	2004	Fructosamine 3-kinase (FN3K), an enzyme initially identified in erythrocytes, catalyses the phosphorylation of fructosamines on their third carbon, leading to their destabilization and their removal from protein.	Carbon	140-146	fructosamine 3 kinase	Homo sapiens	0-21
15137908-4	2004	NMR analysis indicated that 1-deoxy-1-morpholinopsicose (DMP, a substrate for FN3K and FN3K-RP), like 1-deoxy-1-morpholinofructose (DMF, a substrate of FN3K), penetrated erythrocytes and was converted into the corresponding 3-phospho-derivative.	1-deoxy-1-morpholinofructose	102-130	fructosamine 3 kinase	Homo sapiens	87-91
15137908-6	2004	1.9-2.6-fold higher if DMP, a competitive inhibitor of both FN3K and FN3K-RP, was present in the incubation medium.	1-deoxy-1-morpholino-psicose	23-26	fructosamine 3 kinase	Homo sapiens	60-64
15137908-1	2004	Fructosamine 3-kinase (FN3K), an enzyme initially identified in erythrocytes, catalyses the phosphorylation of fructosamines on their third carbon, leading to their destabilization and their removal from protein.	Carbon	140-146	fructosamine 3 kinase	Homo sapiens	23-27
15137908-8	2004	By contrast, DMF, a specific inhibitor of FN3K, only affected the glucose-dependent accumulation of glycated haemoglobin and ketoamine 3-phosphates.	1-deoxy-1-morpholinofructose	13-16	fructosamine 3 kinase	Homo sapiens	42-46
15137908-4	2004	NMR analysis indicated that 1-deoxy-1-morpholinopsicose (DMP, a substrate for FN3K and FN3K-RP), like 1-deoxy-1-morpholinofructose (DMF, a substrate of FN3K), penetrated erythrocytes and was converted into the corresponding 3-phospho-derivative.	1-deoxy-1-morpholino-psicose	57-60	fructosamine 3 kinase	Homo sapiens	78-82
15137908-8	2004	By contrast, DMF, a specific inhibitor of FN3K, only affected the glucose-dependent accumulation of glycated haemoglobin and ketoamine 3-phosphates.	Glucose	66-73	fructosamine 3 kinase	Homo sapiens	42-46
15366734-2	2004	Quite to the contrary, a mammalian enzyme, fructosamine 3-kinase, has recently been identified, which phosphorylates fructosamines on their third carbon, making them unstable and leading to their shedding from proteins.	Fructosamine	117-130	fructosamine 3 kinase	Homo sapiens	43-64
15137908-8	2004	By contrast, DMF, a specific inhibitor of FN3K, only affected the glucose-dependent accumulation of glycated haemoglobin and ketoamine 3-phosphates.	ketoamine 3-phosphates	125-147	fructosamine 3 kinase	Homo sapiens	42-46
15102834-0	2004	Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin.	Fructosamine	18-30	fructosamine 3 kinase	Homo sapiens	54-75
15102834-1	2004	Fructosamine-3-kinase (FN3K) phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein.	Fructosamine	44-56	fructosamine 3 kinase	Homo sapiens	0-21
15102834-1	2004	Fructosamine-3-kinase (FN3K) phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein.	Fructosamine	44-56	fructosamine 3 kinase	Homo sapiens	23-27
15102834-2	2004	Support for the occurrence of this deglycation mechanism in intact cells has been obtained by showing that hemoglobin is significantly more glycated when human erythrocytes are incubated with an elevated glucose concentration in the presence of 1-deoxy-1-morpholinofructose (DMF), a cell-permeable inhibitor of FN3K, than in its absence.	Glucose	204-211	fructosamine 3 kinase	Homo sapiens	311-315
15102834-3	2004	The aim of this work was to identify the fructosamine residues on hemoglobin that are removed as a result of the action of FN3K in intact erythrocytes.	Fructosamine	41-53	fructosamine 3 kinase	Homo sapiens	123-127
15102834-10	2004	The radiolabeled peptides containing reduced fructosamine 3-phosphates bound to Lys-alpha-16, Lys-alpha-139, and Lys-beta-17 were much less abundant if the hemoglobin substrate used for the in vitro phosphorylation with FN3K and [gamma-(32)P]ATP came from erythrocytes incubated with an elevated glucose concentration in the absence of DMF, indicating that these lysine residues had been substantially deglycated in intact cells when FN3K action was unrefrained.	fructosamine 3-phosphates	45-70	fructosamine 3 kinase	Homo sapiens	220-224
15102834-10	2004	The radiolabeled peptides containing reduced fructosamine 3-phosphates bound to Lys-alpha-16, Lys-alpha-139, and Lys-beta-17 were much less abundant if the hemoglobin substrate used for the in vitro phosphorylation with FN3K and [gamma-(32)P]ATP came from erythrocytes incubated with an elevated glucose concentration in the absence of DMF, indicating that these lysine residues had been substantially deglycated in intact cells when FN3K action was unrefrained.	fructosamine 3-phosphates	45-70	fructosamine 3 kinase	Homo sapiens	434-438
15366734-2	2004	Quite to the contrary, a mammalian enzyme, fructosamine 3-kinase, has recently been identified, which phosphorylates fructosamines on their third carbon, making them unstable and leading to their shedding from proteins.	Carbon	146-152	fructosamine 3 kinase	Homo sapiens	43-64
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fructosyl-lysine	132-146	fructosamine 3 kinase	Homo sapiens	81-102
14641081-4	2003	These include, among others, the fact that while the apparent deglycation mechanism does not operate on L-glucose, semi-purified FN3K appears to be able to use both D- and L-fructosamines as substrates.	d- and l-fructosamines	165-187	fructosamine 3 kinase	Homo sapiens	129-133
14633848-0	2003	A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines.	psicosamines	91-103	fructosamine 3 kinase	Homo sapiens	34-55
14633848-0	2003	A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines.	ribulosamines	108-121	fructosamine 3 kinase	Homo sapiens	34-55
14633848-0	2003	A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines.	Fructosamine	133-146	fructosamine 3 kinase	Homo sapiens	34-55
14633848-1	2003	Fructosamine-3-kinase (FN3K) is an enzyme that appears to be responsible for the removal of fructosamines from proteins.	Fructosamine	92-105	fructosamine 3 kinase	Homo sapiens	0-21
14633848-1	2003	Fructosamine-3-kinase (FN3K) is an enzyme that appears to be responsible for the removal of fructosamines from proteins.	Fructosamine	92-105	fructosamine 3 kinase	Homo sapiens	23-27
14633848-11	2003	This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines.	Fructosamine	131-144	fructosamine 3 kinase	Homo sapiens	23-44
14641062-4	2003	Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates.	Fructosamine	98-111	fructosamine 3 kinase	Homo sapiens	0-21
14641062-4	2003	Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates.	Carbon	125-131	fructosamine 3 kinase	Homo sapiens	0-21
14641062-4	2003	Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates.	deoxyfructose	141-154	fructosamine 3 kinase	Homo sapiens	0-21
14641062-4	2003	Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates.	fructosamine 3-phosphates	191-216	fructosamine 3 kinase	Homo sapiens	0-21
11975663-1	2002	Fructosamine 3-kinase, which phosphorylates low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, is quite active in erythrocytes, and was proposed to initiate a process removing fructosamine residues from proteins.	Fructosamine	81-94	fructosamine 3 kinase	Homo sapiens	0-21
11975663-1	2002	Fructosamine 3-kinase, which phosphorylates low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, is quite active in erythrocytes, and was proposed to initiate a process removing fructosamine residues from proteins.	Carbon	108-114	fructosamine 3 kinase	Homo sapiens	0-21
11975663-1	2002	Fructosamine 3-kinase, which phosphorylates low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, is quite active in erythrocytes, and was proposed to initiate a process removing fructosamine residues from proteins.	deoxyfructose	124-137	fructosamine 3 kinase	Homo sapiens	0-21
11975663-1	2002	Fructosamine 3-kinase, which phosphorylates low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, is quite active in erythrocytes, and was proposed to initiate a process removing fructosamine residues from proteins.	Fructosamine	81-93	fructosamine 3 kinase	Homo sapiens	0-21
11975663-4	2002	1-Deoxy-1-morpholinofructose (DMF), a substrate and competitive inhibitor of fructosamine 3-kinase, doubled the rate of accumulation of glycated haemoglobin, but markedly decreased the amount of haemoglobin containing alkali-labile phosphate.	1-deoxy-1-morpholinofructose	0-28	fructosamine 3 kinase	Homo sapiens	77-98
11975663-4	2002	1-Deoxy-1-morpholinofructose (DMF), a substrate and competitive inhibitor of fructosamine 3-kinase, doubled the rate of accumulation of glycated haemoglobin, but markedly decreased the amount of haemoglobin containing alkali-labile phosphate.	1-deoxy-1-morpholinofructose	30-33	fructosamine 3 kinase	Homo sapiens	77-98
11975663-4	2002	1-Deoxy-1-morpholinofructose (DMF), a substrate and competitive inhibitor of fructosamine 3-kinase, doubled the rate of accumulation of glycated haemoglobin, but markedly decreased the amount of haemoglobin containing alkali-labile phosphate.	Phosphates	232-241	fructosamine 3 kinase	Homo sapiens	77-98
11975663-7	2002	These effects were prevented by DMF, indicating that fructosamine 3-kinase is involved in the removal of fructosamine residues.	1-deoxy-1-morpholinofructose	32-35	fructosamine 3 kinase	Homo sapiens	53-74
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fructosyl-lysine	132-146	fructosamine 3 kinase	Homo sapiens	104-108
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fructosyl-lysine	148-150	fructosamine 3 kinase	Homo sapiens	81-102
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fructosyl-lysine	148-150	fructosamine 3 kinase	Homo sapiens	104-108
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fl-3-phosphate	186-200	fructosamine 3 kinase	Homo sapiens	81-102
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fl-3-phosphate	186-200	fructosamine 3 kinase	Homo sapiens	104-108
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fl3p	202-206	fructosamine 3 kinase	Homo sapiens	81-102
11522682-3	2001	In this report, we describe the purification and characterization of a mammalian fructosamine-3-kinase (FN3K), which phosphorylates fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P).	fl3p	202-206	fructosamine 3 kinase	Homo sapiens	104-108
11522682-8	2001	The lability of FL3P, the high affinity of FN3K for FL, and the wide distribution of FN3K suggest that the function of this enzyme is deglycation of nonenzymatically glycated proteins.	fl3p	16-20	fructosamine 3 kinase	Homo sapiens	85-89
11522682-9	2001	Because the condensation of glucose and lysine residues is an ubiquitous and unavoidable process in homeothermic organisms, a deglycation system mediated by FN3K may be an important factor in protecting cells from the deleterious effects of nonenzymatic glycation.	Glucose	28-35	fructosamine 3 kinase	Homo sapiens	157-161
11522682-9	2001	Because the condensation of glucose and lysine residues is an ubiquitous and unavoidable process in homeothermic organisms, a deglycation system mediated by FN3K may be an important factor in protecting cells from the deleterious effects of nonenzymatic glycation.	Lysine	40-46	fructosamine 3 kinase	Homo sapiens	157-161
11016445-12	2000	The physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins.	fructosyl-lysine	111-125	fructosamine 3 kinase	Homo sapiens	30-51
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
34314247-8	2021	It operates intracellularly by catalyzing ATP-dependent removal of Maillard adducts, D-fructoselysines, from proteins thereby reducing the Maillard reaction flux from glucose to AGE"s When FN3K was isolated, a closely related but distinct protein copurified with it.	Adenosine Triphosphate	42-45	fructosamine 3 kinase	Homo sapiens	189-193
34314247-8	2021	It operates intracellularly by catalyzing ATP-dependent removal of Maillard adducts, D-fructoselysines, from proteins thereby reducing the Maillard reaction flux from glucose to AGE"s When FN3K was isolated, a closely related but distinct protein copurified with it.	d-fructoselysines	85-102	fructosamine 3 kinase	Homo sapiens	189-193
34314247-8	2021	It operates intracellularly by catalyzing ATP-dependent removal of Maillard adducts, D-fructoselysines, from proteins thereby reducing the Maillard reaction flux from glucose to AGE"s When FN3K was isolated, a closely related but distinct protein copurified with it.	Glucose	167-174	fructosamine 3 kinase	Homo sapiens	189-193
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
33466626-7	2021	FN3K is a unique protein that mediates deglycation by phosphorylating basic amino acids lysine and arginine in various proteins such as Nrf2.	Amino Acids, Basic	70-87	fructosamine 3 kinase	Homo sapiens	0-4
33466626-7	2021	FN3K is a unique protein that mediates deglycation by phosphorylating basic amino acids lysine and arginine in various proteins such as Nrf2.	Lysine	88-94	fructosamine 3 kinase	Homo sapiens	0-4
33466626-7	2021	FN3K is a unique protein that mediates deglycation by phosphorylating basic amino acids lysine and arginine in various proteins such as Nrf2.	Arginine	99-107	fructosamine 3 kinase	Homo sapiens	0-4
32899850-3	2020	AGE-type autofluorescence was measured to evaluate the effects of FN3K on glycolaldehyde-induced AGE-modified neural porcine retinas and unmodified human neural retinas.	glycolaldehyde	74-88	fructosamine 3 kinase	Homo sapiens	66-70
33208304-5	2020	Serum FN3K protein and AGE levels were assessed by ELISA in patients with COPD exacerbations receiving metformin.	Metformin	103-112	fructosamine 3 kinase	Homo sapiens	6-10
33208304-10	2020	Metformin enhanced systemic levels of FN3K in COPD subjects independent of their high-expression or low-expression status.	Metformin	0-9	fructosamine 3 kinase	Homo sapiens	38-42
33208304-11	2020	DISCUSSION: The data highlight that low and high FN3K expressors exist within our study cohort and metformin induces FN3K levels, highlighting a potential mechanism to reduce the risk of CVD comorbidity and mortality.	Metformin	99-108	fructosamine 3 kinase	Homo sapiens	117-121
32899850-5	2020	Automated optical image analysis of human tissue sections was performed to compare control- and FN3K-treated drusen and near-infrared (NIR) microspectroscopy was performed to examine biochemical differences.	drusen	109-115	fructosamine 3 kinase	Homo sapiens	96-100
32899850-6	2020	Optical coherence tomography (OCT) was used to evaluate the effect of FN3K on drusenoid deposits after treatment of post-mortem human eyes.	drusenoid	78-87	fructosamine 3 kinase	Homo sapiens	70-74
32390412-7	2020	Finally, we establish that the known oncoprotein and hexose deglycase, fructosamine 3-kinase (FN3K), recognizes and facilitates the removal of 5-AR glycation adducts in live cells, supporting the dynamic regulation of ribose glycation as well as validating the probe as a new chemical tool to monitor FN3K activity.	Ribose	218-224	fructosamine 3 kinase	Homo sapiens	71-92
32636308-3	2020	The crystal structure of the FN3K homolog from Arabidopsis thaliana revealed that it forms an unexpected strand-exchange dimer in which the ATP-binding P-loop and adjoining beta strands are swapped between two chains in the dimer.	Adenosine Triphosphate	140-143	fructosamine 3 kinase	Homo sapiens	29-33
32636308-5	2020	Mutational analysis and solution studies confirmed that the strained disulfides function as redox "switches" to reversibly regulate the activity and dimerization of FN3K.	Disulfides	69-79	fructosamine 3 kinase	Homo sapiens	165-169
32636308-6	2020	Human FN3K, which contains an equivalent P-loop Cys, was also redox sensitive, whereas ancestral bacterial FN3K homologs, which lack a P-loop Cys, were not.	Cysteine	48-51	fructosamine 3 kinase	Homo sapiens	6-10
32636308-6	2020	Human FN3K, which contains an equivalent P-loop Cys, was also redox sensitive, whereas ancestral bacterial FN3K homologs, which lack a P-loop Cys, were not.	Cysteine	142-145	fructosamine 3 kinase	Homo sapiens	6-10
32636308-7	2020	Furthermore, CRISPR-mediated knockout of FN3K in human liver cancer cells altered the abundance of redox metabolites, including an increase in glutathione.	Glutathione	143-154	fructosamine 3 kinase	Homo sapiens	41-45
32390412-7	2020	Finally, we establish that the known oncoprotein and hexose deglycase, fructosamine 3-kinase (FN3K), recognizes and facilitates the removal of 5-AR glycation adducts in live cells, supporting the dynamic regulation of ribose glycation as well as validating the probe as a new chemical tool to monitor FN3K activity.	Ribose	218-224	fructosamine 3 kinase	Homo sapiens	94-98
32390412-7	2020	Finally, we establish that the known oncoprotein and hexose deglycase, fructosamine 3-kinase (FN3K), recognizes and facilitates the removal of 5-AR glycation adducts in live cells, supporting the dynamic regulation of ribose glycation as well as validating the probe as a new chemical tool to monitor FN3K activity.	Ribose	218-224	fructosamine 3 kinase	Homo sapiens	301-305
31398338-5	2019	N-acetyl cysteine treatment partially rescues the effects of FN3K loss on NRF2 driven tumor phenotypes indicating a key role for NRF2-mediated redox balance.	Acetylcysteine	0-17	fructosamine 3 kinase	Homo sapiens	61-65
28287856-6	2018	FN3K inhibitor, 1-deoxy-1-morpholinofructose, suppressed only about 20% of CS-0777 phosphorylation activity in human erythrocyte lysate.	1-deoxy-1-morpholinofructose	16-44	fructosamine 3 kinase	Homo sapiens	0-4
28287856-6	2018	FN3K inhibitor, 1-deoxy-1-morpholinofructose, suppressed only about 20% of CS-0777 phosphorylation activity in human erythrocyte lysate.	Cesium	75-77	fructosamine 3 kinase	Homo sapiens	0-4
28287856-2	2018	CS-0777, a candidate compound for autoimmune diseases, becomes phosphorylated active metabolite, M1, by fructosamine 3-kinase (FN3K), FN3K-related protein (FN3K-RP); and M1 is reverted back to CS-0777 by alkaline phosphatase (ALP) in the body.	Cesium	0-2	fructosamine 3 kinase	Homo sapiens	104-125
28287856-2	2018	CS-0777, a candidate compound for autoimmune diseases, becomes phosphorylated active metabolite, M1, by fructosamine 3-kinase (FN3K), FN3K-related protein (FN3K-RP); and M1 is reverted back to CS-0777 by alkaline phosphatase (ALP) in the body.	Cesium	0-2	fructosamine 3 kinase	Homo sapiens	127-131
28287856-2	2018	CS-0777, a candidate compound for autoimmune diseases, becomes phosphorylated active metabolite, M1, by fructosamine 3-kinase (FN3K), FN3K-related protein (FN3K-RP); and M1 is reverted back to CS-0777 by alkaline phosphatase (ALP) in the body.	Cesium	193-195	fructosamine 3 kinase	Homo sapiens	104-125
28287856-3	2018	We performed enzyme kinetic analysis of phosphorylation of CS-0777 by FN3K, FN3K-RP, human erythrocytes and human platelets; and dephosphorylation of M1 by various ALP isozymes and human liver, kidney, lung and small intestine microsomes.	Cesium	59-61	fructosamine 3 kinase	Homo sapiens	70-74
28287856-5	2018	The Michaelis constants of human FN3K, FN3K-RP and erythrocytes for CS-0777 phosphorylation were in the range from 498 muM to 1060 muM.	Cesium	68-70	fructosamine 3 kinase	Homo sapiens	33-37