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ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
CS-0777
-
-
ir
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
ATP + 1-deoxy-1-morpholin-4-yl-D-psicose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-psicose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-ribulose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-ribulose
-
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
ATP + N-alpha-hippuryl-N-epsilon-psicosyllysine
ADP + ?
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
ATP + N2-(1-deoxy-D-fructosyl)-glycylglycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycylglycine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-L-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-L-valine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
ATP + N5-D-fructosyl-L-ornithine
ADP + N5-(O3-phosphono-D-fructosyl)-L-ornithine
-
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-L-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-L-lysine
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
ATP + N6-D-fructosyl-L-lysine
ADP + N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
-
-
-
?
ATP + Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine
ADP + Nalpha-hippuryl-Nepsilon-(1-deoxy-3-phospho-D-fructosyl)lysine
-
-
Nalpha-hippuryl-Nepsilon-(3-phosphofructosyl)lysine like other 3-phosphofructosylamines, is not stable. Terminating the enzyme reaction with trichloracetic acid stabilises the analyte
-
?
ATP + [hemoglobin]-N6-D-fructosyl-L-lysine
ADP + [hemoglobin]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
mass-spectrometric identification of the fructosamine residues that are removed from hemoglobin in intact erythrocytes as a result of the action of fructosamine-3-kinase: Lys16, Lys61 and Lys139 in the alpha-chain of hemoglobin, Val1, Lys17, Lys59, Lys66, Lys132, and Lys144 in the beta-chain of hemoglobin. Some (e.g. Lys139 in the alph-chain of hemoglobin) are readily phosphorylated to a maximal extent by fructosamine-3-kinase in vitro whereas others (e.g. Val1 in the beta-chain of hemoglobin) are slowly and only very partially phosphorylated
-
-
?
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
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?
glycated bovine serum albumin + ATP
?
derived from dialyzed glycated bovine serum albumin
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-
?
additional information
?
-
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose

ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + D-fructose

ADP + O3-phosphono-D-fructose
-
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
-
Vmax is 35% of the value for N6-D-fructosyl-L-lysine
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine

ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine

ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine

ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine

ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine

ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Spontaneous conversion of fructosamine 3-phosphates into 3-deoxyglucosone
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as protein-bound fructoselysines. The fructosamine most frequently encountered in nature is fructoselysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins and protecting cells from the deleterious effects of nonenzymatic glycation
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
protein repair mechanism. 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. The latter are unstable and spontaneously decompose into inorganic phosphate and 3-deoxyglucosone, with concomitant regeneration of the unglycated amine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
repairing glucose-mediated non-enzymatic modification of proteins. The function of fructosamine-3-kinase is seen in catalysing the ATP-dependent phosphorylation of the protein-bound fructosamine (Amadori compound) fructoselysine, which is the first stable intermediate resulting from the Maillard reaction between glucose and lysine, on its 3-hydroxy group to 3-phosphofructosyllysine. The phosphorylation destabilises the fructose-amine linkage leading to a spontaneous decomposition of 3-phosphofructosyllysine to the unmodified lysine residue as well as to 3-deoxyglucosulose and inorganic phosphate
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
[histone]-N6-D-fructosyl-L-lysine, [hemoglobin]-N6-D-fructosyl-L-lysine. Similar experiments with other glycated proteins, including bovine serum albumin, and lysozyme indicate that fructoselysine residues on glycated proteins are readily phosphorylated by fructosamine 3-kinase, apparently irrespective of the protein. Phosphorylation destablilizes the fructoselysine adduct and leads to its spontaneous decomposition
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone. This pathway appears to dominate 3-deoxyglucosone production in vivo, making it possible to modulate 3-deoxyglucosone levels by stimulating or inhibiting the reaction
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
additional information

?
-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
-
-
?
additional information
?
-
-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
-
-
?
additional information
?
-
-
the kinase is specific for 1-deoxy-1-amino fructose adducts and does not catalyze phosphorylation of other monosaccharides and polyols, such as glucose, galactose, mannose, glucosamine, galactosamine, or myo-inositol
-
-
?
additional information
?
-
development of a PLC-based assay with substrate N-alpha-hippuryl-N-epsilon-psicosyllysine for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes, method evaluation, overview
-
-
?
additional information
?
-
development of a simple colorimetric method for assaying FN3K activity in human body fluids
-
-
?
additional information
?
-
-
development of a simple colorimetric method for assaying FN3K activity in human body fluids
-
-
?
additional information
?
-
the fructosamines bound to Lys139alpha, located near the C-terminus of the alpha subunits, and Lys16alpha, located on a loop of the alpha subunits, are good substrates. The N-terminal glycated valine is a poor substrate, consistent with free fructosevaline being a much poorer substrate than free fructoselysine
-
-
?
additional information
?
-
-
the fructosamines bound to Lys139alpha, located near the C-terminus of the alpha subunits, and Lys16alpha, located on a loop of the alpha subunits, are good substrates. The N-terminal glycated valine is a poor substrate, consistent with free fructosevaline being a much poorer substrate than free fructoselysine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + (R)-1-(5-(3-amino-4-hydroxy-3-methylbutyl)-1-methyl-1H-pyrrol-2-yl)-4-(p-tolyl)butan-1-one
ADP + (2R)-2-amino-2-methyl-4-(1-methyl)-5-[4-(4-methylphenyl)butanoyl]-1H-pyrrol-2-yl)butyl dihydrogen phosphate
CS-0777
-
-
ir
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine

ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine

ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Spontaneous conversion of fructosamine 3-phosphates into 3-deoxyglucosone
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as protein-bound fructoselysines. The fructosamine most frequently encountered in nature is fructoselysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins and protecting cells from the deleterious effects of nonenzymatic glycation
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
protein repair mechanism. 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. The latter are unstable and spontaneously decompose into inorganic phosphate and 3-deoxyglucosone, with concomitant regeneration of the unglycated amine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
repairing glucose-mediated non-enzymatic modification of proteins. The function of fructosamine-3-kinase is seen in catalysing the ATP-dependent phosphorylation of the protein-bound fructosamine (Amadori compound) fructoselysine, which is the first stable intermediate resulting from the Maillard reaction between glucose and lysine, on its 3-hydroxy group to 3-phosphofructosyllysine. The phosphorylation destabilises the fructose-amine linkage leading to a spontaneous decomposition of 3-phosphofructosyllysine to the unmodified lysine residue as well as to 3-deoxyglucosulose and inorganic phosphate
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone. This pathway appears to dominate 3-deoxyglucosone production in vivo, making it possible to modulate 3-deoxyglucosone levels by stimulating or inhibiting the reaction
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.