J Delplanque, G Delpierre, FR Opperdoes, E … - Journal of Biological Chemistry, 2004 - ASBMB Fructosamine 3-kinase (FN3K) and FN3K-related protein (FN3K-RP) catalyze the
phosphorylation of the Amadori products ribulosamines, psicosamines, and, in the
case of FN3K, fructosamines. BLAST searches in chordate genomes revealed ... Cited by 18 - Related articles - BL Direct - All 5 versions
F Collard, E Wiame, N Bergans, J Fortpied, D … - Biochemical Journal, 2004 - pubmedcentral.nih.gov 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. We show that human ... Cited by 13 - Related articles - BL Direct - All 8 versions
J Fortpied, R Gemayel, V Stroobant, E Van … - Biochemical Journal, 2005 - pubmedcentral.nih.gov FN3K (fructosamine 3-kinase) is a mammalian enzyme that catalyses the
phosphorylation of fructosamines, which thereby becomes unstable and detaches
from proteins. The homologous mammalian enzyme, FN3K-RP (FN3K-related ... Cited by 11 - Related articles - All 8 versions
JR Conner, PJ Beisswenger, BS Szwergold - ANNALS-NEW YORK ACADEMY OF SCIENCES, 2005 - interscience.wiley.com Abstract: Fructosamine-3-kinase (FN3K) and the more recently discovered
fructosamine-3-kinase-related protein (FN3KRP) appear to protect proteins from
nonenzymatic glycation. To gain a better understanding of these enzymes we ... Cited by 11 - Related articles - BL Direct - All 5 versions
- ►nih.gov [PDF] E Wiame, E Van Schaftingen - Biochemical Journal, 2004 - pubmedcentral.nih.gov The frl (fructoselysine) operon encodes fructoselysine 6-kinase and
fructoselysine 6-phosphate deglycase, allowing the conver- sion of
fructoselysine into glucose 6-phosphate and lysine. We now show that a ... Cited by 11 - Related articles - BL Direct - All 8 versions
BS Szwergold, SK Howell, PJ Beisswenger - ANNALS-NEW YORK ACADEMY OF SCIENCES, 2005 - interscience.wiley.com Abstract: Nonenzymatic glycation is believed to play a major role in the
development of diabetic complications. Over the past several years we and others
have shown that in cells this nonenzymatic process can be reversed by an ... Cited by 9 - Related articles - BL Direct - All 5 versions
JR Conner, PJ Beisswenger, BS Szwergold - Biochemical and Biophysical Research …, 2004 - Elsevier Fructosamine-3-kinase (FN3K) and the more recently discovered
fructosamine-3-kinase related protein (FN3KRP) appear to protect proteins from
nonenzymatic glycation. To elucidate the patterns of transcriptional ... Cited by 7 - Related articles - All 5 versions
N Vaisman, E Niv, Y Izkhakov - Clinical Nutrition, 2006 - Elsevier A double-blind, placebo-controlled study. Twenty-six subjects with uncontrolled
NIDDM as indicated by high levels of hemoglobin A1C (Hgb A1c ) and 2-h
postprandial glucose levels >200 mg% were assigned to either fructose or ... Cited by 4 - Related articles - All 14 versions
M da-Cunha, P Jacquemin, G Delpierre, C … - Biochem. J, 2006 - biochemj.org Amines, including those present on proteins, spontaneously react with glucose to
form fructosamines in a reaction known as glycation. In the present paper, we
have explored, through a targeted gene inactivation approach, the role of ... Cited by 3 - Related articles - Cached - BL Direct - All 4 versions
R Gemayel, J Fortpied, R Rzem, D Vertommen … - FEBS journal, 2007 - interscience.wiley.com 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. FN3K homologues were identified in ≈ 200 (ie ... Cited by 2 - Related articles - BL Direct - All 5 versions
