Structural basis for FN3K-mediated protein deglycation.
Lokhandwala J, Matlack JK, Smalley TB, Miner RE 3rd, Tran TH, Binning JM.,

A redox-active switch in fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily.
Shrestha S, Katiyar S, Sanz-Rodriguez CE, Kemppinen NR, Kim HW, Kadirvelraj R, Panagos C, Keyhaninejad N, Colonna M, Chopra P, Byrne DP, Boons GJ, van der Knaap E, Eyers PA, Edison AS, Wood ZA, Kannan N., Free PMC Article

FN3K expression in COPD: a potential comorbidity factor for cardiovascular disease.
Alderawi A, Caramori G, Baker EH, Hitchings AW, Rahman I, Rossios C, Adcock I, Cassolari P, Papi A, Ortega VE, Curtis JL, Dunmore S, Kirkham P., Free PMC Article

The Oncogenic Action of NRF2 Depends on De-glycation by Fructosamine-3-Kinase.
Sanghvi VR, Leibold J, Mina M, Mohan P, Berishaj M, Li Z, Miele MM, Lailler N, Zhao C, de Stanchina E, Viale A, Akkari L, Lowe SW, Ciriello G, Hendrickson RC, Wendel HG., Free PMC Article

The association between fructosamine-3 kinase 900C/G polymorphism, transferrin polymorphism and human herpesvirus-8 infection in diabetics living in South Kivu.
Cikomola JC, Vandepoele K, Katchunga PB, Kishabongo AS, Padalko EY, Speeckaert MM, Delanghe JR.

Possible role of fructosamine 3-kinase genotyping for the management of diabetic patients.
Avemaria F, Carrera P, Lapolla A, Sartore G, Chilelli NC, Paleari R, Ambrosi A, Ferrari M, Mosca A.

Fructosamine 3-kinase and glyoxalase I polymorphisms and their association with soluble RAGE and adhesion molecules in diabetes.
Škrha J Jr, Muravská A, Flekač M, Horová E, Novák J, Novotný A, Prázný M, Škrha J, Kvasnička J, Landová L, Jáchymová M, Zima T, Kalousová M.

Genetic variability in enzymes of metabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality.
Tanhäuserová V, Kuricová K, Pácal L, Bartáková V, Rehořová J, Svojanovský J, Olšovský J, Bělobrádková J, Kaňková K.

Genetic variability of the fructosamine 3-kinase gene in diabetic patients.
Mosca L, Penco S, Patrosso MC, Marocchi A, Lapolla A, Sartore G, Chilelli NC, Paleari R, Mosca A.

Low red blood cell levels of deglycating enzymes in colorectal cancer patients.
Notarnicola M, Caruso MG, Tutino V, Guerra V, Misciagna G., Free PMC Article

Common variants at 10 genomic loci influence hemoglobin A₁(C) levels via glycemic and nonglycemic pathways.
Soranzo N, Sanna S, Wheeler E, Gieger C, Radke D, Dupuis J, Bouatia-Naji N, Langenberg C, Prokopenko I, Stolerman E, Sandhu MS, Heeney MM, Devaney JM, Reilly MP, Ricketts SL, Stewart AF, Voight BF, Willenborg C, Wright B, Altshuler D, Arking D, Balkau B, Barnes D, Boerwinkle E, Böhm B, Bonnefond A, Bonnycastle LL, Boomsma DI, Bornstein SR, Böttcher Y, Bumpstead S, Burnett-Miller MS, Campbell H, Cao A, Chambers J, Clark R, Collins FS, Coresh J, de Geus EJ, Dei M, Deloukas P, Döring A, Egan JM, Elosua R, Ferrucci L, Forouhi N, Fox CS, Franklin C, Franzosi MG, Gallina S, Goel A, Graessler J, Grallert H, Greinacher A, Hadley D, Hall A, Hamsten A, Hayward C, Heath S, Herder C, Homuth G, Hottenga JJ, Hunter-Merrill R, Illig T, Jackson AU, Jula A, Kleber M, Knouff CW, Kong A, Kooner J, Köttgen A, Kovacs P, Krohn K, Kühnel B, Kuusisto J, Laakso M, Lathrop M, Lecoeur C, Li M, Li M, Loos RJ, Luan J, Lyssenko V, Mägi R, Magnusson PK, Mälarstig A, Mangino M, Martínez-Larrad MT, März W, McArdle WL, McPherson R, Meisinger C, Meitinger T, Melander O, Mohlke KL, Mooser VE, Morken MA, Narisu N, Nathan DM, Nauck M, O'Donnell C, Oexle K, Olla N, Pankow JS, Payne F, Peden JF, Pedersen NL, Peltonen L, Perola M, Polasek O, Porcu E, Rader DJ, Rathmann W, Ripatti S, Rocheleau G, Roden M, Rudan I, Salomaa V, Saxena R, Schlessinger D, Schunkert H, Schwarz P, Seedorf U, Selvin E, Serrano-Ríos M, Shrader P, Silveira A, Siscovick D, Song K, Spector TD, Stefansson K, Steinthorsdottir V, Strachan DP, Strawbridge R, Stumvoll M, Surakka I, Swift AJ, Tanaka T, Teumer A, Thorleifsson G, Thorsteinsdottir U, Tönjes A, Usala G, Vitart V, Völzke H, Wallaschofski H, Waterworth DM, Watkins H, Wichmann HE, Wild SH, Willemsen G, Williams GH, Wilson JF, Winkelmann J, Wright AF, WTCCC, Zabena C, Zhao JH, Epstein SE, Erdmann J, Hakonarson HH, Kathiresan S, Khaw KT, Roberts R, Samani NJ, Fleming MD, Sladek R, Abecasis G, Boehnke M, Froguel P, Groop L, McCarthy MI, Kao WH, Florez JC, Uda M, Wareham NJ, Barroso I, Meigs JB., Free PMC Article

A polymorphism within the fructosamine-3-kinase gene is associated with HbA1c Levels and the onset of type 2 diabetes mellitus.
Mohás M, Kisfali P, Baricza E, Mérei A, Maász A, Cseh J, Mikolás E, Szijártó IA, Melegh B, Wittmann I, Mohás M, Kisfali P, Baricza E, Mérei A, Maász A, Cseh J, Mikolás E, Szijártó IA, Melegh B, Wittmann I.

A polymorphism within the fructosamine-3-kinase gene is associated with HbA1c Levels and the onset of type 2 diabetes mellitus.
Mohás M, Kisfali P, Baricza E, Mérei A, Maász A, Cseh J, Mikolás E, Szijártó IA, Melegh B, Wittmann I, Mohás M, Kisfali P, Baricza E, Mérei A, Maász A, Cseh J, Mikolás E, Szijártó IA, Melegh B, Wittmann I.

Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites.
Delpierre G, Veiga-da-Cunha M, Vertommen D, Buysschaert M, Van Schaftingen E.

The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinase-related protein appears to be constitutive and unaffected by environmental signals.
Conner JR, Beisswenger PJ, Szwergold BS.

Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin.
Delpierrre G, Vertommen D, Communi D, Rider MH, Van Schaftingen E.

Some clues as to the regulation, expression, function, and distribution of fructosamine-3-kinase and fructosamine-3-kinase-related protein.
Conner JR, Beisswenger PJ, Szwergold BS.

Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes.
Delpierre G, Collard F, Fortpied J, Van Schaftingen E., Free PMC Article

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).
Szwergold BS.