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Volumn 51, Issue 3, 2016, Pages 150-161

New insights: A role for O-GlcNAcylation in diabetic complications

Author keywords

Cardiovascular disease; diabetes; diabetic nephropathy; diabetic retinopathy; glucose toxicity; hexosamine biosynthetic pathway; hyperglycemia; O GlcNAc

Indexed keywords

HEXOSAMINE; HYDROLASE; N ACETYLGLUCOSAMINE; O LINKED BETA N ACETYLGLUCOSAMINE; SERINE; THREONINE; TRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE;

EID: 84958036239     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2015.1135102     Document Type: Review
Times cited : (109)

References (111)
  • 1
    • 0042362101 scopus 로고    scopus 로고
    • Elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase in corneas of diabetic Goto-Kakizaki rats
    • Y.Akimoto, H.Kawakami, K.Yamamoto,. (2003). Elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase in corneas of diabetic Goto-Kakizaki rats. Invest Ophthalmol Vis Sci 44:3802–9
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 3802-3809
    • Akimoto, Y.1    Kawakami, H.2    Yamamoto, K.3
  • 2
    • 84860620024 scopus 로고    scopus 로고
    • Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4
    • Y.Akimoto, Y.Miura, T.Toda,. (2011). Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4. Clin Proteomics 8:15
    • (2011) Clin Proteomics , vol.8 , pp. 15
    • Akimoto, Y.1    Miura, Y.2    Toda, T.3
  • 3
    • 84975856269 scopus 로고    scopus 로고
    • Economic costs of diabetes in the U.S. in 2012
    • American Diabetes Association. (2013). Economic costs of diabetes in the U.S. in 2012. Diabetes Care 36:1033–46
    • (2013) Diabetes Care , vol.36 , pp. 1033-1046
  • 4
    • 34447515852 scopus 로고    scopus 로고
    • Glucose mediates the translocation of NeuroD1 by O-linked glycosylation
    • S.S.Andrali, Q.Qian, S.Ozcan (2007). Glucose mediates the translocation of NeuroD1 by O-linked glycosylation. J Biol Chem 282:15589–96
    • (2007) J Biol Chem , vol.282 , pp. 15589-15596
    • Andrali, S.S.1    Qian, Q.2    Ozcan, S.3
  • 5
    • 43749099640 scopus 로고    scopus 로고
    • Pdx1 and BETA2/NeuroD1 participate in a transcriptional complex that mediates short-range DNA looping at the insulin gene
    • D.A.Babu, S.K.Chakrabarti, J.C.Garmey, R.G.Mirmira (2008). Pdx1 and BETA2/NeuroD1 participate in a transcriptional complex that mediates short-range DNA looping at the insulin gene. J Biol Chem 283:8164–72
    • (2008) J Biol Chem , vol.283 , pp. 8164-8172
    • Babu, D.A.1    Chakrabarti, S.K.2    Garmey, J.C.3    Mirmira, R.G.4
  • 6
    • 33644698706 scopus 로고    scopus 로고
    • Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1
    • L.E.Ball, M.N.Berkaw, M.G.Buse (2006). Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1. Mol Cell Proteomics 5:313–23
    • (2006) Mol Cell Proteomics , vol.5 , pp. 313-323
    • Ball, L.E.1    Berkaw, M.N.2    Buse, M.G.3
  • 7
    • 84929191592 scopus 로고    scopus 로고
    • Diabetes-associated dysregulation of O-GlcNAcylation in rat cardiac mitochondria
    • P.S.Banerjee, J.Ma, G.W.Hart (2015). Diabetes-associated dysregulation of O-GlcNAcylation in rat cardiac mitochondria. Proc Natl Acad Sci USA, 112:6050–5
    • (2015) Proc Natl Acad Sci USA , vol.112 , pp. 6050-6055
    • Banerjee, P.S.1    Ma, J.2    Hart, G.W.3
  • 8
    • 0034034757 scopus 로고    scopus 로고
    • NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome
    • N.Boute, O.Gribouval, S.Roselli,. (2000). NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome. Nat Genet 24:349–54
    • (2000) Nat Genet , vol.24 , pp. 349-354
    • Boute, N.1    Gribouval, O.2    Roselli, S.3
  • 9
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • M.Brownlee (2001). Biochemistry and molecular cell biology of diabetic complications. Nature 414:813–20
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 10
    • 33644873810 scopus 로고    scopus 로고
    • Hexosamines, insulin resistance, and the complications of diabetes: current status
    • M.G.Buse (2006). Hexosamines, insulin resistance, and the complications of diabetes: current status. Am J Physiol Endocrinol Metab 290:E1–8
    • (2006) Am J Physiol Endocrinol Metab , vol.290 , pp. E1-E8
    • Buse, M.G.1
  • 11
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • C.Butkinaree, K.Park, G.W.Hart (2010). O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim Biophys Acta 1800:96–106
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 12
    • 0032478827 scopus 로고    scopus 로고
    • Sp1 sites mediate activation of the plasminogen activator inhibitor-1 promoter by glucose in vascular smooth muscle cells
    • Y.Q.Chen, M.Su, R.R.Walia,. (1998). Sp1 sites mediate activation of the plasminogen activator inhibitor-1 promoter by glucose in vascular smooth muscle cells. J Biol Chem 273:8225–31
    • (1998) J Biol Chem , vol.273 , pp. 8225-8231
    • Chen, Y.Q.1    Su, M.2    Walia, R.R.3
  • 13
    • 57749088688 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
    • W.D.Cheung, K.Sakabe, M.P.Housley,. (2008). O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. J Biol Chem 283:33935–41
    • (2008) J Biol Chem , vol.283 , pp. 33935-33941
    • Cheung, W.D.1    Sakabe, K.2    Housley, M.P.3
  • 14
    • 0027506091 scopus 로고
    • Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18
    • C.F.Chou, M.B.Omary (1993). Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18. J Biol Chem 268:4465–72
    • (1993) J Biol Chem , vol.268 , pp. 4465-4472
    • Chou, C.F.1    Omary, M.B.2
  • 15
    • 84855890614 scopus 로고    scopus 로고
    • TGF-β-stimulated aberrant expression of class III β-tubulin via the ERK signaling pathway in cultured retinal pigment epithelial cells
    • E.J.Chung, J.N.Chun, S.A.Jung,. (2011). TGF-β-stimulated aberrant expression of class III β-tubulin via the ERK signaling pathway in cultured retinal pigment epithelial cells. Biochem Biophys Res Commun 415:367–72
    • (2011) Biochem Biophys Res Commun , vol.415 , pp. 367-372
    • Chung, E.J.1    Chun, J.N.2    Jung, S.A.3
  • 16
    • 0242582455 scopus 로고    scopus 로고
    • Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation
    • R.J.Clark, P.M.McDonough, E.Swanson,. (2003). Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation. J Biol Chem 278:44230–7
    • (2003) J Biol Chem , vol.278 , pp. 44230-44237
    • Clark, R.J.1    McDonough, P.M.2    Swanson, E.3
  • 17
    • 33750809382 scopus 로고
    • Retinal vascular patterns. IV. Diabetic retinopathy
    • D.G.Cogan, D.Toussaint, T.Kuwabara (1961). Retinal vascular patterns. IV. Diabetic retinopathy. Arch Ophthalmol 66:366–78
    • (1961) Arch Ophthalmol , vol.66 , pp. 366-378
    • Cogan, D.G.1    Toussaint, D.2    Kuwabara, T.3
  • 18
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • F.I.Comer, G.W.Hart (1999). O-GlcNAc and the control of gene expression. Biochim Biophys Acta 1473:161–71
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 19
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • F.I.Comer, G.W.Hart (2001). Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 40:7845–52
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.I.1    Hart, G.W.2
  • 20
    • 0035204171 scopus 로고    scopus 로고
    • Interaction of metabolic and haemodynamic factors in mediating experimental diabetic nephropathy
    • M.E.Cooper (2001). Interaction of metabolic and haemodynamic factors in mediating experimental diabetic nephropathy. Diabetologia 44:1957–72
    • (2001) Diabetologia , vol.44 , pp. 1957-1972
    • Cooper, M.E.1
  • 21
    • 50349093142 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity
    • R.J.Copeland, J.W.Bullen, G.W.Hart (2008). Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity. Am J Physiol Endocrinol Metab 295:E17–28
    • (2008) Am J Physiol Endocrinol Metab , vol.295 , pp. E17-E28
    • Copeland, R.J.1    Bullen, J.W.2    Hart, G.W.3
  • 22
    • 27144515984 scopus 로고    scopus 로고
    • Role of O-linked beta-N-acetylglucosamine modification in the subcellular distribution of alpha4 phosphoprotein and Sp1 in rat lymphoma cells
    • S.M.Dauphinee, M.Ma, C.K.Too (2005). Role of O-linked beta-N-acetylglucosamine modification in the subcellular distribution of alpha4 phosphoprotein and Sp1 in rat lymphoma cells. J Cell Biochem 96:579–88
    • (2005) J Cell Biochem , vol.96 , pp. 579-588
    • Dauphinee, S.M.1    Ma, M.2    Too, C.K.3
  • 23
    • 61849097234 scopus 로고    scopus 로고
    • Evidence of O-linked N-acetylglucosamine in diabetic nephropathy
    • P.Degrell, J.Cseh, M.Mohas,. (2009). Evidence of O-linked N-acetylglucosamine in diabetic nephropathy. Life Sci 84:389–93
    • (2009) Life Sci , vol.84 , pp. 389-393
    • Degrell, P.1    Cseh, J.2    Mohas, M.3
  • 24
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • R.Dentin, S.Hedrick, J.Xie,. (2008). Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319:1402–5
    • (2008) Science , vol.319 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3
  • 25
    • 84922381746 scopus 로고    scopus 로고
    • O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells
    • K.Donovan, O.Alekseev, X.Qi,. (2014). O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells. Invest Ophthalmol Vis Sci 55:7862–73
    • (2014) Invest Ophthalmol Vis Sci , vol.55 , pp. 7862-7873
    • Donovan, K.1    Alekseev, O.2    Qi, X.3
  • 26
    • 0034948819 scopus 로고    scopus 로고
    • Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN
    • D.B.Donoviel, D.D.Freed, H.Vogel,. (2001). Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN. Mol Cell Biol 21:4829–36
    • (2001) Mol Cell Biol , vol.21 , pp. 4829-4836
    • Donoviel, D.B.1    Freed, D.D.2    Vogel, H.3
  • 27
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • X.L.Du, D.Edelstein, L.Rossetti,. (2000). Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc Natl Acad Sci USA 97:12222–6
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12222-12226
    • Du, X.L.1    Edelstein, D.2    Rossetti, L.3
  • 28
    • 0036396628 scopus 로고    scopus 로고
    • Analysis of MGEA5 on 10q24.1-q24.3 encoding the beta-O-linked N-acetylglucosaminidase as a candidate gene for type 2 diabetes mellitus in Pima Indians
    • V.S.Farook, C.Bogardus, M.Prochazka (2002). Analysis of MGEA5 on 10q24.1-q24.3 encoding the beta-O-linked N-acetylglucosaminidase as a candidate gene for type 2 diabetes mellitus in Pima Indians. Mol Genet Metab 77:189–93
    • (2002) Mol Genet Metab , vol.77 , pp. 189-193
    • Farook, V.S.1    Bogardus, C.2    Prochazka, M.3
  • 30
    • 33747081065 scopus 로고    scopus 로고
    • Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer
    • M.E.Forsythe, D.C.Love, B.D.Lazarus,. (2006). Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer. Proc Natl Acad Sci USA 103:11952–7
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11952-11957
    • Forsythe, M.E.1    Love, D.C.2    Lazarus, B.D.3
  • 31
    • 34247336440 scopus 로고    scopus 로고
    • Impact of Type 2 diabetes and aging on cardiomyocyte function and O-linked N-acetylglucosamine levels in the heart
    • N.Fulop, M.M.Mason, K.Dutta,. (2007). Impact of Type 2 diabetes and aging on cardiomyocyte function and O-linked N-acetylglucosamine levels in the heart. Am J Physiol Cell Physiol 292:C1370–8
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. C1370-C1378
    • Fulop, N.1    Mason, M.M.2    Dutta, K.3
  • 32
    • 0037709390 scopus 로고    scopus 로고
    • The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells
    • Y.Gao, J.Miyazaki, G.W.Hart (2003). The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells. Arch Biochem Biophys 415:155–63
    • (2003) Arch Biochem Biophys , vol.415 , pp. 155-163
    • Gao, Y.1    Miyazaki, J.2    Hart, G.W.3
  • 33
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
    • Y.Gao, L.Wells, F.I.Comer,. (2001). Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. J Biol Chem 276:9838–45
    • (2001) J Biol Chem , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3
  • 34
    • 0033860359 scopus 로고    scopus 로고
    • Insulin resistance and cardiovascular disease
    • H.N.Ginsberg (2000). Insulin resistance and cardiovascular disease. J Clin Invest 106:453–8
    • (2000) J Clin Invest , vol.106 , pp. 453-458
    • Ginsberg, H.N.1
  • 35
    • 80053280712 scopus 로고    scopus 로고
    • O-linked β-N-acetylglucosamine supports p38 MAPK activation by high glucose in glomerular mesangial cells
    • H.Goldberg, C.Whiteside, I.G.Fantus (2011). O-linked β-N-acetylglucosamine supports p38 MAPK activation by high glucose in glomerular mesangial cells. Am J Physiol Endocrinol Metab 301:E713–26
    • (2011) Am J Physiol Endocrinol Metab , vol.301 , pp. E713-E726
    • Goldberg, H.1    Whiteside, C.2    Fantus, I.G.3
  • 36
    • 0034083716 scopus 로고    scopus 로고
    • Glucosamine activates the plasminogen activator inhibitor 1 gene promoter through Sp1 DNA binding sites in glomerular mesangial cells
    • H.J.Goldberg, J.Scholey, I.G.Fantus (2000). Glucosamine activates the plasminogen activator inhibitor 1 gene promoter through Sp1 DNA binding sites in glomerular mesangial cells. Diabetes 49:863–71
    • (2000) Diabetes , vol.49 , pp. 863-871
    • Goldberg, H.J.1    Scholey, J.2    Fantus, I.G.3
  • 37
    • 29344459211 scopus 로고    scopus 로고
    • Posttranslational, reversible O-glycosylation is stimulated by high glucose and mediates plasminogen activator inhibitor-1 gene expression and Sp1 transcriptional activity in glomerular mesangial cells
    • H.J.Goldberg, C.I.Whiteside, G.W.Hart, I.G.Fantus (2006). Posttranslational, reversible O-glycosylation is stimulated by high glucose and mediates plasminogen activator inhibitor-1 gene expression and Sp1 transcriptional activity in glomerular mesangial cells. Endocrinology 147:222–31
    • (2006) Endocrinology , vol.147 , pp. 222-231
    • Goldberg, H.J.1    Whiteside, C.I.2    Hart, G.W.3    Fantus, I.G.4
  • 38
    • 84878211324 scopus 로고    scopus 로고
    • Retinal O-linked N-acetylglucosamine protein modifications: implications for postnatal retinal vascularization and the pathogenesis of diabetic retinopathy
    • Z.Gurel, K.M.Sieg, K.D.Shallow,. (2013). Retinal O-linked N-acetylglucosamine protein modifications: implications for postnatal retinal vascularization and the pathogenesis of diabetic retinopathy. Mol Vis 19:1047–59
    • (2013) Mol Vis , vol.19 , pp. 1047-1059
    • Gurel, Z.1    Sieg, K.M.2    Shallow, K.D.3
  • 39
    • 84900391018 scopus 로고    scopus 로고
    • Identification of O-GlcNAc modification targets in mouse retinal pericytes: implication of p53 in pathogenesis of diabetic retinopathy
    • Z.Gurel, B.W.Zaro, M.R.Pratt, N.Sheibani (2014). Identification of O-GlcNAc modification targets in mouse retinal pericytes: implication of p53 in pathogenesis of diabetic retinopathy. PLoS One 9:e95561
    • (2014) PLoS One , vol.9 , pp. e95561
    • Gurel, Z.1    Zaro, B.W.2    Pratt, M.R.3    Sheibani, N.4
  • 40
    • 0037440370 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
    • J.A.Hanover, S.Yu, W.B.Lubas,. (2003). Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch Biochem Biophys 409:287–97
    • (2003) Arch Biochem Biophys , vol.409 , pp. 287-297
    • Hanover, J.A.1    Yu, S.2    Lubas, W.B.3
  • 41
    • 84905723395 scopus 로고    scopus 로고
    • Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation
    • S.Hardiville, G.W.Hart (2014). Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation. Cell Metab 20:208–13
    • (2014) Cell Metab , vol.20 , pp. 208-213
    • Hardiville, S.1    Hart, G.W.2
  • 42
    • 0025766468 scopus 로고
    • Global glomerular sclerosis and glomerular arteriolar hyalinosis in insulin dependent diabetes
    • R.D.Harris, M.W.Steffes, R.W.Bilous,. (1991). Global glomerular sclerosis and glomerular arteriolar hyalinosis in insulin dependent diabetes. Kidney Int 40:107–14
    • (1991) Kidney Int , vol.40 , pp. 107-114
    • Harris, R.D.1    Steffes, M.W.2    Bilous, R.W.3
  • 43
    • 84884164424 scopus 로고    scopus 로고
    • Nutrient regulation of immunity: O-GlcNAcylation regulates stimulus-specific NF-κB-dependent transcription
    • G.W.Hart (2013). Nutrient regulation of immunity: O-GlcNAcylation regulates stimulus-specific NF-κB-dependent transcription. Sci Signal 6:pe26
    • (2013) Sci Signal , vol.6 , pp. pe26
    • Hart, G.W.1
  • 44
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • G.W.Hart, M.P.Housley, C.Slawson (2007). Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446:1017–22
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 45
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
    • G.W.Hart, C.Slawson, G.Ramirez-Correa, O.Lagerlof (2011). Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem 80:825–58
    • (2011) Annu Rev Biochem , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 46
    • 0036021405 scopus 로고    scopus 로고
    • Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development
    • L.M.Hartweck, C.L.Scott, N.E.Olszewski (2002). Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development. Genetics 161:1279–91
    • (2002) Genetics , vol.161 , pp. 1279-1291
    • Hartweck, L.M.1    Scott, C.L.2    Olszewski, N.E.3
  • 47
    • 0028863503 scopus 로고
    • Overexpression of glucose transporters in rat mesangial cells cultured in a normal glucose milieu mimics the diabetic phenotype
    • C.W.Heilig, L.A.Concepcion, B.L.Riser,. (1995). Overexpression of glucose transporters in rat mesangial cells cultured in a normal glucose milieu mimics the diabetic phenotype. J Clin Invest 96:1802–14
    • (1995) J Clin Invest , vol.96 , pp. 1802-1814
    • Heilig, C.W.1    Concepcion, L.A.2    Riser, B.L.3
  • 48
    • 84865754804 scopus 로고    scopus 로고
    • Acute O-GlcNAcylation prevents inflammation-induced vascular dysfunction
    • R.H.Hilgers, D.Xing, K.Gong,. (2012). Acute O-GlcNAcylation prevents inflammation-induced vascular dysfunction. Am J Physiol Heart Circ Physiol 303:H513–22
    • (2012) Am J Physiol Heart Circ Physiol , vol.303 , pp. H513-H522
    • Hilgers, R.H.1    Xing, D.2    Gong, K.3
  • 49
    • 0023037076 scopus 로고
    • The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc
    • G.D.Holt, G.W.Hart (1986). The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J Biol Chem 261:8049–57
    • (1986) J Biol Chem , vol.261 , pp. 8049-8057
    • Holt, G.D.1    Hart, G.W.2
  • 50
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • G.D.Holt, C.M.Snow, A.Senior,. (1987). Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol 104:1157–64
    • (1987) J Cell Biol , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3
  • 51
    • 47749149232 scopus 로고    scopus 로고
    • O-GlcNAc regulates FoxO activation in response to glucose
    • M.P.Housley, J.T.Rodgers, N.D.Udeshi,. (2008). O-GlcNAc regulates FoxO activation in response to glucose. J Biol Chem 283:16283–92
    • (2008) J Biol Chem , vol.283 , pp. 16283-16292
    • Housley, M.P.1    Rodgers, J.T.2    Udeshi, N.D.3
  • 52
    • 64149111641 scopus 로고    scopus 로고
    • A PGC-1alpha-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose
    • M.P.Housley, N.D.Udeshi, J.T.Rodgers,. (2009). A PGC-1alpha-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J Biol Chem 284:5148–57
    • (2009) J Biol Chem , vol.284 , pp. 5148-5157
    • Housley, M.P.1    Udeshi, N.D.2    Rodgers, J.T.3
  • 53
    • 19044377730 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of O-GlcNAcase improves contractile function in the diabetic heart
    • Y.Hu, D.Belke, J.Suarez,. (2005). Adenovirus-mediated overexpression of O-GlcNAcase improves contractile function in the diabetic heart. Circ Res 96:1006–13
    • (2005) Circ Res , vol.96 , pp. 1006-1013
    • Hu, Y.1    Belke, D.2    Suarez, J.3
  • 54
    • 58649095123 scopus 로고    scopus 로고
    • Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose
    • Y.Hu, J.Suarez, E.Fricovsky,. (2009). Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. J Biol Chem 284:547–55
    • (2009) J Biol Chem , vol.284 , pp. 547-555
    • Hu, Y.1    Suarez, J.2    Fricovsky, E.3
  • 55
    • 0037648473 scopus 로고    scopus 로고
    • Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase
    • S.P.Iyer, Y.Akimoto, G.W.Hart (2003). Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. J Biol Chem 278:5399–409
    • (2003) J Biol Chem , vol.278 , pp. 5399-5409
    • Iyer, S.P.1    Akimoto, Y.2    Hart, G.W.3
  • 56
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation
    • S.P.Jackson, R.Tjian (1988). O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell 55:125–33
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 57
    • 79954435787 scopus 로고    scopus 로고
    • O-GlcNAcylation of tubulin inhibits its polymerization
    • S.Ji, J.G.Kang, S.Y.Park,. (2011). O-GlcNAcylation of tubulin inhibits its polymerization. Amino Acids 40:809–18
    • (2011) Amino Acids , vol.40 , pp. 809-818
    • Ji, S.1    Kang, J.G.2    Park, S.Y.3
  • 58
    • 84924898037 scopus 로고    scopus 로고
    • Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis
    • C.Keembiyehetty, D.C.Love, K.R.Harwood,. (2015). Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis. J Biol Chem 290:7097–113
    • (2015) J Biol Chem , vol.290 , pp. 7097-7113
    • Keembiyehetty, C.1    Love, D.C.2    Harwood, K.R.3
  • 59
    • 0032015551 scopus 로고    scopus 로고
    • Positionally cloned gene for a novel glomerular protein-nephrin-is mutated in congenital nephrotic syndrome.
    • M.Kestila, U.Lenkkeri, M.Mannikko,. (1998). Positionally cloned gene for a novel glomerular protein-nephrin-is mutated in congenital nephrotic syndrome. Mol Cell 1:575–82
    • (1998) Mol Cell , vol.1 , pp. 575-582
    • Kestila, M.1    Lenkkeri, U.2    Mannikko, M.3
  • 60
    • 0036834748 scopus 로고    scopus 로고
    • The role of O-linked protein glycosylation in beta-cell dysfunction
    • R.J.Konrad, J.E.Kudlow (2002). The role of O-linked protein glycosylation in beta-cell dysfunction. Int J Mol Med 10:535–9
    • (2002) Int J Mol Med , vol.10 , pp. 535-539
    • Konrad, R.J.1    Kudlow, J.E.2
  • 61
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • L.K.Kreppel, M.A.Blomberg, G.W.Hart (1997). Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272:9308–15
    • (1997) J Biol Chem , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 62
    • 0033527739 scopus 로고    scopus 로고
    • Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
    • L.K.Kreppel, G.W.Hart (1999). Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 274:32015–22
    • (1999) J Biol Chem , vol.274 , pp. 32015-32022
    • Kreppel, L.K.1    Hart, G.W.2
  • 63
    • 79251611901 scopus 로고    scopus 로고
    • Structure of human O-GlcNAc transferase and its complex with a peptide substrate
    • M.B.Lazarus, Y.Nam, J.Jiang,. (2011). Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469:564–7
    • (2011) Nature , vol.469 , pp. 564-567
    • Lazarus, M.B.1    Nam, Y.2    Jiang, J.3
  • 64
    • 20144389168 scopus 로고    scopus 로고
    • A single nucleotide polymorphism in MGEA5 encoding O-GlcNAc-selective N-acetyl-beta-D glucosaminidase is associated with type 2 diabetes in Mexican Americans
    • D.M.Lehman, D.J.Fu, A.B.Freeman,. (2005). A single nucleotide polymorphism in MGEA5 encoding O-GlcNAc-selective N-acetyl-beta-D glucosaminidase is associated with type 2 diabetes in Mexican Americans. Diabetes 54:1214–21
    • (2005) Diabetes , vol.54 , pp. 1214-1221
    • Lehman, D.M.1    Fu, D.J.2    Freeman, A.B.3
  • 65
    • 34547467760 scopus 로고    scopus 로고
    • Podocyte biology in diabetic nephropathy
    • J.J.Li, S.J.Kwak, D.S.Jung,. (2007). Podocyte biology in diabetic nephropathy. Kidney Int Suppl 106:S36–42
    • (2007) Kidney Int Suppl , vol.106 , pp. S36-S42
    • Li, J.J.1    Kwak, S.J.2    Jung, D.S.3
  • 66
    • 0037442984 scopus 로고    scopus 로고
    • Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase
    • D.C.Love, J.Kochan, R.L.Cathey,. (2003). Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase. J Cell Sci 116:647–54
    • (2003) J Cell Sci , vol.116 , pp. 647-654
    • Love, D.C.1    Kochan, J.2    Cathey, R.L.3
  • 67
    • 77955273167 scopus 로고    scopus 로고
    • O-GlcNAc cycling: emerging roles in development and epigenetics
    • D.C.Love, M.W.Krause, J.A.Hanover (2010). O-GlcNAc cycling: emerging roles in development and epigenetics. Semin Cell Dev Biol 21:646–54
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 646-654
    • Love, D.C.1    Krause, M.W.2    Hanover, J.A.3
  • 68
    • 0034646669 scopus 로고    scopus 로고
    • Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
    • W.A.Lubas, J.A.Hanover (2000). Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J Biol Chem 275:10983–8
    • (2000) J Biol Chem , vol.275 , pp. 10983-10988
    • Lubas, W.A.1    Hanover, J.A.2
  • 69
    • 42249106688 scopus 로고    scopus 로고
    • Protein modification by O-linked GlcNAc reduces angiogenesis by inhibiting Akt activity in endothelial cells
    • B.Luo, Y.Soesanto, D.A.McClain (2008). Protein modification by O-linked GlcNAc reduces angiogenesis by inhibiting Akt activity in endothelial cells. Arterioscler Thromb Vasc Biol 28:651–7
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 651-657
    • Luo, B.1    Soesanto, Y.2    McClain, D.A.3
  • 70
    • 77956961240 scopus 로고    scopus 로고
    • Elevation of Global O-GlcNAc in rodents using a selective O-GlcNAcase inhibitor does not cause insulin resistance or perturb glucohomeostasis
    • M.S.Macauley, X.Shan, S.A.Yuzwa,. (2010). Elevation of Global O-GlcNAc in rodents using a selective O-GlcNAcase inhibitor does not cause insulin resistance or perturb glucohomeostasis. Chem Biol 17:949–58
    • (2010) Chem Biol , vol.17 , pp. 949-958
    • Macauley, M.S.1    Shan, X.2    Yuzwa, S.A.3
  • 71
    • 61449183458 scopus 로고    scopus 로고
    • Is hyperfiltration associated with the future risk of developing diabetic nephropathy? A meta-analysis
    • G.M.Magee, R.W.Bilous, C.R.Cardwell,. (2009). Is hyperfiltration associated with the future risk of developing diabetic nephropathy? A meta-analysis. Diabetologia 52:691–7
    • (2009) Diabetologia , vol.52 , pp. 691-697
    • Magee, G.M.1    Bilous, R.W.2    Cardwell, C.R.3
  • 72
    • 84946067197 scopus 로고    scopus 로고
    • O-GlcNAcase overexpression reverses coronary endothelial cell dysfunction in type 1 diabetic mice
    • A.Makino, A.Dai, Y.Han,. (2015). O-GlcNAcase overexpression reverses coronary endothelial cell dysfunction in type 1 diabetic mice. Am J Physiol Cell Physiol 309:C593–9
    • (2015) Am J Physiol Cell Physiol , vol.309 , pp. C593-C599
    • Makino, A.1    Dai, A.2    Han, Y.3
  • 73
    • 79954433818 scopus 로고    scopus 로고
    • Activation of the hexosamine biosynthesis pathway and protein O-GlcNAcylation modulate hypertrophic and cell signaling pathways in cardiomyocytes from diabetic mice
    • S.A.Marsh, L.J.Dell'Italia, J.C.Chatham (2008). Activation of the hexosamine biosynthesis pathway and protein O-GlcNAcylation modulate hypertrophic and cell signaling pathways in cardiomyocytes from diabetic mice. Amino Acids 40:819–28
    • (2008) Amino Acids , vol.40 , pp. 819-828
    • Marsh, S.A.1    Dell'Italia, L.J.2    Chatham, J.C.3
  • 74
    • 20544441287 scopus 로고    scopus 로고
    • Glucosamine induces cell-cycle arrest and hypertrophy of mesangial cells: implication of gangliosides
    • E.Masson, N.Wiernsperger, M.Lagarde, S.El Bawab (2005). Glucosamine induces cell-cycle arrest and hypertrophy of mesangial cells: implication of gangliosides. Biochem J 388:537–44
    • (2005) Biochem J , vol.388 , pp. 537-544
    • Masson, E.1    Wiernsperger, N.2    Lagarde, M.3    El Bawab, S.4
  • 75
    • 0036679303 scopus 로고    scopus 로고
    • Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia
    • D.A.McClain, W.A.Lubas, R.C.Cooksey,. (2002). Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia. Proc Natl Acad Sci USA 99:10695–9
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10695-10699
    • McClain, D.A.1    Lubas, W.A.2    Cooksey, R.C.3
  • 76
    • 84947018456 scopus 로고    scopus 로고
    • Diet-induced podocyte dysfunction in Drosophila and mammals
    • J.Na, M.T.Sweetwyne, A.S.Park,. (2015). Diet-induced podocyte dysfunction in Drosophila and mammals. Cell Rep 12:636–47
    • (2015) Cell Rep , vol.12 , pp. 636-647
    • Na, J.1    Sweetwyne, M.T.2    Park, A.S.3
  • 77
    • 77953713601 scopus 로고    scopus 로고
    • Modulation of transcription factor function by O-GlcNAc modification
    • S.Ozcan, S.S.Andrali, J.E.Cantrell (2010). Modulation of transcription factor function by O-GlcNAc modification. Biochim Biophys Acta 1799:353–64
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 353-364
    • Ozcan, S.1    Andrali, S.S.2    Cantrell, J.E.3
  • 78
    • 77954308587 scopus 로고    scopus 로고
    • Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals with pre-diabetes and diabetes
    • K.Park, C.D.Saudek, G.W.Hart (2010). Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals with pre-diabetes and diabetes. Diabetes 59:1845–50
    • (2010) Diabetes , vol.59 , pp. 1845-1850
    • Park, K.1    Saudek, C.D.2    Hart, G.W.3
  • 79
    • 84941024243 scopus 로고    scopus 로고
    • The active site of O-GlcNAc transferase imposes constraints on substrate sequence
    • S.Pathak, J.Alonso, M.Schimpl,. (2015). The active site of O-GlcNAc transferase imposes constraints on substrate sequence. Nat Struct Mol Biol 22:744–50
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 744-750
    • Pathak, S.1    Alonso, J.2    Schimpl, M.3
  • 80
    • 58149379890 scopus 로고    scopus 로고
    • O-linked GlcNAc modification of cardiac myofilament proteins: a novel regulator of myocardial contractile function
    • G.A.Ramirez-Correa, W.Jin, Z.Wang,. (2008). O-linked GlcNAc modification of cardiac myofilament proteins: a novel regulator of myocardial contractile function. Circ Res 103:1354–8
    • (2008) Circ Res , vol.103 , pp. 1354-1358
    • Ramirez-Correa, G.A.1    Jin, W.2    Wang, Z.3
  • 81
    • 84949017406 scopus 로고    scopus 로고
    • Removal of abnormal myofilament O-GlcNAcylation restores Ca2 + sensitivity in diabetic cardiac muscle
    • G.A.Ramirez-Correa, J.Ma, C.Slawson,. (2015). Removal of abnormal myofilament O-GlcNAcylation restores Ca2 + sensitivity in diabetic cardiac muscle. Diabetes 64:3573–87
    • (2015) Diabetes , vol.64 , pp. 3573-3587
    • Ramirez-Correa, G.A.1    Ma, J.2    Slawson, C.3
  • 82
    • 84863610013 scopus 로고    scopus 로고
    • Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo
    • S.M.Ranuncolo, S.Ghosh, J.A.Hanover,. (2012). Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo. J Biol Chem 287:23549–61
    • (2012) J Biol Chem , vol.287 , pp. 23549-23561
    • Ranuncolo, S.M.1    Ghosh, S.2    Hanover, J.A.3
  • 83
    • 33645462551 scopus 로고    scopus 로고
    • Prevention and treatment of diabetic renal disease in type 2 diabetes: the BENEDICT study
    • G.Remuzzi, M.Macia, P.Ruggenenti (2006). Prevention and treatment of diabetic renal disease in type 2 diabetes: the BENEDICT study. J Am Soc Nephrol 17:S90–7
    • (2006) J Am Soc Nephrol , vol.17 , pp. S90-S97
    • Remuzzi, G.1    Macia, M.2    Ruggenenti, P.3
  • 84
    • 0029670515 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin
    • E.P.Roquemore, M.R.Chevrier, R.J.Cotter, G.W.Hart (1996). Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry 35:3578–86
    • (1996) Biochemistry , vol.35 , pp. 3578-3586
    • Roquemore, E.P.1    Chevrier, M.R.2    Cotter, R.J.3    Hart, G.W.4
  • 85
    • 0026541971 scopus 로고
    • Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine
    • E.P.Roquemore, A.Dell, H.R.Morris,. (1992). Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. J Biol Chem 267:555–63
    • (1992) J Biol Chem , vol.267 , pp. 555-563
    • Roquemore, E.P.1    Dell, A.2    Morris, H.R.3
  • 86
    • 84898547546 scopus 로고    scopus 로고
    • The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy
    • R.D.Semba, H.Huang, G.A.Lutty,. (2014). The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy. Proteomics Clin Appl 8:218–31
    • (2014) Proteomics Clin Appl , vol.8 , pp. 218-231
    • Semba, R.D.1    Huang, H.2    Lutty, G.A.3
  • 87
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • R.Shafi, S.P.Iyer, L.G.Ellies,. (2000). The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc Natl Acad Sci USA 97:5735–9
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3
  • 88
    • 77449129055 scopus 로고    scopus 로고
    • Phosphorylation of alpha-actinin 4 upon epidermal growth factor exposure regulates its interaction with actin
    • H.Shao, C.Wu, A.Wells (2010). Phosphorylation of alpha-actinin 4 upon epidermal growth factor exposure regulates its interaction with actin. J Biol Chem 285:2591–600
    • (2010) J Biol Chem , vol.285 , pp. 2591-2600
    • Shao, H.1    Wu, C.2    Wells, A.3
  • 90
    • 0033536599 scopus 로고    scopus 로고
    • Congenital nephrotic syndrome in mice lacking CD2-associated protein
    • N.Y.Shih, J.Li, V.Karpitskii,. (1999). Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science 286:312–15
    • (1999) Science , vol.286 , pp. 312-315
    • Shih, N.Y.1    Li, J.2    Karpitskii, V.3
  • 91
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: implications for cancer cell biology
    • C.Slawson, G.W.Hart (2011). O-GlcNAc signalling: implications for cancer cell biology. Nat Rev Cancer 11:678–84
    • (2011) Nat Rev Cancer , vol.11 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 92
    • 25444501339 scopus 로고    scopus 로고
    • Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis
    • C.Slawson, N.E.Zachara, K.Vosseller,. (2005). Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J Biol Chem 280:32944–56
    • (2005) J Biol Chem , vol.280 , pp. 32944-32956
    • Slawson, C.1    Zachara, N.E.2    Vosseller, K.3
  • 93
    • 84901407632 scopus 로고    scopus 로고
    • Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function
    • E.P.Tan, M.T.Villar, L.EL,. (2014). Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function. J Biol Chem 289:14719–30
    • (2014) J Biol Chem , vol.289 , pp. 14719-14730
    • Tan, E.P.1    Villar, M.T.2
  • 94
    • 0027370108 scopus 로고
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus
    • The Diabetes Control and Complications Trial Research Group. (1993). The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. N Engl J Med 329:977–86
    • (1993) N Engl J Med , vol.329 , pp. 977-986
  • 95
    • 11144246904 scopus 로고    scopus 로고
    • Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities
    • C.Toleman, A.J.Paterson, T.R.Whisenhunt, J.E.Kudlow (2004). Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J Biol Chem 279:53665–73
    • (2004) J Biol Chem , vol.279 , pp. 53665-53673
    • Toleman, C.1    Paterson, A.J.2    Whisenhunt, T.R.3    Kudlow, J.E.4
  • 96
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • C.R.Torres, G.W.Hart (1984). Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 259:3308–17
    • (1984) J Biol Chem , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 97
    • 0032511583 scopus 로고    scopus 로고
    • Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33)
    • UK Prospective Diabetes Study (UKPDS) Group. (1998). Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33). Lancet 352:837–53
    • (1998) Lancet , vol.352 , pp. 837-853
  • 98
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • K.Vosseller, L.Wells, M.D.Lane, G.W.Hart (2002). Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc Natl Acad Sci USA 99:5313–18
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 99
    • 0037304213 scopus 로고    scopus 로고
    • High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin
    • J.L.Walgren, T.S.Vincent, K.L.Schey, M.G.Buse (2003). High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am J Physiol Endocrinol Metab 284:E424–34
    • (2003) Am J Physiol Endocrinol Metab , vol.284 , pp. E424-E434
    • Walgren, J.L.1    Vincent, T.S.2    Schey, K.L.3    Buse, M.G.4
  • 100
    • 63249106433 scopus 로고    scopus 로고
    • Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes
    • Z.Wang, K.Park, F.Comer,. (2009). Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 58:309–17
    • (2009) Diabetes , vol.58 , pp. 309-317
    • Wang, Z.1    Park, K.2    Comer, F.3
  • 101
    • 0031848378 scopus 로고    scopus 로고
    • Effects of diabetes and level of glycemia on all-cause and cardiovascular mortality. The San Antonio Heart Study
    • M.Wei, S.P.Gaskill, S.M.Haffner, M.P.Stern (1998). Effects of diabetes and level of glycemia on all-cause and cardiovascular mortality. The San Antonio Heart Study. Diabetes Care 21:1167–72
    • (1998) Diabetes Care , vol.21 , pp. 1167-1172
    • Wei, M.1    Gaskill, S.P.2    Haffner, S.M.3    Stern, M.P.4
  • 102
    • 77949332132 scopus 로고    scopus 로고
    • Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes
    • S.A.Whelan, W.B.Dias, L.Thiruneelakantapillai,. (2010). Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes. J Biol Chem 285:5204–11
    • (2010) J Biol Chem , vol.285 , pp. 5204-5211
    • Whelan, S.A.1    Dias, W.B.2    Thiruneelakantapillai, L.3
  • 103
    • 33751019949 scopus 로고    scopus 로고
    • Identification of O-GlcNAc sites on proteins
    • S.A.Whelan, G.W.Hart (2006). Identification of O-GlcNAc sites on proteins. Meth Enzymol 415:113–33
    • (2006) Meth Enzymol , vol.415 , pp. 113-133
    • Whelan, S.A.1    Hart, G.W.2
  • 104
    • 0032510639 scopus 로고    scopus 로고
    • Prediction of coronary heart disease using risk factor categories
    • P.W.Wilson, R.B.D'Agostino, D.Levy,. (1998). Prediction of coronary heart disease using risk factor categories. Circulation 97:1837–47
    • (1998) Circulation , vol.97 , pp. 1837-1847
    • Wilson, P.W.1    D'Agostino, R.B.2    Levy, D.3
  • 106
    • 0033864452 scopus 로고    scopus 로고
    • Cell cycle regulation in diabetic nephropathy
    • G.Wolf (2000). Cell cycle regulation in diabetic nephropathy. Kidney Int Suppl 77:S59–66
    • (2000) Kidney Int Suppl , vol.77 , pp. S59-S66
    • Wolf, G.1
  • 107
    • 0032815449 scopus 로고    scopus 로고
    • Molecular mechanisms of diabetic renal hypertrophy
    • G.Wolf, F.N.Ziyadeh (1999). Molecular mechanisms of diabetic renal hypertrophy. Kidney Int 56:393–405
    • (1999) Kidney Int , vol.56 , pp. 393-405
    • Wolf, G.1    Ziyadeh, F.N.2
  • 108
    • 39749104251 scopus 로고    scopus 로고
    • Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance
    • X.Yang, P.P.Ongusaha, P.D.Miles,. (2008). Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451:964–9
    • (2008) Nature , vol.451 , pp. 964-969
    • Yang, X.1    Ongusaha, P.P.2    Miles, P.D.3
  • 109
    • 84859030420 scopus 로고    scopus 로고
    • Global prevalence and major risk factors of diabetic retinopathy
    • J.W.Yau, S.L.Rogers, R.Kawasaki,. (2012). Global prevalence and major risk factors of diabetic retinopathy. Diabetes Care 35:556–64
    • (2012) Diabetes Care , vol.35 , pp. 556-564
    • Yau, J.W.1    Rogers, S.L.2    Kawasaki, R.3
  • 110
    • 77953531317 scopus 로고    scopus 로고
    • O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins
    • Q.Zeidan, Z.Wang, A.De Maio, G.W.Hart (2010). O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins. Mol Biol Cell 21:1922–36
    • (2010) Mol Biol Cell , vol.21 , pp. 1922-1936
    • Zeidan, Q.1    Wang, Z.2    De Maio, A.3    Hart, G.W.4
  • 111
    • 0029969728 scopus 로고    scopus 로고
    • Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier
    • X.Zhang, V.Bennett (1996). Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. J Biol Chem 271:31391–8
    • (1996) J Biol Chem , vol.271 , pp. 31391-31398
    • Zhang, X.1    Bennett, V.2


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