메뉴 건너뛰기




Volumn 90, Issue 5, 2008, Pages 679-685

O-GlcNAc modification of FoxO1 increases its transcriptional activity: A role in the glucotoxicity phenomenon?

Author keywords

Diabetes; Glucose 6 phosphatase; Glucotoxicity; O Glycosylation; PGC1

Indexed keywords

GLUCOSE; GLUCOSE 6 PHOSPHATASE; HEXOSAMINE; LUCIFERASE; N ACETYLGLUCOSAMINE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; TRANSCRIPTION FACTOR FKHR;

EID: 42649105106     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.03.005     Document Type: Review
Times cited : (56)

References (48)
  • 1
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414 (2001) 813-820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 2
    • 0034703095 scopus 로고    scopus 로고
    • O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate
    • Comer F.I., and Hart G.W. O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J. Biol. Chem. 275 (2000) 29179-29182
    • (2000) J. Biol. Chem. , vol.275 , pp. 29179-29182
    • Comer, F.I.1    Hart, G.W.2
  • 3
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • Hanover J.A. Glycan-dependent signaling: O-linked N-acetylglucosamine. Faseb J. 15 (2001) 1865-1876
    • (2001) Faseb J. , vol.15 , pp. 1865-1876
    • Hanover, J.A.1
  • 4
    • 0037524357 scopus 로고    scopus 로고
    • O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar
    • Wells L., and Hart G.W. O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar. FEBS Lett. 546 (2003) 154-158
    • (2003) FEBS Lett. , vol.546 , pp. 154-158
    • Wells, L.1    Hart, G.W.2
  • 7
    • 0033664020 scopus 로고    scopus 로고
    • Overexpression of glutamine: fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance
    • Veerababu G., Tang J., Hoffman R.T., Daniels M.C., Hebert Jr. L.F., Crook E.D., Cooksey R.C., and McClain D.A. Overexpression of glutamine: fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance. Diabetes 49 (2000) 2070-2078
    • (2000) Diabetes , vol.49 , pp. 2070-2078
    • Veerababu, G.1    Tang, J.2    Hoffman, R.T.3    Daniels, M.C.4    Hebert Jr., L.F.5    Crook, E.D.6    Cooksey, R.C.7    McClain, D.A.8
  • 8
    • 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
    • Vosseller K., Wells L., Lane M.D., and Hart G.W. Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 5313-5318
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 9
    • 0035180299 scopus 로고    scopus 로고
    • Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site
    • Du X.L., Edelstein D., Dimmeler S., Ju Q., Sui C., and Brownlee M. Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site. J. Clin. Invest. 108 (2001) 1341-1348
    • (2001) J. Clin. Invest. , vol.108 , pp. 1341-1348
    • Du, X.L.1    Edelstein, D.2    Dimmeler, S.3    Ju, Q.4    Sui, C.5    Brownlee, M.6
  • 10
    • 23844523172 scopus 로고    scopus 로고
    • Inactivation of phosphorylated endothelial nitric oxide synthase (Ser-1177) by O-GlcNAc in diabetes-associated erectile dysfunction
    • Musicki B., Kramer M.F., Becker R.E., and Burnett A.L. Inactivation of phosphorylated endothelial nitric oxide synthase (Ser-1177) by O-GlcNAc in diabetes-associated erectile dysfunction. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 11870-11875
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 11870-11875
    • Musicki, B.1    Kramer, M.F.2    Becker, R.E.3    Burnett, A.L.4
  • 11
    • 0037162342 scopus 로고    scopus 로고
    • Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells
    • Federici M., Menghini R., Mauriello A., Hribal M.L., Ferrelli F., Lauro D., Sbraccia P., Spagnoli L.G., Sesti G., and Lauro R. Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells. Circulation 106 (2002) 466-472
    • (2002) Circulation , vol.106 , pp. 466-472
    • Federici, M.1    Menghini, R.2    Mauriello, A.3    Hribal, M.L.4    Ferrelli, F.5    Lauro, D.6    Sbraccia, P.7    Spagnoli, L.G.8    Sesti, G.9    Lauro, R.10
  • 12
    • 0042362101 scopus 로고    scopus 로고
    • Elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase in corneas of diabetic Goto-Kakizaki rats
    • Akimoto Y., Kawakami H., Yamamoto K., Munetomo E., Hida T., and Hirano H. Elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase in corneas of diabetic Goto-Kakizaki rats. Invest. Ophthalmol. Vis. Sci. 44 (2003) 3802-3809
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 3802-3809
    • Akimoto, Y.1    Kawakami, H.2    Yamamoto, K.3    Munetomo, E.4    Hida, T.5    Hirano, H.6
  • 13
    • 2542453754 scopus 로고    scopus 로고
    • Activation of the hexosamine pathway leads to phosphorylation of insulin receptor substrate-1 on Ser307 and Ser612 and impairs the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin insulin biosynthetic pathway in RIN pancreatic beta-cells
    • Andreozzi F., D'Alessandris C., Federici M., Laratta E., Del Guerra S., Del Prato S., Marchetti P., Lauro R., Perticone F., and Sesti G. Activation of the hexosamine pathway leads to phosphorylation of insulin receptor substrate-1 on Ser307 and Ser612 and impairs the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin insulin biosynthetic pathway in RIN pancreatic beta-cells. Endocrinology 145 (2004) 2845-2857
    • (2004) Endocrinology , vol.145 , pp. 2845-2857
    • Andreozzi, F.1    D'Alessandris, C.2    Federici, M.3    Laratta, E.4    Del Guerra, S.5    Del Prato, S.6    Marchetti, P.7    Lauro, R.8    Perticone, F.9    Sesti, G.10
  • 14
    • 0034646330 scopus 로고    scopus 로고
    • Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: linkage of O-linked GlcNAc to beta cell death
    • Liu K., Paterson A.J., Chin E., and Kudlow J.E. Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: linkage of O-linked GlcNAc to beta cell death. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 2820-2825
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2820-2825
    • Liu, K.1    Paterson, A.J.2    Chin, E.3    Kudlow, J.E.4
  • 16
    • 0028287877 scopus 로고
    • Isolation of a cDNA for the catalytic subunit of rat liver glucose-6-phosphatase: regulation of gene expression in FAO hepatoma cells by insulin, dexamethasone and cAMP
    • Lange A.J., Argaud D., el-Maghrabi M.R., Pan W., Maitra S.R., and Pilkis S.J. Isolation of a cDNA for the catalytic subunit of rat liver glucose-6-phosphatase: regulation of gene expression in FAO hepatoma cells by insulin, dexamethasone and cAMP. Biochem. Biophys. Res. Commun. 201 (1994) 302-309
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 302-309
    • Lange, A.J.1    Argaud, D.2    el-Maghrabi, M.R.3    Pan, W.4    Maitra, S.R.5    Pilkis, S.J.6
  • 17
    • 0029939780 scopus 로고    scopus 로고
    • Glucose regulates in vivo glucose-6-phosphatase gene expression in the liver of diabetic rats
    • Massillon D., Barzilai N., Chen W., Hu M., and Rossetti L. Glucose regulates in vivo glucose-6-phosphatase gene expression in the liver of diabetic rats. J. Biol. Chem. 271 (1996) 9871-9874
    • (1996) J. Biol. Chem. , vol.271 , pp. 9871-9874
    • Massillon, D.1    Barzilai, N.2    Chen, W.3    Hu, M.4    Rossetti, L.5
  • 18
    • 0030925598 scopus 로고    scopus 로고
    • Stimulation of glucose-6-phosphatase gene expression by glucose and fructose-2,6-bisphosphate
    • Argaud D., Kirby T.L., Newgard C.B., and Lange A.J. Stimulation of glucose-6-phosphatase gene expression by glucose and fructose-2,6-bisphosphate. J. Biol. Chem. 272 (1997) 12854-12861
    • (1997) J. Biol. Chem. , vol.272 , pp. 12854-12861
    • Argaud, D.1    Kirby, T.L.2    Newgard, C.B.3    Lange, A.J.4
  • 19
    • 0035830941 scopus 로고    scopus 로고
    • Regulation of the glucose-6-phosphatase gene by glucose occurs by transcriptional and post-transcriptional mechanisms. Differential effect of glucose and xylitol
    • Massillon D. Regulation of the glucose-6-phosphatase gene by glucose occurs by transcriptional and post-transcriptional mechanisms. Differential effect of glucose and xylitol. J. Biol. Chem. 276 (2001) 4055-4062
    • (2001) J. Biol. Chem. , vol.276 , pp. 4055-4062
    • Massillon, D.1
  • 20
    • 0033546439 scopus 로고    scopus 로고
    • Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B
    • Rena G., Guo S., Cichy S.C., Unterman T.G., and Cohen P. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274 (1999) 17179-17183
    • (1999) J. Biol. Chem. , vol.274 , pp. 17179-17183
    • Rena, G.1    Guo, S.2    Cichy, S.C.3    Unterman, T.G.4    Cohen, P.5
  • 21
    • 0033546192 scopus 로고    scopus 로고
    • Phosphorylation of serine 256 by protein kinase B disrupts transactivation by FKHR and mediates effects of insulin on insulin-like growth factor-binding protein-1 promoter activity through a conserved insulin response sequence
    • Guo S., Rena G., Cichy S., He X., Cohen P., and Unterman T. Phosphorylation of serine 256 by protein kinase B disrupts transactivation by FKHR and mediates effects of insulin on insulin-like growth factor-binding protein-1 promoter activity through a conserved insulin response sequence. J. Biol. Chem. 274 (1999) 17184-17192
    • (1999) J. Biol. Chem. , vol.274 , pp. 17184-17192
    • Guo, S.1    Rena, G.2    Cichy, S.3    He, X.4    Cohen, P.5    Unterman, T.6
  • 24
    • 0034680839 scopus 로고    scopus 로고
    • Regulation of glucose-6-phosphatase gene expression by protein kinase Balpha and the forkhead transcription factor FKHR. Evidence for insulin response unit-dependent and -independent effects of insulin on promoter activity
    • Schmoll D., Walker K.S., Alessi D.R., Grempler R., Burchell A., Guo S., Walther R., and Unterman T.G. Regulation of glucose-6-phosphatase gene expression by protein kinase Balpha and the forkhead transcription factor FKHR. Evidence for insulin response unit-dependent and -independent effects of insulin on promoter activity. J. Biol. Chem. 275 (2000) 36324-36333
    • (2000) J. Biol. Chem. , vol.275 , pp. 36324-36333
    • Schmoll, D.1    Walker, K.S.2    Alessi, D.R.3    Grempler, R.4    Burchell, A.5    Guo, S.6    Walther, R.7    Unterman, T.G.8
  • 26
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • Comer F.I., and Hart G.W. O-GlcNAc and the control of gene expression. Biochim. Biophys. Acta 1473 (1999) 161-171
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 27
    • 39749171700 scopus 로고    scopus 로고
    • O-glycosylation of FoxO1 increases its transcriptional activity towards the glucose 6-phosphatase gene
    • Kuo M., Zilberfarb V., Gangneux N., Christeff N., and Issad T. O-glycosylation of FoxO1 increases its transcriptional activity towards the glucose 6-phosphatase gene. FEBS Lett. 582 (2008) 829-834
    • (2008) FEBS Lett. , vol.582 , pp. 829-834
    • Kuo, M.1    Zilberfarb, V.2    Gangneux, N.3    Christeff, N.4    Issad, T.5
  • 28
    • 0037160050 scopus 로고    scopus 로고
    • Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms. Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding
    • Zhang X., Gan L., Pan H., Guo S., He X., Olson S.T., Mesecar A., Adam S., and Unterman T.G. Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms. Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding. J. Biol. Chem. 277 (2002) 45276-45284
    • (2002) J. Biol. Chem. , vol.277 , pp. 45276-45284
    • Zhang, X.1    Gan, L.2    Pan, H.3    Guo, S.4    He, X.5    Olson, S.T.6    Mesecar, A.7    Adam, S.8    Unterman, T.G.9
  • 31
    • 0037342151 scopus 로고    scopus 로고
    • Regulation of PGC-1 promoter activity by protein kinase B and the forkhead transcription factor FKHR
    • Daitoku H., Yamagata K., Matsuzaki H., Hatta M., and Fukamizu A. Regulation of PGC-1 promoter activity by protein kinase B and the forkhead transcription factor FKHR. Diabetes 52 (2003) 642-649
    • (2003) Diabetes , vol.52 , pp. 642-649
    • Daitoku, H.1    Yamagata, K.2    Matsuzaki, H.3    Hatta, M.4    Fukamizu, A.5
  • 32
    • 21244457607 scopus 로고    scopus 로고
    • Intestinal glucose-dependent expression of glucose-6-phosphatase: involvement of the aryl receptor nuclear translocator transcription factor
    • Carriere V., Le Gall M., Gouyon-Saumande F., Schmoll D., Brot-Laroche E., Chauffeton V., Chambaz J., and Rousset M. Intestinal glucose-dependent expression of glucose-6-phosphatase: involvement of the aryl receptor nuclear translocator transcription factor. J. Biol. Chem. 280 (2005) 20094-20101
    • (2005) J. Biol. Chem. , vol.280 , pp. 20094-20101
    • Carriere, V.1    Le Gall, M.2    Gouyon-Saumande, F.3    Schmoll, D.4    Brot-Laroche, E.5    Chauffeton, V.6    Chambaz, J.7    Rousset, M.8
  • 33
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I., and Kudlow J.E. Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol. Cell. Biol. 17 (1997) 2550-2558
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 34
    • 13444266255 scopus 로고    scopus 로고
    • O-GlcNAc glycosylation: a signal for the nuclear transport of cytosolic proteins?
    • Guinez C., Morelle W., Michalski J.C., and Lefebvre T. O-GlcNAc glycosylation: a signal for the nuclear transport of cytosolic proteins?. Int. J. Biochem. Cell Biol. 37 (2005) 765-774
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 765-774
    • Guinez, C.1    Morelle, W.2    Michalski, J.C.3    Lefebvre, T.4
  • 35
    • 34447515852 scopus 로고    scopus 로고
    • Glucose mediates the translocation of NeuroD1 by O-linked glycosylation
    • Andrali S.S., Qian Q., and Ozcan S. Glucose mediates the translocation of NeuroD1 by O-linked glycosylation. J. Biol. Chem. 282 (2007) 15589-15596
    • (2007) J. Biol. Chem. , vol.282 , pp. 15589-15596
    • Andrali, S.S.1    Qian, Q.2    Ozcan, S.3
  • 36
    • 0942287200 scopus 로고    scopus 로고
    • The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5
    • Gewinner C., Hart G., Zachara N., Cole R., Beisenherz-Huss C., and Groner B. The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5. J. Biol. Chem. 279 (2004) 3563-3572
    • (2004) J. Biol. Chem. , vol.279 , pp. 3563-3572
    • Gewinner, C.1    Hart, G.2    Zachara, N.3    Cole, R.4    Beisenherz-Huss, C.5    Groner, B.6
  • 37
    • 13244287966 scopus 로고    scopus 로고
    • Regulation of FoxO activity by CBP/p300-mediated acetylation
    • van der Heide L.P., and Smidt M.P. Regulation of FoxO activity by CBP/p300-mediated acetylation. Trends Biochem. Sci. 30 (2005) 81-86
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 81-86
    • van der Heide, L.P.1    Smidt, M.P.2
  • 38
    • 0037341310 scopus 로고    scopus 로고
    • Palmitate-induced activation of the hexosamine pathway in human myotubes: increased expression of glutamine:fructose-6-phosphate aminotransferase
    • Weigert C., Klopfer K., Kausch C., Brodbeck K., Stumvoll M., Haring H.U., and Schleicher E.D. Palmitate-induced activation of the hexosamine pathway in human myotubes: increased expression of glutamine:fructose-6-phosphate aminotransferase. Diabetes 52 (2003) 650-656
    • (2003) Diabetes , vol.52 , pp. 650-656
    • Weigert, C.1    Klopfer, K.2    Kausch, C.3    Brodbeck, K.4    Stumvoll, M.5    Haring, H.U.6    Schleicher, E.D.7
  • 39
    • 0030071548 scopus 로고    scopus 로고
    • Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus
    • Shaw P., Freeman J., Bovey R., and Iggo R. Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus. Oncogene 12 (1996) 921-930
    • (1996) Oncogene , vol.12 , pp. 921-930
    • Shaw, P.1    Freeman, J.2    Bovey, R.3    Iggo, R.4
  • 40
    • 0036231781 scopus 로고    scopus 로고
    • Flux through the hexosamine pathway is a determinant of nuclear factor kappaB- dependent promoter activation
    • James L.R., Tang D., Ingram A., Ly H., Thai K., Cai L., and Scholey J.W. Flux through the hexosamine pathway is a determinant of nuclear factor kappaB- dependent promoter activation. Diabetes 51 (2002) 1146-1156
    • (2002) Diabetes , vol.51 , pp. 1146-1156
    • James, L.R.1    Tang, D.2    Ingram, A.3    Ly, H.4    Thai, K.5    Cai, L.6    Scholey, J.W.7
  • 41
    • 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
    • Gao Y., Miyazaki J., and Hart G.W. 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 (2003) 155-163
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 155-163
    • Gao, Y.1    Miyazaki, J.2    Hart, G.W.3
  • 42
    • 33748579587 scopus 로고    scopus 로고
    • Alternative O-GlcNAcylation/O-phosphorylation of Ser16 induce different conformational disturbances to the N terminus of murine estrogen receptor beta
    • Chen Y.X., Du J.T., Zhou L.X., Liu X.H., Zhao Y.F., Nakanishi H., and Li Y.M. Alternative O-GlcNAcylation/O-phosphorylation of Ser16 induce different conformational disturbances to the N terminus of murine estrogen receptor beta. Chem. Biol. 13 (2006) 937-944
    • (2006) Chem. Biol. , vol.13 , pp. 937-944
    • Chen, Y.X.1    Du, J.T.2    Zhou, L.X.3    Liu, X.H.4    Zhao, Y.F.5    Nakanishi, H.6    Li, Y.M.7
  • 43
    • 33748548999 scopus 로고    scopus 로고
    • Fine-tuning ER-beta structure with PTMs
    • Hart G.W., and Sakabe K. Fine-tuning ER-beta structure with PTMs. Chem. Biol. 13 (2006) 923-924
    • (2006) Chem. Biol. , vol.13 , pp. 923-924
    • Hart, G.W.1    Sakabe, K.2
  • 44
    • 0036153256 scopus 로고    scopus 로고
    • Minireview: secondary beta-cell failure in type 2 diabetes-a convergence of glucotoxicity and lipotoxicity
    • Poitout V., and Robertson R.P. Minireview: secondary beta-cell failure in type 2 diabetes-a convergence of glucotoxicity and lipotoxicity. Endocrinology 143 (2002) 339-342
    • (2002) Endocrinology , vol.143 , pp. 339-342
    • Poitout, V.1    Robertson, R.P.2
  • 45
    • 34250326302 scopus 로고    scopus 로고
    • The emerging role of FOXO transcription factors in pancreatic beta cells
    • Glauser D.A., and Schlegel W. The emerging role of FOXO transcription factors in pancreatic beta cells. J. Endocrinol. 193 (2007) 195-207
    • (2007) J. Endocrinol. , vol.193 , pp. 195-207
    • Glauser, D.A.1    Schlegel, W.2
  • 46
    • 34548289502 scopus 로고    scopus 로고
    • Dynamic FoxO transcription factors
    • Huang H., and Tindall D.J. Dynamic FoxO transcription factors. J. Cell Sci. 120 (2007) 2479-2487
    • (2007) J. Cell Sci. , vol.120 , pp. 2479-2487
    • Huang, H.1    Tindall, D.J.2
  • 47
    • 0035964998 scopus 로고    scopus 로고
    • Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in N-acetylglucosamine containing proteins
    • Slawson C., Pidala J., and Potter R. Increased N-acetyl-beta-glucosaminidase activity in primary breast carcinomas corresponds to a decrease in N-acetylglucosamine containing proteins. Biochim. Biophys. Acta. 1537 (2001) 147-157
    • (2001) Biochim. Biophys. Acta. , vol.1537 , pp. 147-157
    • Slawson, C.1    Pidala, J.2    Potter, R.3
  • 48
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara N.E., and Hart G.W. O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim. Biophys. Acta 1673 (2004) 13-28
    • (2004) Biochim. Biophys. Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.