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Volumn 1800, Issue 2, 2010, Pages 107-121

Increasing O-GlcNAc levels: An overview of small-molecule inhibitors of O-GlcNAcase

Author keywords

Enzyme inhibitor; Glycoprotein; Glycoside hydrolase; Nucleocytoplasmic glycosylation; O GlcNAc; O GlcNAcase; OGA; Substrate assisted catalysis

Indexed keywords

1 ACETAMIDO EPIVALIENAMINE; 1,2 DIDEOXY 2' METHYL ALPHA DEXTRO GLUCOPYRANOSO[2,1 D] DELTA 2' THIAZOLINE; ACETYLGLUCOSAMINIDASE; ENZYME INHIBITOR; GLUCOIMIDAZOLE DERIVATIVE; GLYCOSIDASE; GLYCOSIDASE INHIBITOR; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINE THIAZOLINE; N ACETYLGLUCOSAMINYLTRANSFERASE; N BUTYL THIAZOLINE; STREPTOZOCIN; THIAZOLINE DERIVATIVE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

EID: 77949305110     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.07.028     Document Type: Review
Times cited : (109)

References (159)
  • 1
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres C.R., and Hart G.W. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J. Biol. Chem. 259 (1984) 3308-3317
    • (1984) J. Biol. Chem. , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 2
    • 34247583996 scopus 로고    scopus 로고
    • Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
    • Hart G.W., Housley M.P., and Slawson C. Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446 (2007) 1017-1022
    • (2007) Nature , vol.446 , pp. 1017-1022
    • Hart, G.W.1    Housley, M.P.2    Slawson, C.3
  • 3
    • 0026662974 scopus 로고
    • Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18
    • Chou C.F., Smith A.J., and Omary M.B. Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18. J. Biol. Chem. 267 (1992) 3901-3906
    • (1992) J. Biol. Chem. , vol.267 , pp. 3901-3906
    • Chou, C.F.1    Smith, A.J.2    Omary, M.B.3
  • 4
    • 0029670515 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin
    • Roquemore E.P., Chevrier M.R., Cotter R.J., and Hart G.W. Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry 35 (1996) 3578-3586
    • (1996) Biochemistry , vol.35 , pp. 3578-3586
    • Roquemore, E.P.1    Chevrier, M.R.2    Cotter, R.J.3    Hart, G.W.4
  • 5
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase
    • Haltiwanger R.S., Holt G.D., and Hart G.W. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine:peptide beta-N-acetylglucosaminyltransferase. J. Biol. Chem. 265 (1990) 2563-2568
    • (1990) J. Biol. Chem. , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 6
    • 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
    • Kreppel L.K., Blomberg M.A., and Hart G.W. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9308-9315
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 7
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-d-glucosaminidase from rat spleen cytosol
    • Dong D.L., and Hart G.W. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-d-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269 (1994) 19321-19330
    • (1994) J. Biol. Chem. , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 8
    • 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
    • Gao Y., Wells L., Comer F.I., Parker G.J., and Hart G.W. 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 (2001) 9838-9845
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 9
    • 52949123249 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
    • Wang Z., Gucek M., and Hart G.W. Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc. Natl. Acad. Sci. USA 105 (2008) 13793-13798
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13793-13798
    • Wang, Z.1    Gucek, M.2    Hart, G.W.3
  • 10
    • 0027328373 scopus 로고
    • Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M
    • Dong D.L., Xu Z.S., Chevrier M.R., Cotter R.J., Cleveland D.W., and Hart G.W. Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. J. Biol. Chem. 268 (1993) 16679-16687
    • (1993) J. Biol. Chem. , vol.268 , pp. 16679-16687
    • Dong, D.L.1    Xu, Z.S.2    Chevrier, M.R.3    Cotter, R.J.4    Cleveland, D.W.5    Hart, G.W.6
  • 12
    • 0031943723 scopus 로고    scopus 로고
    • Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo
    • Yki-Jarvinen H., Virkamaki A., Daniels M.C., McClain D., and Gottschalk W.K. Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo. Metabolism 47 (1998) 449-455
    • (1998) Metabolism , vol.47 , pp. 449-455
    • Yki-Jarvinen, H.1    Virkamaki, A.2    Daniels, M.C.3    McClain, D.4    Gottschalk, W.K.5
  • 13
    • 2042540707 scopus 로고    scopus 로고
    • Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance
    • Hazel M., Cooksey R.C., Jones D., Parker G., Neidigh J.L., Witherbee B., Gulve E.A., and McClain D.A. Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance. Endocrinology 145 (2004) 2118-2128
    • (2004) Endocrinology , vol.145 , pp. 2118-2128
    • Hazel, M.1    Cooksey, R.C.2    Jones, D.3    Parker, G.4    Neidigh, J.L.5    Witherbee, B.6    Gulve, E.A.7    McClain, D.A.8
  • 14
    • 0242582455 scopus 로고    scopus 로고
    • Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation
    • Clark R.J., McDonough P.M., Swanson E., Trost S.U., Suzuki M., Fukuda M., and Dillmann W.H. Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation. J. Biol. Chem. 278 (2003) 44230-44237
    • (2003) J. Biol. Chem. , vol.278 , pp. 44230-44237
    • Clark, R.J.1    McDonough, P.M.2    Swanson, E.3    Trost, S.U.4    Suzuki, M.5    Fukuda, M.6    Dillmann, W.H.7
  • 15
    • 64149111641 scopus 로고    scopus 로고
    • A PGC-1{alpha}-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose
    • Housley M.P., Udeshi N.D., Rodgers J.T., Shabanowitz J., Puigserver P., Hunt D.F., and Hart G.W. A PGC-1{alpha}-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J. Biol. Chem. 284 (2009) 5148-5157
    • (2009) J. Biol. Chem. , vol.284 , pp. 5148-5157
    • Housley, M.P.1    Udeshi, N.D.2    Rodgers, J.T.3    Shabanowitz, J.4    Puigserver, P.5    Hunt, D.F.6    Hart, G.W.7
  • 16
    • 57749088688 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
    • Cheung W.D., Sakabe K., Housley M.P., Dias W.B., and Hart G.W. O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. J. Biol. Chem. 283 (2008) 33935-33941
    • (2008) J. Biol. Chem. , vol.283 , pp. 33935-33941
    • Cheung, W.D.1    Sakabe, K.2    Housley, M.P.3    Dias, W.B.4    Hart, G.W.5
  • 17
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate
    • Haltiwanger R.S., Grove K., and Philipsberg G.A. Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate. J. Biol. Chem. 273 (1998) 3611-3617
    • (1998) J. Biol. Chem. , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 18
    • 21844464281 scopus 로고    scopus 로고
    • O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors
    • Macauley M.S., Whitworth G.E., Debowski A.W., Chin D., and Vocadlo D.J. O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J. Biol. Chem. 280 (2005) 25313-25322
    • (2005) J. Biol. Chem. , vol.280 , pp. 25313-25322
    • Macauley, M.S.1    Whitworth, G.E.2    Debowski, A.W.3    Chin, D.4    Vocadlo, D.J.5
  • 20
    • 33845944034 scopus 로고    scopus 로고
    • GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-GlcNAcylation levels
    • Dorfmueller H.C., Borodkin V.S., Schimpl M., Shepherd S.M., Shpiro N.A., and van Aalten D.M. GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-GlcNAcylation levels. J. Am. Chem. Soc. 128 (2006) 16484-16485
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16484-16485
    • Dorfmueller, H.C.1    Borodkin, V.S.2    Schimpl, M.3    Shepherd, S.M.4    Shpiro, N.A.5    van Aalten, D.M.6
  • 21
    • 58049197848 scopus 로고    scopus 로고
    • Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance
    • Macauley M.S., Bubb A.K., Martinez-Fleites C., Davies G.J., and Vocadlo D.J. Elevation of global O-GlcNAc levels in 3T3-L1 adipocytes by selective inhibition of O-GlcNAcase does not induce insulin resistance. J. Biol. Chem. 283 (2008) 34687-34695
    • (2008) J. Biol. Chem. , vol.283 , pp. 34687-34695
    • Macauley, M.S.1    Bubb, A.K.2    Martinez-Fleites, C.3    Davies, G.J.4    Vocadlo, D.J.5
  • 22
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • Knight Z.A., and Shokat K.M. Features of selective kinase inhibitors. Chem. Biol. 12 (2005) 621-637
    • (2005) Chem. Biol. , vol.12 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2
  • 23
    • 4143074732 scopus 로고    scopus 로고
    • Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: differential effects on glucosamine 6-phosphate, UDP-N-acetylglucosamine, and ATP levels
    • Marshall S., Nadeau O., and Yamasaki K. Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes: differential effects on glucosamine 6-phosphate, UDP-N-acetylglucosamine, and ATP levels. J. Biol. Chem. 279 (2004) 35313-35319
    • (2004) J. Biol. Chem. , vol.279 , pp. 35313-35319
    • Marshall, S.1    Nadeau, O.2    Yamasaki, K.3
  • 24
    • 2442520383 scopus 로고    scopus 로고
    • Hexosamines are unlikely to function as a nutrient-sensor in 3T3-L1 adipocytes: a comparison of UDP-hexosamine levels after increased glucose flux and glucosamine treatment
    • Bosch R.R., Pouwels M.J., Span P.N., Olthaar A.J., Tack C.J., Hermus A.R., and Sweep C.G. Hexosamines are unlikely to function as a nutrient-sensor in 3T3-L1 adipocytes: a comparison of UDP-hexosamine levels after increased glucose flux and glucosamine treatment. Endocrine 23 (2004) 17-24
    • (2004) Endocrine , vol.23 , pp. 17-24
    • Bosch, R.R.1    Pouwels, M.J.2    Span, P.N.3    Olthaar, A.J.4    Tack, C.J.5    Hermus, A.R.6    Sweep, C.G.7
  • 25
    • 0026496182 scopus 로고
    • Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase
    • McKnight G.L., Mudri S.L., Mathewes S.L., Traxinger R.R., Marshall S., Sheppard P.O., and O'Hara P.J. Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase. J. Biol. Chem. 267 (1992) 25208-25212
    • (1992) J. Biol. Chem. , vol.267 , pp. 25208-25212
    • McKnight, G.L.1    Mudri, S.L.2    Mathewes, S.L.3    Traxinger, R.R.4    Marshall, S.5    Sheppard, P.O.6    O'Hara, P.J.7
  • 27
    • 33947109881 scopus 로고    scopus 로고
    • Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes
    • Robinson K.A., Ball L.E., and Buse M.G. Reduction of O-GlcNAc protein modification does not prevent insulin resistance in 3T3-L1 adipocytes. Am. J. Physiol., Endocrinol. Metab. 292 (2007) E884-890
    • (2007) Am. J. Physiol., Endocrinol. Metab. , vol.292
    • Robinson, K.A.1    Ball, L.E.2    Buse, M.G.3
  • 28
    • 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. USA 99 (2002) 5313-5318
    • (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
  • 29
    • 0032493655 scopus 로고    scopus 로고
    • Glucosamine-induced insulin resistance in 3T3-L1 adipocytes is caused by depletion of intracellular ATP
    • Hresko R.C., Heimberg H., Chi M.M., and Mueckler M. Glucosamine-induced insulin resistance in 3T3-L1 adipocytes is caused by depletion of intracellular ATP. J. Biol. Chem. 273 (1998) 20658-20668
    • (1998) J. Biol. Chem. , vol.273 , pp. 20658-20668
    • Hresko, R.C.1    Heimberg, H.2    Chi, M.M.3    Mueckler, M.4
  • 30
    • 14844282748 scopus 로고    scopus 로고
    • Glucosamine induces rapid desensitization of glucose transport in isolated adipocytes by increasing GlcN-6-P levels
    • Marshall S., Yamasaki K., and Okuyama R. Glucosamine induces rapid desensitization of glucose transport in isolated adipocytes by increasing GlcN-6-P levels. Biochem. Biophys. Res. Commun. 329 (2005) 1155-1161
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 1155-1161
    • Marshall, S.1    Yamasaki, K.2    Okuyama, R.3
  • 31
    • 34247194251 scopus 로고    scopus 로고
    • Glucosamine-induced increase in Akt phosphorylation corresponds to increased endoplasmic reticulum stress in astroglial cells
    • Matthews J.A., Belof J.L., Acevedo-Duncan M., and Potter R.L. Glucosamine-induced increase in Akt phosphorylation corresponds to increased endoplasmic reticulum stress in astroglial cells. Mol. Cell. Biochem. 298 (2007) 109-123
    • (2007) Mol. Cell. Biochem. , vol.298 , pp. 109-123
    • Matthews, J.A.1    Belof, J.L.2    Acevedo-Duncan, M.3    Potter, R.L.4
  • 32
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau K.S., Partridge E.A., Grigorian A., Silvescu C.I., Reinhold V.N., Demetriou M., and Dennis J.W. Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129 (2007) 123-134
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 33
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • Ohtsubo K., Takamatsu S., Minowa M.T., Yoshida A., Takeuchi M., and Marth J.D. Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes. Cell 123 (2005) 1307-1321
    • (2005) Cell , vol.123 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6
  • 34
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., and Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell 126 (2006) 855-867
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 36
    • 0037648473 scopus 로고    scopus 로고
    • Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase
    • Iyer S.P., Akimoto Y., and Hart G.W. Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. J. Biol. Chem. 278 (2003) 5399-5409
    • (2003) J. Biol. Chem. , vol.278 , pp. 5399-5409
    • Iyer, S.P.1    Akimoto, Y.2    Hart, G.W.3
  • 37
    • 0042090275 scopus 로고    scopus 로고
    • Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
    • Iyer S.P., and Hart G.W. Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. J. Biol. Chem. 278 (2003) 24608-24616
    • (2003) J. Biol. Chem. , vol.278 , pp. 24608-24616
    • Iyer, S.P.1    Hart, G.W.2
  • 38
  • 39
    • 57349187712 scopus 로고    scopus 로고
    • A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin
    • Slawson C., Lakshmanan T., Knapp S., and Hart G.W. A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin. Mol. Biol. Cell 19 (2008) 4130-4140
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4130-4140
    • Slawson, C.1    Lakshmanan, T.2    Knapp, S.3    Hart, G.W.4
  • 40
    • 67650076327 scopus 로고    scopus 로고
    • Essential role of the glycosyltransferase sxc/Ogt in polycomb repression
    • Gambetta M.C., Oktaba K., and Muller J. Essential role of the glycosyltransferase sxc/Ogt in polycomb repression. Science 325 (2009) 93-96
    • (2009) Science , vol.325 , pp. 93-96
    • Gambetta, M.C.1    Oktaba, K.2    Muller, J.3
  • 42
    • 0021670304 scopus 로고
    • A gene that regulates the bithorax complex differentially in larval and adult cells of Drosophila
    • Ingham P.W. A gene that regulates the bithorax complex differentially in larval and adult cells of Drosophila. Cell 37 (1984) 815-823
    • (1984) Cell , vol.37 , pp. 815-823
    • Ingham, P.W.1
  • 43
    • 44649200464 scopus 로고    scopus 로고
    • Polycomb complexes and epigenetic states
    • Schwartz Y.B., and Pirrotta V. Polycomb complexes and epigenetic states. Curr. Opin. Cell Biol. 20 (2008) 266-273
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 266-273
    • Schwartz, Y.B.1    Pirrotta, V.2
  • 45
    • 25444501339 scopus 로고    scopus 로고
    • Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis
    • Slawson C., Zachara N.E., Vosseller K., Cheung W.D., Lane M.D., and Hart G.W. Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J. Biol. Chem. 280 (2005) 32944-32956
    • (2005) J. Biol. Chem. , vol.280 , pp. 32944-32956
    • Slawson, C.1    Zachara, N.E.2    Vosseller, K.3    Cheung, W.D.4    Lane, M.D.5    Hart, G.W.6
  • 47
    • 59649107122 scopus 로고    scopus 로고
    • Unique hexosaminidase reduces metabolic survival signal and sensitizes cardiac myocytes to hypoxia/reoxygenation injury
    • Ngoh G.A., Facundo H.T., Hamid T., Dillmann W., Zachara N.E., and Jones S.P. Unique hexosaminidase reduces metabolic survival signal and sensitizes cardiac myocytes to hypoxia/reoxygenation injury. Circ. Res. 104 (2009) 41-49
    • (2009) Circ. Res. , vol.104 , pp. 41-49
    • Ngoh, G.A.1    Facundo, H.T.2    Hamid, T.3    Dillmann, W.4    Zachara, N.E.5    Jones, S.P.6
  • 48
    • 0038400185 scopus 로고    scopus 로고
    • Chemical genetics: tailoring tools for cell biology
    • Mayer T.U. Chemical genetics: tailoring tools for cell biology. Trends Cell Biol. 13 (2003) 270-277
    • (2003) Trends Cell Biol. , vol.13 , pp. 270-277
    • Mayer, T.U.1
  • 49
    • 33846676987 scopus 로고    scopus 로고
    • Chemical genetics: where genetics and pharmacology meet
    • Knight Z.A., and Shokat K.M. Chemical genetics: where genetics and pharmacology meet. Cell 128 (2007) 425-430
    • (2007) Cell , vol.128 , pp. 425-430
    • Knight, Z.A.1    Shokat, K.M.2
  • 50
    • 1842580187 scopus 로고    scopus 로고
    • Prolonged incubation in PUGNAc results in increased protein O-Linked glycosylation and insulin resistance in rat skeletal muscle
    • Arias E.B., Kim J., and Cartee G.D. Prolonged incubation in PUGNAc results in increased protein O-Linked glycosylation and insulin resistance in rat skeletal muscle. Diabetes 53 (2004) 921-930
    • (2004) Diabetes , vol.53 , pp. 921-930
    • Arias, E.B.1    Kim, J.2    Cartee, G.D.3
  • 51
    • 33846488647 scopus 로고    scopus 로고
    • Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats
    • Akimoto Y., Hart G.W., Wells L., Vosseller K., Yamamoto K., Munetomo E., Ohara-Imaizumi M., Nishiwaki C., Nagamatsu S., Hirano H., and Kawakami H. Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats. Glycobiology 17 (2007) 127-140
    • (2007) Glycobiology , vol.17 , pp. 127-140
    • Akimoto, Y.1    Hart, G.W.2    Wells, L.3    Vosseller, K.4    Yamamoto, K.5    Munetomo, E.6    Ohara-Imaizumi, M.7    Nishiwaki, C.8    Nagamatsu, S.9    Hirano, H.10    Kawakami, H.11
  • 52
    • 34247110931 scopus 로고    scopus 로고
    • The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels
    • Zou L., Yang S., Hu S., Chaudry I.H., Marchase R.B., and Chatham J.C. The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels. Shock 27 (2007) 402-408
    • (2007) Shock , vol.27 , pp. 402-408
    • Zou, L.1    Yang, S.2    Hu, S.3    Chaudry, I.H.4    Marchase, R.B.5    Chatham, J.C.6
  • 54
    • 34547560123 scopus 로고    scopus 로고
    • The SUMO conjugating enzyme Ubc9 is a regulator of GLUT4 turnover and targeting to the insulin-responsive storage compartment in 3T3-L1 adipocytes
    • Liu L.B., Omata W., Kojima I., and Shibata H. The SUMO conjugating enzyme Ubc9 is a regulator of GLUT4 turnover and targeting to the insulin-responsive storage compartment in 3T3-L1 adipocytes. Diabetes 56 (2007) 1977-1985
    • (2007) Diabetes , vol.56 , pp. 1977-1985
    • Liu, L.B.1    Omata, W.2    Kojima, I.3    Shibata, H.4
  • 55
    • 0142135181 scopus 로고    scopus 로고
    • Effects of nonlipolytic ligand function of endothelial lipase on high density lipoprotein metabolism in vivo
    • Broedl U.C., Maugeais C., Marchadier D., Glick J.M., and Rader D.J. Effects of nonlipolytic ligand function of endothelial lipase on high density lipoprotein metabolism in vivo. J. Biol. Chem. 278 (2003) 40688-40693
    • (2003) J. Biol. Chem. , vol.278 , pp. 40688-40693
    • Broedl, U.C.1    Maugeais, C.2    Marchadier, D.3    Glick, J.M.4    Rader, D.J.5
  • 56
    • 77949309755 scopus 로고    scopus 로고
    • Structural analyses of enzymes involved in the O-GlcNAc modification
    • Martinez-Fleites C., Yuan H., and Davies G. Structural analyses of enzymes involved in the O-GlcNAc modification. Biochim. Biophys. Acta 1800 (2010) 122-133
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 122-133
    • Martinez-Fleites, C.1    Yuan, H.2    Davies, G.3
  • 57
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B., and Bairoch A. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316 (1996) 695-696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 58
    • 11144246904 scopus 로고    scopus 로고
    • Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities
    • Toleman C., Paterson A.J., Whisenhunt T.R., and Kudlow J.E. Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J. Biol. Chem. 279 (2004) 53665-53673
    • (2004) J. Biol. Chem. , vol.279 , pp. 53665-53673
    • Toleman, C.1    Paterson, A.J.2    Whisenhunt, T.R.3    Kudlow, J.E.4
  • 59
    • 53049097590 scopus 로고    scopus 로고
    • Characterization of beta-N-acetylglucosaminidase (O-GlcNAcase) cleavage by caspase-3 during apoptosis
    • Butkinaree C., Cheung W.D., Park S.J., Park K., Barber M., and Hart G.W. Characterization of beta-N-acetylglucosaminidase (O-GlcNAcase) cleavage by caspase-3 during apoptosis. J. Biol. Chem. 283 (2008) 23557-23566
    • (2008) J. Biol. Chem. , vol.283 , pp. 23557-23566
    • Butkinaree, C.1    Cheung, W.D.2    Park, S.J.3    Park, K.4    Barber, M.5    Hart, G.W.6
  • 60
    • 33646139397 scopus 로고    scopus 로고
    • Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate
    • Kim E.J., Kang D.O., Love D.C., and Hanover J.A. Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate. Carbohydr. Res. 341 (2006) 971-982
    • (2006) Carbohydr. Res. , vol.341 , pp. 971-982
    • Kim, E.J.1    Kang, D.O.2    Love, D.C.3    Hanover, J.A.4
  • 61
    • 65649143861 scopus 로고    scopus 로고
    • Enzymatic characterization and inhibition of the nuclear variant of human O-GlcNAcase
    • Macauley M.S., and Vocadlo D.J. Enzymatic characterization and inhibition of the nuclear variant of human O-GlcNAcase. Carbohydr. Res. 344 (2009) 1079-1084
    • (2009) Carbohydr. Res. , vol.344 , pp. 1079-1084
    • Macauley, M.S.1    Vocadlo, D.J.2
  • 62
    • 0034816237 scopus 로고    scopus 로고
    • Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase
    • Comtesse N., Maldener E., and Meese E. Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase. Biochem. Biophys. Res. Commun. 283 (2001) 634-640
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 634-640
    • Comtesse, N.1    Maldener, E.2    Meese, E.3
  • 63
    • 0016271953 scopus 로고
    • Separation and properties of human brain hexosaminidase C
    • Braidman I., Carroll M., Dance N., and Robinson D. Separation and properties of human brain hexosaminidase C. Biochem. J. 143 (1974) 295-301
    • (1974) Biochem. J. , vol.143 , pp. 295-301
    • Braidman, I.1    Carroll, M.2    Dance, N.3    Robinson, D.4
  • 64
    • 0025903560 scopus 로고
    • Purification and properties of neutral beta-N-acetylglucosaminidase from carp blood
    • Ueno R., and Yuan C.S. Purification and properties of neutral beta-N-acetylglucosaminidase from carp blood. Biochim. Biophys. Acta 1074 (1991) 79-84
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 79-84
    • Ueno, R.1    Yuan, C.S.2
  • 66
    • 33645735070 scopus 로고    scopus 로고
    • Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis
    • Rao F.V., Dorfmueller H.C., Villa F., Allwood M., Eggleston I.M., and van Aalten D.M. Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25 (2006) 1569-1578
    • (2006) EMBO J. , vol.25 , pp. 1569-1578
    • Rao, F.V.1    Dorfmueller, H.C.2    Villa, F.3    Allwood, M.4    Eggleston, I.M.5    van Aalten, D.M.6
  • 68
    • 33645226771 scopus 로고    scopus 로고
    • Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants
    • Cetinbas N., Macauley M.S., Stubbs K.A., Drapala R., and Vocadlo D.J. Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants. Biochemistry 45 (2006) 3835-3844
    • (2006) Biochemistry , vol.45 , pp. 3835-3844
    • Cetinbas, N.1    Macauley, M.S.2    Stubbs, K.A.3    Drapala, R.4    Vocadlo, D.J.5
  • 69
    • 65649151773 scopus 로고    scopus 로고
    • Portrait of an enzyme: A complete structural analysis of a multi-modular beta-N-acetylglucosaminidase from clostridium perfringens
    • Ficko-Blean E., Gregg K.J., Adams J.J., Hehemann J.H., Czjzek M., Smith S.P., and Boraston A.B. Portrait of an enzyme: A complete structural analysis of a multi-modular beta-N-acetylglucosaminidase from clostridium perfringens. J. Biol. Chem. 284 (2009) 9876-9884
    • (2009) J. Biol. Chem. , vol.284 , pp. 9876-9884
    • Ficko-Blean, E.1    Gregg, K.J.2    Adams, J.J.3    Hehemann, J.H.4    Czjzek, M.5    Smith, S.P.6    Boraston, A.B.7
  • 70
    • 53849121583 scopus 로고    scopus 로고
    • Mechanistic insights into glycosidase chemistry
    • Vocadlo D.J., and Davies G.J. Mechanistic insights into glycosidase chemistry. Curr. Opin. Chem. Biol. 12 (2008) 539-555
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 539-555
    • Vocadlo, D.J.1    Davies, G.J.2
  • 71
    • 66549119673 scopus 로고    scopus 로고
    • GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation
    • Dorfmueller H.C., Borodkin V.S., Schimpl M., and van Aalten D.M. GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation. Biochem. J. 420 (2009) 221-227
    • (2009) Biochem. J. , vol.420 , pp. 221-227
    • Dorfmueller, H.C.1    Borodkin, V.S.2    Schimpl, M.3    van Aalten, D.M.4
  • 73
    • 33845200606 scopus 로고    scopus 로고
    • A cellular FRET-based sensor for beta-O-GlcNAc, a dynamic carbohydrate modification involved in signaling
    • Carrillo L.D., Krishnamoorthy L., and Mahal L.K. A cellular FRET-based sensor for beta-O-GlcNAc, a dynamic carbohydrate modification involved in signaling. J. Am. Chem. Soc. 128 (2006) 14768-14769
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14768-14769
    • Carrillo, L.D.1    Krishnamoorthy, L.2    Mahal, L.K.3
  • 74
    • 0025782244 scopus 로고
    • N-acetylglucosaminono-1, 5-lactone oxime and the corresponding (phenylcarbamoyl)oxime. Novel and potent inhibitors of beta-N-acetylglucosaminidase
    • Horsch M., Hoesch L., Vasella A., and Rast D.M. N-acetylglucosaminono-1, 5-lactone oxime and the corresponding (phenylcarbamoyl)oxime. Novel and potent inhibitors of beta-N-acetylglucosaminidase. Eur. J. Biochem. 197 (1991) 815-818
    • (1991) Eur. J. Biochem. , vol.197 , pp. 815-818
    • Horsch, M.1    Hoesch, L.2    Vasella, A.3    Rast, D.M.4
  • 75
    • 0027234804 scopus 로고
    • Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida
    • Miller D.J., Gong X., and Shur B.D. Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida. Development 118 (1993) 1279-1289
    • (1993) Development , vol.118 , pp. 1279-1289
    • Miller, D.J.1    Gong, X.2    Shur, B.D.3
  • 76
    • 0035233113 scopus 로고    scopus 로고
    • Naturally occurring mutations in GM2 gangliosidosis: a compendium
    • Triggs-Raine B., Mahuran D.J., and Gravel R.A. Naturally occurring mutations in GM2 gangliosidosis: a compendium. Adv. Genet. 44 (2001) 199-224
    • (2001) Adv. Genet. , vol.44 , pp. 199-224
    • Triggs-Raine, B.1    Mahuran, D.J.2    Gravel, R.A.3
  • 78
    • 59949096567 scopus 로고    scopus 로고
    • O-GlcNAc post-translational modifications regulate the entry of neurons into an axon branching program
    • Francisco H., Kollins K., Varghis N., Vocadlo D., Vosseller K., and Gallo G. O-GlcNAc post-translational modifications regulate the entry of neurons into an axon branching program. Dev. Neurobiol. 69 (2009) 162-173
    • (2009) Dev. Neurobiol. , vol.69 , pp. 162-173
    • Francisco, H.1    Kollins, K.2    Varghis, N.3    Vocadlo, D.4    Vosseller, K.5    Gallo, G.6
  • 80
    • 0025817121 scopus 로고
    • A specific type of ganglioside as a modulator of insulin-dependent cell growth and insulin receptor tyrosine kinase activity. Possible association of ganglioside-induced inhibition of insulin receptor function and monocytic differentiation induction in HL-60 cells
    • Nojiri H., Stroud M., and Hakomori S. A specific type of ganglioside as a modulator of insulin-dependent cell growth and insulin receptor tyrosine kinase activity. Possible association of ganglioside-induced inhibition of insulin receptor function and monocytic differentiation induction in HL-60 cells. J. Biol. Chem. 266 (1991) 4531-4537
    • (1991) J. Biol. Chem. , vol.266 , pp. 4531-4537
    • Nojiri, H.1    Stroud, M.2    Hakomori, S.3
  • 82
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance
    • Stubbs K.A., Balcewich M., Mark B.L., and Vocadlo D.J. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance. J. Biol. Chem. 282 (2007) 21382-21391
    • (2007) J. Biol. Chem. , vol.282 , pp. 21382-21391
    • Stubbs, K.A.1    Balcewich, M.2    Mark, B.L.3    Vocadlo, D.J.4
  • 84
    • 0034810802 scopus 로고    scopus 로고
    • Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: diagnostic, clinical, and biological implications
    • Yogalingam G., and Hopwood J.J. Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: diagnostic, clinical, and biological implications. Hum. Mutat. 18 (2001) 264-281
    • (2001) Hum. Mutat. , vol.18 , pp. 264-281
    • Yogalingam, G.1    Hopwood, J.J.2
  • 86
    • 0028604486 scopus 로고
    • STZ transport and cytotoxicity. Specific enhancement in GLUT2-expressing cells
    • Schnedl W.J., Ferber S., Johnson J.H., and Newgard C.B. STZ transport and cytotoxicity. Specific enhancement in GLUT2-expressing cells. Diabetes 43 (1994) 1326-1333
    • (1994) Diabetes , vol.43 , pp. 1326-1333
    • Schnedl, W.J.1    Ferber, S.2    Johnson, J.H.3    Newgard, C.B.4
  • 87
    • 0019501634 scopus 로고
    • Alkylation of DNA in rat tissues following administration of streptozotocin
    • Bennett R.A., and Pegg A.E. Alkylation of DNA in rat tissues following administration of streptozotocin. Cancer Res. 41 (1981) 2786-2790
    • (1981) Cancer Res. , vol.41 , pp. 2786-2790
    • Bennett, R.A.1    Pegg, A.E.2
  • 88
    • 0029257151 scopus 로고
    • Nitric oxide generation during cellular metabolization of the diabetogenic N-methyl-N-nitroso-urea streptozotozin contributes to islet cell DNA damage
    • Kroncke K.D., Fehsel K., Sommer A., Rodriguez M.L., and Kolb-Bachofen V. Nitric oxide generation during cellular metabolization of the diabetogenic N-methyl-N-nitroso-urea streptozotozin contributes to islet cell DNA damage. Biol. Chem. Hoppe-Seyler 376 (1995) 179-185
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 179-185
    • Kroncke, K.D.1    Fehsel, K.2    Sommer, A.3    Rodriguez, M.L.4    Kolb-Bachofen, V.5
  • 89
    • 0019812690 scopus 로고
    • Streptozotocin and alloxan induce DNA strand breaks and poly(ADP-ribose) synthetase in pancreatic islets
    • Yamamoto H., Uchigata Y., and Okamoto H. Streptozotocin and alloxan induce DNA strand breaks and poly(ADP-ribose) synthetase in pancreatic islets. Nature 294 (1981) 284-286
    • (1981) Nature , vol.294 , pp. 284-286
    • Yamamoto, H.1    Uchigata, Y.2    Okamoto, H.3
  • 90
    • 0035872219 scopus 로고    scopus 로고
    • The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase
    • Konrad R.J., Mikolaenko I., Tolar J.F., Liu K., and Kudlow J.E. The potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase. Biochem. J. 356 (2001) 31-41
    • (2001) Biochem. J. , vol.356 , pp. 31-41
    • Konrad, R.J.1    Mikolaenko, I.2    Tolar, J.F.3    Liu, K.4    Kudlow, J.E.5
  • 92
    • 0033080192 scopus 로고    scopus 로고
    • Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells
    • Hanover J.A., Lai Z., Lee G., Lubas W.A., and Sato S.M. Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells. Arch. Biochem. Biophys. 362 (1999) 38-45
    • (1999) Arch. Biochem. Biophys. , vol.362 , pp. 38-45
    • Hanover, J.A.1    Lai, Z.2    Lee, G.3    Lubas, W.A.4    Sato, S.M.5
  • 94
    • 33747179908 scopus 로고    scopus 로고
    • The diabetogenic antibiotic streptozotocin modifies the tryptic digest pattern for peptides of the enzyme O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase that contain amino acid residues essential for enzymatic activity
    • Lee T.N., Alborn W.E., Knierman M.D., and Konrad R.J. The diabetogenic antibiotic streptozotocin modifies the tryptic digest pattern for peptides of the enzyme O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase that contain amino acid residues essential for enzymatic activity. Biochem. Pharmacol. 72 (2006) 710-718
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 710-718
    • Lee, T.N.1    Alborn, W.E.2    Knierman, M.D.3    Konrad, R.J.4
  • 95
    • 49449101898 scopus 로고    scopus 로고
    • Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death
    • Pathak S., Dorfmueller H.C., Borodkin V.S., and van Aalten D.M. Chemical dissection of the link between streptozotocin, O-GlcNAc, and pancreatic cell death. Chem. Biol. 15 (2008) 799-807
    • (2008) Chem. Biol. , vol.15 , pp. 799-807
    • Pathak, S.1    Dorfmueller, H.C.2    Borodkin, V.S.3    van Aalten, D.M.4
  • 96
    • 62549165181 scopus 로고    scopus 로고
    • Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase
    • He Y., Martinez-Fleites C., Bubb A., Gloster T.M., and Davies G.J. Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase. Carbohydr. Res. 340 (2008) 627-631
    • (2008) Carbohydr. Res. , vol.340 , pp. 627-631
    • He, Y.1    Martinez-Fleites, C.2    Bubb, A.3    Gloster, T.M.4    Davies, G.J.5
  • 97
    • 29644436424 scopus 로고    scopus 로고
    • Streptozotocin inhibits O-GlcNAcase via the production of a transition state analog
    • Toleman C., Paterson A.J., Shin R., and Kudlow J.E. Streptozotocin inhibits O-GlcNAcase via the production of a transition state analog. Biochem. Biophys. Res. Commun. 340 (2006) 526-534
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 526-534
    • Toleman, C.1    Paterson, A.J.2    Shin, R.3    Kudlow, J.E.4
  • 98
    • 0034669371 scopus 로고    scopus 로고
    • Streptozotocin-induced beta-cell death is independent of its inhibition of O-GlcNAcase in pancreatic Min6 cells
    • Gao Y., Parker G.J., and Hart G.W. Streptozotocin-induced beta-cell death is independent of its inhibition of O-GlcNAcase in pancreatic Min6 cells. Arch. Biochem. Biophys. 383 (2000) 296-302
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 296-302
    • Gao, Y.1    Parker, G.J.2    Hart, G.W.3
  • 99
    • 0035929167 scopus 로고    scopus 로고
    • Cytosolic O-GlcNAc accumulation is not involved in beta-cell death in HIT-T15 or Min6
    • Okuyama R., and Yachi M. Cytosolic O-GlcNAc accumulation is not involved in beta-cell death in HIT-T15 or Min6. Biochem. Biophys. Res. Commun. 287 (2001) 366-371
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 366-371
    • Okuyama, R.1    Yachi, M.2
  • 100
    • 62549161375 scopus 로고    scopus 로고
    • Loss of p53 enhances catalytic activity of IKK{beta} through O-linked {beta}-N-acetyl glucosamine modification
    • Kawauchi K., Araki K., Tobiume K., and Tanaka N. Loss of p53 enhances catalytic activity of IKK{beta} through O-linked {beta}-N-acetyl glucosamine modification. Proc. Natl. Acad. Sci. USA 106 (2009) 3431-3436
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3431-3436
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 101
    • 33749160125 scopus 로고    scopus 로고
    • Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang W.H., Kim J.E., Nam H.W., Ju J.W., Kim H.S., Kim Y.S., and Cho J.W. Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat. Cell Biol. 8 (2006) 1074-1083
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1074-1083
    • Yang, W.H.1    Kim, J.E.2    Nam, H.W.3    Ju, J.W.4    Kim, H.S.5    Kim, Y.S.6    Cho, J.W.7
  • 102
    • 0029947945 scopus 로고    scopus 로고
    • NAG-thiazoline, an N-acetyl-beta-hexosaminidase inhibitor that implicates acetamido participation
    • Knapp S., Vocadlo D., Gao Z.N., Kirk B., Lou J.P., and Withers S.G. NAG-thiazoline, an N-acetyl-beta-hexosaminidase inhibitor that implicates acetamido participation. J. Am. Chem. Soc. 118 (1996) 6804-6805
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6804-6805
    • Knapp, S.1    Vocadlo, D.2    Gao, Z.N.3    Kirk, B.4    Lou, J.P.5    Withers, S.G.6
  • 103
    • 0344837327 scopus 로고    scopus 로고
    • Crystal structure of human beta-hexosaminidase B: Understanding the molecular basis of Sandhoff and Tay-Sachs disease
    • Mark B.L., Mahuran D.J., Cherney M.M., Zhao D.L., Knapp S., and James M.N.G. Crystal structure of human beta-hexosaminidase B: Understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol. 327 (2003) 1093-1109
    • (2003) J. Mol. Biol. , vol.327 , pp. 1093-1109
    • Mark, B.L.1    Mahuran, D.J.2    Cherney, M.M.3    Zhao, D.L.4    Knapp, S.5    James, M.N.G.6
  • 105
    • 33846412613 scopus 로고    scopus 로고
    • Analysis of PUGNAc and NAG-thiazoline as transition state analogues for human O-GlcNAcase: mechanistic and structural insights into inhibitor selectivity and transition state poise
    • Whitworth G.E., Macauley M.S., Stubbs K.A., Dennis R.J., Taylor E.J., Davies G.J., Greig I.R., and Vocadlo D.J. Analysis of PUGNAc and NAG-thiazoline as transition state analogues for human O-GlcNAcase: mechanistic and structural insights into inhibitor selectivity and transition state poise. J. Am. Chem. Soc. 129 (2007) 635-644
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 635-644
    • Whitworth, G.E.1    Macauley, M.S.2    Stubbs, K.A.3    Dennis, R.J.4    Taylor, E.J.5    Davies, G.J.6    Greig, I.R.7    Vocadlo, D.J.8
  • 106
    • 60149092312 scopus 로고    scopus 로고
    • A selective inhibitor Gal-PUGNAc of human lysosomal beta-hexosaminidases modulates levels of the ganglioside GM2 in neuroblastoma cells
    • Stubbs K.A., Macauley M.S., and Vocadlo D.J. A selective inhibitor Gal-PUGNAc of human lysosomal beta-hexosaminidases modulates levels of the ganglioside GM2 in neuroblastoma cells. Angew Chem., Int. Ed. 48 (2009) 1300-1303
    • (2009) Angew Chem., Int. Ed. , vol.48 , pp. 1300-1303
    • Stubbs, K.A.1    Macauley, M.S.2    Vocadlo, D.J.3
  • 107
    • 29044433378 scopus 로고    scopus 로고
    • O-GlcNAcase catalyzes cleavage of thioglycosides without general acid catalysis
    • Macauley M.S., Stubbs K.A., and Vocadlo D.J. O-GlcNAcase catalyzes cleavage of thioglycosides without general acid catalysis. J. Am. Chem. Soc. 127 (2005) 17202-17203
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17202-17203
    • Macauley, M.S.1    Stubbs, K.A.2    Vocadlo, D.J.3
  • 108
    • 84963951245 scopus 로고    scopus 로고
    • Theoretical study of structure, pKa, lipophilicity, solubility, absorption, and polar surface area of some centrally acting antihypertensives
    • Remko M., Swart M., and Bickelhaupt F.M. Theoretical study of structure, pKa, lipophilicity, solubility, absorption, and polar surface area of some centrally acting antihypertensives. Bioorg. Med. Chem. 14 (2006) 1715-1728
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 1715-1728
    • Remko, M.1    Swart, M.2    Bickelhaupt, F.M.3
  • 111
    • 33344473040 scopus 로고    scopus 로고
    • A divergent synthesis of 2-acyl derivatives of PUGNAc yields selective inhibitors of O-GlcNAcase
    • Stubbs K.A., Zhang N., and Vocadlo D.J. A divergent synthesis of 2-acyl derivatives of PUGNAc yields selective inhibitors of O-GlcNAcase. Org. Biomol. Chem. 4 (2006) 839-845
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 839-845
    • Stubbs, K.A.1    Zhang, N.2    Vocadlo, D.J.3
  • 112
    • 33645469261 scopus 로고    scopus 로고
    • An O-GlcNAcase-specific inhibitor and substrate engineered by the extension of the N-acetyl moiety
    • Kim E.J., Perreira M., Thomas C.J., and Hanover J.A. An O-GlcNAcase-specific inhibitor and substrate engineered by the extension of the N-acetyl moiety. J. Am. Chem. Soc. 128 (2006) 4234-4235
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4234-4235
    • Kim, E.J.1    Perreira, M.2    Thomas, C.J.3    Hanover, J.A.4
  • 113
    • 67650070343 scopus 로고    scopus 로고
    • Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ
    • Balcewich M.D., Stubbs K.A., He Y., James T.W., Davies G.J., Vocadlo D.J., and Mark B.L. Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci. 18 (2009) 1541-1551
    • (2009) Protein Sci. , vol.18 , pp. 1541-1551
    • Balcewich, M.D.1    Stubbs, K.A.2    He, Y.3    James, T.W.4    Davies, G.J.5    Vocadlo, D.J.6    Mark, B.L.7
  • 115
    • 0026778638 scopus 로고
    • Nagstatin, a new inhibitor of N-acetyl-beta-d-glucosaminidase, produced by Streptomyces amakusaensis MG846-fF3. Taxonomy, production, isolation, physico-chemical properties and biological activities
    • Aoyagi T., Suda H., Uotani K., Kojima F., Aoyama T., Horiguchi K., Hamada M., and Takeuchi T. Nagstatin, a new inhibitor of N-acetyl-beta-d-glucosaminidase, produced by Streptomyces amakusaensis MG846-fF3. Taxonomy, production, isolation, physico-chemical properties and biological activities. J. Antibiot. (Tokyo) 45 (1992) 1404-1408
    • (1992) J. Antibiot. (Tokyo) , vol.45 , pp. 1404-1408
    • Aoyagi, T.1    Suda, H.2    Uotani, K.3    Kojima, F.4    Aoyama, T.5    Horiguchi, K.6    Hamada, M.7    Takeuchi, T.8
  • 116
    • 14644432504 scopus 로고    scopus 로고
    • Synthesis of N-acetylglucosamine-derived nagstatin analogues and their evaluation as glycosidase inhibitors
    • Terinek M., and Vasella A. Synthesis of N-acetylglucosamine-derived nagstatin analogues and their evaluation as glycosidase inhibitors. Helv. Chim. Acta. 88 (2005) 10-22
    • (2005) Helv. Chim. Acta. , vol.88 , pp. 10-22
    • Terinek, M.1    Vasella, A.2
  • 118
  • 119
    • 67749092463 scopus 로고    scopus 로고
    • Molecular basis for inhibition of GH84 glycoside hydrolases by substituted azepanes: conformational flexibility enables probing of substrate distortion
    • Marcelo F., He Y., Yuzwa S.A., Nieto L., Jimenez-Barbero J., Sollogoub M., Vocadlo D.J., Davies G.D., and Bleriot Y. Molecular basis for inhibition of GH84 glycoside hydrolases by substituted azepanes: conformational flexibility enables probing of substrate distortion. J. Am. Chem. Soc. 131 (2009) 5390-5392
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5390-5392
    • Marcelo, F.1    He, Y.2    Yuzwa, S.A.3    Nieto, L.4    Jimenez-Barbero, J.5    Sollogoub, M.6    Vocadlo, D.J.7    Davies, G.D.8    Bleriot, Y.9
  • 121
    • 0022363751 scopus 로고
    • Glucose as a regulator of insulin-sensitive hexose uptake in 3T3 adipocytes
    • van Putten J.P., and Krans H.M. Glucose as a regulator of insulin-sensitive hexose uptake in 3T3 adipocytes. J. Biol. Chem. 260 (1985) 7996-8001
    • (1985) J. Biol. Chem. , vol.260 , pp. 7996-8001
    • van Putten, J.P.1    Krans, H.M.2
  • 122
    • 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
  • 123
    • 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
  • 124
    • 0027295399 scopus 로고
    • Regulation of insulin-stimulated glycogen synthase activity by overexpression of glutamine: fructose-6-phosphate amidotransferase in rat-1 fibroblasts
    • Crook E.D., Daniels M.C., Smith T.M., and McClain D.A. Regulation of insulin-stimulated glycogen synthase activity by overexpression of glutamine: fructose-6-phosphate amidotransferase in rat-1 fibroblasts. Diabetes 42 (1993) 1289-1296
    • (1993) Diabetes , vol.42 , pp. 1289-1296
    • Crook, E.D.1    Daniels, M.C.2    Smith, T.M.3    McClain, D.A.4
  • 125
    • 0025855139 scopus 로고
    • Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance
    • Marshall S., Bacote V., and Traxinger R.R. Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J. Biol. Chem. 266 (1991) 4706-4712
    • (1991) J. Biol. Chem. , vol.266 , pp. 4706-4712
    • Marshall, S.1    Bacote, V.2    Traxinger, R.R.3
  • 126
    • 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
  • 127
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • Nemoto S., Fergusson M.M., and Finkel T. Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science 306 (2004) 2105-2108
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 128
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers J.T., Lerin C., Haas W., Gygi S.P., Spiegelman B.M., and Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434 (2005) 113-118
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 129
    • 22244471058 scopus 로고    scopus 로고
    • O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes
    • Park S.Y., Ryu J., and Lee W. O-GlcNAc modification on IRS-1 and Akt2 by PUGNAc inhibits their phosphorylation and induces insulin resistance in rat primary adipocytes. Exp. Mol. Med. 37 (2005) 220-229
    • (2005) Exp. Mol. Med. , vol.37 , pp. 220-229
    • Park, S.Y.1    Ryu, J.2    Lee, W.3
  • 130
    • 40449128605 scopus 로고    scopus 로고
    • Hepatic glucose sensing via the CREB coactivator CRTC2
    • Dentin R., Hedrick S., Xie J., Yates III J., and Montminy M. Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319 (2008) 1402-1405
    • (2008) Science , vol.319 , pp. 1402-1405
    • Dentin, R.1    Hedrick, S.2    Xie, J.3    Yates III, J.4    Montminy, M.5
  • 131
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara N.E., O'Donnell N., Cheung W.D., Mercer J.J., Marth J.D., and Hart G.W. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J. Biol. Chem. 279 (2004) 30133-30142
    • (2004) J. Biol. Chem. , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6
  • 132
    • 45149095784 scopus 로고    scopus 로고
    • AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation
    • Cheung W.D., and Hart G.W. AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation. J. Biol. Chem. 283 (2008) 13009-13020
    • (2008) J. Biol. Chem. , vol.283 , pp. 13009-13020
    • Cheung, W.D.1    Hart, G.W.2
  • 133
    • 44449166220 scopus 로고    scopus 로고
    • Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase
    • Taylor R.P., Parker G.J., Hazel M.W., Soesanto Y., Fuller W., Yazzie M.J., and McClain D.A. Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase. J. Biol. Chem. 283 (2008) 6050-6057
    • (2008) J. Biol. Chem. , vol.283 , pp. 6050-6057
    • Taylor, R.P.1    Parker, G.J.2    Hazel, M.W.3    Soesanto, Y.4    Fuller, W.5    Yazzie, M.J.6    McClain, D.A.7
  • 135
    • 33846317766 scopus 로고    scopus 로고
    • Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc
    • Champattanachai V., Marchase R.B., and Chatham J.C. Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc. Am. J. Physiol., Cell Physiol. 292 (2007) C178-187
    • (2007) Am. J. Physiol., Cell Physiol. , vol.292
    • Champattanachai, V.1    Marchase, R.B.2    Chatham, J.C.3
  • 137
    • 47249102179 scopus 로고    scopus 로고
    • Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2
    • Champattanachai V., Marchase R.B., and Chatham J.C. Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2. Am. J. Physiol., Cell Physiol. 294 (2008) C1509-C1520
    • (2008) Am. J. Physiol., Cell Physiol. , vol.294
    • Champattanachai, V.1    Marchase, R.B.2    Chatham, J.C.3
  • 138
    • 2142790225 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation
    • Griffith L.S., and Schmitz B. O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation. Eur. J. Biochem. 262 (1999) 824-831
    • (1999) Eur. J. Biochem. , vol.262 , pp. 824-831
    • Griffith, L.S.1    Schmitz, B.2
  • 139
    • 0035800086 scopus 로고    scopus 로고
    • Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II
    • Comer F.I., and Hart G.W. Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 40 (2001) 7845-7852
    • (2001) Biochemistry , vol.40 , pp. 7845-7852
    • Comer, F.I.1    Hart, G.W.2
  • 140
    • 0034718570 scopus 로고    scopus 로고
    • Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta
    • Cheng X., Cole R.N., Zaia J., and Hart G.W. Alternative O-glycosylation/O-phosphorylation of the murine estrogen receptor beta. Biochemistry 39 (2000) 11609-11620
    • (2000) Biochemistry , vol.39 , pp. 11609-11620
    • Cheng, X.1    Cole, R.N.2    Zaia, J.3    Hart, G.W.4
  • 141
    • 0029049198 scopus 로고
    • c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • Chou T.Y., Hart G.W., and Dang C.V. c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J. Biol. Chem. 270 (1995) 18961-18965
    • (1995) J. Biol. Chem. , vol.270 , pp. 18961-18965
    • Chou, T.Y.1    Hart, G.W.2    Dang, C.V.3
  • 142
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease
    • Liu F., Iqbal K., Grundke-Iqbal I., Hart G.W., and Gong C.X. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 101 (2004) 10804-10809
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 145
    • 4444337997 scopus 로고    scopus 로고
    • Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain
    • Khidekel N., Ficarro S.B., Peters E.C., and Hsieh-Wilson L.C. Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain. Proc. Natl. Acad. Sci. USA 101 (2004) 13132-13137
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13132-13137
    • Khidekel, N.1    Ficarro, S.B.2    Peters, E.C.3    Hsieh-Wilson, L.C.4
  • 146
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J., and Hart G.W. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell. Proteomics 1 (2002) 791-804
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 147
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., and Burlingame A.L. Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 5 (2005) 388-398
    • (2005) Proteomics , vol.5 , pp. 388-398
    • Vosseller, K.1    Hansen, K.C.2    Chalkley, R.J.3    Trinidad, J.C.4    Wells, L.5    Hart, G.W.6    Burlingame, A.L.7
  • 150
    • 44649107616 scopus 로고    scopus 로고
    • Sp1 modulates ncOGT activity to alter target recognition and enhanced thermotolerance in E. coli
    • Riu I.H., Shin I.S., and Do S.I. Sp1 modulates ncOGT activity to alter target recognition and enhanced thermotolerance in E. coli. Biochem. Biophys. Res. Commun. 372 (2008) 203-209
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 203-209
    • Riu, I.H.1    Shin, I.S.2    Do, S.I.3
  • 152
    • 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
  • 153
    • 0019201785 scopus 로고
    • Mutagenicity of d- and l-azaserine, 6-diazo-5-oxo-L-norleucine and N-(N-methyl-N-nitroso-carbamyl)-l-ornithine in the Salmonella test system
    • Staiano N., Everson R.B., Cooney D.A., Longnecker D.S., and Thorgeirsson S.S. Mutagenicity of d- and l-azaserine, 6-diazo-5-oxo-L-norleucine and N-(N-methyl-N-nitroso-carbamyl)-l-ornithine in the Salmonella test system. Mutat. Res. 79 (1980) 387-390
    • (1980) Mutat. Res. , vol.79 , pp. 387-390
    • Staiano, N.1    Everson, R.B.2    Cooney, D.A.3    Longnecker, D.S.4    Thorgeirsson, S.S.5
  • 154
    • 0033166518 scopus 로고    scopus 로고
    • A mechanism behind the antitumour effect of 6-diazo-5-oxo-l-norleucine (DON): disruption of mitochondria
    • Wu F., Lukinius A., Bergstrom M., Eriksson B., Watanabe Y., and Langstrom B. A mechanism behind the antitumour effect of 6-diazo-5-oxo-l-norleucine (DON): disruption of mitochondria. Eur. J. Cancer 35 (1999) 1155-1161
    • (1999) Eur. J. Cancer , vol.35 , pp. 1155-1161
    • Wu, F.1    Lukinius, A.2    Bergstrom, M.3    Eriksson, B.4    Watanabe, Y.5    Langstrom, B.6
  • 156
    • 0026597569 scopus 로고
    • Extracellular reduction of alloxan results in oxygen radical-mediated attack on plasma and lysosomal membranes
    • Zhang H., Gao G., and Brunk U.T. Extracellular reduction of alloxan results in oxygen radical-mediated attack on plasma and lysosomal membranes. Apmis 100 (1992) 317-325
    • (1992) Apmis , vol.100 , pp. 317-325
    • Zhang, H.1    Gao, G.2    Brunk, U.T.3
  • 157
    • 27144455345 scopus 로고    scopus 로고
    • Discovery of O-GlcNAc transferase inhibitors
    • Gross B.J., Kraybill B.C., and Walker S. Discovery of O-GlcNAc transferase inhibitors. J. Am. Chem. Soc. 127 (2005) 14588-14589
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14588-14589
    • Gross, B.J.1    Kraybill, B.C.2    Walker, S.3
  • 158
    • 56849104094 scopus 로고    scopus 로고
    • Marine toxins and the cytoskeleton: okadaic acid and dinophysistoxins
    • Vale C., and Botana L.M. Marine toxins and the cytoskeleton: okadaic acid and dinophysistoxins. FEBS J. 275 (2008) 6060-6066
    • (2008) FEBS J. , vol.275 , pp. 6060-6066
    • Vale, C.1    Botana, L.M.2


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