메뉴 건너뛰기




Volumn 6, Issue 5, 2009, Pages 451-454

O-GlcNAc modification and the tauopathies: Insights from chemical biology

Author keywords

Glucosaminidase; Glycoside hydrolase; O GlcNAc; Phosphorylation; Tau

Indexed keywords

1,2 DIDEOXY 2' PROPYL ALPHA DEXTRO GLUCOPYRANOSO [2,1 D] DELTA2' THIAZOLINE; GLYCOSIDASE; GLYCOSIDASE INHIBITOR; N ACETYLGLUCOSAMINE; O (2 ACETAMIDO 2 DEOXY DEXTRO GLUCOPYRANOSYLIDENE)AMINO N PHENYLCARBAMATE; OKADAIC ACID; TAU PROTEIN; THIAMET G; UNCLASSIFIED DRUG;

EID: 70249096980     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720509789207967     Document Type: Conference Paper
Times cited : (24)

References (28)
  • 3
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. a component of Alzheimer paired helical filaments
    • Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, Wisniewski HM. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261: 6084-6089 (1986). (Pubitemid 17207447)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.13 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3
  • 4
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 83: 4044-4048 (1986).
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 5
    • 0026676007 scopus 로고
    • Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments
    • DOI 10.1016/0006-8993(92)91476-U
    • Ksiezak-Reding H, Liu WK, Yen SH. Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments. Brain Res 597: 209-219 (1992). (Pubitemid 23003689)
    • (1992) Brain Research , vol.597 , Issue.2 , pp. 209-219
    • Ksiezak-Reding, H.1    Liu, W.-K.2    Yen, S.-H.3
  • 6
    • 49149098525 scopus 로고    scopus 로고
    • Tau aggregates: Toxic, inert, or protective species?
    • Bretteville A, Planel E. Tau aggregates: toxic, inert, or protective species? J Alzheimers Dis 14: 431-436 (2008).
    • (2008) J Alzheimers Dis , vol.14 , pp. 431-436
    • Bretteville, A.1    Planel, E.2
  • 9
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • Torres CR, Hart, GW. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 259: 3308-3317 (1984).
    • (1984) J Biol Chem , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2
  • 10
    • 0029670515 scopus 로고    scopus 로고
    • Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin
    • Roquemore EP, Chevrier MR, Cotter RJ, Hart GW. Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry 35: 3578-3586 (1996).
    • (1996) Biochemistry , vol.35 , pp. 3578-3586
    • Roquemore, E.P.1    Chevrier, M.R.2    Cotter, R.J.3    Hart, G.W.4
  • 11
    • 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 LK, Blomberg MA, Hart GW. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272: 9308-9315 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 12
    • 0030944105 scopus 로고    scopus 로고
    • O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • DOI 10.1074/jbc.272.14.9316
    • Lubas WA, Frank DW, Krause M, Hanover JA. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J Biol Chem 272: 9316-9324 (1997). (Pubitemid 27154944)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 13
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol
    • Dong DL, Hart GW. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J Biol Chem 269: 19321-19330 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 14
    • 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
    • DOI 10.1074/jbc.M010420200
    • Gao Y, Wells L, Comer FI, Parker GJ, Hart GW. 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: 9838-9845 (2001). (Pubitemid 37391884)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.13 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 15
    • 0842347416 scopus 로고    scopus 로고
    • Ogt-Dependent X-Chromosome-Linked Protein Glycosylation Is a Requisite Modification in Somatic Cell Function and Embryo Viability
    • DOI 10.1128/MCB.24.4.1680-1690.2004
    • O'Donnell N, Zachara NE, Hart GW, Marth JD. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability. Mol Cell Biol. 24: 1680-1690 (2004). (Pubitemid 38167089)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.4 , pp. 1680-1690
    • O'Donnell, N.1    Zachara, N.E.2    Hart, G.W.3    Marth, J.D.4
  • 16
    • 0026628626 scopus 로고
    • Inhibitory effect of okadaic acid derivatives on protein phosphatases. A study on structure-affinity relationship
    • Takai A, Murata M, Torigoe K, Isobe M, Mieskes G, Yasumoto T. Inhibitory effect of okadaic acid derivatives on protein phosphatases. A study on structure-affinity relationship. Biochem J 284 (Pt 2): 539-544 (1992).
    • (1992) Biochem J , vol.284 , Issue.PART 2 , pp. 539-544
    • Takai, A.1    Murata, M.2    Torigoe, K.3    Isobe, M.4    Mieskes, G.5    Yasumoto, T.6
  • 18
    • 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, Rast DM. N-acetylglucosaminono-1,5-lactone oxime and the corresponding (phenylcarbamoyl) oxime. Novel and potent inhibitors of beta-N-acetylglucosaminidase. Eur J Biochem 197: 815-818 (1991).
    • (1991) Eur J Biochem , vol.197 , pp. 815-818
    • Horsch, M.1    Hoesch, L.2    Vasella, A.3    Rast, D.M.4
  • 19
    • 33646008860 scopus 로고    scopus 로고
    • Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting
    • Li X, Lu F, Wang JZ, Gong CX. Concurrent alterations of O-GlcNAcylation and phosphorylation of tau in mouse brains during fasting. Eur J Neurosci 23: 2078-2086 (2006).
    • (2006) Eur J Neurosci , vol.23 , pp. 2078-2086
    • Li, X.1    Lu, F.2    Wang, J.Z.3    Gong, C.X.4
  • 20
    • 34247110931 scopus 로고    scopus 로고
    • The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels
    • DOI 10.1097/01.shk.0000245031.31859.29, PII 0002438220070400000011
    • Zou L, Yang S, Hu S, Chaudry IH, Marchase RB, Chatham JC. The protective effects of PUGNAc on cardiac function after trauma-hemorrhage are mediated via increased protein O-GlcNAc levels. Shock 27: 402-408 (2007). (Pubitemid 46594972)
    • (2007) Shock , vol.27 , Issue.4 , pp. 402-408
    • Zou, L.1    Yang, S.2    Hu, S.3    Chaudry, I.H.4    Marchase, R.B.5    Chatham, J.C.6
  • 21
    • 21844464281 scopus 로고    scopus 로고
    • O-GlcNAcase uses substrate-assisted catalysis: Kinetic analysis and development of highly selective mechanism-inspired inhibitors
    • DOI 10.1074/jbc.M413819200
    • Macauley MS, Whitworth GE, Debowski AW, Chin D, Vocadlo DJ. O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J Biol Chem 280: 25313-25322 (2005). (Pubitemid 40962233)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25313-25322
    • Macauley, M.S.1    Whitworth, G.E.2    Debowski, A.W.3    Chin, D.4    Vocadlo, D.J.5
  • 22
    • 60149092312 scopus 로고    scopus 로고
    • A selective inhibitor of human lysosomal β-hexosaminidases: Gal-PUGNAc modulates levels of the ganglioside GM2 in neuroblastoma cells
    • Stubbs KA, Macauley MS, Vocadlo DJ. A selective inhibitor of human lysosomal β-hexosaminidases: Gal-PUGNAc modulates levels of the ganglioside GM2 in neuroblastoma cells. Angew Chem Int Ed 48: 1300-1303 (2009).
    • (2009) Angew Chem Int Ed , vol.48 , pp. 1300-1303
    • Stubbs, K.A.1    Macauley, M.S.2    Vocadlo, D.J.3
  • 23
    • 0035876021 scopus 로고    scopus 로고
    • Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine
    • DOI 10.1006/abio.2001.5132
    • Comer FI, Vosseller K, Wells L, Accavitti, MA, Hart GW. Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine. Anal Biochem 293: 169-177 (2001). (Pubitemid 32547901)
    • (2001) Analytical Biochemistry , vol.293 , Issue.2 , pp. 169-177
    • Comer, F.I.1    Vosseller, K.2    Wells, L.3    Accavitti, M.A.4    Hart, G.W.5
  • 24
    • 47649114560 scopus 로고    scopus 로고
    • A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
    • Yuzwa SA, Macauley MS, Davies GJ, Vocadlo DJ. A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat Chem Biol 4: 483-490 (2008).
    • (2008) Nat Chem Biol , vol.4 , pp. 483-490
    • Yuzwa, S.A.1    Macauley, M.S.2    Davies, G.J.3    Vocadlo, D.J.4
  • 25
    • 33644870413 scopus 로고    scopus 로고
    • 396 of microtubule-associated protein tau by a sequential mechanism
    • DOI 10.1021/bi051634r
    • Li T, Hawkes C, Qureshi HY, Kar S, Paudel, HK. Cyclin-dependent protein kinase 5 primes microtubule-associated protein tau site-specifically for glycogen synthase kinase 3β. Biochemistry 45: 3134-3145 (2006). (Pubitemid 43376331)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3125-3133
    • Li, T.1    Paudel, H.K.2
  • 26
    • 0346457015 scopus 로고    scopus 로고
    • Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules
    • Cho JH, Johnson GV. Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3beta (GSK3beta) plays a critical role in regulating tau's ability to bind and stabilize microtubules. J Neurochem 88: 349-358 (2004).
    • (2004) J Neurochem , vol.88 , pp. 349-358
    • Cho, J.H.1    Johnson, G.V.2
  • 27
    • 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, Hart GW. Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc Natl Acad Sci USA 105: 13793-13798 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13793-13798
    • Wang, Z.1    Gucek, M.2    Hart, G.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.