메뉴 건너뛰기




Volumn 290, Issue 2, 2015, Pages 841-850

Glycogen phosphomonoester distribution in mouse models of the progressive myoclonic epilepsy, Lafora disease

Author keywords

[No Author keywords available]

Indexed keywords

GENES; GLUCOSE; MUSCLE; NEUROLOGY; PHOSPHORYLATION;

EID: 84920887582     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.607796     Document Type: Article
Times cited : (34)

References (44)
  • 1
    • 84855929671 scopus 로고    scopus 로고
    • Glycogen and its metabolism: Some new developments and old themes
    • Roach, P. J., Depaoli-Roach, A. A., Hurley, T. D., and Tagliabracci, V. S. (2012) Glycogen and its metabolism: some new developments and old themes. Biochem. J. 441, 763-787
    • (2012) Biochem. J. , vol.441 , pp. 763-787
    • Roach, P.J.1    Depaoli-Roach, A.A.2    Hurley, T.D.3    Tagliabracci, V.S.4
  • 3
    • 0030771358 scopus 로고    scopus 로고
    • How did glycogen structure evolve to satisfy the requirement for rapid mobilization of glucose? A problem of physical constraints in structure building
    • Meléndez, R., Meléndez-Hevia, E., and Cascante, M. (1997) How did glycogen structure evolve to satisfy the requirement for rapid mobilization of glucose? A problem of physical constraints in structure building. J. Mol. Evol. 45, 446-455
    • (1997) J. Mol. Evol. , vol.45 , pp. 446-455
    • Meléndez, R.1    Meléndez-Hevia, E.2    Cascante, M.3
  • 4
    • 0027496663 scopus 로고
    • Optimization of molecular design in the evolution of metabolism: The glycogen molecule
    • Meléndez-Hevia, E., Waddell, T. G., and Shelton, E. D. (1993) Optimization of molecular design in the evolution of metabolism: the glycogen molecule. Biochem. J. 295, 477-483
    • (1993) Biochem. J. , vol.295 , pp. 477-483
    • Meléndez-Hevia, E.1    Waddell, T.G.2    Shelton, E.D.3
  • 5
    • 0018865145 scopus 로고
    • The presence of phosphate in glycogen
    • Fontana, J. D. (1980) The presence of phosphate in glycogen. FEBS Lett. 109, 85-92
    • (1980) FEBS Lett. , vol.109 , pp. 85-92
    • Fontana, J.D.1
  • 7
    • 0027222075 scopus 로고
    • Glycogen contains phosphodiester groups that can be introduced by UDPglucose: Glycogen glucose 1-phosphotransferase
    • Lomako, J., Lomako, W. M., Whelan, W. J., and Marchase, R. B. (1993) Glycogen contains phosphodiester groups that can be introduced by UDPglucose: glycogen glucose 1-phosphotransferase. FEBS Lett. 329, 263-267
    • (1993) FEBS Lett. , vol.329 , pp. 263-267
    • Lomako, J.1    Lomako, W.M.2    Whelan, W.J.3    Marchase, R.B.4
  • 8
    • 34548710836 scopus 로고    scopus 로고
    • Advances in lafora progressive myoclonus epilepsy
    • Delgado-Escueta, A. V. (2007) Advances in lafora progressive myoclonus epilepsy. Curr Neurol. Neurosci. Rep. 7, 428-433
    • (2007) Curr Neurol. Neurosci. Rep. , vol.7 , pp. 428-433
    • Delgado-Escueta, A.V.1
  • 10
    • 70449955237 scopus 로고    scopus 로고
    • Lafora disease: Insights into neurodegeneration from plant metabolism
    • Gentry, M. S., Dixon, J. E., and Worby, C. A. (2009) Lafora disease: insights into neurodegeneration from plant metabolism. Trends Biochem. Sci 34, 628-639
    • (2009) Trends Biochem. Sci , vol.34 , pp. 628-639
    • Gentry, M.S.1    Dixon, J.E.2    Worby, C.A.3
  • 11
    • 31544471203 scopus 로고    scopus 로고
    • Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy
    • Ganesh, S., Puri, R., Singh, S., Mittal, S., and Dubey, D. (2006) Recent advances in the molecular basis of Lafora's progressive myoclonus epilepsy. J. Hum. Genet. 51, 1-8
    • (2006) J. Hum. Genet. , vol.51 , pp. 1-8
    • Ganesh, S.1    Puri, R.2    Singh, S.3    Mittal, S.4    Dubey, D.5
  • 12
    • 84920894567 scopus 로고    scopus 로고
    • Glycogen metabolism and lafora disease
    • (Bence, K. K. ed.) pp. 239-262, Springer Science + Business Media, New York
    • Roach, P. J., and DePaoli-Roach, A. A. (2013) Glycogen metabolism and lafora disease. In Protein Tyrosine Phosphatase Control of Metabolism (Bence, K. K. ed.) pp. 239-262, Springer Science + Business Media, New York
    • (2013) Protein Tyrosine Phosphatase Control of Metabolism
    • Roach, P.J.1    DePaoli-Roach, A.A.2
  • 17
    • 77955486949 scopus 로고    scopus 로고
    • Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin
    • DePaoli-Roach, A. A., Tagliabracci, V. S., Segvich, D. M., Meyer, C. M., Irimia, J. M., and Roach, P. J. (2010) Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin. J. Biol. Chem. 285, 25372-25381
    • (2010) J. Biol. Chem. , vol.285 , pp. 25372-25381
    • DePaoli-Roach, A.A.1    Tagliabracci, V.S.2    Segvich, D.M.3    Meyer, C.M.4    Irimia, J.M.5    Roach, P.J.6
  • 23
    • 33749620777 scopus 로고    scopus 로고
    • Laforin: A dual specificity phosphatase that dephosphorylates complex carbohydrates
    • Worby, C. A., Gentry, M. S., and Dixon, J. E. (2006) Laforin: a dual specificity phosphatase that dephosphorylates complex carbohydrates. J. Biol. Chem. 281, 30412-30418
    • (2006) J. Biol. Chem. , vol.281 , pp. 30412-30418
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 28
    • 84858203942 scopus 로고    scopus 로고
    • Laforin and malin knockout mice have normal glucose disposal and insulin sensitivity
    • DePaoli-Roach, A. A., Segvich, D. M., Meyer, C. M., Rahimi, Y., Worby, C. A., Gentry, M. S., and Roach, P. J. (2012) Laforin and malin knockout mice have normal glucose disposal and insulin sensitivity. Hum. Mol. Downloaded from http://www.jbc.org/ at ELSEVIER BV on January 15, 2015 Genet. 21, 1604-1610
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1604-1610
    • DePaoli-Roach, A.A.1    Segvich, D.M.2    Meyer, C.M.3    Rahimi, Y.4    Worby, C.A.5    Gentry, M.S.6    Roach, P.J.7
  • 31
    • 0016631203 scopus 로고
    • Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range
    • Hess, H. H., and Derr, J. E. (1975) Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range. Anal. Biochem. 63, 607-613
    • (1975) Anal. Biochem. , vol.63 , pp. 607-613
    • Hess, H.H.1    Derr, J.E.2
  • 32
    • 63149156356 scopus 로고    scopus 로고
    • An enzymatic fluorimetric assay for glucose-6-phosphate: Application in an in vitro Warburg-like effect
    • Zhu, A., Romero, R., and Petty, H. R. (2009) An enzymatic fluorimetric assay for glucose-6-phosphate: application in an in vitro Warburg-like effect. Anal. Biochem. 388, 97-101
    • (2009) Anal. Biochem. , vol.388 , pp. 97-101
    • Zhu, A.1    Romero, R.2    Petty, H.R.3
  • 34
    • 0000421646 scopus 로고
    • Phosphates and other inorganic esters
    • Elsevier, New York
    • MacDonald, D. L. (1972) Phosphates and other inorganic esters. In The Carbohydrates 2E V1A, pp. 253-278, Elsevier, New York
    • (1972) The Carbohydrates 2E V1a , pp. 253-278
    • MacDonald, D.L.1
  • 35
    • 0038240724 scopus 로고    scopus 로고
    • Mechanism of 2-O-3-O silyl migration in cyclomaltosehexaose (a-cyclodextrin)
    • Teranishi, K., and Ueno, F. (2003) Mechanism of 2-O-3-O silyl migration in cyclomaltosehexaose (a-cyclodextrin). Tetrahedron Lett. 44, 4843-4848
    • (2003) Tetrahedron Lett. , vol.44 , pp. 4843-4848
    • Teranishi, K.1    Ueno, F.2
  • 36
    • 84872538351 scopus 로고    scopus 로고
    • Control of phosphoryl migratory transesterifications allows regioselective access to sugar phosphates
    • Patel, M. K., and Davis, B. G. (2013) Control of phosphoryl migratory transesterifications allows regioselective access to sugar phosphates. Org. Lett. 15, 346-349
    • (2013) Org. Lett. , vol.15 , pp. 346-349
    • Patel, M.K.1    Davis, B.G.2
  • 38
    • 33748605055 scopus 로고    scopus 로고
    • Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases
    • Ritte, G., Heydenreich, M., Mahlow, S., Haebel, S., Kötting, O., and Steup, M. (2006) Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases. FEBS Lett. 580, 4872-4876
    • (2006) FEBS Lett. , vol.580 , pp. 4872-4876
    • Ritte, G.1    Heydenreich, M.2    Mahlow, S.3    Haebel, S.4    Kötting, O.5    Steup, M.6
  • 39
    • 77952466937 scopus 로고    scopus 로고
    • Starch: Its metabolism, evolution, and biotechnological modification in plants
    • Zeeman, S. C., Kossmann, J., and Smith, A. M. (2010) Starch: its metabolism, evolution, and biotechnological modification in plants. Annu. Rev. Plant Biol. 61, 209-234
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 209-234
    • Zeeman, S.C.1    Kossmann, J.2    Smith, A.M.3
  • 40
    • 0000869954 scopus 로고
    • Studies on uridine-diphosphateglucose
    • Paladini, A. C., and Leloir, L. F. (1952) Studies on uridine-diphosphateglucose. Biochem. J. 51, 426-430
    • (1952) Biochem. J. , vol.51 , pp. 426-430
    • Paladini, A.C.1    Leloir, L.F.2
  • 43
    • 77950519125 scopus 로고    scopus 로고
    • Helix-breaking news: Fighting crystalline starch energy deposits in the cell
    • Blennow, A., and Engelsen, S. B. (2010) Helix-breaking news: fighting crystalline starch energy deposits in the cell. Trends Plant Sci. 15, 236-240
    • (2010) Trends Plant Sci. , vol.15 , pp. 236-240
    • Blennow, A.1    Engelsen, S.B.2
  • 44
    • 66649116284 scopus 로고    scopus 로고
    • Eukaryotic starch degradation: Integration of plastidial and cytosolic pathways
    • Fettke, J., Hejazi, M., Smirnova, J., Höchel, E., Stage, M., and Steup, M. (2009) Eukaryotic starch degradation: integration of plastidial and cytosolic pathways. J. Exp. Bot. 60, 2907-2922
    • (2009) J. Exp. Bot. , vol.60 , pp. 2907-2922
    • Fettke, J.1    Hejazi, M.2    Smirnova, J.3    Höchel, E.4    Stage, M.5    Steup, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.