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Volumn 11, Issue 11, 2013, Pages

Role of Autophagy in Glycogen Breakdown and Its Relevance to Chloroquine Myopathy

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHLOROQUINE; GLYCOGEN; GLYCOGEN SYNTHASE; PROTEIN ATG8; UNCLASSIFIED DRUG;

EID: 84889069304     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001708     Document Type: Article
Times cited : (97)

References (65)
  • 1
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie Z, Klionsky DJ, (2007) Autophagosome formation: core machinery and adaptations. Nat Cell Biol 9: 1102-1109.
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 2
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y, (2004) In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 15: 1101-1111.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 3
    • 83455243361 scopus 로고    scopus 로고
    • Autophagy in lysosomal myopathies
    • Malicdan MC, Nishino I, (2012) Autophagy in lysosomal myopathies. Brain Pathol 22: 82-88.
    • (2012) Brain Pathol , vol.22 , pp. 82-88
    • Malicdan, M.C.1    Nishino, I.2
  • 4
    • 46449126749 scopus 로고    scopus 로고
    • Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle
    • Malicdan MC, Noguchi S, Nonaka I, Saftig P, Nishino I, (2008) Lysosomal myopathies: an excessive build-up in autophagosomes is too much to handle. Neuromuscul Disord 18: 521-529.
    • (2008) Neuromuscul Disord , vol.18 , pp. 521-529
    • Malicdan, M.C.1    Noguchi, S.2    Nonaka, I.3    Saftig, P.4    Nishino, I.5
  • 5
    • 0036086765 scopus 로고    scopus 로고
    • Acid alpha-glucosidase deficiency (glycogenosis type II, Pompe disease)
    • Raben N, Plotz P, Byrne BJ, (2002) Acid alpha-glucosidase deficiency (glycogenosis type II, Pompe disease). Curr Mol Med 2: 145-166.
    • (2002) Curr Mol Med , vol.2 , pp. 145-166
    • Raben, N.1    Plotz, P.2    Byrne, B.J.3
  • 6
    • 0014094248 scopus 로고
    • Muscular form of glycogenosis, type II (Pompe)
    • Smith J, Zellweger H, Afifi AK, (1967) Muscular form of glycogenosis, type II (Pompe). Neurology 17: 537-549.
    • (1967) Neurology , vol.17 , pp. 537-549
    • Smith, J.1    Zellweger, H.2    Afifi, A.K.3
  • 7
    • 73649187940 scopus 로고
    • alpha-Glucosidase deficiency in generalized glycogenstorage disease (Pompe's disease)
    • Hers HG, (1963) alpha-Glucosidase deficiency in generalized glycogenstorage disease (Pompe's disease). Biochem J 86: 11-16.
    • (1963) Biochem J , vol.86 , pp. 11-16
    • Hers, H.G.1
  • 9
    • 14444274334 scopus 로고    scopus 로고
    • Targeted disruption of the acid alpha-glucosidase gene in mice causes an illness with critical features of both infantile and adult human glycogen storage disease type II
    • Raben N, Nagaraju K, Lee E, Kessler P, Byrne B, et al. (1998) Targeted disruption of the acid alpha-glucosidase gene in mice causes an illness with critical features of both infantile and adult human glycogen storage disease type II. J Biol Chem 273: 19086-19092.
    • (1998) J Biol Chem , vol.273 , pp. 19086-19092
    • Raben, N.1    Nagaraju, K.2    Lee, E.3    Kessler, P.4    Byrne, B.5
  • 10
    • 58149468046 scopus 로고    scopus 로고
    • When more is less: excess and deficiency of autophagy coexist in skeletal muscle in Pompe disease
    • Raben N, Baum R, Schreiner C, Takikita S, Mizushima N, et al. (2009) When more is less: excess and deficiency of autophagy coexist in skeletal muscle in Pompe disease. Autophagy 5: 111-113.
    • (2009) Autophagy , vol.5 , pp. 111-113
    • Raben, N.1    Baum, R.2    Schreiner, C.3    Takikita, S.4    Mizushima, N.5
  • 11
    • 84866082112 scopus 로고    scopus 로고
    • The role of autophagy in the pathogenesis of glycogen storage disease type II (GSDII)
    • Nascimbeni AC, Fanin M, Masiero E, Angelini C, Sandri M, (2012) The role of autophagy in the pathogenesis of glycogen storage disease type II (GSDII). Cell Death Differ 19 (10) (): 1698-1708.
    • (2012) Cell Death Differ , vol.19 , Issue.10 , pp. 1698-1708
    • Nascimbeni, A.C.1    Fanin, M.2    Masiero, E.3    Angelini, C.4    Sandri, M.5
  • 12
    • 78649288882 scopus 로고    scopus 로고
    • Suppression of autophagy permits successful enzyme replacement therapy in a lysosomal storage disorder-murine Pompe disease
    • Raben N, Schreiner C, Baum R, Takikita S, Xu S, et al. (2010) Suppression of autophagy permits successful enzyme replacement therapy in a lysosomal storage disorder-murine Pompe disease. Autophagy 6: 1078-1089.
    • (2010) Autophagy , vol.6 , pp. 1078-1089
    • Raben, N.1    Schreiner, C.2    Baum, R.3    Takikita, S.4    Xu, S.5
  • 13
    • 33749261091 scopus 로고    scopus 로고
    • Autophagic vacuolar myopathy
    • Nishino I, (2006) Autophagic vacuolar myopathy. Semin Pediatr Neurol 13: 90-95.
    • (2006) Semin Pediatr Neurol , vol.13 , pp. 90-95
    • Nishino, I.1
  • 14
    • 33144467273 scopus 로고    scopus 로고
    • Antimalarial myopathy: an underdiagnosed complication? Prospective longitudinal study of 119 patients
    • Casado E, Gratacos J, Tolosa C, Martinez JM, Ojanguren I, et al. (2006) Antimalarial myopathy: an underdiagnosed complication? Prospective longitudinal study of 119 patients. Ann Rheum Dis 65: 385-390.
    • (2006) Ann Rheum Dis , vol.65 , pp. 385-390
    • Casado, E.1    Gratacos, J.2    Tolosa, C.3    Martinez, J.M.4    Ojanguren, I.5
  • 16
    • 0029978974 scopus 로고    scopus 로고
    • Controlled trial with chloroquine diphosphate in systemic lupus erythematosus
    • Meinao IM, Sato EI, Andrade LE, Ferraz MB, Atra E, (1996) Controlled trial with chloroquine diphosphate in systemic lupus erythematosus. Lupus 5: 237-241.
    • (1996) Lupus , vol.5 , pp. 237-241
    • Meinao, I.M.1    Sato, E.I.2    Andrade, L.E.3    Ferraz, M.B.4    Atra, E.5
  • 17
    • 79955017501 scopus 로고    scopus 로고
    • Re-evaluation of antimalarials in treating rheumatic diseases: re-appreciation and insights into new mechanisms of action
    • Katz SJ, Russell AS, (2011) Re-evaluation of antimalarials in treating rheumatic diseases: re-appreciation and insights into new mechanisms of action. Curr Opin Rheumatol 23: 278-281.
    • (2011) Curr Opin Rheumatol , vol.23 , pp. 278-281
    • Katz, S.J.1    Russell, A.S.2
  • 18
    • 0019382259 scopus 로고
    • Inhibition of lysosomal function in red and white skeletal muscles by chloroquine
    • Stauber WT, Hedge AM, Trout JJ, Schottelius BA, (1981) Inhibition of lysosomal function in red and white skeletal muscles by chloroquine. Exp Neurol 71: 295-306.
    • (1981) Exp Neurol , vol.71 , pp. 295-306
    • Stauber, W.T.1    Hedge, A.M.2    Trout, J.J.3    Schottelius, B.A.4
  • 19
    • 79956014819 scopus 로고    scopus 로고
    • Induction of lysosomal dilatation, arrested autophagy, and cell death by chloroquine in cultured ARPE-19 cells
    • Yoon YH, Cho KS, Hwang JJ, Lee SJ, Choi JA, et al. (2010) Induction of lysosomal dilatation, arrested autophagy, and cell death by chloroquine in cultured ARPE-19 cells. Invest Ophthalmol Vis Sci 51: 6030-6037.
    • (2010) Invest Ophthalmol Vis Sci , vol.51 , pp. 6030-6037
    • Yoon, Y.H.1    Cho, K.S.2    Hwang, J.J.3    Lee, S.J.4    Choi, J.A.5
  • 21
    • 0017720734 scopus 로고
    • Vacuolar myopathy associated with chloroquine, lupus erythematosus and thymoma. Report of a case with unusual mitochondrial changes and lipid accumulation in muscle
    • Mastaglia FL, Papadimitriou JM, Dawkins RL, Beveridge B, (1977) Vacuolar myopathy associated with chloroquine, lupus erythematosus and thymoma. Report of a case with unusual mitochondrial changes and lipid accumulation in muscle. J Neurol Sci 34: 315-328.
    • (1977) J Neurol Sci , vol.34 , pp. 315-328
    • Mastaglia, F.L.1    Papadimitriou, J.M.2    Dawkins, R.L.3    Beveridge, B.4
  • 22
    • 0027275063 scopus 로고
    • Effect of denervation on overdevelopment of chloroquine-induced autophagic vacuoles in skeletal muscles
    • Kumamoto T, Ueyama H, Watanabe S, Murakami T, Araki S, (1993) Effect of denervation on overdevelopment of chloroquine-induced autophagic vacuoles in skeletal muscles. Muscle Nerve 16: 819-826.
    • (1993) Muscle Nerve , vol.16 , pp. 819-826
    • Kumamoto, T.1    Ueyama, H.2    Watanabe, S.3    Murakami, T.4    Araki, S.5
  • 23
    • 0015042658 scopus 로고
    • Fine structural aspects of the mobilization of hepatic glycogen. I. Acceleration of glycogen breakdown
    • Kotoulas OB, Phillips MJ, (1971) Fine structural aspects of the mobilization of hepatic glycogen. I. Acceleration of glycogen breakdown. Am J Pathol 63: 1-22.
    • (1971) Am J Pathol , vol.63 , pp. 1-22
    • Kotoulas, O.B.1    Phillips, M.J.2
  • 25
    • 0015251008 scopus 로고
    • Autophagic degradation of glycogen in skeletal muscles of the newborn rat
    • Schiaffino S, Hanzlikova V, (1972) Autophagic degradation of glycogen in skeletal muscles of the newborn rat. J Cell Biol 52: 41-51.
    • (1972) J Cell Biol , vol.52 , pp. 41-51
    • Schiaffino, S.1    Hanzlikova, V.2
  • 26
    • 48249111779 scopus 로고    scopus 로고
    • The role of autophagy in neonatal tissues: just a response to amino acid starvation
    • Schiaffino S, Mammucari C, Sandri M, (2008) The role of autophagy in neonatal tissues: just a response to amino acid starvation? Autophagy 4: 727-730.
    • (2008) Autophagy , vol.4 , pp. 727-730
    • Schiaffino, S.1    Mammucari, C.2    Sandri, M.3
  • 27
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: molecular machinery for self-eating
    • Yorimitsu T, Klionsky DJ, (2005) Autophagy: molecular machinery for self-eating. Cell Death Differ 12 Suppl 2: 1542-1552.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 28
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: core molecular machinery and signaling regulation
    • Yang Z, Klionsky DJ, (2011) Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol 22: 124-131.
    • (2011) Curr Opin Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 29
    • 79953153833 scopus 로고    scopus 로고
    • The late stage of autophagy: cellular events and molecular regulation
    • Tong J, Yan X, Yu L, (2010) The late stage of autophagy: cellular events and molecular regulation. Protein Cell 1: 907-915.
    • (2010) Protein Cell , vol.1 , pp. 907-915
    • Tong, J.1    Yan, X.2    Yu, L.3
  • 30
    • 57049094929 scopus 로고    scopus 로고
    • Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease
    • Raben N, Hill V, Shea L, Takikita S, Baum R, et al. (2008) Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease. Hum Mol Genet 17: 3897-3908.
    • (2008) Hum Mol Genet , vol.17 , pp. 3897-3908
    • Raben, N.1    Hill, V.2    Shea, L.3    Takikita, S.4    Baum, R.5
  • 31
    • 61849085267 scopus 로고    scopus 로고
    • Murine muscle cell models for Pompe disease and their use in studying therapeutic approaches
    • Takikita S, Myerowitz R, Zaal K, Raben N, Plotz PH, (2009) Murine muscle cell models for Pompe disease and their use in studying therapeutic approaches. Mol Genet Metab 96: 208-217.
    • (2009) Mol Genet Metab , vol.96 , pp. 208-217
    • Takikita, S.1    Myerowitz, R.2    Zaal, K.3    Raben, N.4    Plotz, P.H.5
  • 32
    • 79953139746 scopus 로고    scopus 로고
    • Drosophila as a model system to study autophagy
    • Zirin J, Perrimon N, (2010) Drosophila as a model system to study autophagy. Semin Immunopathol 32: 363-372.
    • (2010) Semin Immunopathol , vol.32 , pp. 363-372
    • Zirin, J.1    Perrimon, N.2
  • 33
    • 77950509930 scopus 로고    scopus 로고
    • Autophagy takes flight in Drosophila
    • Chang YY, Neufeld TP, (2011) Autophagy takes flight in Drosophila. FEBS Lett 584: 1342-1349.
    • (2011) FEBS Lett , vol.584 , pp. 1342-1349
    • Chang, Y.Y.1    Neufeld, T.P.2
  • 34
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima N, Noda T, Yoshimori T, Tanaka Y, Ishii T, et al. (1998) A protein conjugation system essential for autophagy. Nature 395: 395-398.
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1    Noda, T.2    Yoshimori, T.3    Tanaka, Y.4    Ishii, T.5
  • 35
    • 56349141577 scopus 로고    scopus 로고
    • Myopathies in the adult patient
    • Damian MS, (2008) Myopathies in the adult patient. Medicine 36: 658-664.
    • (2008) Medicine , vol.36 , pp. 658-664
    • Damian, M.S.1
  • 36
    • 67649308215 scopus 로고    scopus 로고
    • Toxic and iatrogenic myopathies
    • Mastaglia FL, Argov Z, (2007) Toxic and iatrogenic myopathies. Handb Clin Neurol 86: 321-341.
    • (2007) Handb Clin Neurol , vol.86 , pp. 321-341
    • Mastaglia, F.L.1    Argov, Z.2
  • 37
    • 78650905611 scopus 로고    scopus 로고
    • The Drosophila NR4A nuclear receptor DHR38 regulates carbohydrate metabolism and glycogen storage
    • Ruaud AF, Lam G, Thummel CS, (2011) The Drosophila NR4A nuclear receptor DHR38 regulates carbohydrate metabolism and glycogen storage. Mol Endocrinol 25: 83-91.
    • (2011) Mol Endocrinol , vol.25 , pp. 83-91
    • Ruaud, A.F.1    Lam, G.2    Thummel, C.S.3
  • 38
    • 0038393057 scopus 로고    scopus 로고
    • The Drosophila homolog of Aut1 is essential for autophagy and development
    • Juhasz G, Csikos G, Sinka R, Erdelyi M, Sass M, (2003) The Drosophila homolog of Aut1 is essential for autophagy and development. FEBS Lett 543: 154-158.
    • (2003) FEBS Lett , vol.543 , pp. 154-158
    • Juhasz, G.1    Csikos, G.2    Sinka, R.3    Erdelyi, M.4    Sass, M.5
  • 39
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E, Tao RN, Whitworth AJ, (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A 107: 5018-5023.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 40
    • 78751482244 scopus 로고    scopus 로고
    • Bcl-2 proteins and autophagy regulate mitochondrial dynamics during programmed cell death in the Drosophila ovary
    • Tanner EA, Blute TA, Brachmann CB, McCall K, (2011) Bcl-2 proteins and autophagy regulate mitochondrial dynamics during programmed cell death in the Drosophila ovary. Development 138: 327-338.
    • (2011) Development , vol.138 , pp. 327-338
    • Tanner, E.A.1    Blute, T.A.2    Brachmann, C.B.3    McCall, K.4
  • 41
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • Laplante M, Sabatini DM, (2012) mTOR signaling in growth control and disease. Cell 149: 274-293.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 42
    • 33645990907 scopus 로고    scopus 로고
    • Regulation of protein synthesis by insulin
    • Proud CG, (2006) Regulation of protein synthesis by insulin. Biochem Soc Trans 34: 213-216.
    • (2006) Biochem Soc Trans , vol.34 , pp. 213-216
    • Proud, C.G.1
  • 43
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • Mizushima N, (2010) The role of the Atg1/ULK1 complex in autophagy regulation. Curr Opin Cell Biol 22: 132-139.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 44
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW, (2010) Network organization of the human autophagy system. Nature 466: 68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 45
    • 57249083972 scopus 로고    scopus 로고
    • Structural basis of target recognition by Atg8/LC3 during selective autophagy
    • Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, et al. (2008) Structural basis of target recognition by Atg8/LC3 during selective autophagy. Genes Cells 13: 1211-1218.
    • (2008) Genes Cells , vol.13 , pp. 1211-1218
    • Noda, N.N.1    Kumeta, H.2    Nakatogawa, H.3    Satoo, K.4    Adachi, W.5
  • 47
    • 0019025978 scopus 로고
    • Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase
    • Rylatt DB, Aitken A, Bilham T, Condon GD, Embi N, et al. (1980) Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase. Eur J Biochem 107: 529-537.
    • (1980) Eur J Biochem , vol.107 , pp. 529-537
    • Rylatt, D.B.1    Aitken, A.2    Bilham, T.3    Condon, G.D.4    Embi, N.5
  • 48
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase
    • Embi N, Rylatt DB, Cohen P, (1980) Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur J Biochem 107: 519-527.
    • (1980) Eur J Biochem , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 49
    • 74549133523 scopus 로고    scopus 로고
    • Chaperone-assisted selective autophagy is essential for muscle maintenance
    • Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, et al. (2010) Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr Biol 20: 143-148.
    • (2010) Curr Biol , vol.20 , pp. 143-148
    • Arndt, V.1    Dick, N.2    Tawo, R.3    Dreiseidler, M.4    Wenzel, D.5
  • 50
    • 78650918920 scopus 로고    scopus 로고
    • FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging
    • Demontis F, Perrimon N, (2010) FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging. Cell 143: 813-825.
    • (2010) Cell , vol.143 , pp. 813-825
    • Demontis, F.1    Perrimon, N.2
  • 51
    • 77649200841 scopus 로고    scopus 로고
    • Autophagy in skeletal muscle: implications for Pompe disease
    • Shea L, Raben N, (2009) Autophagy in skeletal muscle: implications for Pompe disease. Int J Clin Pharmacol Ther 47 Suppl 1: S42-47.
    • (2009) Int J Clin Pharmacol Ther , vol.47 , Issue.SUPPL. 1
    • Shea, L.1    Raben, N.2
  • 52
    • 81455148191 scopus 로고    scopus 로고
    • Progress and problems in muscle glycogenoses
    • DiMauro S, Spiegel R, (2011) Progress and problems in muscle glycogenoses. Acta Myol 30: 96-102.
    • (2011) Acta Myol , vol.30 , pp. 96-102
    • DiMauro, S.1    Spiegel, R.2
  • 53
    • 34250661859 scopus 로고    scopus 로고
    • Glycogen storage diseases: new perspectives
    • Ozen H, (2007) Glycogen storage diseases: new perspectives. World J Gastroenterol 13: 2541-2553.
    • (2007) World J Gastroenterol , vol.13 , pp. 2541-2553
    • Ozen, H.1
  • 54
    • 84862276149 scopus 로고    scopus 로고
    • Malin knockout mice support a primary role of autophagy in the pathogenesis of Lafora disease
    • Knecht E, Criado-Garcia O, Aguado C, Gayarre J, Duran-Trio L, et al. (2012) Malin knockout mice support a primary role of autophagy in the pathogenesis of Lafora disease. Autophagy 8 (4) (): 701-703.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 701-703
    • Knecht, E.1    Criado-Garcia, O.2    Aguado, C.3    Gayarre, J.4    Duran-Trio, L.5
  • 55
    • 84858183902 scopus 로고    scopus 로고
    • Lafora bodies and neurological defects in malin-deficient mice correlate with impaired autophagy
    • Criado O, Aguado C, Gayarre J, Duran-Trio L, Garcia-Cabrero AM, et al. (2012) Lafora bodies and neurological defects in malin-deficient mice correlate with impaired autophagy. Hum Mol Genet 21: 1521-1533.
    • (2012) Hum Mol Genet , vol.21 , pp. 1521-1533
    • Criado, O.1    Aguado, C.2    Gayarre, J.3    Duran-Trio, L.4    Garcia-Cabrero, A.M.5
  • 56
    • 77954486784 scopus 로고    scopus 로고
    • Laforin, the most common protein mutated in Lafora disease, regulates autophagy
    • Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, et al. (2010) Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet 19: 2867-2876.
    • (2010) Hum Mol Genet , vol.19 , pp. 2867-2876
    • Aguado, C.1    Sarkar, S.2    Korolchuk, V.I.3    Criado, O.4    Vernia, S.5
  • 57
    • 83455206095 scopus 로고    scopus 로고
    • Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease
    • Puri R, Suzuki T, Yamakawa K, Ganesh S, (2012) Dysfunctions in endosomal-lysosomal and autophagy pathways underlie neuropathology in a mouse model for Lafora disease. Hum Mol Genet 21: 175-184.
    • (2012) Hum Mol Genet , vol.21 , pp. 175-184
    • Puri, R.1    Suzuki, T.2    Yamakawa, K.3    Ganesh, S.4
  • 58
    • 80053177304 scopus 로고    scopus 로고
    • Multiple glycogen-binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen
    • Baskaran S, Chikwana VM, Contreras CJ, Davis KD, Wilson WA, et al. (2011) Multiple glycogen-binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen. J Biol Chem 286: 33999-34006.
    • (2011) J Biol Chem , vol.286 , pp. 33999-34006
    • Baskaran, S.1    Chikwana, V.M.2    Contreras, C.J.3    Davis, K.D.4    Wilson, W.A.5
  • 60
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor
    • McBride A, Ghilagaber S, Nikolaev A, Hardie DG, (2009) The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab 9: 23-34.
    • (2009) Cell Metab , vol.9 , pp. 23-34
    • McBride, A.1    Ghilagaber, S.2    Nikolaev, A.3    Hardie, D.G.4
  • 61
    • 63849158634 scopus 로고    scopus 로고
    • AMP-activated protein kinase-a sensor of glycogen as well as AMP and ATP
    • McBride A, Hardie DG, (2009) AMP-activated protein kinase-a sensor of glycogen as well as AMP and ATP? Acta Physiol (Oxf) 196: 99-113.
    • (2009) Acta Physiol (Oxf) , vol.196 , pp. 99-113
    • McBride, A.1    Hardie, D.G.2
  • 62
    • 82055191530 scopus 로고    scopus 로고
    • Increased throughput assays of locomotor dysfunction in Drosophila larvae
    • Sinadinos C, Cowan CM, Wyttenbach A, Mudher A, (2012) Increased throughput assays of locomotor dysfunction in Drosophila larvae. J Neurosci Methods 203: 325-334.
    • (2012) J Neurosci Methods , vol.203 , pp. 325-334
    • Sinadinos, C.1    Cowan, C.M.2    Wyttenbach, A.3    Mudher, A.4
  • 63
    • 33751313078 scopus 로고    scopus 로고
    • Selected methods for the anatomical study of Drosophila embryonic and larval neuromuscular junctions
    • Budnik V, Gorczyca M, Prokop A, (2006) Selected methods for the anatomical study of Drosophila embryonic and larval neuromuscular junctions. Int Rev Neurobiol 75: 323-365.
    • (2006) Int Rev Neurobiol , vol.75 , pp. 323-365
    • Budnik, V.1    Gorczyca, M.2    Prokop, A.3
  • 64
    • 77956288664 scopus 로고    scopus 로고
    • Electron microscopy of Drosophila larval neuromuscular junctions
    • Ramachandran P, Budnik V, (2010) Electron microscopy of Drosophila larval neuromuscular junctions. Cold Spring Harb Protoc 2010: pdb prot5474.
    • (2010) Cold Spring Harb Protoc , vol.2010
    • Ramachandran, P.1    Budnik, V.2
  • 65
    • 60649099790 scopus 로고    scopus 로고
    • Drosophila HNF4 regulates lipid mobilization and beta-oxidation
    • Palanker L, Tennessen JM, Lam G, Thummel CS, (2009) Drosophila HNF4 regulates lipid mobilization and beta-oxidation. Cell Metab 9: 228-239.
    • (2009) Cell Metab , vol.9 , pp. 228-239
    • Palanker, L.1    Tennessen, J.M.2    Lam, G.3    Thummel, C.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.