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Volumn 21, Issue 11, 2012, Pages 2432-2449

Suppression of α-synuclein toxicity and vesicle trafficking defects by phosphorylation at S129 in yeast depends on genetic context

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; CASEIN KINASE I; RAB PROTEIN;

EID: 84861144992     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds058     Document Type: Article
Times cited : (55)

References (89)
  • 1
    • 0034531475 scopus 로고    scopus 로고
    • The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy
    • Spillantini, M.G. and Goedert, M. (2000) The alpha-synucleinopathies: Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Ann. NY Acad. Sci., 920, 16-27.
    • (2000) Ann. NY Acad. Sci. , vol.920 , pp. 16-27
    • Spillantini, M.G.1    Goedert, M.2
  • 2
    • 58549089901 scopus 로고    scopus 로고
    • Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling
    • Ben Gedalya, T., Loeb, V., Israeli, E., Altschuler, Y., Selkoe, D.J. and Sharon, R. (2009) Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling. Traffic, 10, 218-234.
    • (2009) Traffic , vol.10 , pp. 218-234
    • Ben Gedalya, T.1    Loeb, V.2    Israeli, E.3    Altschuler, Y.4    Selkoe, D.J.5    Sharon, R.6
  • 3
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein
    • Cabin, D.E., Shimazu, K., Murphy, D., Cole, N.B., Gottschalk, W., McIlwain, K.L., Orrison, B., Chen, A., Ellis, C.E., Paylor, R. et al. (2002) Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J. Neurosci., 22, 8797-8807.
    • (2002) J. Neurosci. , vol.22 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6    Orrison, B.7    Chen, A.8    Ellis, C.E.9    Paylor, R.10
  • 4
    • 27544507306 scopus 로고    scopus 로고
    • Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration
    • Chandra, S., Gallardo, G., Fernandez-Chacon, R., Schluter, O.M. and Sudhof, T.C. (2005) Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell, 123, 383-396.
    • (2005) Cell , vol.123 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 7
    • 33747811791 scopus 로고    scopus 로고
    • Fragmentation of Golgi apparatus of nigral neurons with alpha-synuclein-positive inclusions in patients with Parkinson's disease
    • Fujita, Y., Ohama, E., Takatama, M., Al-Sarraj, S. and Okamoto, K. (2006) Fragmentation of Golgi apparatus of nigral neurons with alpha-synuclein-positive inclusions in patients with Parkinson's disease. Acta Neuropathol., 112, 261-265.
    • (2006) Acta Neuropathol , vol.112 , pp. 261-265
    • Fujita, Y.1    Ohama, E.2    Takatama, M.3    Al-Sarraj, S.4    Okamoto, K.5
  • 8
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi, N., Lee, H.J., Lee, J.S., Patel, S. and Lee, S.J. (2002) Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J. Biol. Chem., 277, 48984-48992.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 10
    • 33845656077 scopus 로고    scopus 로고
    • Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein
    • Lee, H.J., Khoshaghideh, F., Lee, S. and Lee, S.J. (2006) Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein. Eur. J. Neurosci., 24, 3153-3162.
    • (2006) Eur. J. Neurosci. , vol.24 , pp. 3153-3162
    • Lee, H.J.1    Khoshaghideh, F.2    Lee, S.3    Lee, S.J.4
  • 11
    • 77952900626 scopus 로고    scopus 로고
    • Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi, N., Helm, J.R., Nycz, D.C., Bentley, M., Liang, Y. and Hay, J.C. (2010) Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol. Biol. Cell, 21, 1850-1863.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 17
    • 52949083619 scopus 로고    scopus 로고
    • A systematic RNAi screen reveals involvement of endocytic pathway in neuronal dysfunction in alpha-synuclein transgenic C. elegans
    • Kuwahara, T., Koyama, A., Koyama, S., Yoshina, S., Ren, C.H., Kato, T., Mitani, S. and Iwatsubo, T. (2008) A systematic RNAi screen reveals involvement of endocytic pathway in neuronal dysfunction in alpha-synuclein transgenic C. elegans. Hum. Mol. Genet., 17, 2997-3009.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2997-3009
    • Kuwahara, T.1    Koyama, A.2    Koyama, S.3    Yoshina, S.4    Ren, C.H.5    Kato, T.6    Mitani, S.7    Iwatsubo, T.8
  • 19
  • 20
    • 0345189365 scopus 로고    scopus 로고
    • Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein
    • Willingham, S., Outeiro, T.F., DeVit, M.J., Lindquist, S.L. and Muchowski, P.J. (2003) Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science, 302, 1769-1772.
    • (2003) Science , vol.302 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5
  • 22
    • 43249108653 scopus 로고    scopus 로고
    • Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein
    • Waxman, E.A. and Giasson, B.I. (2008) Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein. J. Neuropathol. Exp. Neurol., 67, 402-416.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 402-416
    • Waxman, E.A.1    Giasson, B.I.2
  • 23
    • 34548702649 scopus 로고    scopus 로고
    • Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human alpha-synuclein: implication for alpha-synucleinopathies
    • Ishii, A., Nonaka, T., Taniguchi, S., Saito, T., Arai, T., Mann, D., Iwatsubo, T., Hisanaga, S., Goedert, M. and Hasegawa, M. (2007) Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human alpha-synuclein: implication for alpha-synucleinopathies. FEBS Lett., 581, 4711-4717.
    • (2007) FEBS Lett , vol.581 , pp. 4711-4717
    • Ishii, A.1    Nonaka, T.2    Taniguchi, S.3    Saito, T.4    Arai, T.5    Mann, D.6    Iwatsubo, T.7    Hisanaga, S.8    Goedert, M.9    Hasegawa, M.10
  • 26
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • Pronin, A.N., Morris, A.J., Surguchov, A. and Benovic, J.L. (2000) Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J. Biol. Chem., 275, 26515-26522.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 27
    • 67651008224 scopus 로고    scopus 로고
    • Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications
    • Qing, H., Wong, W., McGeer, E.G. and McGeer, P.L. (2009) Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications. Biochem. Biophys. Res. Commun., 387, 149-152.
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 149-152
    • Qing, H.1    Wong, W.2    McGeer, E.G.3    McGeer, P.L.4
  • 30
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen, L. and Feany, M.B. (2005) Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci., 8, 657-663.
    • (2005) Nat. Neurosci. , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 33
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • Outeiro, T.F. and Lindquist, S. (2003) Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science, 302, 1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 35
    • 0033739781 scopus 로고    scopus 로고
    • Polar transmembrane domains target proteins to the interior of the yeast vacuole
    • Reggiori, F., Black, M.W. and Pelham, H.R. (2000) Polar transmembrane domains target proteins to the interior of the yeast vacuole. Mol. Biol. Cell, 11, 3737-3749.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3737-3749
    • Reggiori, F.1    Black, M.W.2    Pelham, H.R.3
  • 36
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting
    • Reggiori, F. and Pelham, H.R. (2001) Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. EMBO J., 20, 5176-5186.
    • (2001) EMBO J , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.2
  • 37
    • 0036153176 scopus 로고    scopus 로고
    • Casein kinase I controls a late step in the endocytic trafficking of yeast uracil permease
    • Marchal, C., Dupre, S. and Urban-Grimal, D. (2002) Casein kinase I controls a late step in the endocytic trafficking of yeast uracil permease. J. Cell Sci., 115, 217-226.
    • (2002) J. Cell Sci. , vol.115 , pp. 217-226
    • Marchal, C.1    Dupre, S.2    Urban-Grimal, D.3
  • 38
    • 0034604290 scopus 로고    scopus 로고
    • Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease
    • Marchal, C., Haguenauer-Tsapis, R. and Urban-Grimal, D. (2000) Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease. J. Biol. Chem., 275, 23608-23614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23608-23614
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 39
    • 0034496262 scopus 로고    scopus 로고
    • Identification of Rgp1p, a novel Golgi recycling factor, as a protein required for efficient localization of yeast casein kinase 1 to the plasma membrane
    • Panek, H.R., Conibear, E., Bryan, J.D., Colvin, R.T., Goshorn, C.D. and Robinson, L.C. (2000) Identification of Rgp1p, a novel Golgi recycling factor, as a protein required for efficient localization of yeast casein kinase 1 to the plasma membrane. J. Cell Sci., 113, 4545-4555.
    • (2000) J. Cell Sci. , vol.113 , pp. 4545-4555
    • Panek, H.R.1    Conibear, E.2    Bryan, J.D.3    Colvin, R.T.4    Goshorn, C.D.5    Robinson, L.C.6
  • 41
    • 67650496503 scopus 로고    scopus 로고
    • Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: relevance to Parkinson's disease pathogenesis
    • Chau, K.Y., Ching, H.L., Schapira, A.H. and Cooper, J.M. (2009) Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: relevance to Parkinson's disease pathogenesis. J. Neurochem., 110, 1005-1013.
    • (2009) J. Neurochem. , vol.110 , pp. 1005-1013
    • Chau, K.Y.1    Ching, H.L.2    Schapira, A.H.3    Cooper, J.M.4
  • 43
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen, D.C., Yang, B.C. and Kuo, T.T. (1992) One-step transformation of yeast in stationary phase. Curr. Genet., 21, 83-84.
    • (1992) Curr. Genet. , vol.21 , pp. 83-84
    • Chen, D.C.1    Yang, B.C.2    Kuo, T.T.3
  • 44
    • 0042733228 scopus 로고    scopus 로고
    • Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor
    • Veal, E.A., Ross, S.J., Malakasi, P., Peacock, E. and Morgan, B.A. (2003) Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor. J. Biol. Chem., 278, 30896-30904.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30896-30904
    • Veal, E.A.1    Ross, S.J.2    Malakasi, P.3    Peacock, E.4    Morgan, B.A.5
  • 45
    • 33751372793 scopus 로고    scopus 로고
    • alpha-Synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson's disease
    • Witt, S.N. and Flower, T.R. (2006) alpha-Synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson's disease. FEMS Yeast Res., 6, 1107-1116.
    • (2006) FEMS Yeast Res , vol.6 , pp. 1107-1116
    • Witt, S.N.1    Flower, T.R.2
  • 46
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders
    • Masliah, E., Rockenstein, E., Veinbergs, I., Mallory, M., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A. and Mucke, L. (2000) Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science, 287, 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 47
    • 0035889404 scopus 로고    scopus 로고
    • Early formation of mature amyloid-beta protein deposits in a mutant APP transgenic model depends on levels of Abeta(1-42)
    • Rockenstein, E., Mallory, M., Mante, M., Sisk, A. and Masliaha, E. (2001) Early formation of mature amyloid-beta protein deposits in a mutant APP transgenic model depends on levels of Abeta(1-42). J. Neurosci. Res., 66, 573-582.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 573-582
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    Sisk, A.4    Masliaha, E.5
  • 48
    • 0035242503 scopus 로고    scopus 로고
    • Catalytic activity of protein kinase CK1 delta (casein kinase 1delta) is essential for its normal subcellular localization
    • Milne, D.M., Looby, P. and Meek, D.W. (2001) Catalytic activity of protein kinase CK1 delta (casein kinase 1delta) is essential for its normal subcellular localization. Exp. Cell Res., 263, 43-54.
    • (2001) Exp. Cell Res. , vol.263 , pp. 43-54
    • Milne, D.M.1    Looby, P.2    Meek, D.W.3
  • 49
    • 0036677592 scopus 로고    scopus 로고
    • Casein kinase I regulates membrane binding by ARF GAP1
    • Yu, S. and Roth, M.G. (2002) Casein kinase I regulates membrane binding by ARF GAP1. Mol. Biol. Cell, 13, 2559-2570.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2559-2570
    • Yu, S.1    Roth, M.G.2
  • 50
    • 0034685703 scopus 로고    scopus 로고
    • Casein kinase 1 delta mRNA is upregulated in Alzheimer disease brain
    • Yasojima, K., Kuret, J., DeMaggio, A.J., McGeer, E. and McGeer, P.L. (2000) Casein kinase 1 delta mRNA is upregulated in Alzheimer disease brain. Brain Res., 865, 116-120.
    • (2000) Brain Res , vol.865 , pp. 116-120
    • Yasojima, K.1    Kuret, J.2    DeMaggio, A.J.3    McGeer, E.4    McGeer, P.L.5
  • 51
    • 77954215793 scopus 로고    scopus 로고
    • Alpha-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis
    • Darios, F., Ruiperez, V., Lopez, I., Villanueva, J., Gutierrez, L.M. and Davletov, B. (2010) Alpha-Synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis. EMBO Rep., 11, 528-533.
    • (2010) EMBO Rep , vol.11 , pp. 528-533
    • Darios, F.1    Ruiperez, V.2    Lopez, I.3    Villanueva, J.4    Gutierrez, L.M.5    Davletov, B.6
  • 53
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression
    • Mumberg, D., Muller, R. and Funk, M. (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res., 22, 5767-5768.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 54
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., Muller, R. and Funk, M. (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene, 156, 119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 55
    • 1942453869 scopus 로고    scopus 로고
    • The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p
    • Lafourcade, C., Galan, J.M., Gloor, Y., Haguenauer-Tsapis, R. and Peter, M. (2004) The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p. Mol. Cell. Biol., 24, 3815-3826.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3815-3826
    • Lafourcade, C.1    Galan, J.M.2    Gloor, Y.3    Haguenauer-Tsapis, R.4    Peter, M.5
  • 56
    • 0037428439 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments
    • Luo, Z. and Gallwitz, D. (2003) Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments. J. Biol. Chem., 278, 791-799.
    • (2003) J. Biol. Chem. , vol.278 , pp. 791-799
    • Luo, Z.1    Gallwitz, D.2
  • 57
    • 2342457804 scopus 로고    scopus 로고
    • Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease
    • Dalfo, E., Barrachina, M., Rosa, J.L., Ambrosio, S. and Ferrer, I. (2004) Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease. Neurobiol. Dis., 16, 92-97.
    • (2004) Neurobiol. Dis. , vol.16 , pp. 92-97
    • Dalfo, E.1    Barrachina, M.2    Rosa, J.L.3    Ambrosio, S.4    Ferrer, I.5
  • 58
    • 18044381951 scopus 로고    scopus 로고
    • Alpha-synuclein binding to rab3a in multiple system atrophy
    • Dalfo, E. and Ferrer, I. (2005) Alpha-synuclein binding to rab3a in multiple system atrophy. Neurosci. Lett., 380, 170-175.
    • (2005) Neurosci. Lett. , vol.380 , pp. 170-175
    • Dalfo, E.1    Ferrer, I.2
  • 59
    • 0034091659 scopus 로고    scopus 로고
    • Expression of the endocytosis regulatory proteins Rab5 and Rabaptin-5 in glial cytoplasmic inclusions from brains with multiple system atrophy
    • Nakamura, S., Kawamoto, Y., Nakano, S. and Akiguchi, I. (2000) Expression of the endocytosis regulatory proteins Rab5 and Rabaptin-5 in glial cytoplasmic inclusions from brains with multiple system atrophy. Clin. Neuropathol., 19, 51-56.
    • (2000) Clin. Neuropathol. , vol.19 , pp. 51-56
    • Nakamura, S.1    Kawamoto, Y.2    Nakano, S.3    Akiguchi, I.4
  • 60
    • 0017288256 scopus 로고
    • Ultrastructure of Lewy bodies in the stellate ganglion
    • Forno, L.S. and Norville, R.L. (1976) Ultrastructure of Lewy bodies in the stellate ganglion. Acta Neuropathol., 34, 183-197.
    • (1976) Acta Neuropathol , vol.34 , pp. 183-197
    • Forno, L.S.1    Norville, R.L.2
  • 61
    • 0017641210 scopus 로고
    • Dense core vesicles around the Lewy body in incidental Parkinson's disease: an electron microscopic study
    • Watanabe, I., Vachal, E. and Tomita, T. (1977) Dense core vesicles around the Lewy body in incidental Parkinson's disease: an electron microscopic study. Acta Neuropathol., 39, 173-175.
    • (1977) Acta Neuropathol , vol.39 , pp. 173-175
    • Watanabe, I.1    Vachal, E.2    Tomita, T.3
  • 63
    • 0026730464 scopus 로고
    • The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway
    • van der Sluijs, P., Hull, M., Webster, P., Male, P., Goud, B. and Mellman, I. (1992) The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway. Cell, 70, 729-740.
    • (1992) Cell , vol.70 , pp. 729-740
    • van der Sluijs, P.1    Hull, M.2    Webster, P.3    Male, P.4    Goud, B.5    Mellman, I.6
  • 66
    • 4143067071 scopus 로고    scopus 로고
    • Phosphorylated alpha-synuclein in normal mouse brain
    • Hirai, Y., Fujita, S.C., Iwatsubo, T. and Hasegawa, M. (2004) Phosphorylated alpha-synuclein in normal mouse brain. FEBS Lett., 572, 227-232.
    • (2004) FEBS Lett , vol.572 , pp. 227-232
    • Hirai, Y.1    Fujita, S.C.2    Iwatsubo, T.3    Hasegawa, M.4
  • 67
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease
    • Flower, T.R., Chesnokova, L.S., Froelich, C.A., Dixon, C. and Witt, S.N. (2005) Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. J. Mol. Biol., 351, 1081-1100.
    • (2005) J. Mol. Biol. , vol.351 , pp. 1081-1100
    • Flower, T.R.1    Chesnokova, L.S.2    Froelich, C.A.3    Dixon, C.4    Witt, S.N.5
  • 69
    • 0033836583 scopus 로고    scopus 로고
    • The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform
    • Faundez, V.V. and Kelly, R.B. (2000) The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform. Mol. Biol. Cell, 11, 2591-2604.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2591-2604
    • Faundez, V.V.1    Kelly, R.B.2
  • 70
    • 0027511827 scopus 로고
    • Casein kinase II phosphorylates the synaptic vesicle protein p65
    • Bennett, M.K., Miller, K.G. and Scheller, R.H. (1993) Casein kinase II phosphorylates the synaptic vesicle protein p65. J. Neurosci., 13, 1701-1707.
    • (1993) J. Neurosci. , vol.13 , pp. 1701-1707
    • Bennett, M.K.1    Miller, K.G.2    Scheller, R.H.3
  • 72
    • 0030965452 scopus 로고    scopus 로고
    • Phosphorylation of a vesicular monoamine transporter by casein kinase II
    • Krantz, D.E., Peter, D., Liu, Y. and Edwards, R.H. (1997) Phosphorylation of a vesicular monoamine transporter by casein kinase II. J. Biol. Chem., 272, 6752-6759.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6752-6759
    • Krantz, D.E.1    Peter, D.2    Liu, Y.3    Edwards, R.H.4
  • 73
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 74
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • Mari, M., Griffith, J., Rieter, E., Krisnappa, L., Klionsky, D.J. and Reggiori, F. (2010) An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J. Cell Biol., 190, 1005-1022.
    • (2010) J. Cell Biol. , vol.190 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3    Krisnappa, L.4    Klionsky, D.J.5    Reggiori, F.6
  • 75
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C.B., Davies, A., Cost, G.J., Caputo, E., Li, J., Hieter, P. and Boeke, J.D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast, 14, 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 77
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R.D., Schiestl, R.H., Willems, A.R. and Woods, R.A. (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast, 11, 355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 79
    • 0035834076 scopus 로고    scopus 로고
    • Beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
    • Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M. and Mucke, L. (2001) Beta-amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc. Natl Acad. Sci. USA, 98, 12245-12250.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12245-12250
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Sagara, Y.4    Mallory, M.5    Hashimoto, M.6    Mucke, L.7
  • 80
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters
    • Rockenstein, E., Mallory, M., Hashimoto, M., Song, D., Shults, C.W., Lang, I. and Masliah, E. (2002) Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the platelet-derived growth factor and Thy-1 promoters. J. Neurosci. Res., 68, 568-578.
    • (2002) J. Neurosci. Res. , vol.68 , pp. 568-578
    • Rockenstein, E.1    Mallory, M.2    Hashimoto, M.3    Song, D.4    Shults, C.W.5    Lang, I.6    Masliah, E.7
  • 81
    • 0031922359 scopus 로고    scopus 로고
    • Frontal cortical synaptophysin in Lewy body diseases: relation to Alzheimer's disease and dementia
    • Hansen, L.A., Daniel, S.E., Wilcock, G.K. and Love, S. (1998) Frontal cortical synaptophysin in Lewy body diseases: relation to Alzheimer's disease and dementia. J. Neurol. Neurosurg. Psychiatry, 64, 653-656.
    • (1998) J. Neurol. Neurosurg. Psychiatry , vol.64 , pp. 653-656
    • Hansen, L.A.1    Daniel, S.E.2    Wilcock, G.K.3    Love, S.4
  • 82
    • 0025878695 scopus 로고
    • Entorhinal neurofibrillary tangles in Alzheimer disease with Lewy bodies
    • Hansen, L.A., Masliah, E., Quijada-Fawcett, S. and Rexin, D. (1991) Entorhinal neurofibrillary tangles in Alzheimer disease with Lewy bodies. Neurosci. Lett., 129, 269-272.
    • (1991) Neurosci. Lett. , vol.129 , pp. 269-272
    • Hansen, L.A.1    Masliah, E.2    Quijada-Fawcett, S.3    Rexin, D.4
  • 83
    • 0026305017 scopus 로고
    • Morphological changes in the human cerebral cortex in dementia
    • Braak, H. and Braak, E. (1991) Morphological changes in the human cerebral cortex in dementia. J. Hirnforsch., 32, 277-282.
    • (1991) J. Hirnforsch. , vol.32 , pp. 277-282
    • Braak, H.1    Braak, E.2
  • 84
    • 0006164301 scopus 로고    scopus 로고
    • Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop
    • McKeith, I.G., Galasko, D., Kosaka, K., Perry, E.K., Dickson, D.W., Hansen, L.A., Salmon, D.P., Lowe, J., Mirra, S.S., Byrne, E.J. et al. (1996) Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology, 47, 1113-1124.
    • (1996) Neurology , vol.47 , pp. 1113-1124
    • McKeith, I.G.1    Galasko, D.2    Kosaka, K.3    Perry, E.K.4    Dickson, D.W.5    Hansen, L.A.6    Salmon, D.P.7    Lowe, J.8    Mirra, S.S.9    Byrne, E.J.10
  • 85
    • 46349104022 scopus 로고    scopus 로고
    • A cryosectioning procedure for the ultrastructural analysis and the immunogold labelling of yeast Saccharomyces cerevisiae
    • Griffith, J., Mari, M., De Maziere, A. and Reggiori, F. (2008) A cryosectioning procedure for the ultrastructural analysis and the immunogold labelling of yeast Saccharomyces cerevisiae. Traffic, 9, 1060-1072.
    • (2008) Traffic , vol.9 , pp. 1060-1072
    • Griffith, J.1    Mari, M.2    De Maziere, A.3    Reggiori, F.4
  • 86
    • 38449099776 scopus 로고    scopus 로고
    • Cryosectioning and immunolabeling
    • Slot, J.W. and Geuze, H.J. (2007) Cryosectioning and immunolabeling. Nat. Protoc., 2, 2480-2491.
    • (2007) Nat. Protoc. , vol.2 , pp. 2480-2491
    • Slot, J.W.1    Geuze, H.J.2
  • 88
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C. and Schekman, R. (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell, 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 89
    • 0024370763 scopus 로고
    • The genetic control of direct-repeat recombination in Saccharomyces: the effect of rad52 and rad1 on mitotic recombination at GAL10, a transcriptionally regulated gene
    • Thomas, B.J. and Rothstein, R. (1989) The genetic control of direct-repeat recombination in Saccharomyces: the effect of rad52 and rad1 on mitotic recombination at GAL10, a transcriptionally regulated gene. Genetics, 123, 725-738.
    • (1989) Genetics , vol.123 , pp. 725-738
    • Thomas, B.J.1    Rothstein, R.2


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