메뉴 건너뛰기




Volumn 13, Issue , 2011, Pages

Autophagic pathways in Parkinson disease and related disorders

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; CATHEPSIN D; ELONGATION FACTOR 1ALPHA; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR 37; GLIAL FIBRILLARY ACIDIC PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LEUCINE RICH REPEAT KINASE 2; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; PARKIN; PARKIN 2; PINK1 PROTEIN; PROTEIN SERINE THREONINE KINASE; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG; CHAPERONE;

EID: 79956124664     PISSN: 14623994     EISSN: 14623994     Source Type: Journal    
DOI: 10.1017/S1462399411001803     Document Type: Article
Times cited : (86)

References (140)
  • 2
    • 0034735536 scopus 로고    scopus 로고
    • Autophagic tubes: Vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding
    • Muller, O. et al. (2000) Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding. Journal of Cell Biology 151, 519-528
    • (2000) Journal of Cell Biology , vol.151 , pp. 519-528
    • Muller, O.1
  • 3
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • DOI 10.1126/science.1099993
    • Shintani, T. and Klionsky, D.J. (2004) Autophagy in health and disease: a double-edged sword. Science 306, 990-995 (Pubitemid 39482894)
    • (2004) Science , vol.306 , Issue.5698 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 4
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: From protein metabolism to bactericide
    • DOI 10.1038/sj.cdd.4401728, PII 4401728
    • Mizushima, N. (2005) The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell Death and Differentiation 12 (Suppl 2), 1535-1541 (Pubitemid 41553990)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.SUPPL. 2 , pp. 1535-1541
    • Mizushima, N.1
  • 5
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • Hayashi-Nishino, M. et al. (2009) A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nature Cell Biology 11, 1433-1437
    • (2009) Nature Cell Biology , vol.11 , pp. 1433-1437
    • Hayashi-Nishino, M.1
  • 6
    • 77956414236 scopus 로고    scopus 로고
    • The origin of the autophagosomal membrane
    • Tooze, S.A. and Yoshimori, T. (2010) The origin of the autophagosomal membrane. Nature Cell Biology 12, 831-835
    • (2010) Nature Cell Biology , vol.12 , pp. 831-835
    • Tooze, S.A.1    Yoshimori, T.2
  • 7
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang, Z. and Klionsky, D.J. (2010) Mammalian autophagy: core molecular machinery and signaling regulation. Current Opinion in Cell Biology 22, 124-131
    • (2010) Current Opinion in Cell Biology , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 8
    • 33645120442 scopus 로고    scopus 로고
    • Microtubules facilitate autophagosome formation and fusion of autophagosomeswith endosomes
    • Kochl, R. et al. (2006) Microtubules facilitate autophagosome formation and fusion of autophagosomeswith endosomes. Traffic 7, 129-145
    • (2006) Traffic , vol.7 , pp. 129-145
    • Kochl, R.1
  • 9
    • 0027419879 scopus 로고
    • Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport
    • Hollenbeck, P.J. (1993) Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport. Journal of Cell Biology 121, 305-315 (Pubitemid 23110875)
    • (1993) Journal of Cell Biology , vol.121 , Issue.2 , pp. 305-315
    • Hollenbeck, P.J.1
  • 10
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • DOI 10.1038/35056522
    • Ohsumi, Y. (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nature Reviews. Molecular Cell Biology 2, 211-216 (Pubitemid 33675746)
    • (2001) Nature Reviews Molecular Cell Biology , vol.2 , Issue.3 , pp. 211-216
    • Ohsumi, Y.1
  • 11
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: Unanswered questions
    • DOI 10.1242/jcs.01620
    • Klionsky, D.J. (2005) The molecular machinery of autophagy: unanswered questions. Journal of Cell Science 118, 7-18 (Pubitemid 40277100)
    • (2005) Journal of Cell Science , vol.118 , Issue.1 , pp. 7-18
    • Klionsky, D.J.1
  • 12
    • 77950501014 scopus 로고    scopus 로고
    • Mtor regulation of autophagy
    • Jung, C.H. et al. (2010) mTOR regulation of autophagy. FEBS Letters 584, 1287-1295
    • (2010) FEBS Letters , vol.584 , pp. 1287-1295
    • Jung, C.H.1
  • 13
    • 78149475088 scopus 로고    scopus 로고
    • Regulation of mammalian autophagy in physiology and pathophysiology
    • Ravikumar, B. et al. (2010) Regulation of mammalian autophagy in physiology and pathophysiology. Physiological Reviews 90, 1383-1435
    • (2010) Physiological Reviews , vol.90 , pp. 1383-1435
    • Ravikumar, B.1
  • 14
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C. and Klionsky, D.J. (2009) Regulation mechanisms and signaling pathways of autophagy. Annual Review of Genetics 43, 67-93
    • (2009) Annual Review of Genetics , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 15
    • 70349644856 scopus 로고    scopus 로고
    • Atg101 a novel mammalian autophagy protein interacting with Atg13
    • Hosokawa, N. et al. (2009) Atg101, a novel mammalian autophagy protein interacting with Atg13. Autophagy 5, 973-979
    • (2009) Autophagy , vol.5 , pp. 973-979
    • Hosokawa, N.1
  • 16
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • DOI 10.1038/nrm2245, PII NRM2245
    • Klionsky, D.J. (2007) Autophagy: from phenomenology to molecular understanding in less than a decade. Nature Reviews. Molecular Cell Biology 8, 931-937 (Pubitemid 47622558)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 931-937
    • Klionsky, D.J.1
  • 18
    • 48249092267 scopus 로고    scopus 로고
    • Bcl-2 family members: Dual regulators of apoptosis and autophagy
    • Levine, B., Sinha, S. and Kroemer, G. (2008) Bcl-2 family members: dual regulators of apoptosis and autophagy. Autophagy 4, 600-606
    • (2008) Autophagy , vol.4 , pp. 600-606
    • Levine, B.1    Sinha, S.2    Kroemer, G.3
  • 19
    • 78049271501 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase class III sub-complex containing VPS15 VPS34 Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic
    • Thoresen, S.B. et al. (2010) A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic. Experimental Cell Research 316, 3368-3378
    • (2010) Experimental Cell Research , vol.316 , pp. 3368-3378
    • Thoresen, S.B.1
  • 20
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex-at the crossroads of autophagy and beyond
    • Funderburk, S.F.,Wang, Q.J. and Yue, Z. (2010) The Beclin 1-VPS34 complex-at the crossroads of autophagy and beyond. Trends in Cell Biology 20, 355-362
    • (2010) Trends in Cell Biology , vol.20 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 21
    • 59249105964 scopus 로고    scopus 로고
    • Monitoring autophagic degradation of p62/SQSTM1
    • Bjorkoy, G. et al. (2009) Monitoring autophagic degradation of p62/SQSTM1. Methods in Enzymology 452, 181-197
    • (2009) Methods in Enzymology , vol.452 , pp. 181-197
    • Bjorkoy, G.1
  • 22
    • 33645926989 scopus 로고    scopus 로고
    • p62/ SQSTM1: A missing link between protein aggregates and the autophagy machinery
    • Bjorkoy, G., Lamark, T. and Johansen, T. (2006) p62/ SQSTM1: a missing link between protein aggregates and the autophagy machinery. Autophagy 2, 138-139
    • (2006) Autophagy , vol.2 , pp. 138-139
    • Bjorkoy, G.1    Lamark, T.2    Johansen, T.3
  • 24
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky, D.J. et al. (2008) Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4, 151-175 (Pubitemid 351231180)
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2
  • 25
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi, Y. et al. (2003) The deacetylaseHDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727-738 (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 26
    • 33947149637 scopus 로고    scopus 로고
    • Atg19 mediates a dual interaction cargo sorting mechanism in selective autophagy
    • Chang, C.Y. and Huang,W.P. (2007) Atg19 mediates a dual interaction cargo sorting mechanism in selective autophagy. Molecular Biology of the Cell 18, 919-929
    • (2007) Molecular Biology of the Cell , vol.18 , pp. 919-929
    • Chang, C.Y.1    Huang, W.P.2
  • 27
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston, T.L. et al. (2009) The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nature Immunology 10, 1215-1221
    • (2009) Nature Immunology , vol.10 , pp. 1215-1221
    • Thurston, T.L.1
  • 28
    • 74049153002 scopus 로고    scopus 로고
    • Nix is a selective autophagy receptor for mitochondrial clearance
    • Novak, I. et al. (2010) Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Reports 11, 45-51
    • (2010) EMBO Reports , vol.11 , pp. 45-51
    • Novak, I.1
  • 29
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki, T. et al. (2009) Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Developmental Cell 17, 98-109
    • (2009) Developmental Cell , vol.17 , pp. 98-109
    • Kanki, T.1
  • 30
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin, V. et al. (2009) A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Molecular Cell 33, 505-516
    • (2009) Molecular Cell , vol.33 , pp. 505-516
    • Kirkin, V.1
  • 31
    • 77950903972 scopus 로고    scopus 로고
    • The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein alfy
    • Filimonenko, M. et al. (2010) The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy. Molecular Cell 38, 265-279
    • (2010) Molecular Cell , vol.38 , pp. 265-279
    • Filimonenko, M.1
  • 32
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara, T. et al. (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441, 885-889
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1
  • 33
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu, M. et al. (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441, 880-884
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1
  • 35
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk, V.I. et al. (2009) Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Molecular Cell 33, 517-527
    • (2009) Molecular Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1
  • 37
    • 0026521660 scopus 로고
    • Genes necessary for directed axonal elongation or fasciculation in C elegans
    • McIntire, S.L. et al. (1992) Genes necessary for directed axonal elongation or fasciculation in C. elegans. Neuron 8, 307-322
    • (1992) Neuron , vol.8 , pp. 307-322
    • McIntire, S.L.1
  • 39
    • 34347344990 scopus 로고    scopus 로고
    • Ambra1 regulates autophagy and development of the nervous system
    • Fimia, G.M. et al. (2007) Ambra1 regulates autophagy and development of the nervous system. Nature 447, 1121-1125
    • (2007) Nature , vol.447 , pp. 1121-1125
    • Fimia, G.M.1
  • 40
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • Lee, J.A. et al. (2007) ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Current Biology 17, 1561-1567
    • (2007) Current Biology , vol.17 , pp. 1561-1567
    • Lee, J.A.1
  • 41
    • 4344712684 scopus 로고    scopus 로고
    • Methods for monitoring autophagy
    • DOI 10.1016/j.biocel.2004.02.005, PII S135727250400055X
    • Mizushima, N. (2004) Methods for monitoring autophagy. International Journal of Biochemistry and Cell Biology 36, 2491-2502 (Pubitemid 39119761)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.12 , pp. 2491-2502
    • Mizushima, N.1
  • 42
    • 84934440488 scopus 로고    scopus 로고
    • Autophagosomes in GFP-LC3 transgenic mice
    • Mizushima, N. and Kuma, A. (2008) Autophagosomes in GFP-LC3 transgenic mice. Methods in Molecular Biology 445, 119-124
    • (2008) Methods in Molecular Biology , vol.445 , pp. 119-124
    • Mizushima, N.1    Kuma, A.2
  • 43
    • 59249095218 scopus 로고    scopus 로고
    • Methods for monitoring autophagy using GFP-LC3 transgenic mice
    • Mizushima, N. (2009) Methods for monitoring autophagy using GFP-LC3 transgenic mice. Methods in Enzymology 452, 13-23
    • (2009) Methods in Enzymology , vol.452 , pp. 13-23
    • Mizushima, N.1
  • 44
    • 70349162889 scopus 로고    scopus 로고
    • Protein turnover differences between neurons and other cells
    • Epub ahead of print
    • Tsvetkov, A.S., Mitra, S. and Finkbeiner, S. (2009) Protein turnover differences between neurons and other cells. Autophagy 5 [Epub ahead of print]
    • (2009) Autophagy , vol.5
    • Tsvetkov, A.S.1    Mitra, S.2    Finkbeiner, S.3
  • 45
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimers disease
    • Boland, B. et al. (2008) Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. Journal of Neuroscience 28, 6926-6937
    • (2008) Journal of Neuroscience , vol.28 , pp. 6926-6937
    • Boland, B.1
  • 46
    • 63249135140 scopus 로고    scopus 로고
    • Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease
    • Mitra, S., Tsvetkov, A.S. and Finkbeiner, S. (2009) Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease. Journal of Biological Chemistry 284, 4398-4403
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 4398-4403
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 48
    • 69349090907 scopus 로고    scopus 로고
    • The cellular pathways of neuronal autophagy and their implication in neurodegenerative diseases
    • Yue, Z. et al. (2009) The cellular pathways of neuronal autophagy and their implication in neurodegenerative diseases. Biochimica et Biophysica Acta 1793, 1496-1507
    • (2009) Biochimica et Biophysica Acta , vol.1793 , pp. 1496-1507
    • Yue, Z.1
  • 50
    • 33745026738 scopus 로고    scopus 로고
    • Autophagy and aging: The importance of maintaining clean cells
    • Cuervo, A.M. et al. (2005) Autophagy and aging: the importance of maintaining clean cells. Autophagy 1, 131-140
    • (2005) Autophagy , vol.1 , pp. 131-140
    • Cuervo, A.M.1
  • 51
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo, A.M. and Dice, J.F. (2000) Age-related decline in chaperone-mediated autophagy. Journal of Biological Chemistry 275, 31505-31513
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 53
    • 38949099761 scopus 로고    scopus 로고
    • Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
    • Simonsen, A. et al. (2008) Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila. Autophagy 4, 176-184 (Pubitemid 351231181)
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 176-184
    • Simonsen, A.1    Cumming, R.C.2    Brech, A.3    Isakson, P.4    Schubert, D.R.5    Finley, K.D.6
  • 54
    • 34548068573 scopus 로고    scopus 로고
    • Linking lysosomal trafficking defects with changes in aging and stress response in Drosophila
    • Simonsen, A., Cumming, R.C. and Finley, K.D. (2007) Linking lysosomal trafficking defects with changes in aging and stress response in Drosophila. Autophagy 3, 499-501 (Pubitemid 47293739)
    • (2007) Autophagy , vol.3 , Issue.5 , pp. 499-501
    • Simonsen, A.1    Cumming, R.C.2    Finley, K.D.3
  • 55
    • 34250728186 scopus 로고    scopus 로고
    • Genetic modifiers of the drosophila blue cheese gene link defects in lysosomal transport with decreased life span and altered ubiquitinated-protein profiles
    • DOI 10.1534/genetics.106.065011
    • Simonsen, A. et al. (2007) Genetic modifiers of the Drosophila blue cheese gene link defects in lysosomal transport with decreased life span and altered ubiquitinated-protein profiles. Genetics 176, 1283-1297 (Pubitemid 46961121)
    • (2007) Genetics , vol.176 , Issue.2 , pp. 1283-1297
    • Simonsen, A.1    Cumming, R.C.2    Lindmo, K.3    Galaviz, V.4    Cheng, S.5    Rusten, T.E.6    Finley, K.D.7
  • 56
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H.L. et al. (1989) A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382-385
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1
  • 57
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • DOI 10.1074/jbc.272.9.5606
    • Cuervo, A.M., Dice, J.F. and Knecht, E. (1997) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. Journal of Biological Chemistry 272, 5606-5615 (Pubitemid 27102386)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 58
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A.M. and Dice, J.F. (1996)Areceptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501-503 (Pubitemid 26286451)
    • (1996) Science , vol.273 , Issue.5274 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 59
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes, F.A. and Dice, J.F. (2001) A molecular chaperone complex at the lysosomal membrane is required for protein translocation. Journal of Cell Science 114, 2491-2499 (Pubitemid 32684803)
    • (2001) Journal of Cell Science , vol.114 , Issue.13 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 60
    • 51349130544 scopus 로고    scopus 로고
    • The chaperonemediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay, U. et al. (2008) The chaperonemediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Molecular Cell Biol 28, 5747-5763
    • (2008) Molecular Cell Biol. , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1
  • 61
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice, J.F. (1990) Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends in Biochemical Sciences 15, 305-309 (Pubitemid 20223216)
    • (1990) Trends in Biochemical Sciences , vol.15 , Issue.8 , pp. 305-309
    • Dice, J.F.1
  • 62
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang, H.L. and Dice, J.F. (1988) Peptide sequences that target proteins for enhanced degradation during serum withdrawal. Journal of Biological Chemistry 263, 6797-6805
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 6797-6805
    • Chiang, H.L.1    Dice, J.F.2
  • 63
    • 0029047863 scopus 로고
    • Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2 resulting in alternative transmembrane and cytoplasmic domains
    • Hatem, C.L., Gough, N.R. and Fambrough, D.M. (1995) Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2, resulting in alternative transmembrane and cytoplasmic domains. Journal of Cell Science 108(Pt 5), 2093-2100
    • (1995) Journal of Cell Science , vol.108 , Issue.5 , pp. 2093-2100
    • Hatem, C.L.1    Gough, N.R.2    Fambrough, D.M.3
  • 64
    • 77955989034 scopus 로고    scopus 로고
    • Identification of regulators of chaperone-mediated autophagy
    • Bandyopadhyay, U. et al. (2010) Identification of regulators of chaperone-mediated autophagy. Molecular Cell 39, 535-547
    • (2010) Molecular Cell , vol.39 , pp. 535-547
    • Bandyopadhyay, U.1
  • 65
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo, A.M. and Dice, J.F. (2000) Regulation of lamp2a levels in the lysosomal membrane. Traffic 1, 570-583
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 66
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo, A.M. et al. (1995) Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. American Journal of Physiology 269, C1200-C1208 (Pubitemid 3005885)
    • (1995) The American journal of physiology , vol.269 , Issue.51
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 67
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • DOI 10.1083/jcb.137.4.825
    • Agarraberes, F.A., Terlecky, S.R. and Dice, J.F. (1997) An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. Journal of Cell Biology 137, 825-834 (Pubitemid 27215505)
    • (1997) Journal of Cell Biology , vol.137 , Issue.4 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 68
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: When the cleaning crew goes on strike
    • DOI 10.1016/S1474-4422(07)70076-5, PII S1474442207700765
    • Martinez-Vicente, M. and Cuervo, A.M. (2007) Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurology 6, 352-361 (Pubitemid 46367949)
    • (2007) Lancet Neurology , vol.6 , Issue.4 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 69
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi, T. et al. (2008)Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. Journal of Biological Chemistry 283, 23542-23556
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1
  • 71
    • 41949125675 scopus 로고    scopus 로고
    • Loss of macroautophagy promotes or prevents fibroblast apoptosis depending on the death stimulus
    • Wang, Y. et al. (2007) Loss of macroautophagy promotes or prevents fibroblast apoptosis depending on the death stimulus. Journal of Biological Chemistry 283, 4766-4777
    • (2007) Journal of Biological Chemistry , vol.283 , pp. 4766-4777
    • Wang, Y.1
  • 72
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • Kaushik, S. et al. (2008) Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Molecular Biology of the Cell 19, 2179-2192
    • (2008) Molecular Biology of the Cell , vol.19 , pp. 2179-2192
    • Kaushik, S.1
  • 73
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to other lamp2 isoforms
    • Cuervo, A.M. and Dice, J.F. (2000) Unique properties of lamp2a compared to other lamp2 isoforms. Journal of Cell Science 113(Pt 24), 4441-4450 (Pubitemid 32117905)
    • (2000) Journal of Cell Science , vol.113 , Issue.24 , pp. 4441-4450
    • Cuervo, A.M.1    Dice, J.F.2
  • 74
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
    • Zhang, C. and Cuervo, A.M. (2008) Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nature Medicine 14, 959-965
    • (2008) Nature Medicine , vol.14 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 75
    • 78149469728 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy markers in parkinson disease brains
    • Alvarez-Erviti, L. et al. (2010) Chaperone-Mediated Autophagy Markers in Parkinson Disease Brains. Archives of Neurology 67, 1464-1472
    • (2010) Archives of Neurology , vol.67 , pp. 1464-1472
    • Alvarez-Erviti, L.1
  • 76
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri, M. et al. (2009) Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS One 4, e5515
    • (2009) PLoS One , vol.4
    • Xilouri, M.1
  • 77
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy
    • DOI 10.1126/science.1101738
    • Cuervo, A.M. et al. (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305, 1292-1295 (Pubitemid 39129234)
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stafanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 78
    • 38849174979 scopus 로고    scopus 로고
    • Dopaminemodified alpha-synuclein blocks chaperonemediated autophagy
    • Martinez-Vicente, M. et al. (2008) Dopaminemodified alpha-synuclein blocks chaperonemediated autophagy. Journal of Clinical Investigation 118, 777-788
    • (2008) Journal of Clinical Investigation , vol.118 , pp. 777-788
    • Martinez-Vicente, M.1
  • 79
    • 58149215720 scopus 로고    scopus 로고
    • Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy
    • Yang, Q. et al. (2009) Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science 323, 124-127
    • (2009) Science , vol.323 , pp. 124-127
    • Yang, Q.1
  • 80
    • 65549099222 scopus 로고    scopus 로고
    • All-you-caneat: Autophagy in neurodegeneration and neuroprotection
    • Jaeger, P.A. andWyss-Coray, T. (2009) All-you-caneat: autophagy in neurodegeneration and neuroprotection.MolecularNeurodegeneration4,16
    • (2009) MolecularNeurodegeneration 4 , vol.16
    • Jaeger, P.A.1    Wyss-Coray, T.2
  • 81
    • 26444515364 scopus 로고    scopus 로고
    • Autophagy and its possible roles in nervous system diseases damage and repair
    • Rubinsztein, D.C. et al. (2005) Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 1, 11-22
    • (2005) Autophagy , vol.1 , pp. 11-22
    • Rubinsztein, D.C.1
  • 82
    • 44149124887 scopus 로고    scopus 로고
    • Autophagy in neuroprotection and neurodegeneration: A question of balance
    • DOI 10.2217/14796708.3.3.309
    • Cherra, S.J. and Chu, C.T. (2008) Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurology 3, 309-323 (Pubitemid 351715775)
    • (2008) Future Neurology , vol.3 , Issue.3 , pp. 309-323
    • Cherra III, S.J.1    Chu, C.T.2
  • 83
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong, E. and Cuervo, A.M. (2010) Autophagy gone awry in neurodegenerative diseases. Nature Neuroscience 13, 805-811
    • (2010) Nature Neuroscience , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 84
    • 33846186851 scopus 로고    scopus 로고
    • Autophagy is one of the multiple mechanisms active in photoreceptor degeneration
    • Kunchithapautham, K. and Rohrer, B. (2007) Autophagy is one of the multiple mechanisms active in photoreceptor degeneration. Autophagy 3, 65-66 (Pubitemid 46100719)
    • (2007) Autophagy , vol.3 , Issue.1 , pp. 65-66
    • Kunchithapautham, K.1    Rohrer, B.2
  • 85
    • 0024370374 scopus 로고
    • Endocytosis and autophagy in dying neurons: An ultrastructural study in chick embryos
    • DOI 10.1002/cne.902830310
    • Hornung, J.P., Koppel, H. and Clarke, P.G. (1989) Endocytosis and autophagy in dying neurons: an ultrastructural study in chick embryos. Journal of Comparative Neurology 283, 425-437 (Pubitemid 19160399)
    • (1989) Journal of Comparative Neurology , vol.283 , Issue.3 , pp. 425-437
    • Hornung, J.P.1    Koppel, H.2    Clarke, P.G.H.3
  • 86
    • 33744913540 scopus 로고    scopus 로고
    • Multiple, parallel cellular suicide mechanisms participate in photoreceptor cell death
    • DOI 10.1016/j.exer.2006.01.014, PII S0014483506001485
    • Lohr, H.R. et al. (2006) Multiple, parallel cellular suicide mechanisms participate in photoreceptor cell death. Experimental Eye Research 83, 380-389 (Pubitemid 43850954)
    • (2006) Experimental Eye Research , vol.83 , Issue.2 , pp. 380-389
    • Lohr, H.R.1    Kuntchithapautham, K.2    Sharma, A.K.3    Rohrer, B.4
  • 88
    • 58449101589 scopus 로고    scopus 로고
    • Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in drosophila
    • Ling, D. et al. (2009) Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila. PLoS ONE 4, e4201
    • (2009) PLoS One , vol.4
    • Ling, D.1
  • 92
    • 0030882856 scopus 로고    scopus 로고
    • Alpha-synuclein in lewy bodies
    • Spillantini, M.G. et al. (1997) Alpha-synuclein in Lewy bodies. Nature 388, 839-840
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1
  • 93
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • DOI 10.1038/nm1066
    • Ross, C.A. and Poirier, M.A. (2004) Protein aggregation and neurodegenerative disease. Nature Medicine 10 (Suppl), S10-S17 (Pubitemid 38901862)
    • (2004) Nature Medicine , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 94
    • 0141741347 scopus 로고    scopus 로고
    • Parkinsons disease: Mechanisms and models
    • Dauer, W. and Przedborski, S. (2003) Parkinson's disease: mechanisms and models. Neuron 39, 889-909
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 95
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • DOI 10.1038/nrn1868, PII N1868
    • Abou-Sleiman, P.M., Muqit, M.M. andWood, N.W. (2006) Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nature Reviews. Neuroscience 7, 207-219 (Pubitemid 43292466)
    • (2006) Nature Reviews Neuroscience , vol.7 , Issue.3 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.K.2    Wood, N.W.3
  • 96
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • Giasson, B.I. et al. (2000) Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 290, 985-989
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1
  • 97
    • 62449129138 scopus 로고    scopus 로고
    • Cell death pathways in Parkinsons disease: Proximal triggers distal effectors and final steps
    • Levy, O.A., Malagelada, C. and Greene, L.A. (2009) Cell death pathways in Parkinson's disease: proximal triggers, distal effectors, and final steps. Apoptosis 14, 478-500
    • (2009) Apoptosis , vol.14 , pp. 478-500
    • Levy, O.A.1    Malagelada, C.2    Greene, L.A.3
  • 98
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease: Insights from genetic studies
    • Gasser, T. (2009) Molecular pathogenesis of Parkinson disease: insights from genetic studies. Expert Reviews in Molecular Medicine 11, e22
    • (2009) Expert Reviews in Molecular Medicine , vol.11
    • Gasser, T.1
  • 99
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade, P. et al. (1997) Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histology and Histopathology 12, 25-31 (Pubitemid 27106916)
    • (1997) Histology and Histopathology , vol.12 , Issue.1 , pp. 25-31
    • Anglade, P.1
  • 100
    • 0242499488 scopus 로고    scopus 로고
    • Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in lewy body diseases
    • Zhu, J.H. et al. (2003) Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathology 13, 473-481
    • (2003) Brain Pathology , vol.13 , pp. 473-481
    • Zhu, J.H.1
  • 101
    • 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 Neuropathologica 34, 183197
    • (1976) Acta Neuropathologica , vol.34 , pp. 183197
    • Forno, L.S.1    Norville, R.L.2
  • 102
    • 77956855813 scopus 로고    scopus 로고
    • Pathogenic lysosomal depletion in Parkinsons disease
    • Dehay, B. et al. (2010) Pathogenic lysosomal depletion in Parkinson's disease. Journal of Neuroscience 30, 12535-12544
    • (2010) Journal of Neuroscience , vol.30 , pp. 12535-12544
    • Dehay, B.1
  • 103
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinsons disease: Relationship to alpha-synuclein inclusions
    • Chu, Y. et al. (2009) Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiology of Disease 35, 385-398
    • (2009) Neurobiology of Disease , vol.35 , pp. 385-398
    • Chu, Y.1
  • 104
    • 12944305793 scopus 로고    scopus 로고
    • Neuromelanin biosynthesis is driven by excess cytosolic catecholamines not accumulated by synaptic vesicles
    • Sulzer,D. et al. (2000) Neuromelanin biosynthesis is driven by excess cytosolic catecholamines not accumulated by synaptic vesicles. Proceedings of the National Academy of Sciences of the United States of America 97, 11869-11874
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , pp. 11869-11874
    • Sulzer, D.1
  • 105
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with lewy body disease and in models of alphasynucleinopathy
    • Crews, L. et al. (2010) Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alphasynucleinopathy. PLoS One 5, e9313
    • (2010) PLoS One , vol.5
    • Crews, L.1
  • 106
    • 68449089023 scopus 로고    scopus 로고
    • Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein
    • Yu,W.H. et al. (2009) Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein. American Journal of Pathology 175, 736-747
    • (2009) American Journal of Pathology , vol.175 , pp. 736-747
    • Yu, W.H.1
  • 107
    • 29744442267 scopus 로고    scopus 로고
    • Gene expression profiling of sporadic Parkinson's disease substantia nigra pars compacta reveals impairment of ubiquitin-proteasome subunits, SKP1A, aldehyde dehydrogenase, and chaperone HSC-70
    • DOI 10.1196/annals.1344.031
    • Mandel, S. et al. (2005) Gene expression profiling of sporadic Parkinson's disease substantia nigra pars compacta reveals impairment of ubiquitinproteasome subunits, SKP1A, aldehyde dehydrogenase, and chaperone HSC-70. Annals of the New York Academy of Sciences 1053, 356-375 (Pubitemid 43031116)
    • (2005) Annals of the New York Academy of Sciences , vol.1053 , pp. 356-375
    • Mandel, S.1    Grunblatt, E.2    Riederer, P.3    Amariglio, N.4    Hirsch, J.J.5    Rechavi, G.6    Youdim, M.B.H.7
  • 108
    • 53549118274 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by autophagic pathways: A potential key to Parkinsons disease pathogenesis
    • Xilouri, M. et al. (2008) Alpha-synuclein degradation by autophagic pathways: a potential key to Parkinson's disease pathogenesis. Autophagy 4, 917-919
    • (2008) Autophagy , vol.4 , pp. 917-919
    • Xilouri, M.1
  • 111
    • 70350319531 scopus 로고    scopus 로고
    • Multicenter analysis of glucocerebrosidase mutations in Parkinsons disease
    • Sidransky, E. et al. (2009) Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease. New England Journal of Medicine 361, 1651-1661
    • (2009) New England Journal of Medicine , vol.361 , pp. 1651-1661
    • Sidransky, E.1
  • 112
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinsons disease
    • Chartier-Harlin, M.C. et al. (2004) Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364, 1167-1169
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1
  • 114
    • 0031990490 scopus 로고    scopus 로고
    • Ala 30Pro mutation in the gene encoding alpha-synuclein in Parkinsons disease
    • Kruger, R. et al. (1998) Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nature Genetics 18, 106-108
    • (1998) Nature Genetics , vol.18 , pp. 106-108
    • Kruger, R.1
  • 117
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinsons disease
    • Simon-Sanchez, J. et al. (2009) Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nature Genetics 41, 1308-1312
    • (2009) Nature Genetics , vol.41 , pp. 1308-1312
    • Simon-Sanchez, J.1
  • 118
    • 0033607801 scopus 로고    scopus 로고
    • Degradation of alphasynuclein by proteasome
    • Bennett, M.C. et al. (1999) Degradation of alphasynuclein by proteasome. Journal of Biological Chemistry 274, 33855-33858
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 33855-33858
    • Bennett, M.C.1
  • 119
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai, Y., Soda, M. and Takahashi, R. (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. Journal of Biological Chemistry 275, 35661-35664
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 121
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • Lee, H.J. et al. (2004) Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. Journal of Neuroscience 24, 1888-1896
    • (2004) Journal of Neuroscience , vol.24 , pp. 1888-1896
    • Lee, H.J.1
  • 122
    • 77951541740 scopus 로고    scopus 로고
    • Lysosomal degradation of alpha-synuclein in vivo
    • Mak, S.K. et al. (2010) Lysosomal degradation of alpha-synuclein in vivo. Journal of Biological Chemistry 285, 13621-13629
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 13621-13629
    • Mak, S.K.1
  • 123
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis, L. et al. (2001) Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. Journal of Neuroscience 21, 9549-9560 (Pubitemid 34184043)
    • (2001) Journal of Neuroscience , vol.21 , Issue.24 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 124
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alphasynuclein models of Parkinsons and Lewy body diseases
    • Spencer, B. et al. (2009) Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alphasynuclein models of Parkinson's and Lewy body diseases. Journal of Neuroscience 29, 13578-13588
    • (2009) Journal of Neuroscience , vol.29 , pp. 13578-13588
    • Spencer, B.1
  • 125
    • 77957189194 scopus 로고    scopus 로고
    • Alpha-Synuclein impairs macroautophagy: Implications for Parkinsons disease
    • Winslow, A.R. et al. (2010) alpha-Synuclein impairs macroautophagy: implications for Parkinson's disease. Journal of Cell Biology 190, 1023-1037
    • (2010) Journal of Cell Biology , vol.190 , pp. 1023-1037
    • Winslow, A.R.1
  • 126
    • 53049101345 scopus 로고    scopus 로고
    • Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy
    • Kabuta,T. et al. (2008) Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy. Journal of Biological Chemistry 283, 23731-23738
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 23731-23738
    • Kabuta, T.1
  • 127
    • 70349991886 scopus 로고    scopus 로고
    • LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model
    • Alegre-Abarrategui, J. et al. (2009) LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model. Human Molecular Genetics 18, 4022-4034
    • (2009) Human Molecular Genetics , vol.18 , pp. 4022-4034
    • Alegre-Abarrategui, J.1
  • 128
    • 73449124773 scopus 로고    scopus 로고
    • Parkinson disease LRRK2 and the endocyticautophagic pathway
    • Alegre-Abarrategui, J. andWade-Martins, R. (2009) Parkinson disease, LRRK2 and the endocyticautophagic pathway. Autophagy 5, 1208-1210
    • (2009) Autophagy , vol.5 , pp. 1208-1210
    • Alegre-Abarrategui, J.1    Wade-Martins, R.2
  • 129
    • 70349574622 scopus 로고    scopus 로고
    • Abnormal localization of leucine-rich repeat kinase 2 to the endosomallysosomal compartment in lewy body disease
    • Higashi, S. et al. (2009) Abnormal localization of leucine-rich repeat kinase 2 to the endosomallysosomal compartment in lewy body disease. Journal of Neuropathology and Experimental Neurology 68, 994-1005
    • (2009) Journal of Neuropathology and Experimental Neurology , vol.68 , pp. 994-1005
    • Higashi, S.1
  • 130
    • 77953090478 scopus 로고    scopus 로고
    • Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways accumulation of alpha-synuclein, and apoptotic cell death in aged mice
    • Tong, Y. et al. (2010) Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of alpha-synuclein, and apoptotic cell death in aged mice. Proceedings of the National Academy of Sciences of the United States of America 107, 9879-9884
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , pp. 9879-9884
    • Tong, Y.1
  • 131
    • 39549117093 scopus 로고    scopus 로고
    • Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells
    • DOI 10.1111/j.1471-4159.2008.05217.x
    • Plowey, E.D. et al. (2008) Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells. Journal of Neurochemistry 105, 1048-1056 (Pubitemid 351565713)
    • (2008) Journal of Neurochemistry , vol.105 , Issue.3 , pp. 1048-1056
    • Plowey, E.D.1    Cherra III, S.J.2    Liu, Y.-J.3    Chu, C.T.4
  • 132
    • 68949209958 scopus 로고    scopus 로고
    • Cell death pathways in Parkinsons disease: Role of mitochondria
    • Yao, Z. andWood, N.W. (2009) Cell death pathways in Parkinson's disease: role of mitochondria. Antioxidants and Redox Signaling 11, 2135-2149
    • (2009) Antioxidants and Redox Signaling , vol.11 , pp. 2135-2149
    • Yao, Z.1    Wood, N.W.2
  • 133
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D. et al. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. Journal ofCell Biology 183, 795-803
    • (2008) Journal ofCell Biology , vol.183 , pp. 795-803
    • Narendra, D.1
  • 134
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • Narendra, D.P. et al. (2010) PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biology 8, e1000298
    • (2010) PLoS Biology , vol.8
    • Narendra, D.P.1
  • 136
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda, R.K. et al. (2009) Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. Journal of Biological Chemistry 284, 13843-13855
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 13843-13855
    • Dagda, R.K.1
  • 137
    • 77952242572 scopus 로고    scopus 로고
    • The Parkinson-associated protein PINK1 interacts with beclin1 and promotes autophagy
    • Michiorri, S. et al. (2010) The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy. Cell Death and Differentiation 17, 962-974
    • (2010) Cell Death and Differentiation , vol.17 , pp. 962-974
    • Michiorri, S.1
  • 138
    • 67649354547 scopus 로고    scopus 로고
    • Induction of macroautophagy by overexpression of the Parkinsons disease-associated GPR37 receptor
    • Marazziti, D. et al. (2009) Induction of macroautophagy by overexpression of the Parkinson's disease-associated GPR37 receptor. FASEB Journal 23, 1978-1987
    • (2009) FASEB Journal , vol.23 , pp. 1978-1987
    • Marazziti, D.1
  • 139
    • 77952648551 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival
    • Emmanouilidou, E. et al. (2010) Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival. Journal of Neuroscience 30, 6838-6851
    • (2010) Journal of Neuroscience , vol.30 , pp. 6838-6851
    • Emmanouilidou, E.1
  • 140
    • 38149044992 scopus 로고    scopus 로고
    • Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells
    • Fader, C.M. et al. (2008) Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells. Traffic 9, 230-250
    • (2008) Traffic , vol.9 , pp. 230-250
    • Fader, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.