메뉴 건너뛰기




Volumn 52, Issue 3, 2015, Pages 1190-1209

Mechanism and Regulation of Autophagy and Its Role in Neuronal Diseases

Author keywords

Autophagy; Autophagy flux; Brain ischemia; Myelin disease; Neurodegenerative diseases; Neurons

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN; PROTEASOME; UBIQUITIN; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; NERVE PROTEIN; RAS PROTEIN; TARGET OF RAPAMYCIN KINASE; TOR COMPLEX 2;

EID: 84942754615     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-014-8921-4     Document Type: Review
Times cited : (62)

References (258)
  • 1
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases. Nat Rev Drug Discov 11:709–730. doi:10.1038/nrd3802
    • Rubinsztein DC, Codogno P, Levine B (2012) Autophagy modulation as a potential therapeutic target for diverse diseases. Nat Rev Drug Discov 11:709–730. doi:10.1038/nrd3802, Review
    • (2012) Review
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 2
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: renovation of cells and tissues
    • COI: 1:CAS:528:DC%2BC3MXhsVKgsLnN, PID: 22078875
    • Mizushima N, Komatsu M (2011) Autophagy: renovation of cells and tissues. Cell 147(4):728–741. doi:10.1016/j.cell.2011.10.026
    • (2011) Cell , vol.147 , Issue.4 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 3
    • 84855500993 scopus 로고    scopus 로고
    • Autophagy: for better or for worse
    • COI: 1:CAS:528:DC%2BC38Xks1Chtg%3D%3D, PID: 21912435
    • Wirawan E, Vanden Berghe T, Lippens S et al (2012) Autophagy: for better or for worse. Cell Res 22:43–61. doi:10.1038/cr.2011.152
    • (2012) Cell Res , vol.22 , pp. 43-61
    • Wirawan, E.1    Vanden Berghe, T.2    Lippens, S.3
  • 4
    • 79957916809 scopus 로고    scopus 로고
    • V-ATPase engagement in autophagic processes
    • COI: 1:CAS:528:DC%2BC38Xks1ylsw%3D%3D, PID: 21494095
    • Mijaljica D, Prescott M, Devenish RJ (2011) V-ATPase engagement in autophagic processes. Autophagy 7(6):666–668
    • (2011) Autophagy , vol.7 , Issue.6 , pp. 666-668
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 5
    • 78651423598 scopus 로고    scopus 로고
    • Microautophagy of cytosolic proteins by late endosomes
    • COI: 1:CAS:528:DC%2BC3MXnsVelsQ%3D%3D, PID: 21238931
    • Sahu R, Kaushik S, Clement CC et al (2011) Microautophagy of cytosolic proteins by late endosomes. Dev Cell 20(1):131–139. doi:10.1016/j.devcel.2010.12.003
    • (2011) Dev Cell , vol.20 , Issue.1 , pp. 131-139
    • Sahu, R.1    Kaushik, S.2    Clement, C.C.3
  • 6
    • 84934440405 scopus 로고    scopus 로고
    • Microautophagy in the yeast Saccharomyces cerevisiae
    • COI: 1:CAS:528:DC%2BD1cXmsV2ls7s%3D, PID: 18425455
    • Uttenweiler A, Mayer A (2008) Microautophagy in the yeast Saccharomyces cerevisiae. Methods Mol Biol 445:245–259. doi:10.1007/978-1-59745-157-4-16
    • (2008) Methods Mol Biol , vol.445 , pp. 245-259
    • Uttenweiler, A.1    Mayer, A.2
  • 7
    • 38849105061 scopus 로고    scopus 로고
    • A picky eater: exploring the mechanisms of selective autophagy in human pathologies
    • PID: 17988219
    • van der Vaart A, Mari M, Reggiori F (2008) A picky eater: exploring the mechanisms of selective autophagy in human pathologies. Traffic 9(3):281–289
    • (2008) Traffic , vol.9 , Issue.3 , pp. 281-289
    • van der Vaart, A.1    Mari, M.2    Reggiori, F.3
  • 8
    • 69349102568 scopus 로고    scopus 로고
    • Kraft C, Reggiori F, Peter M (2009) Selective types of autophagy in yeast. Biochim Biophys Acta 1793(9):1404–12. Review
    • Kraft C, Reggiori F, Peter M (2009) Selective types of autophagy in yeast. Biochim Biophys Acta 1793(9):1404–12. doi:10.1038/cdd.2012.73, Review
  • 9
    • 46049116842 scopus 로고    scopus 로고
    • Beau I, Esclatine A, Codogno P (2008) Lost to translation: when autophagy targets mature ribosomes. Trends Cell Biol 18(7):311–314. Review
    • Beau I, Esclatine A, Codogno P (2008) Lost to translation: when autophagy targets mature ribosomes. Trends Cell Biol 18(7):311–314. doi:10.1016/j.tcb.2008.05.001, Review
  • 10
    • 79951580982 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: machinery, regulation and biological consequences
    • COI: 1:CAS:528:DC%2BC3MXhvVWhur0%3D, PID: 20976518
    • Li W, Yang Q, Mao Z (2011) Chaperone-mediated autophagy: machinery, regulation and biological consequences. Cell Mol Life Sci 68(5):749–763. doi:10.1007/s00018-010-0565-6
    • (2011) Cell Mol Life Sci , vol.68 , Issue.5 , pp. 749-763
    • Li, W.1    Yang, Q.2    Mao, Z.3
  • 11
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • COI: 1:CAS:528:DyaK3MXlvFegsg%3D%3D, PID: 2204156
    • Dice JF (1990) Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 15(8):305–309
    • (1990) Trends Biochem Sci , vol.15 , Issue.8 , pp. 305-309
    • Dice, J.F.1
  • 12
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: from protein metabolism to bactericide
    • COI: 1:CAS:528:DC%2BD2MXhtFCjt7%2FP, PID: 16247501
    • Mizushima N (2005) The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell Death Differ 12(Suppl 2):1535–41
    • (2005) Cell Death Differ , vol.12 , pp. 1535-1541
    • Mizushima, N.1
  • 13
    • 34548093280 scopus 로고    scopus 로고
    • How shall I eat thee?
    • PID: 17568180
    • Klionsky DJ, Cuervo AM, Dunn WA Jr et al (2007) How shall I eat thee? Autophagy 3(5):413–416
    • (2007) Autophagy , vol.3 , Issue.5 , pp. 413-416
    • Klionsky, D.J.1    Cuervo, A.M.2    Dunn, W.A.3
  • 14
    • 65549142204 scopus 로고    scopus 로고
    • Kirkin V, McEwan DG, Novak I et al (2009) A role for ubiquitin in selective autophagy. Mol Cell 34(3):259–69. Review
    • Kirkin V, McEwan DG, Novak I et al (2009) A role for ubiquitin in selective autophagy. Mol Cell 34(3):259–69. doi:10.1016/j.molcel.2009.04.026, Review
  • 15
    • 33645829816 scopus 로고    scopus 로고
    • Consequences of the selective blockage of chaperone-mediated autophagy
    • COI: 1:CAS:528:DC%2BD28XktFaitro%3D, PID: 16585521
    • Massey AC, Kaushik S, Sovak G et al (2006) Consequences of the selective blockage of chaperone-mediated autophagy. Proc Natl Acad Sci U S A 103(15):5805–5810
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.15 , pp. 5805-5810
    • Massey, A.C.1    Kaushik, S.2    Sovak, G.3
  • 16
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • COI: 1:CAS:528:DC%2BD1cXlslelsb8%3D, PID: 18337468
    • Kaushik S, Massey AC, Mizushima N et al (2008) Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 19(5):2179–2192. doi:10.1091/mbc.E07-11-1155
    • (2008) Mol Biol Cell , vol.19 , Issue.5 , pp. 2179-2192
    • Kaushik, S.1    Massey, A.C.2    Mizushima, N.3
  • 17
    • 0018992813 scopus 로고
    • ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • COI: 1:CAS:528:DyaL3cXitFSgsrc%3D, PID: 6769112
    • Ciechanover A, Heller H, Elias S et al (1980) ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc Natl Acad Sci U S A 77(3):1365–1368
    • (1980) Proc Natl Acad Sci U S A , vol.77 , Issue.3 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3
  • 18
    • 33645669213 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system
    • COI: 1:CAS:528:DC%2BD28XjvFWjs7Y%3D, PID: 16595883, Review
    • Nandi D, Tahiliani P, Kumar A (2006) The ubiquitin-proteasome system. J Biosci 31(1):137–155, Review
    • (2006) J Biosci , vol.31 , Issue.1 , pp. 137-155
    • Nandi, D.1    Tahiliani, P.2    Kumar, A.3
  • 19
    • 0037401773 scopus 로고    scopus 로고
    • Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions
    • COI: 1:CAS:528:DC%2BD3sXisFShtLk%3D, PID: 12672457
    • Fuertes G, Villarroya A, Knecht E (2003) Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions. Int J Biochem Cell Biol 35(5):651–64
    • (2003) Int J Biochem Cell Biol , vol.35 , Issue.5 , pp. 651-664
    • Fuertes, G.1    Villarroya, A.2    Knecht, E.3
  • 20
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • COI: 1:CAS:528:DC%2BD3sXnsVyju70%3D, PID: 12841850
    • Fuertes G, Martín De Llano JJ, Villarroya A et al (2003) Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 375(Pt 1):75–86
    • (2003) Biochem J , vol.375 , pp. 75-86
    • Fuertes, G.1    Martín De Llano, J.J.2    Villarroya, A.3
  • 21
    • 0036840193 scopus 로고    scopus 로고
    • The cellular response to aggregated proteins associated with human disease
    • COI: 1:CAS:528:DC%2BD38XosF2gurY%3D, PID: 12417557
    • Perlmutter DH (2002) The cellular response to aggregated proteins associated with human disease. J Clin Invest 110:1219–1220
    • (2002) J Clin Invest , vol.110 , pp. 1219-1220
    • Perlmutter, D.H.1
  • 22
    • 4344618623 scopus 로고    scopus 로고
    • Autophagy, proteasomes, lipofuscin, and oxidative stress in the aging brain
    • COI: 1:CAS:528:DC%2BD2cXmvFemurc%3D, PID: 15325579
    • Keller JN, Dimayuga E, Chen Q et al (2004) Autophagy, proteasomes, lipofuscin, and oxidative stress in the aging brain. Int J Biochem Cell Biol 36:2376–2391
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2376-2391
    • Keller, J.N.1    Dimayuga, E.2    Chen, Q.3
  • 23
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • COI: 1:CAS:528:DC%2BD3MXktVyqs74%3D, PID: 11375494
    • Bence NF, Sampat RM, Kopito RR (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292:1552–1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 24
    • 0035976919 scopus 로고    scopus 로고
    • The proteasome participates in degradation of mutant α1-antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes
    • COI: 1:CAS:528:DC%2BD3MXovFegurs%3D, PID: 11577074
    • Teckman JH, Burrows J, Hidvegi T et al (2001) The proteasome participates in degradation of mutant α1-antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes. J Biol Chem 276:44865–44872
    • (2001) J Biol Chem , vol.276 , pp. 44865-44872
    • Teckman, J.H.1    Burrows, J.2    Hidvegi, T.3
  • 25
    • 9644254067 scopus 로고    scopus 로고
    • Can autophagy protect against neurodegeneration caused by aggregate-prone proteins?
    • PID: 15538170
    • Ravikumar B, Rubinsztein DC (2004) Can autophagy protect against neurodegeneration caused by aggregate-prone proteins? Neuroreport 15:2443–2445
    • (2004) Neuroreport , vol.15 , pp. 2443-2445
    • Ravikumar, B.1    Rubinsztein, D.C.2
  • 26
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant α(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • COI: 1:CAS:528:DC%2BD3cXotFaqtrk%3D
    • Teckman JH, Perlmutter DH (2000) Retention of mutant α(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physio 279:G961–G974
    • (2000) Am J Physio , vol.279 , pp. G961-G974
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 27
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • COI: 1:CAS:528:DC%2BD2cXksVajt7s%3D, PID: 15146184
    • Ravikumar B, Vacher C, Berger Z et al (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 36:585–595
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 28
    • 33645216184 scopus 로고    scopus 로고
    • Intracellular inclusions containing mutant α1-antitrypsin Z are propagated in the absence of autophagic activity
    • COI: 1:CAS:528:DC%2BD28XhtlKrsr0%3D, PID: 16365039
    • Kamimoto T, Shoji S, Hidvegi T et al (2006) Intracellular inclusions containing mutant α1-antitrypsin Z are propagated in the absence of autophagic activity. J Biol Chem 281:4467–4476
    • (2006) J Biol Chem , vol.281 , pp. 4467-4476
    • Kamimoto, T.1    Shoji, S.2    Hidvegi, T.3
  • 29
    • 33744916798 scopus 로고    scopus 로고
    • Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
    • COI: 1:CAS:528:DC%2BD28XksFeitL4%3D, PID: 16522639
    • Shibata M, Lu T, Furuya T et al (2006) Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1. J Biol Chem 281:14474–14485
    • (2006) J Biol Chem , vol.281 , pp. 14474-14485
    • Shibata, M.1    Lu, T.2    Furuya, T.3
  • 30
    • 30044436220 scopus 로고    scopus 로고
    • Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human α-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ
    • COI: 1:CAS:528:DC%2BD28Xjslamtg%3D%3D, PID: 16267277
    • Kruse KB, Brodsky JL, McCracken AA (2006) Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human α-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ. Mol Biol Cell 17:203–212
    • (2006) Mol Biol Cell , vol.17 , pp. 203-212
    • Kruse, K.B.1    Brodsky, J.L.2    McCracken, A.A.3
  • 31
    • 33645451010 scopus 로고    scopus 로고
    • Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: an explanation for liver disease
    • COI: 1:CAS:528:DC%2BD28XjslOhurw%3D, PID: 16565503
    • Kruse KB, Dear A, Kaltenbrun ER et al (2006) Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: an explanation for liver disease. Am J Pathol 168:1299–1308
    • (2006) Am J Pathol , vol.168 , pp. 1299-1308
    • Kruse, K.B.1    Dear, A.2    Kaltenbrun, E.R.3
  • 32
    • 35948958216 scopus 로고    scopus 로고
    • HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration
    • COI: 1:CAS:528:DC%2BD2sXhtlOhsL7F, PID: 17912024
    • Pandey UB, Batlevi Y, Baehrecke EH et al (2007) HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration. Autophagy 3(6):643–645
    • (2007) Autophagy , vol.3 , Issue.6 , pp. 643-645
    • Pandey, U.B.1    Batlevi, Y.2    Baehrecke, E.H.3
  • 33
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • PID: 16286508
    • Bjørkøy G, Lamark T, Brech A et al (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 171(4):603–614
    • (2005) J Cell Biol , vol.171 , Issue.4 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3
  • 34
    • 4944247868 scopus 로고    scopus 로고
    • Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes
    • COI: 1:CAS:528:DC%2BD2cXotlGrt7c%3D, PID: 15292400
    • Simonsen A, Birkeland HC, Gillooly DJ et al (2004) Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes. J Cell Sci 117(Pt 18):4239–4251
    • (2004) J Cell Sci , vol.117 , pp. 4239-4251
    • Simonsen, A.1    Birkeland, H.C.2    Gillooly, D.J.3
  • 35
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • COI: 1:CAS:528:DC%2BD1MXltFSnu7Y%3D, PID: 19250912
    • Korolchuk VI, Mansilla A et al (2009) Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 33(4):517–527. doi:10.1016/j.molcel.2009.01.021
    • (2009) Mol Cell , vol.33 , Issue.4 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2
  • 36
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • COI: 1:CAS:528:DC%2BC3cXjs12msro%3D, PID: 20040365
    • Korolchuk VI, Menzies FM, Rubinsztein DC (2010) Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett 584(7):1393–1398. doi:10.1016/j.febslet.2009.12.047
    • (2010) FEBS Lett , vol.584 , Issue.7 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 37
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • COI: 1:CAS:528:DC%2BD2sXpsFaiu7w%3D, PID: 17620365
    • Ding WX, Ni HM, Gao W et al (2007) Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 171(2):513–524
    • (2007) Am J Pathol , vol.171 , Issue.2 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3
  • 38
    • 84855645313 scopus 로고    scopus 로고
    • Mechanisms of autophagosome biogenesis. Curr Biol 22:R229–R234. doi:10.1016/j.cub.2011.11.034
    • Rubinsztein DC, Shpilka T, Elazar Z (2012) Mechanisms of autophagosome biogenesis. Curr Biol 22:R229–R234. doi:10.1016/j.cub.2011.11.034, Review
    • (2012) Review
    • Rubinsztein, D.C.1    Shpilka, T.2    Elazar, Z.3
  • 39
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • COI: 1:CAS:528:DC%2BD1MXhsF2qtrjK, PID: 19653858
    • He C, Klionsky DJ (2009) Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 43:67–93. doi:10.1146/annurev-genet-102808-114910
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 40
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • COI: 1:CAS:528:DC%2BD3sXotlSqu7o%3D, PID: 14536056
    • Klionsky DJ, Cregg JM, Dunn WA Jr et al (2003) A unified nomenclature for yeast autophagy-related genes. Dev Cell 5(4):539–545
    • (2003) Dev Cell , vol.5 , Issue.4 , pp. 539-545
    • Klionsky, D.J.1    Cregg, J.M.2    Dunn, W.A.3
  • 41
    • 0027936092 scopus 로고
    • Isolation of autophagocytosis mutants of Saccharomyces cerevisiae
    • COI: 1:CAS:528:DyaK2cXmtVSks78%3D, PID: 8050581
    • Thumm M, Egner R, Koch B et al (1994) Isolation of autophagocytosis mutants of Saccharomyces cerevisiae. FEBS Lett 349(2):275–280
    • (1994) FEBS Lett , vol.349 , Issue.2 , pp. 275-280
    • Thumm, M.1    Egner, R.2    Koch, B.3
  • 42
    • 84857802958 scopus 로고    scopus 로고
    • Molecules and their functions in autophagy
    • COI: 1:CAS:528:DC%2BC38Xmtlymt7k%3D, PID: 22257882, Review
    • Pyo JO, Nah J, Jung YK (2012) Molecules and their functions in autophagy. Exp Mol Med 44(2):73–80. doi:10.3858/emm.2012.44.2.029, Review
    • (2012) Exp Mol Med , vol.44 , Issue.2 , pp. 73-80
    • Pyo, J.O.1    Nah, J.2    Jung, Y.K.3
  • 43
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • COI: 1:CAS:528:DC%2BD1cXhtV2rurzK, PID: 18725538
    • Axe EL, Walker SA, Manifava M et al (2008) Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 182:685–701. doi:10.1083/jcb.200803137
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3
  • 44
    • 39449108917 scopus 로고    scopus 로고
    • The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae
    • COI: 1:CAS:528:DC%2BD1cXlslenur8%3D, PID: 18077553
    • Cheong H, Nair U, Geng J (2008) The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae. Mol Biol Cell 19:668–681
    • (2008) Mol Biol Cell , vol.19 , pp. 668-681
    • Cheong, H.1    Nair, U.2    Geng, J.3
  • 45
    • 18244394277 scopus 로고    scopus 로고
    • Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy
    • COI: 1:CAS:528:DC%2BD2MXjvVKit7w%3D, PID: 15743910
    • Kabeya Y, Kamada Y, Baba M et al (2005) Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy. Mol Biol Cell 16:2544–2553
    • (2005) Mol Biol Cell , vol.16 , pp. 2544-2553
    • Kabeya, Y.1    Kamada, Y.2    Baba, M.3
  • 46
    • 0034683568 scopus 로고    scopus 로고
    • Tor-mediated induction of autophagy via an Apg1 protein kinase complex
    • COI: 1:CAS:528:DC%2BD3cXmslGlsr4%3D, PID: 10995454
    • Kamada Y, Funakoshi T, Shintani T et al (2000) Tor-mediated induction of autophagy via an Apg1 protein kinase complex. J Cell Biol 150:1507–1513
    • (2000) J Cell Biol , vol.150 , pp. 1507-1513
    • Kamada, Y.1    Funakoshi, T.2    Shintani, T.3
  • 47
    • 48249129649 scopus 로고    scopus 로고
    • Dual role of Atg1 in regulation of autophagy-specific PAS assembly in Saccharomyces cerevisiae
    • COI: 1:CAS:528:DC%2BD1cXpsVCkur0%3D, PID: 18552550
    • Cheong H, Klionsky DJ (2008) Dual role of Atg1 in regulation of autophagy-specific PAS assembly in Saccharomyces cerevisiae. Autophagy 4:724–726
    • (2008) Autophagy , vol.4 , pp. 724-726
    • Cheong, H.1    Klionsky, D.J.2
  • 48
    • 43149125546 scopus 로고    scopus 로고
    • Organization of the pre-autophagosomal structure responsible for autophagosome formation
    • COI: 1:CAS:528:DC%2BD1cXlslels7Y%3D, PID: 18287526
    • Kawamata T, Kamada Y, Kabeya Y (2008) Organization of the pre-autophagosomal structure responsible for autophagosome formation. Mol Biol Cell 19:2039–2050. doi:10.1091/mbc.E07-10-1048
    • (2008) Mol Biol Cell , vol.19 , pp. 2039-2050
    • Kawamata, T.1    Kamada, Y.2    Kabeya, Y.3
  • 49
    • 33846514235 scopus 로고    scopus 로고
    • Hierarchy of Atg proteins in pre-autophagosomal structure organization
    • COI: 1:CAS:528:DC%2BD2sXitVKrtrs%3D, PID: 17295840
    • Suzuki K, Kubota Y, Sekito T, Ohsumi Y (2007) Hierarchy of Atg proteins in pre-autophagosomal structure organization. Genes Cells 12:209–218
    • (2007) Genes Cells , vol.12 , pp. 209-218
    • Suzuki, K.1    Kubota, Y.2    Sekito, T.3    Ohsumi, Y.4
  • 50
    • 66449083078 scopus 로고    scopus 로고
    • ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy
    • COI: 1:CAS:528:DC%2BD1MXltVCmu7c%3D, PID: 19258318
    • Ganley IG, du Lam H, Wang J et al (2009) ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. J Biol Chem 284:12297–12305. doi:10.1074/jbc.M900573200
    • (2009) J Biol Chem , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    du Lam, H.2    Wang, J.3
  • 51
    • 65249119430 scopus 로고    scopus 로고
    • Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy
    • COI: 1:CAS:528:DC%2BD1MXotVyqsL4%3D, PID: 19211835
    • Hosokawa N, Hara T, Kaizuka T et al (2009) Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy. Mol Biol Cell 20:1981–1991. doi:10.1091/mbc.E08-12-1248
    • (2009) Mol Biol Cell , vol.20 , pp. 1981-1991
    • Hosokawa, N.1    Hara, T.2    Kaizuka, T.3
  • 52
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • COI: 1:CAS:528:DC%2BD1MXotVyqsL8%3D, PID: 19225151
    • Jung CH, Jun CB, Ro SH et al (2009) ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell 20:1992–2003. doi:10.1091/mbc.E08-12-1249
    • (2009) Mol Biol Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3
  • 53
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • PID: 16625204
    • Nakahara Y, Suzuki-Migishima R, Yokoyama M 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
    • Nakahara, Y.1    Suzuki-Migishima, R.2    Yokoyama, M.3
  • 54
    • 67549110195 scopus 로고    scopus 로고
    • A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy
    • Mercer CA, Kaliappan A, Dennis PB (2009) A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy. Autophagy 5(7):973–979
    • (2009) Autophagy , vol.5 , Issue.7 , pp. 973-979
    • Mercer, C.A.1    Kaliappan, A.2    Dennis, P.B.3
  • 55
    • 70349644856 scopus 로고    scopus 로고
    • Atg101, a novel mammalian autophagy protein interacting with Atg13
    • COI: 1:CAS:528:DC%2BC3cXmt1ChtQ%3D%3D, PID: 19597335
    • Hosokawa N, Sasaki T, Iemura S et al (2009) Atg101, a novel mammalian autophagy protein interacting with Atg13. Autophagy 5(7):973–979
    • (2009) Autophagy , vol.5 , Issue.7 , pp. 973-979
    • Hosokawa, N.1    Sasaki, T.2    Iemura, S.3
  • 56
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • COI: 1:CAS:528:DC%2BD1cXhsVynu77M, PID: 18843052
    • Itakura E, Kishi C, Inoue K et al (2008) Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 19:5360–5372
    • (2008) Mol Biol Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3
  • 57
    • 58049192897 scopus 로고    scopus 로고
    • Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase
    • COI: 1:CAS:528:DC%2BD1cXhsFamu7zM, PID: 19050071
    • Sun Q, Fan W, Chen K et al (2008) Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A 105:19211–19216. doi:10.1073/pnas.0810452105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19211-19216
    • Sun, Q.1    Fan, W.2    Chen, K.3
  • 58
    • 85117876522 scopus 로고    scopus 로고
    • Regulation of the autophagic bcl-2/beclin 1 interaction
    • COI: 1:CAS:528:DC%2BC38XhvVSrsLjF, PID: 24710477
    • Decuypere JP, Parys JB, Bultynck G (2012) Regulation of the autophagic bcl-2/beclin 1 interaction. Cells 1(3):284–312. doi:10.3390/cells1030284
    • (2012) Cells , vol.1 , Issue.3 , pp. 284-312
    • Decuypere, J.P.1    Parys, J.B.2    Bultynck, G.3
  • 59
    • 0037107491 scopus 로고    scopus 로고
    • Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase
    • COI: 1:CAS:528:DC%2BD38Xos12ktLs%3D, PID: 12244127
    • Burda P, Padilla SM, Sarkar S (2002) Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase. J Cell Sci 115:3889–390060
    • (2002) J Cell Sci , vol.115 , pp. 3889-390060
    • Burda, P.1    Padilla, S.M.2    Sarkar, S.3
  • 60
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • COI: 1:CAS:528:DC%2BC3cXks1SrtLo%3D, PID: 20097051
    • He C, Levine B (2010) The Beclin 1 interactome. Curr Opin Cell Biol 22:140–149. doi:10.1016/j.ceb.2010.01.001
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 140-149
    • He, C.1    Levine, B.2
  • 61
    • 84862257733 scopus 로고    scopus 로고
    • The crosstalk between autophagy and apoptosis: where does this lead?
    • PID: 22314807
    • Gordy C, He YW (2012) The crosstalk between autophagy and apoptosis: where does this lead? Protein Cell 3:17–27. doi:10.1007/s13238-011-1127-x
    • (2012) Protein Cell , vol.3 , pp. 17-27
    • Gordy, C.1    He, Y.W.2
  • 62
    • 84859962405 scopus 로고    scopus 로고
    • Involvement of Beclin 1 in engulfment of apoptotic cells
    • COI: 1:CAS:528:DC%2BC38XlvVGlsbo%3D, PID: 22393062
    • Konishi A, Arakawa S, Yue Z et al (2012) Involvement of Beclin 1 in engulfment of apoptotic cells. J Biol Chem 287:13919–13929. doi:10.1074/jbc.M112.348375
    • (2012) J Biol Chem , vol.287 , pp. 13919-13929
    • Konishi, A.1    Arakawa, S.2    Yue, Z.3
  • 63
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex—at the crossroads of autophagy and beyond
    • COI: 1:CAS:528:DC%2BC3cXntVOrsL0%3D, PID: 20356743
    • Funderburk SF, Wang QJ, Yue Z (2010) The Beclin 1-VPS34 complex—at the crossroads of autophagy and beyond. Trends Cell Biol 20:355–362. doi:10.1016/j.tcb.2010.03.002
    • (2010) Trends Cell Biol , vol.20 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 64
    • 46449120732 scopus 로고    scopus 로고
    • Beclin 1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • COI: 1:CAS:528:DC%2BD1cXnvFSju70%3D, PID: 18552835
    • Liang C, Lee JS, Inn KS et al (2008) Beclin 1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat Cell Biol 10:776–787. doi:10.1038/ncb1740
    • (2008) Nat Cell Biol , vol.10 , pp. 776-787
    • Liang, C.1    Lee, J.S.2    Inn, K.S.3
  • 65
    • 64049086758 scopus 로고    scopus 로고
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
    • COI: 1:CAS:528:DC%2BD1MXjvVymsr4%3D, PID: 19270696
    • Matsunaga K, Saitoh T, Tabata K et al (2009) Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol 11:385–396. doi:10.1038/ncb1846
    • (2009) Nat Cell Biol , vol.11 , pp. 385-396
    • Matsunaga, K.1    Saitoh, T.2    Tabata, K.3
  • 66
    • 34347344990 scopus 로고    scopus 로고
    • Ambra1 regulates autophagy and development of the nervous system
    • COI: 1:CAS:528:DC%2BD2sXntlOlu7s%3D, PID: 17589504
    • Fimia GM, Stoykova A, Romagnoli A 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    Stoykova, A.2    Romagnoli, A.3
  • 67
    • 34848899280 scopus 로고    scopus 로고
    • Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis
    • COI: 1:CAS:528:DC%2BD2sXhtFSntb%2FL, PID: 17891140
    • Takahashi Y, Coppola D, Matsushita N et al (2007) Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis. Nat Cell Biol 9:1142–1151
    • (2007) Nat Cell Biol , vol.9 , pp. 1142-1151
    • Takahashi, Y.1    Coppola, D.2    Matsushita, N.3
  • 68
    • 0037194894 scopus 로고    scopus 로고
    • A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice
    • COI: 1:CAS:528:DC%2BD38XntFSksrw%3D, PID: 12372286
    • Yue Z, Horton A, Bravin M et al (2002) A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice. Neuron 35:921–33
    • (2002) Neuron , vol.35 , pp. 921-933
    • Yue, Z.1    Horton, A.2    Bravin, M.3
  • 69
    • 67549135655 scopus 로고    scopus 로고
    • The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1
    • COI: 1:CAS:528:DC%2BD1MXnsV2qs7s%3D, PID: 19325567
    • Vicencio JM, Ortiz C, Criollo A et al (2009) The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1. Cell Death Differ 16:1006–1017. doi:10.1038/cdd.2009.34
    • (2009) Cell Death Differ , vol.16 , pp. 1006-1017
    • Vicencio, J.M.1    Ortiz, C.2    Criollo, A.3
  • 70
    • 37549012209 scopus 로고    scopus 로고
    • The pancreatitis-induced vacuole membrane protein 1 triggers autophagy in mammalian cells
    • COI: 1:CAS:528:DC%2BD2sXhsVamurvN, PID: 17940279
    • Ropolo A, Grasso D, Pardo R et al (2007) The pancreatitis-induced vacuole membrane protein 1 triggers autophagy in mammalian cells. J Biol Chem 282:37124–37133
    • (2007) J Biol Chem , vol.282 , pp. 37124-37133
    • Ropolo, A.1    Grasso, D.2    Pardo, R.3
  • 71
    • 78649242978 scopus 로고    scopus 로고
    • HMGB1: a novel Beclin 1-binding protein active in autophagy
    • COI: 1:CAS:528:DC%2BC3cXhs1WltrbM, PID: 20935509
    • Kang R, Livesey KM, Zeh HJ et al (2010) HMGB1: a novel Beclin 1-binding protein active in autophagy. Autophagy 6:1209–1211
    • (2010) Autophagy , vol.6 , pp. 1209-1211
    • Kang, R.1    Livesey, K.M.2    Zeh, H.J.3
  • 72
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • COI: 1:CAS:528:DC%2BD1cXnvFWntrc%3D, PID: 18570871
    • Wei Y, Pattingre S, Sinha S et al (2008) JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol Cell 30(6):678–88. doi:10.1016/j.molcel.2008.06.001
    • (2008) Mol Cell , vol.30 , Issue.6 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3
  • 73
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • COI: 1:CAS:528:DC%2BD2MXhtVOrurbP, PID: 16179260
    • Pattingre S, Tassa A, Qu X et al (2005) Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 122:927–939
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3
  • 74
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • COI: 1:CAS:528:DC%2BD1MXhtFOqt7k%3D, PID: 19180116
    • Zalckvar E, Berissi H, Mizrachy L (2009) DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep 10(3):285–292. doi:10.1038/embor.2008.246
    • (2009) EMBO Rep , vol.10 , Issue.3 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3
  • 75
    • 0034614934 scopus 로고    scopus 로고
    • Apg9p/Cvt7p is an integral membrane protein required for transport vesicle formation in the Cvt and autophagy pathways
    • COI: 1:CAS:528:DC%2BD3cXhtFSqtrk%3D, PID: 10662773
    • Noda T, Kim J, Huang WP et al (2000) Apg9p/Cvt7p is an integral membrane protein required for transport vesicle formation in the Cvt and autophagy pathways. J Cell Biol 148:465–480
    • (2000) J Cell Biol , vol.148 , pp. 465-480
    • Noda, T.1    Kim, J.2    Huang, W.P.3
  • 76
    • 84864991509 scopus 로고    scopus 로고
    • Atg9 vesicles are an important membrane source during early steps of autophagosome formation
    • COI: 1:CAS:528:DC%2BC38XhtFaisLbO, PID: 22826123
    • Yamamoto H, Kakuta S, Watanabe TM et al (2012) Atg9 vesicles are an important membrane source during early steps of autophagosome formation. J Cell Biol 198(2):219–33. doi:10.1083/jcb.201202061
    • (2012) J Cell Biol , vol.198 , Issue.2 , pp. 219-233
    • Yamamoto, H.1    Kakuta, S.2    Watanabe, T.M.3
  • 77
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • COI: 1:CAS:528:DC%2BC3cXht1ahsbjJ, PID: 20855505
    • Mari MI, Griffith J, Rieter E (2010) An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J Cell Biol 190:1005–1022. doi:10.1083/jcb.200912089
    • (2010) J Cell Biol , vol.190 , pp. 1005-1022
    • Mari, M.I.1    Griffith, J.2    Rieter, E.3
  • 78
    • 84861158462 scopus 로고    scopus 로고
    • Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy
    • COI: 1:CAS:528:DC%2BC38XotlWmu78%3D, PID: 22456507
    • Orsi AI, Razi M, Dooley HC, Robinson D (2012) Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy. Mol Biol Cell 23:1860–1873. doi:10.1091/mbc.E11-09-0746
    • (2012) Mol Biol Cell , vol.23 , pp. 1860-1873
    • Orsi, A.I.1    Razi, M.2    Dooley, H.C.3    Robinson, D.4
  • 79
    • 79959874238 scopus 로고    scopus 로고
    • The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella
    • COI: 1:CAS:528:DC%2BC3MXptVaitrg%3D, PID: 21525242
    • Kageyama S, Omori H, Saitoh T et al (2011) The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella. Mol Biol Cell 22(13):2290–2300. doi:10.1091/mbc.E10-11-0893
    • (2011) Mol Biol Cell , vol.22 , Issue.13 , pp. 2290-2300
    • Kageyama, S.1    Omori, H.2    Saitoh, T.3
  • 80
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • COI: 1:CAS:528:DC%2BC3cXhtFCqsrrP, PID: 20639694
    • Itakura E, Mizushima N (2010) Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy 6:764–776. doi:10.4161/auto.6.6.12709
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 81
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • COI: 1:CAS:528:DC%2BD28XhtFCgt7jO, PID: 16940348
    • Young AR, Chan EY, Hu XW et al (2006) Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 119(Pt 18):3888–900
    • (2006) J Cell Sci , vol.119 , pp. 3888-3900
    • Young, A.R.1    Chan, E.Y.2    Hu, X.W.3
  • 82
    • 84862611041 scopus 로고    scopus 로고
    • TBC1D14 regulates autophagosome formation via Rab11-and ULK1-positive recycling endosomes
    • COI: 1:CAS:528:DC%2BC38XotFWgur8%3D, PID: 22613832
    • Longatti AI, Lamb CA, Razi M (2012) TBC1D14 regulates autophagosome formation via Rab11-and ULK1-positive recycling endosomes. J Cell Biol 197(5):659–675. doi:10.1083/jcb.201111079
    • (2012) J Cell Biol , vol.197 , Issue.5 , pp. 659-675
    • Longatti, A.I.1    Lamb, C.A.2    Razi, M.3
  • 83
    • 27644544004 scopus 로고    scopus 로고
    • Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts
    • COI: 1:CAS:528:DC%2BD2MXhtVyktL7I, PID: 16874040
    • Reggiori F, Shintani T, Nair U et al (2005) Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts. Autophagy 1:101–109
    • (2005) Autophagy , vol.1 , pp. 101-109
    • Reggiori, F.1    Shintani, T.2    Nair, U.3
  • 84
    • 77952495224 scopus 로고    scopus 로고
    • Mitochondria supply membranes for autophagosome biogenesis during starvation
    • COI: 1:CAS:528:DC%2BC3cXms1egsr8%3D, PID: 20478256
    • Hailey DW, Rambold AS, Satpute-Krishnan P et al (2010) Mitochondria supply membranes for autophagosome biogenesis during starvation. Cell 141(4):656–667. doi:10.1016/j.cell.2010.04.009
    • (2010) Cell , vol.141 , Issue.4 , pp. 656-667
    • Hailey, D.W.1    Rambold, A.S.2    Satpute-Krishnan, P.3
  • 85
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • COI: 1:CAS:528:DC%2BC3MXptlektrc%3D, PID: 21784250
    • Moreau K, Ravikumar B, Renna M et al (2011) Autophagosome precursor maturation requires homotypic fusion. Cell 146(2):303–317. doi:10.1016/j.cell.2011.06.023
    • (2011) Cell , vol.146 , Issue.2 , pp. 303-317
    • Moreau, K.1    Ravikumar, B.2    Renna, M.3
  • 86
    • 75649144802 scopus 로고    scopus 로고
    • Macroautophagy signaling and regulation. Curr Top Microbiol Immunol 335:33–70. doi:10.1007/978-3-642-00302-82
    • Esclatine A, Chaumorcel M, Codogno P (2009) Macroautophagy signaling and regulation. Curr Top Microbiol Immunol 335:33–70. doi:10.1007/978-3-642-00302-82, Review
    • (2009) Review
    • Esclatine, A.1    Chaumorcel, M.2    Codogno, P.3
  • 87
    • 46249127490 scopus 로고    scopus 로고
    • Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease
    • COI: 1:CAS:528:DC%2BD1cXotVyiurs%3D, PID: 18430781
    • Ravikumar B, Imarisio S, Sarkar S et al (2008) Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease. J Cell Sci 121:1649–1660. doi:10.1242/jcs.025726
    • (2008) J Cell Sci , vol.121 , pp. 1649-1660
    • Ravikumar, B.1    Imarisio, S.2    Sarkar, S.3
  • 88
    • 1342321743 scopus 로고    scopus 로고
    • Two ubiquitin-like conjugation systems essential for autophagy
    • COI: 1:CAS:528:DC%2BD2cXhsFWksrg%3D, PID: 15209383
    • Ohsumi Y, Mizushima N (2004) Two ubiquitin-like conjugation systems essential for autophagy. Semin Cell Dev Biol 15:231–236
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 231-236
    • Ohsumi, Y.1    Mizushima, N.2
  • 89
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • COI: 1:CAS:528:DC%2BD2sXhsVGjtr7F, PID: 17986448
    • Hanada T, Noda NN, Satomi Y et al (2007) The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 282:37298–37302
    • (2007) J Biol Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3
  • 90
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • COI: 1:CAS:528:DC%2BD1cXlslelsL0%3D, PID: 18321988
    • Fujita N, Itoh T, Omori H et al (2008) The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell 19:2092–2100. doi:10.1091/mbc. E07-12-1257
    • (2008) Mol Biol Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3
  • 91
    • 84896465806 scopus 로고    scopus 로고
    • Neuronal autophagy and neurodevelopmental disorders
    • Lee KM, Hwang SK, Lee JA (2013) Neuronal autophagy and neurodevelopmental disorders. Neurobiol 22(3):133–142. doi:10.5607/en.2013.22.3.133
    • (2013) Neurobiol , vol.22 , Issue.3 , pp. 133-142
    • Lee, K.M.1    Hwang, S.K.2    Lee, J.A.3
  • 92
    • 79953127788 scopus 로고    scopus 로고
    • Autophagosome formation in mammalian cells
    • COI: 1:CAS:528:DC%2BC3cXhsFCgt73F, PID: 20740284
    • Burman C, Ktistakis NT (2010) Autophagosome formation in mammalian cells. Semin Immunopathol 32:397–413. doi:10.1007/s00281-010-0222-z
    • (2010) Semin Immunopathol , vol.32 , pp. 397-413
    • Burman, C.1    Ktistakis, N.T.2
  • 93
    • 0141960205 scopus 로고    scopus 로고
    • The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification
    • COI: 1:CAS:528:DC%2BD3sXnvFantL8%3D, PID: 12890687
    • Nemoto T, Tanida I, Tanida-Miyake E et al (2003) The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification. J Biol Chem 278:39517–39526
    • (2003) J Biol Chem , vol.278 , pp. 39517-39526
    • Nemoto, T.1    Tanida, I.2    Tanida-Miyake, E.3
  • 94
    • 0037134443 scopus 로고    scopus 로고
    • Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, facilitates the conjugation of hApg12p to hApg5p
    • COI: 1:CAS:528:DC%2BD38XjsFWns7s%3D, PID: 11825910
    • Tanida I, Tanida-Miyake E, Komatsu M et al (2002) Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, facilitates the conjugation of hApg12p to hApg5p. J Biol Chem 277:13739–13744
    • (2002) J Biol Chem , vol.277 , pp. 13739-13744
    • Tanida, I.1    Tanida-Miyake, E.2    Komatsu, M.3
  • 95
    • 70349687405 scopus 로고    scopus 로고
    • Discovery of Atg5/Atg7-independent alternative macroautophagy
    • COI: 1:CAS:528:DC%2BD1MXht1SqtrzP, PID: 19794493
    • Nishida Y, Arakawa S, Fujitani K et al (2009) Discovery of Atg5/Atg7-independent alternative macroautophagy. Nature 461:654–658. doi:10.1038/nature08455
    • (2009) Nature , vol.461 , pp. 654-658
    • Nishida, Y.1    Arakawa, S.2    Fujitani, K.3
  • 96
    • 67650230871 scopus 로고    scopus 로고
    • Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation
    • COI: 1:CAS:528:DC%2BD1MXhtVOkurvJ, PID: 19417210
    • Zhang J, Randall MS, Loyd MR et al (2009) Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation. Blood 114(1):157–64. doi:10.1182/blood-2008-04-151639
    • (2009) Blood , vol.114 , Issue.1 , pp. 157-164
    • Zhang, J.1    Randall, M.S.2    Loyd, M.R.3
  • 97
    • 51649124519 scopus 로고    scopus 로고
    • Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation
    • COI: 1:CAS:528:DC%2BD1cXpvVOkur4%3D, PID: 18539900
    • Kundu M, Lindsten T, Yang CY et al (2008) Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood 112(4):1493–1502
    • (2008) Blood , vol.112 , Issue.4 , pp. 1493-1502
    • Kundu, M.1    Lindsten, T.2    Yang, C.Y.3
  • 98
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: their role in cell survival and cell death
    • Codogno P, Meijer AJ (2005) Autophagy and signaling: their role in cell survival and cell death. Cell Death Differ Suppl 2:1509–1518
    • (2005) Cell Death Differ Suppl , vol.2 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 99
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in mammalian cells
    • COI: 1:CAS:528:DC%2BD2MXos1ensLw%3D, PID: 16874026
    • Eskelinen EL (2005) Maturation of autophagic vacuoles in mammalian cells. Autophagy 1:1–10
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 100
    • 67650222474 scopus 로고    scopus 로고
    • In search of an “autophagomometer
    • COI: 1:CAS:528:DC%2BD1MXpvFCjur4%3D, PID: 19411822
    • Rubinsztein DC, Cuervo AM, Ravikumar B et al (2009) In search of an “autophagomometer”. Autophagy 5:585–589
    • (2009) Autophagy , vol.5 , pp. 585-589
    • Rubinsztein, D.C.1    Cuervo, A.M.2    Ravikumar, B.3
  • 101
    • 77957969657 scopus 로고    scopus 로고
    • Beclin 1 complex in autophagy and Alzheimer disease
    • PID: 20937944
    • Jaeger PA, Wyss-Coray T (2010) Beclin 1 complex in autophagy and Alzheimer disease. Arch Neurol 67(10):1181–1184. doi:10.1001/archneurol.2010.258
    • (2010) Arch Neurol , vol.67 , Issue.10 , pp. 1181-1184
    • Jaeger, P.A.1    Wyss-Coray, T.2
  • 102
    • 84864324504 scopus 로고    scopus 로고
    • Neuronal functions of ESCRTs
    • PID: 22438674
    • Lee JA, Gao FB (2012) Neuronal functions of ESCRTs. Exp Neurobiol 21:9–15. doi:10.5607/en.2012.21.1.9
    • (2012) Exp Neurobiol , vol.21 , pp. 9-15
    • Lee, J.A.1    Gao, F.B.2
  • 103
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • COI: 1:CAS:528:DC%2BD2sXhtVGjt7vL, PID: 17683935
    • Lee JA, Beigneux A, Ahmad ST (2007) ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr Biol 17:1561–1567
    • (2007) Curr Biol , vol.17 , pp. 1561-1567
    • Lee, J.A.1    Beigneux, A.2    Ahmad, S.T.3
  • 104
    • 68149096799 scopus 로고    scopus 로고
    • The pharmacology of mTOR inhibition
    • PID: 19383975
    • Guertin DA, Sabatini DM (2009) The pharmacology of mTOR inhibition. Sci Signal 2(67):pe24. doi:10.1126/scisignal.267pe24
    • (2009) Sci Signal , vol.2 , Issue.67 , pp. pe24
    • Guertin, D.A.1    Sabatini, D.M.2
  • 105
    • 34250891313 scopus 로고    scopus 로고
    • AMP-activated protein kinase: a universal regulator of autophagy
    • PID: 17457036
    • Høyer-Hansen MI, Jäättelä M (2007) AMP-activated protein kinase: a universal regulator of autophagy. Autophagy 3:381–338
    • (2007) Autophagy , vol.3 , pp. 338-381
    • Høyer-Hansen, M.I.1    Jäättelä, M.2
  • 106
    • 79952281400 scopus 로고    scopus 로고
    • Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1
    • COI: 1:CAS:528:DC%2BC3MXisFKntrc%3D, PID: 21336308
    • Zheng MI, Wang YH, Wu XN (2011) Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1. Nat Cell Biol 13:263–272. doi:10.1038/ncb2168
    • (2011) Nat Cell Biol , vol.13 , pp. 263-272
    • Zheng, M.I.1    Wang, Y.H.2    Wu, X.N.3
  • 107
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • COI: 1:CAS:528:DC%2BD28Xhslaqs74%3D, PID: 16469695, Review
    • Wullschleger S, Loewith R, Hall MN (2006) TOR signaling in growth and metabolism. Cell 124:471–484, Review
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 108
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • COI: 1:CAS:528:DC%2BC3cXmtVWnsLk%3D, PID: 20381137
    • Sancak YI, Bar-Peled L, Zoncu R (2010) Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141:290–303. doi:10.1016/j.cell.2010.02.024
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.I.1    Bar-Peled, L.2    Zoncu, R.3
  • 109
    • 42949139481 scopus 로고    scopus 로고
    • AMPK phosphorylation of raptor mediates a metabolic checkpoint
    • COI: 1:CAS:528:DC%2BD1cXlsFentbg%3D, PID: 18439900
    • Gwinn DMI, Shackelford DB, Egan DF (2008) AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol Cell 30:214–226. doi:10.1016/j.molcel.2008.03.003
    • (2008) Mol Cell , vol.30 , pp. 214-226
    • Gwinn, D.M.I.1    Shackelford, D.B.2    Egan, D.F.3
  • 110
    • 44649101436 scopus 로고    scopus 로고
    • p53: the Janus of autophagy?
    • COI: 1:CAS:528:DC%2BD1cXmsFyksLs%3D, PID: 18521069
    • Levine B, Abrams J (2008) p53: the Janus of autophagy? Nat Cell Biol 10:637–639. doi:10.1038/ncb0608-637
    • (2008) Nat Cell Biol , vol.10 , pp. 637-639
    • Levine, B.1    Abrams, J.2
  • 111
    • 50249145608 scopus 로고    scopus 로고
    • A dual role of p53 in the control of autophagy
    • COI: 1:CAS:528:DC%2BD1cXhtVynt7nF, PID: 18604159
    • Tasdemir E, Chiara Maiuri M, Morselli E et al (2008) A dual role of p53 in the control of autophagy. Autophagy 4:810–814
    • (2008) Autophagy , vol.4 , pp. 810-814
    • Tasdemir, E.1    Chiara Maiuri, M.2    Morselli, E.3
  • 112
    • 20444363122 scopus 로고    scopus 로고
    • The coordinate regulation of the p53 and mTOR pathways in cells
    • COI: 1:CAS:528:DC%2BD2MXlsV2mt74%3D, PID: 15928081
    • Feng Z, Zhang H, Levine AJ et al (2005) The coordinate regulation of the p53 and mTOR pathways in cells. Proc Natl Acad Sci U S A 102:8204–8209
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8204-8209
    • Feng, Z.1    Zhang, H.2    Levine, A.J.3
  • 113
    • 33745885329 scopus 로고    scopus 로고
    • DRAM, a p53-induced modulator of autophagy, is critical for apoptosis
    • COI: 1:CAS:528:DC%2BD28Xns1Cgt7w%3D, PID: 16839881
    • Crighton D, Wilkinson S, O’Prey J et al (2006) DRAM, a p53-induced modulator of autophagy, is critical for apoptosis. Cell 126:121–124
    • (2006) Cell , vol.126 , pp. 121-124
    • Crighton, D.1    Wilkinson, S.2    O’Prey, J.3
  • 114
    • 75149128169 scopus 로고    scopus 로고
    • The life span-prolonging effect of sirtuin-1 is mediated by autophagy
    • PID: 20023410
    • Morselli EI, Maiuri MC, Markaki M (2010) The life span-prolonging effect of sirtuin-1 is mediated by autophagy. Autophagy 6:186–188
    • (2010) Autophagy , vol.6 , pp. 186-188
    • Morselli, E.I.1    Maiuri, M.C.2    Markaki, M.3
  • 115
    • 44649141966 scopus 로고    scopus 로고
    • Regulation of autophagy by cytoplasmic p53
    • COI: 1:CAS:528:DC%2BD1cXmsFyksbw%3D, PID: 18454141
    • Tasdemir E, Maiuri MC, Galluzzi L et al (2008) Regulation of autophagy by cytoplasmic p53. Nat Cell Biol 10:676–687. doi:10.1038/ncb1730
    • (2008) Nat Cell Biol , vol.10 , pp. 676-687
    • Tasdemir, E.1    Maiuri, M.C.2    Galluzzi, L.3
  • 116
    • 74849124984 scopus 로고    scopus 로고
    • Inhibition of mammalian S6 kinase by resveratrol suppresses autophagy
    • COI: 1:CAS:528:DC%2BD1MXht1GkurfN
    • Armour SM, Baur JA, Hsieh SN et al (2009) Inhibition of mammalian S6 kinase by resveratrol suppresses autophagy. Aging (Albany NY) 1:515–528
    • (2009) Aging (Albany NY) , vol.1 , pp. 515-528
    • Armour, S.M.1    Baur, J.A.2    Hsieh, S.N.3
  • 117
    • 34948828483 scopus 로고    scopus 로고
    • Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae
    • COI: 1:CAS:528:DC%2BD2sXhtFCnsLfK, PID: 17699586
    • Yorimitsu T, Zaman S, Broach JR et al (2007) Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae. Mol Biol Cell 18:4180–4189
    • (2007) Mol Biol Cell , vol.18 , pp. 4180-4189
    • Yorimitsu, T.1    Zaman, S.2    Broach, J.R.3
  • 118
    • 0034722378 scopus 로고    scopus 로고
    • Dissection of autophagosome biogenesis into distinct nucleation and expansion steps
    • COI: 1:CAS:528:DC%2BD3cXovVyks70%3D, PID: 11086004
    • Abeliovich H, Dunn WA Jr, Kim J et al (2000) Dissection of autophagosome biogenesis into distinct nucleation and expansion steps. J Cell Biol 151:1025–1034
    • (2000) J Cell Biol , vol.151 , pp. 1025-1034
    • Abeliovich, H.1    Dunn, W.A.2    Kim, J.3
  • 119
    • 0027178716 scopus 로고
    • Inhibition of protein synthesis separates autophagic sequestration from the delivery of lysosomal enzymes
    • COI: 1:CAS:528:DyaK2cXhtlSnsbo%3D, PID: 8408278
    • Lawrence BP, Brown WJ (1993) Inhibition of protein synthesis separates autophagic sequestration from the delivery of lysosomal enzymes. J Cell Sci 105(Pt 2):473–480
    • (1993) J Cell Sci , vol.105 , pp. 473-480
    • Lawrence, B.P.1    Brown, W.J.2
  • 120
    • 59749098315 scopus 로고    scopus 로고
    • Nutrient-dependent regulation of autophagy through the target of rapamycin pathway
    • COI: 1:CAS:528:DC%2BD1MXotVWlsQ%3D%3D, PID: 19143638
    • Chang YY, Juhasz G, Goraksha-Hicks P et al (2009) Nutrient-dependent regulation of autophagy through the target of rapamycin pathway. Biochem Soc Trans 37:232–236. doi:10.1042/BST0370232
    • (2009) Biochem Soc Trans , vol.37 , pp. 232-236
    • Chang, Y.Y.1    Juhasz, G.2    Goraksha-Hicks, P.3
  • 121
    • 77955716131 scopus 로고    scopus 로고
    • DAP1, a novel substrate of mTOR, negatively regulates autophagy
    • COI: 1:CAS:528:DC%2BC3cXnvVOnsLo%3D, PID: 20537536
    • Koren I, Reem E, Kimchi A (2010) DAP1, a novel substrate of mTOR, negatively regulates autophagy. Curr Biol 20:1093–1098. doi:10.1016/j.cub.2010.04.041
    • (2010) Curr Biol , vol.20 , pp. 1093-1098
    • Koren, I.1    Reem, E.2    Kimchi, A.3
  • 122
    • 65549145048 scopus 로고    scopus 로고
    • An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1
    • COI: 1:CAS:528:DC%2BD1MXjtVSmtLY%3D, PID: 19150980
    • Thoreen CC, Kang SA, Chang JW et al (2009) An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1. J Biol Chem 284:8023–8032. doi:10.1074/jbc.M900301200
    • (2009) J Biol Chem , vol.284 , pp. 8023-8032
    • Thoreen, C.C.1    Kang, S.A.2    Chang, J.W.3
  • 123
    • 36448940798 scopus 로고    scopus 로고
    • FoxO3 controls autophagy in skeletal muscle in vivo
    • COI: 1:CAS:528:DC%2BD2sXhsVektb%2FN, PID: 18054315
    • Mammucari C, Milan G, Romanello V et al (2007) FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab 6:458–471
    • (2007) Cell Metab , vol.6 , pp. 458-471
    • Mammucari, C.1    Milan, G.2    Romanello, V.3
  • 124
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • COI: 1:CAS:528:DyaK1MXitFGgsr0%3D, PID: 10102273
    • Brunet A, Bonni A, Zigmond MJ et al (1999) Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96:857–868
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1    Bonni, A.2    Zigmond, M.J.3
  • 125
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • COI: 1:CAS:528:DC%2BC3cXntVSrtLk%3D, PID: 20526321
    • Yu L, McPhee CK, Zheng L et al (2010) Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature 465:942–946. doi:10.1038/nature09076
    • (2010) Nature , vol.465 , pp. 942-946
    • Yu, L.1    McPhee, C.K.2    Zheng, L.3
  • 126
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • COI: 1:CAS:528:DC%2BD2cXksVGmsbg%3D, PID: 15131264
    • Yu L, Alva A, Su H et al (2004) Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science 304:1500–1502
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1    Alva, A.2    Su, H.3
  • 127
    • 13944273009 scopus 로고    scopus 로고
    • Autophagy and caspases: a new cell death program
    • COI: 1:CAS:528:DC%2BD2MXntVanur8%3D, PID: 15326383, Review
    • Yu L, Lenardo MJ, Baehrecke EH (2004) Autophagy and caspases: a new cell death program. Cell Cycle 3:1124–1126, Review
    • (2004) Cell Cycle , vol.3 , pp. 1124-1126
    • Yu, L.1    Lenardo, M.J.2    Baehrecke, E.H.3
  • 128
    • 48249140222 scopus 로고    scopus 로고
    • The selectivity of autophagy and its role in cell death and survival
    • PID: 18362514
    • Yu L, Strandberg L, Lenardo MJ (2008) The selectivity of autophagy and its role in cell death and survival. Autophagy 4(5):567–573
    • (2008) Autophagy , vol.4 , Issue.5 , pp. 567-573
    • Yu, L.1    Strandberg, L.2    Lenardo, M.J.3
  • 129
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • COI: 1:CAS:528:DyaK3sXhvVGrt7o%3D, PID: 8381210, Review
    • Berridge MJ (1993) Inositol trisphosphate and calcium signalling. Nature 361(6410):315–325, Review
    • (1993) Nature , vol.361 , Issue.6410 , pp. 315-325
    • Berridge, M.J.1
  • 130
    • 77955875002 scopus 로고    scopus 로고
    • Regulation of the autophagy protein LC3 by phosphorylation
    • COI: 1:CAS:528:DC%2BC3cXhtFajtb3O, PID: 20713600
    • Cherra SJ III, Kulich SM, Uechi G et al (2010) Regulation of the autophagy protein LC3 by phosphorylation. J Cell Biol 190:533–539. doi:10.1083/jcb.201002108
    • (2010) J Cell Biol , vol.190 , pp. 533-539
    • Cherra, S.J.1    Kulich, S.M.2    Uechi, G.3
  • 131
    • 33749000851 scopus 로고    scopus 로고
    • Depletion of type IA regulatory subunit (RI) of protein kinase A (PKA) in mammalian cells and tissues activates mTOR and causes autophagic deficiency
    • COI: 1:CAS:528:DC%2BD28XpvFGltrk%3D, PID: 16963469
    • Mavrakis M, Lippincott-Schwartz J, Stratakis CA et al (2006) Depletion of type IA regulatory subunit (RI) of protein kinase A (PKA) in mammalian cells and tissues activates mTOR and causes autophagic deficiency. Hum Mol Genet 15:2962–2971
    • (2006) Hum Mol Genet , vol.15 , pp. 2962-2971
    • Mavrakis, M.1    Lippincott-Schwartz, J.2    Stratakis, C.A.3
  • 132
    • 34247161367 scopus 로고    scopus 로고
    • a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • COI: 1:CAS:528:DC%2BD2sXhvVait7o%3D, PID: 17182613
    • Sarkar S, Davies JE, Huang Z et al (2007) a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 282:5641–5652
    • (2007) J Biol Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3
  • 133
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • COI: 1:CAS:528:DC%2BD2sXjslOmtLs%3D, PID: 17347651
    • Scherz-Shouval R, Shvets E, Fass E et al (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26:1749–1760
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3
  • 134
    • 34248994604 scopus 로고    scopus 로고
    • Small molecules enhance autophagy and reduce toxicity in Huntington’s disease models
    • COI: 1:CAS:528:DC%2BD2sXltlOjurY%3D, PID: 17486044
    • Sarkar S, Perlstein EO, Imarisio S et al (2007) Small molecules enhance autophagy and reduce toxicity in Huntington’s disease models. Nat Chem Biol 3:331–338
    • (2007) Nat Chem Biol , vol.3 , pp. 331-338
    • Sarkar, S.1    Perlstein, E.O.2    Imarisio, S.3
  • 135
    • 56249138284 scopus 로고    scopus 로고
    • Liaisons dangereuses: autophagy, neuronal survival and neurodegeneration
    • COI: 1:CAS:528:DC%2BD1cXhsVajtrvK, PID: 18840524
    • Tooze SA, Schiavo G (2008) Liaisons dangereuses: autophagy, neuronal survival and neurodegeneration. Curr Opin Neurobiol 18:504–515. doi:10.1016/j.conb.2008.09.015
    • (2008) Curr Opin Neurobiol , vol.18 , pp. 504-515
    • Tooze, S.A.1    Schiavo, G.2
  • 136
    • 68349161234 scopus 로고    scopus 로고
    • Autophagy in neurodegeneration: two sides of the same coin
    • COI: 1:CAS:528:DC%2BD1MXosFCisLc%3D, PID: 19558789
    • Lee JA (2009) Autophagy in neurodegeneration: two sides of the same coin. BMB Rep 42(6):324–330
    • (2009) BMB Rep , vol.42 , Issue.6 , pp. 324-330
    • Lee, J.A.1
  • 137
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • COI: 1:CAS:528:DC%2BD28XlvVGlsbY%3D, PID: 16625205
    • Komatsu M, Waguri S, Chiba T et al (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441(7095):880–884
    • (2006) Nature , vol.441 , Issue.7095 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3
  • 138
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD1cXot1OqtLk%3D, PID: 18596167
    • Boland B, Kumar A, Lee S et al (2008) Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer’s disease. J Neurosci 28(27):6926–6937. doi:10.1523/JNEUROSCI.0800-08.2008
    • (2008) J Neurosci , vol.28 , Issue.27 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3
  • 139
    • 35448938087 scopus 로고    scopus 로고
    • Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration
    • COI: 1:CAS:528:DC%2BD2sXhtVGnt7bK, PID: 17726112
    • Komatsu M, Wang QJ, Holstein GR et al (2007) Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration. Proc Natl Acad Sci U S A 104:14489–14494
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14489-14494
    • Komatsu, M.1    Wang, Q.J.2    Holstein, G.R.3
  • 140
    • 69349090907 scopus 로고    scopus 로고
    • The cellular pathways of neuronal autophagy and their implication in neurodegenerative diseases
    • COI: 1:CAS:528:DC%2BD1MXhtV2rs7fM, PID: 19339210
    • Yue Z, Friedman L, Komatsu M et al (2009) The cellular pathways of neuronal autophagy and their implication in neurodegenerative diseases. Biochim Biophys Acta 1793:1496–1507. doi:10.1016/j.bbamcr.2009.01.016
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1496-1507
    • Yue, Z.1    Friedman, L.2    Komatsu, M.3
  • 141
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy-a novel Beta-amyloid peptide-generating pathway activated in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD2MXhtFWitrjI, PID: 16203860
    • Yu WH, Cuervo AM, Kumar A et al (2005) Macroautophagy-a novel Beta-amyloid peptide-generating pathway activated in Alzheimer’s disease. J Cell Biol 171(1):87–98
    • (2005) J Cell Biol , vol.171 , Issue.1 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3
  • 142
    • 14844303381 scopus 로고    scopus 로고
    • Extensive involvement of autophagy in Alzheimer disease: an immunoelectronmicroscopy study
    • PID: 15751225
    • Nixon RA, Wegiel J, Kumar A et al (2005) Extensive involvement of autophagy in Alzheimer disease: an immunoelectronmicroscopy study. J Neuropathol Exp Neurol 64:113–122
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 113-122
    • Nixon, R.A.1    Wegiel, J.2    Kumar, A.3
  • 143
    • 4344712684 scopus 로고    scopus 로고
    • Mizushima N (2004) Methods for monitoring autophagy. Int J Biochem Cell Biol 36(12):2491–2502 Review.
    • Mizushima N (2004) Methods for monitoring autophagy. Int J Biochem Cell Biol 36(12):2491–2502 Review.
  • 144
    • 0014193561 scopus 로고
    • ‘Phagocytic’ lysosomes in chromatolytic neurones
    • COI: 1:STN:280:DyaF1c%2FgsVeisA%3D%3D, PID: 6050233
    • Dixon JS (1967) ‘Phagocytic’ lysosomes in chromatolytic neurones. Nature 215(5101):657–658
    • (1967) Nature , vol.215 , Issue.5101 , pp. 657-658
    • Dixon, J.S.1
  • 145
    • 0015514710 scopus 로고
    • A light and electron microscopic study of the cellular response to axonal injury in the superior cervical ganglion of the rat
    • COI: 1:STN:280:DyaE383gt1Omtw%3D%3D, PID: 4402334
    • Matthews MR, Raisman G (1972) A light and electron microscopic study of the cellular response to axonal injury in the superior cervical ganglion of the rat. Proc R Soc Lond B Biol Sci 181(62):43–79
    • (1972) Proc R Soc Lond B Biol Sci , vol.181 , Issue.62 , pp. 43-79
    • Matthews, M.R.1    Raisman, G.2
  • 146
    • 0021678592 scopus 로고
    • The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. II. Axons and terminals
    • COI: 1:STN:280:DyaL2M%2FotVOktA%3D%3D, PID: 6210310
    • Broadwell RD, Cataldo AM (1984) The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. II. Axons and terminals. J Comp Neurol 230(2):231–248
    • (1984) J Comp Neurol , vol.230 , Issue.2 , pp. 231-248
    • Broadwell, R.D.1    Cataldo, A.M.2
  • 147
    • 0027419879 scopus 로고
    • Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport
    • COI: 1:CAS:528:DyaK3sXitV2qsbY%3D, PID: 7682217
    • Hollenbeck PJ (1993) Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport. J Cell Biol 121(2):305–315
    • (1993) J Cell Biol , vol.121 , Issue.2 , pp. 305-315
    • Hollenbeck, P.J.1
  • 148
    • 84857858536 scopus 로고    scopus 로고
    • Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
    • COI: 1:CAS:528:DC%2BC38XjtV2hsLY%3D, PID: 22331844
    • Maday S, Wallace KE, Holzbaur EL (2012) Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons. J Cell Biol 196(4):407–417
    • (2012) J Cell Biol , vol.196 , Issue.4 , pp. 407-417
    • Maday, S.1    Wallace, K.E.2    Holzbaur, E.L.3
  • 149
    • 77953693051 scopus 로고    scopus 로고
    • Dynein- and activity-dependent retrograde transport of autophagosomes in neuronal axons
    • COI: 1:CAS:528:DC%2BC3cXpt1Wjtbw%3D, PID: 20150763
    • Katsumata K, Nishiyama J, Inoue T et al (2010) Dynein- and activity-dependent retrograde transport of autophagosomes in neuronal axons. Autophagy 6(3):378–385. doi:10.1083/jcb.201106120
    • (2010) Autophagy , vol.6 , Issue.3 , pp. 378-385
    • Katsumata, K.1    Nishiyama, J.2    Inoue, T.3
  • 150
    • 26444515364 scopus 로고    scopus 로고
    • Rubinsztein DC, DiFiglia M, Heintz N, et al. (2005) Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 1(1):11–22 Review
    • Rubinsztein DC, DiFiglia M, Heintz N, et al. (2005) Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 1(1):11–22 Review
  • 151
    • 79951531959 scopus 로고    scopus 로고
    • Akt suppresses retrograde degeneration of dopaminergic axons by inhibition of macroautophagy
    • COI: 1:CAS:528:DC%2BC3MXit1ant7w%3D, PID: 21307249
    • Cheng HC, Kim SR, Oo TF et al (2011) Akt suppresses retrograde degeneration of dopaminergic axons by inhibition of macroautophagy. J Neurosci 31(6):2125–2135. doi:10.1523/JNEUROSCI.5519-10.2011
    • (2011) J Neurosci , vol.31 , Issue.6 , pp. 2125-2135
    • Cheng, H.C.1    Kim, S.R.2    Oo, T.F.3
  • 152
    • 84856760438 scopus 로고    scopus 로고
    • Autophagy promotes survival of retinal ganglion cells after optic nerve axotomy in mice
    • COI: 1:CAS:528:DC%2BC38XislOmt7Y%3D, PID: 21701497
    • Rodriguez-Muela N, Germain F, Marino G et al (2012) Autophagy promotes survival of retinal ganglion cells after optic nerve axotomy in mice. Cell Death Differ 19(1):162–169. doi:10.1038/cdd.2011.88
    • (2012) Cell Death Differ , vol.19 , Issue.1 , pp. 162-169
    • Rodriguez-Muela, N.1    Germain, F.2    Marino, G.3
  • 153
    • 33748154216 scopus 로고    scopus 로고
    • Induction of autophagy in axonal dystrophy and degeneration
    • COI: 1:CAS:528:DC%2BD28XosVeiu74%3D, PID: 16885219
    • Wang QJ, Ding Y, Kohtz DS et al (2006) Induction of autophagy in axonal dystrophy and degeneration. J Neurosci 26(31):8057–8068
    • (2006) J Neurosci , vol.26 , Issue.31 , pp. 8057-8068
    • Wang, Q.J.1    Ding, Y.2    Kohtz, D.S.3
  • 154
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • COI: 1:CAS:528:DC%2BD28XlvVGlsbc%3D, PID: 16625204
    • Hara T, Nakamura K, Matsui M et al (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441(7095):885–889
    • (2006) Nature , vol.441 , Issue.7095 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 155
    • 59049084055 scopus 로고    scopus 로고
    • Starving neurons show sex difference in autophagy
    • COI: 1:CAS:528:DC%2BD1MXlvFeitg%3D%3D, PID: 19036730
    • Du L, Hickey RW, Bayir H et al (2009) Starving neurons show sex difference in autophagy. J Biol Chem 284(4):2383–2396. doi:10.1074/jbc.M804396200
    • (2009) J Biol Chem , vol.284 , Issue.4 , pp. 2383-2396
    • Du, L.1    Hickey, R.W.2    Bayir, H.3
  • 156
    • 77953486943 scopus 로고    scopus 로고
    • Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington’s disease
    • COI: 1:CAS:528:DC%2BC3cXlvVWkt7o%3D, PID: 20190273
    • Rose C, Menzies FM, Renna M et al (2010) Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington’s disease. Hum Mol Genet 19:2144–2153. doi:10.1093/hmg/ddq093
    • (2010) Hum Mol Genet , vol.19 , pp. 2144-2153
    • Rose, C.1    Menzies, F.M.2    Renna, M.3
  • 157
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • PID: 20174468
    • Crews L, Spencer B, Desplats P et al (2010) Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS ONE 5:e9313. doi:10.1371/journal.pone.0009313
    • (2010) PLoS ONE , vol.5 , pp. e9313
    • Crews, L.1    Spencer, B.2    Desplats, P.3
  • 158
    • 59049094829 scopus 로고    scopus 로고
    • Nutrient deprivation induces neuronal autophagy and implicates reduced insulin signaling in neuroprotective autophagy activation
    • COI: 1:CAS:528:DC%2BD1MXlvFeisA%3D%3D, PID: 19017649
    • Young JE, Martinez RA, La Spada AR (2009) Nutrient deprivation induces neuronal autophagy and implicates reduced insulin signaling in neuroprotective autophagy activation. J Biol Chem 284:2363–2373. doi:10.1074/jbc.M806088200
    • (2009) J Biol Chem , vol.284 , pp. 2363-2373
    • Young, J.E.1    Martinez, R.A.2    La Spada, A.R.3
  • 159
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • COI: 1:CAS:528:DC%2BD28XitFCjur4%3D, PID: 16505167
    • Yamamoto A, Cremona ML, Rothman JE (2006) Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J Cell Biol 172:719–731
    • (2006) J Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 160
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine expanded huntingtin and related proteinopathies
    • COI: 1:CAS:528:DC%2BD1cXhsV2it7zF, PID: 18636076
    • Sarkar S, Ravikumar B, Floto RA et al (2009) Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine expanded huntingtin and related proteinopathies. Cell Death Differ 16:46–56. doi:10.1038/cdd.2008.110
    • (2009) Cell Death Differ , vol.16 , pp. 46-56
    • Sarkar, S.1    Ravikumar, B.2    Floto, R.A.3
  • 161
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model
    • COI: 1:CAS:528:DC%2BC3cXht1Oht7fP, PID: 20833817
    • Tsvetkov AS, Miller J, Arrasate M et al (2010) A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. Proc Natl Acad Sci U S A 107:16982–16987. doi:10.1073/pnas.1004498107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1    Miller, J.2    Arrasate, M.3
  • 162
    • 37649024076 scopus 로고    scopus 로고
    • Small molecule regulators of autophagy identified by an image-based highthroughput screen
    • COI: 1:CAS:528:DC%2BD2sXhsVSru7bJ, PID: 18024584
    • Zhang L, Yu J, Pan H et al (2007) Small molecule regulators of autophagy identified by an image-based highthroughput screen. Proc Natl Acad Sci U S A 104:19023–19028
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19023-19028
    • Zhang, L.1    Yu, J.2    Pan, H.3
  • 163
    • 77954898129 scopus 로고    scopus 로고
    • A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions
    • COI: 1:CAS:528:DC%2BC3cXos1KqtLY%3D, PID: 20627085
    • Lipinski MM, Hoffman G, Ng A et al (2010) A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions. Dev Cell 18:1041–1052. doi:10.1016/j.devcel.2010.05.005
    • (2010) Dev Cell , vol.18 , pp. 1041-1052
    • Lipinski, M.M.1    Hoffman, G.2    Ng, A.3
  • 164
    • 78650687327 scopus 로고    scopus 로고
    • IGF-I stimulates Rab7-RILP interaction during neuronal autophagy
    • COI: 1:CAS:528:DC%2BC3MXhs1Gisg%3D%3D, PID: 20849920
    • Bains M, Zaegel V, Mize-Berge J et al (2011) IGF-I stimulates Rab7-RILP interaction during neuronal autophagy. Neurosci Lett 488:112–117. doi:10.1016/j.neulet.2010.09.018
    • (2011) Neurosci Lett , vol.488 , pp. 112-117
    • Bains, M.1    Zaegel, V.2    Mize-Berge, J.3
  • 165
    • 85027948203 scopus 로고    scopus 로고
    • Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3MXlsFGmu78%3D, PID: 21499257
    • Wong AS, Lee RH, Cheung AY et al (2011) Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson’s disease. Nat Cell Biol 13:568–579. doi:10.1038/ncb2217
    • (2011) Nat Cell Biol , vol.13 , pp. 568-579
    • Wong, A.S.1    Lee, R.H.2    Cheung, A.Y.3
  • 166
    • 79951720176 scopus 로고    scopus 로고
    • JNK regulates FoxO-dependent autophagy in neurons
    • COI: 1:CAS:528:DC%2BC3MXjtVait7s%3D, PID: 21325132
    • Xu P, Das M, Reilly J et al (2011) JNK regulates FoxO-dependent autophagy in neurons. Genes Dev 25:310–322. doi:10.1101/gad.1984311
    • (2011) Genes Dev , vol.25 , pp. 310-322
    • Xu, P.1    Das, M.2    Reilly, J.3
  • 167
    • 44149124887 scopus 로고    scopus 로고
    • Autophagy in neuroprotection and neurodegeneration: a question of balance
    • PID: 18806889
    • Cherra SJ, Chu CT (2008) Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurol 3:309–323
    • (2008) Future Neurol , vol.3 , pp. 309-323
    • Cherra, S.J.1    Chu, C.T.2
  • 168
    • 65549101724 scopus 로고    scopus 로고
    • HspB8 participates in protein quality control by a non-chaperone-like mechanism that requires eIF2{alpha} phosphorylation
    • COI: 1:CAS:528:DC%2BD1MXitFSntbc%3D, PID: 19114712
    • Carra S, Brunsting JF, Lambert H et al (2009) HspB8 participates in protein quality control by a non-chaperone-like mechanism that requires eIF2{alpha} phosphorylation. J Biol Chem 284(9):5523–32
    • (2009) J Biol Chem , vol.284 , Issue.9 , pp. 5523-5532
    • Carra, S.1    Brunsting, J.F.2    Lambert, H.3
  • 169
    • 33749041268 scopus 로고    scopus 로고
    • Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy
    • COI: 1:CAS:528:DC%2BD28XhtVagtbvE
    • Eskelinen EL (2006) Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy. Mol Asp Med 27:495–502
    • (2006) Mol Asp Med , vol.27 , pp. 495-502
    • Eskelinen, E.L.1
  • 170
    • 33749261091 scopus 로고    scopus 로고
    • Autophagic vacuolar myopathy
    • PID: 17027858, Review
    • Nishino I (2006) Autophagic vacuolar myopathy. Semin Pediatr Neurol 13:90–95, Review
    • (2006) Semin Pediatr Neurol , vol.13 , pp. 90-95
    • Nishino, I.1
  • 171
    • 56349126024 scopus 로고    scopus 로고
    • Protective role of autophagy in neonatal hypoxia-ischemia induced brain injury
    • COI: 1:CAS:528:DC%2BD1cXhsVCms7vJ
    • Carloni S, Buonocore G, Balduini W (2008) Protective role of autophagy in neonatal hypoxia-ischemia induced brain injury. Neurobiol Dis Dec 32(3):329–39. doi:10.1016/j.nbd.2008.07.022
    • (2008) Neurobiol Dis Dec , vol.32 , Issue.3 , pp. 329-339
    • Carloni, S.1    Buonocore, G.2    Balduini, W.3
  • 172
    • 62249157748 scopus 로고    scopus 로고
    • Autophagy is required for preconditioning by the adenosine A1 receptor-selective agonist CCPA
    • COI: 1:CAS:528:DC%2BD1MXivVSis7c%3D, PID: 19242639
    • Yitzhaki S, Huang C, Liu W et al (2009) Autophagy is required for preconditioning by the adenosine A1 receptor-selective agonist CCPA. Basic Res Cardiol 104:157–67. doi:10.1007/s00395-009-0006-6
    • (2009) Basic Res Cardiol , vol.104 , pp. 157-167
    • Yitzhaki, S.1    Huang, C.2    Liu, W.3
  • 173
    • 84890803688 scopus 로고    scopus 로고
    • Autophagy and apoptosis dysfunction in neurodegenerative disorders
    • COI: 1:CAS:528:DC%2BC3sXhvFyqsbbF, PID: 24211851
    • Ghavami S, Shojaei S, Yeganeh B et al (2014) Autophagy and apoptosis dysfunction in neurodegenerative disorders. Prog Neurobiol 112:24–49
    • (2014) Prog Neurobiol , vol.112 , pp. 24-49
    • Ghavami, S.1    Shojaei, S.2    Yeganeh, B.3
  • 174
    • 39549093998 scopus 로고    scopus 로고
    • Inhibition of autophagy prevents hippocampal pyramidal neuron death after hypoxic-ischemic injury
    • COI: 1:CAS:528:DC%2BD1cXis1aisrY%3D, PID: 18187572
    • Koike M, Shibata M, Tadakoshi M et al (2008) Inhibition of autophagy prevents hippocampal pyramidal neuron death after hypoxic-ischemic injury. Am J Pathol 172:454–469. doi:10.2353/ajpath.2008.070876
    • (2008) Am J Pathol , vol.172 , pp. 454-469
    • Koike, M.1    Shibata, M.2    Tadakoshi, M.3
  • 175
    • 67649996222 scopus 로고    scopus 로고
    • Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia
    • COI: 1:CAS:528:DC%2BD1MXosFekt70%3D, PID: 19571141
    • Lee JA, Gao FB (2009) Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRT-III in frontotemporal dementia. J Neurosci 29:8506–8511. doi:10.1523/JNEUROSCI.0924-09.2009
    • (2009) J Neurosci , vol.29 , pp. 8506-8511
    • Lee, J.A.1    Gao, F.B.2
  • 176
    • 79957663035 scopus 로고    scopus 로고
    • Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer’s-like axonal dystrophy
    • COI: 1:CAS:528:DC%2BC3MXnt1Cnsrs%3D, PID: 21613495
    • Lee S, Sato Y, Nixon RA (2011) Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer’s-like axonal dystrophy. J Neurosci 31:7817–7830. doi:10.1523/JNEUROSCI.6412-10.2011
    • (2011) J Neurosci , vol.31 , pp. 7817-7830
    • Lee, S.1    Sato, Y.2    Nixon, R.A.3
  • 177
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • COI: 1:CAS:528:DC%2BD28XhtVyktbbN, PID: 17051204
    • Rubinsztein DC (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443:780–786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 178
    • 74049124412 scopus 로고    scopus 로고
    • Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
    • COI: 1:CAS:528:DC%2BD1MXhsF2qtbrE, PID: 20008565
    • Ju JS, Fuentealba RA, Miller SE et al (2009) Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease. J Cell Biol 187:875–878. doi:10.1083/jcb.200908115
    • (2009) J Cell Biol , vol.187 , pp. 875-878
    • Ju, J.S.1    Fuentealba, R.A.2    Miller, S.E.3
  • 179
    • 58149340240 scopus 로고    scopus 로고
    • ESCRT, autophagy, and frontotemporal dementia
    • COI: 1:CAS:528:DC%2BD1MXpt1Smuw%3D%3D, PID: 19123971, Review
    • Lee JA, Gao FB (2008) ESCRT, autophagy, and frontotemporal dementia. BMB Rep 41:827–832, Review
    • (2008) BMB Rep , vol.41 , pp. 827-832
    • Lee, J.A.1    Gao, F.B.2
  • 180
    • 77954346346 scopus 로고    scopus 로고
    • The role of autophagy: what can be learned from the genetic forms of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3cXos1Ojsb0%3D, PID: 20406184
    • Pasquali L, Ruffoli R, Fulceri F et al (2010) The role of autophagy: what can be learned from the genetic forms of amyotrophic lateral sclerosis. CNS Neurol Disord Drug Targets 9:268–278
    • (2010) CNS Neurol Disord Drug Targets , vol.9 , pp. 268-278
    • Pasquali, L.1    Ruffoli, R.2    Fulceri, F.3
  • 181
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • COI: 1:CAS:528:DC%2BD1cXisFWjt78%3D, PID: 18305538
    • Mizushima N, Levine B, Cuervo AM et al (2008) Autophagy fights disease through cellular self-digestion. Nature 451:1069–1075. doi:10.1038/nature06639
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3
  • 182
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from Abeta-induced cytotoxicity
    • COI: 1:CAS:528:DC%2BD1MXnvVyrsLg%3D, PID: 19270530
    • Hung SY, Huang WP, Liou HC et al (2009) Autophagy protects neuron from Abeta-induced cytotoxicity. Autophagy 5:502–510
    • (2009) Autophagy , vol.5 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3
  • 183
    • 77957335213 scopus 로고    scopus 로고
    • Amyloid-beta1-42 induces reactive oxygen species-mediated autophagic cell death in U87 and SH-SY5Y cells
    • COI: 1:CAS:528:DC%2BC3cXhtVKiurnK, PID: 20571221
    • Wang H, Ma J, Tan Y et al (2010) Amyloid-beta1-42 induces reactive oxygen species-mediated autophagic cell death in U87 and SH-SY5Y cells. J Alzheimers Dis 21:597–610. doi:10.3233/JAD-2010-091207
    • (2010) J Alzheimers Dis , vol.21 , pp. 597-610
    • Wang, H.1    Ma, J.2    Tan, Y.3
  • 184
    • 78549273390 scopus 로고    scopus 로고
    • Macroautophagy is not directly involved in the metabolism of amyloid precursor protein
    • COI: 1:CAS:528:DC%2BC3cXhsVCrt77F, PID: 20864542
    • Boland B, Smith DA, Mooney D et al (2010) Macroautophagy is not directly involved in the metabolism of amyloid precursor protein. J Biol Chem 285:37415–37426. doi:10.1074/jbc.M110.186411
    • (2010) J Biol Chem , vol.285 , pp. 37415-37426
    • Boland, B.1    Smith, D.A.2    Mooney, D.3
  • 185
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer’s disease. Annu Rev Neurosci 34:185–204. doi:10.1146/annurev-neuro-061010-113613
    • O’Brien RJ, Wong PC (2011) Amyloid precursor protein processing and Alzheimer’s disease. Annu Rev Neurosci 34:185–204. doi:10.1146/annurev-neuro-061010-113613, Review
    • (2011) Review
    • O’Brien, R.J.1    Wong, P.C.2
  • 186
    • 84860919373 scopus 로고    scopus 로고
    • Membrane trafficking pathways in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC38XoslCltrY%3D, PID: 22269004
    • Rajendran L, Annaert W (2012) Membrane trafficking pathways in Alzheimer’s disease. Traffic 13:759–770. doi:10.1111/j.1600-0854.2012.01332.x
    • (2012) Traffic , vol.13 , pp. 759-770
    • Rajendran, L.1    Annaert, W.2
  • 187
    • 45749114895 scopus 로고    scopus 로고
    • The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice
    • COI: 1:CAS:528:DC%2BD1cXntVCmuro%3D, PID: 18497889
    • Pickford F, Masliah E, Britschgi M et al (2008) The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J Clin Invest 118:2190–2199. doi:10.1172/JCI33585
    • (2008) J Clin Invest , vol.118 , pp. 2190-2199
    • Pickford, F.1    Masliah, E.2    Britschgi, M.3
  • 188
    • 77956215864 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein processing by the Beclin 1 complex
    • PID: 20559548
    • Jaeger PA, Pickford F, Sun CH et al (2010) Regulation of amyloid precursor protein processing by the Beclin 1 complex. PLoS ONE 5:e11102. doi:10.1371/journal.pone.0011102
    • (2010) PLoS ONE , vol.5 , pp. e11102
    • Jaeger, P.A.1    Pickford, F.2    Sun, C.H.3
  • 189
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson’s and Lewy body diseases
    • COI: 1:CAS:528:DC%2BD1MXhsVSmtrbF, PID: 19864570
    • Spencer B, Potkar R, Trejo M et al (2009) Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson’s and Lewy body diseases. J Neurosci 29:13578–13588. doi:10.1523/JNEUROSCI.4390-09.2009
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3
  • 190
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer related PS1 mutations
    • COI: 1:CAS:528:DC%2BC3cXovFartbs%3D, PID: 20541250
    • Lee JH, Yu WH, Kumar A et al (2010) Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer related PS1 mutations. Cell 141:1146–1158. doi:10.1016/j.cell.2010.05.008
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1    Yu, W.H.2    Kumar, A.3
  • 191
    • 31544454404 scopus 로고    scopus 로고
    • Rapamycin alleviates toxicity of different aggregate-prone proteins
    • COI: 1:CAS:528:DC%2BD28XmsFOhug%3D%3D, PID: 16368705
    • Berger Z, Ravikumar B, Menzies FM et al (2006) Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum Mol Genet 15:433–442
    • (2006) Hum Mol Genet , vol.15 , pp. 433-442
    • Berger, Z.1    Ravikumar, B.2    Menzies, F.M.3
  • 192
    • 70349987102 scopus 로고    scopus 로고
    • Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
    • COI: 1:CAS:528:DC%2BD1MXht1CrtrrI, PID: 19654187
    • Wang Y, Martinez-Vicente M, Kruger U et al (2009) Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum Mol Genet 18:4153–4170
    • (2009) Hum Mol Genet , vol.18 , pp. 4153-4170
    • Wang, Y.1    Martinez-Vicente, M.2    Kruger, U.3
  • 193
    • 77951227122 scopus 로고    scopus 로고
    • Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: effects on cognitive impairments
    • COI: 1:CAS:528:DC%2BC3cXkvVGisLw%3D, PID: 20178983
    • Caccamo A, Majumder S, Richardson A et al (2010) Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: effects on cognitive impairments. J Biol Chem 285:13107–13120. doi:10.1093/hmg/ddp367
    • (2010) J Biol Chem , vol.285 , pp. 13107-13120
    • Caccamo, A.1    Majumder, S.2    Richardson, A.3
  • 194
    • 77954955573 scopus 로고    scopus 로고
    • Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation
    • COI: 1:CAS:528:DC%2BC3cXpt12nu7g%3D, PID: 20546895
    • Rodriguez-Navarro JA, Rodriguez L, Casarejos MJ et al (2010) Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation. Neurobiol Dis 39:423–438. doi:10.1016/j.nbd.2010.05.014
    • (2010) Neurobiol Dis , vol.39 , pp. 423-438
    • Rodriguez-Navarro, J.A.1    Rodriguez, L.2    Casarejos, M.J.3
  • 195
    • 80053243942 scopus 로고    scopus 로고
    • Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits
    • COI: 1:CAS:528:DC%2BC3MXhtlCjsLzO, PID: 21980451
    • Majumder S, Richardson A, Strong R et al (2011) Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits. PLoS ONE 6:e25416. doi:10.1371/journal.pone.0025416
    • (2011) PLoS ONE , vol.6 , pp. e25416
    • Majumder, S.1    Richardson, A.2    Strong, R.3
  • 196
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • PID: 22689910
    • Schaeffer V, Lavenir I, Ozcelik S et al (2012) Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy. Brain 135:2169–2177. doi:10.1093/brain/aws143
    • (2012) Brain , vol.135 , pp. 2169-2177
    • Schaeffer, V.1    Lavenir, I.2    Ozcelik, S.3
  • 197
    • 77649337122 scopus 로고    scopus 로고
    • HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy
    • COI: 1:CAS:528:DC%2BC3cXhvFGisg%3D%3D, PID: 20075865
    • Lee JY, Koga H, Kawaguchi Y et al (2010) HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy. EMBO J 29:969–980. doi:10.1038/emboj.2009.405
    • (2010) EMBO J , vol.29 , pp. 969-980
    • Lee, J.Y.1    Koga, H.2    Kawaguchi, Y.3
  • 198
    • 0031837533 scopus 로고    scopus 로고
    • Huntington disease
    • COI: 1:STN:280:DyaK1c3lsFyntQ%3D%3D, PID: 9596408, Review
    • Vonsattel JP, DiFiglia M (1998) Huntington disease. J Neuropathol Exp Neurol 57:369–384, Review
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 369-384
    • Vonsattel, J.P.1    DiFiglia, M.2
  • 199
    • 80054792814 scopus 로고    scopus 로고
    • Huntington’s disease
    • PID: 21441583
    • Finkbeiner S (2011) Huntington’s disease. Cold Spring Harb Perspect Biol 3(6):a007476. doi:10.1101/cshperspect.a007476
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , Issue.6 , pp. a007476
    • Finkbeiner, S.1
  • 200
    • 0016148336 scopus 로고
    • Studies on brain biopsies of patients with Huntington’s chorea
    • COI: 1:STN:280:DyaE2c7ktlKgsA%3D%3D, PID: 4150800
    • Tellez-Nagel I, Johnson AB, Terry RD (1974) Studies on brain biopsies of patients with Huntington’s chorea. J Neuropathol Exp Neurol 33:308–332
    • (1974) J Neuropathol Exp Neurol , vol.33 , pp. 308-332
    • Tellez-Nagel, I.1    Johnson, A.B.2    Terry, R.D.3
  • 201
    • 69949180640 scopus 로고    scopus 로고
    • TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease
    • COI: 1:CAS:528:DC%2BD1MXhtFehsLbI, PID: 19720874
    • Wang T, Lao U, Edgar BA (2009) TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease. J Cell Biol 186:703–711. doi:10.1083/jcb.200904090
    • (2009) J Cell Biol , vol.186 , pp. 703-711
    • Wang, T.1    Lao, U.2    Edgar, B.A.3
  • 202
    • 49349090155 scopus 로고    scopus 로고
    • Huntington’s disease: degradation of mutant huntingtin by autophagy
    • COI: 1:CAS:528:DC%2BD1cXhtFCqtr3M, PID: 18637946
    • Sarkar S, Rubinsztein DC (2008) Huntington’s disease: degradation of mutant huntingtin by autophagy. Febs J 275:4263–4270
    • (2008) Febs J , vol.275 , pp. 4263-4270
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 203
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
    • COI: 1:CAS:528:DC%2BC3cXksFarsr4%3D, PID: 20383138
    • Martinez-Vicente M, Talloczy Z, Wong E et al (2010) Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease. Nat Neurosci 13:567–576. doi:10.1038/nn.2528
    • (2010) Nat Neurosci , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1    Talloczy, Z.2    Wong, E.3
  • 204
    • 77955291545 scopus 로고    scopus 로고
    • Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments
    • COI: 1:CAS:528:DC%2BC3cXms1Okt78%3D, PID: 20354076
    • Li X, Wang CE, Huang S et al (2010) Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments. Hum Mol Genet 19:2445–2455. doi:10.1093/hmg/ddq127
    • (2010) Hum Mol Genet , vol.19 , pp. 2445-2455
    • Li, X.1    Wang, C.E.2    Huang, S.3
  • 205
    • 77649219699 scopus 로고    scopus 로고
    • Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice
    • PID: 20140187
    • Zheng S, Clabough EB, Sarkar S et al (2010) Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice. PLoS Genet 6:e1000838. doi:10.1371/journal.pgen.1000838
    • (2010) PLoS Genet , vol.6 , pp. e1000838
    • Zheng, S.1    Clabough, E.B.2    Sarkar, S.3
  • 206
    • 38049053467 scopus 로고    scopus 로고
    • A stress sensitive ER membrane association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy
    • PID: 17986868
    • Atwal RS, Truant R (2008) A stress sensitive ER membrane association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy 4:91–93
    • (2008) Autophagy , vol.4 , pp. 91-93
    • Atwal, R.S.1    Truant, R.2
  • 207
    • 31544454404 scopus 로고    scopus 로고
    • Rapamycin alleviates toxicity of different aggregate-prone proteins
    • COI: 1:CAS:528:DC%2BD28XmsFOhug%3D%3D, PID: 16368705
    • Berger Z, Ravikumar B, Menzies FM et al (2006) Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum Mol Genet 15:433–442. doi:10.1093/hmg/ddi458
    • (2006) Hum Mol Genet , vol.15 , pp. 433-442
    • Berger, Z.1    Ravikumar, B.2    Menzies, F.M.3
  • 208
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington’s disease in an mTOR-independent autophagy pathway
    • COI: 1:CAS:528:DC%2BD1cXkvVSmt7c%3D, PID: 18391949
    • Williams A, Sarkar S, Cuddon P et al (2008) Novel targets for Huntington’s disease in an mTOR-independent autophagy pathway. Nat Chem Biol 4:295–305
    • (2008) Nat Chem Biol , vol.4 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3
  • 209
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model
    • COI: 1:CAS:528:DC%2BC3cXht1Oht7fP, PID: 20833817
    • Tsvetkov AS, Miller J, Arrasate M et al (2010) A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. Proc Natl Acad Sci U S A 107:16982–16987
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1    Miller, J.2    Arrasate, M.3
  • 210
    • 77953486943 scopus 로고    scopus 로고
    • Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington’s disease
    • COI: 1:CAS:528:DC%2BC3cXlvVWkt7o%3D, PID: 20190273
    • Rose C, Menzies FM, Renna M et al (2010) Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington’s disease. Hum Mol Genet 19:2144–2153
    • (2010) Hum Mol Genet , vol.19 , pp. 2144-2153
    • Rose, C.1    Menzies, F.M.2    Renna, M.3
  • 211
    • 69249122087 scopus 로고    scopus 로고
    • Autophagy activation and enhanced mitophagy characterize the Purkinje cells of pcd mice prior to neuronal death
    • Chakrabarti L, Eng J, Ivanov N et al (2009) Autophagy activation and enhanced mitophagy characterize the Purkinje cells of pcd mice prior to neuronal death. Mol Brain 2:2410
    • (2009) Mol Brain , vol.2 , pp. 2410
    • Chakrabarti, L.1    Eng, J.2    Ivanov, N.3
  • 212
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson’s disease
    • COI: 1:CAS:528:DyaK2sXitlOmtro%3D, PID: 9046040
    • Anglade P, Vyas S, Javoy-Agid F et al (1997) Apoptosis and autophagy in nigral neurons of patients with Parkinson’s disease. Histol Histopathol 12:25–31
    • (1997) Histol Histopathol , vol.12 , pp. 25-31
    • Anglade, P.1    Vyas, S.2    Javoy-Agid, F.3
  • 213
    • 0041589248 scopus 로고    scopus 로고
    • Alpha-Synuclein is degraded by both autophagy and the proteasome
    • COI: 1:CAS:528:DC%2BD3sXltVSlsbs%3D, PID: 12719433
    • Webb JL, Ravikumar B, Atkins J et al (2003) Alpha-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 278:25009–25013
    • (2003) J Biol Chem , vol.278 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3
  • 214
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • COI: 1:CAS:528:DC%2BD2cXmvFCit7w%3D, PID: 15333840
    • Cuervo AM, Stefanis L, Fredenburg R et al (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305:1292–1295
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3
  • 215
    • 77954104112 scopus 로고    scopus 로고
    • Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update
    • COI: 1:CAS:528:DC%2BC3cXpslagtL8%3D, PID: 20506312
    • Nuytemans K, Theuns J, Cruts M et al (2010) Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update. Hum Mutat 31:763–780
    • (2010) Hum Mutat , vol.31 , pp. 763-780
    • Nuytemans, K.1    Theuns, J.2    Cruts, M.3
  • 216
    • 74249091150 scopus 로고    scopus 로고
    • The role of autophagy on the survival of dopamine neurons
    • COI: 1:CAS:528:DC%2BD1MXhsVSmt7rK, PID: 19754403
    • Isidoro C, Biagioni F, Giorgi FS et al (2009) The role of autophagy on the survival of dopamine neurons. Curr Top Med Chem 9:869–879
    • (2009) Curr Top Med Chem , vol.9 , pp. 869-879
    • Isidoro, C.1    Biagioni, F.2    Giorgi, F.S.3
  • 217
    • 77957189194 scopus 로고    scopus 로고
    • Alpha-synuclein impairs macroautophagy: implications for Parkinson’s disease
    • Winslow AR, Chen CW, Corrochano S et al (2011) Alpha-synuclein impairs macroautophagy: implications for Parkinson’s disease. J Cell Biol 190:1023–1037. doi:10.1083/jcb.201003122
    • (2011) J Cell Biol , vol.190 , pp. 1023-1037
    • Winslow, A.R.1    Chen, C.W.2    Corrochano, S.3
  • 218
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • PID: 19436756
    • Xilouri M, Vogiatzi T, Vekrellis K et al (2009) Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 4:e5515. doi:10.1371/journal.pone.0005515
    • (2009) PLoS ONE , vol.4 , pp. e5515
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3
  • 219
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • COI: 1:CAS:528:DC%2BD1cXhsVOjtrjJ, PID: 19029340
    • Narendra D, Tanaka A, Suen DF et al (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183:795–803. doi:10.1083/jcb.200809125
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3
  • 220
    • 75949098487 scopus 로고    scopus 로고
    • PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
    • COI: 1:CAS:528:DC%2BC3cXnsFCruw%3D%3D, PID: 19966284
    • Vives-Bauza C, Zhou C, Huang Y et al (2010) PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proc Natl Acad Sci U S A 107:378–383. doi:10.1073/pnas.0911187107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 378-383
    • Vives-Bauza, C.1    Zhou, C.2    Huang, Y.3
  • 221
    • 77952242572 scopus 로고    scopus 로고
    • The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy
    • COI: 1:CAS:528:DC%2BC3cXlslyhu7k%3D, PID: 20057503
    • Michiorri S, Gelmetti V, Giarda E et al (2010) The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy. Cell Death Differ 17:962–974. doi:10.1038/cdd.2009.200
    • (2010) Cell Death Differ , vol.17 , pp. 962-974
    • Michiorri, S.1    Gelmetti, V.2    Giarda, E.3
  • 222
    • 79956048660 scopus 로고    scopus 로고
    • Parkin mediates Beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models
    • COI: 1:CAS:528:DC%2BC3MXmtVyqt7c%3D, PID: 21378096
    • Khandelwal PJ, Herman AM, Hoe HS et al (2011) Parkin mediates Beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models. Hum Mol Genet 20:2091–2102
    • (2011) Hum Mol Genet , vol.20 , pp. 2091-2102
    • Khandelwal, P.J.1    Herman, A.M.2    Hoe, H.S.3
  • 223
    • 0035894855 scopus 로고    scopus 로고
    • 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
    • COI: 1:CAS:528:DC%2BD38XivV2i, PID: 11739566
    • Stefanis L, Larsen KE, Rideout HJ 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. J Neurosci 21:9549–9560
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3
  • 224
    • 79953202481 scopus 로고    scopus 로고
    • Mutant A53T (alpha)-synuclein induces neuronal death by increasing mitochondrial autophagy
    • COI: 1:CAS:528:DC%2BC3MXjsVyqsbs%3D, PID: 21252228
    • Choubey V, Safiulina D, Vaarmann A et al (2011) Mutant A53T (alpha)-synuclein induces neuronal death by increasing mitochondrial autophagy. J Biol Chem 286:10814–10824. doi:10.1074/jbc.M110.132514
    • (2011) J Biol Chem , vol.286 , pp. 10814-10824
    • Choubey, V.1    Safiulina, D.2    Vaarmann, A.3
  • 225
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • COI: 1:CAS:528:DC%2BD2sXhsV2gtbc%3D, PID: 17200184
    • Zhu JH, Horbinski C, Guo F et al (2007) Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 170:75–86
    • (2007) Am J Pathol , vol.170 , pp. 75-86
    • Zhu, J.H.1    Horbinski, C.2    Guo, F.3
  • 226
    • 72849127046 scopus 로고    scopus 로고
    • A novel mTOR activating protein protects dopamine neurons against oxidative stress by repressing autophagy related cell death
    • COI: 1:CAS:528:DC%2BC3cXhtVGju78%3D, PID: 19878437
    • Choi KC, Kim SH, Ha JY et al (2010) A novel mTOR activating protein protects dopamine neurons against oxidative stress by repressing autophagy related cell death. J Neurochem 112:366–376. doi:10.1111/j.1471-4159.2009.06463.x
    • (2010) J Neurochem , vol.112 , pp. 366-376
    • Choi, K.C.1    Kim, S.H.2    Ha, J.Y.3
  • 227
    • 84866610524 scopus 로고    scopus 로고
    • Lysosome-dependent pathways as a unifying theme in Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3sXhs1aktbo%3D, PID: 22927213
    • Tofaris GK (2012) Lysosome-dependent pathways as a unifying theme in Parkinson’s disease. Mov Disord 27:1364–1369. doi:10.1002/mds.25136
    • (2012) Mov Disord , vol.27 , pp. 1364-1369
    • Tofaris, G.K.1
  • 228
    • 84880756245 scopus 로고    scopus 로고
    • Defective autophagy in Parkinson’s disease: role of oxidative stress
    • COI: 1:CAS:528:DC%2BC38Xhs1Gqsb%2FP, PID: 22899187
    • Janda E, Isidoro C, Carresi C et al (2012) Defective autophagy in Parkinson’s disease: role of oxidative stress. Mol Neurobiol 46:639–661. doi:10.1007/s12035-012-8318-1
    • (2012) Mol Neurobiol , vol.46 , pp. 639-661
    • Janda, E.1    Isidoro, C.2    Carresi, C.3
  • 229
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: what do we really know?
    • COI: 1:CAS:528:DC%2BC3MXhsVahur3I, PID: 21989245
    • Andersen PM, Al-Chalabi A (2011) Clinical genetics of amyotrophic lateral sclerosis: what do we really know? Nat Rev Neurol 7(11):603–615. doi:10.1038/nrneurol.2011.150
    • (2011) Nat Rev Neurol , vol.7 , Issue.11 , pp. 603-615
    • Andersen, P.M.1    Al-Chalabi, A.2
  • 230
    • 80755128213 scopus 로고    scopus 로고
    • Clinical diagnosis and management of amyotrophic lateral sclerosis
    • COI: 1:CAS:528:DC%2BC3MXhsVahur3M, PID: 21989247
    • Hardiman O, van den Berg LH, Kiernan MC (2011) Clinical diagnosis and management of amyotrophic lateral sclerosis. Nat Rev Neurol 7(11):639–649
    • (2011) Nat Rev Neurol , vol.7 , Issue.11 , pp. 639-649
    • Hardiman, O.1    van den Berg, L.H.2    Kiernan, M.C.3
  • 231
    • 79955522014 scopus 로고    scopus 로고
    • Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis
    • PID: 21487309
    • Sasaki S (2011) Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 70(5):349–359. doi:10.1038/nrneurol.2011.153
    • (2011) J Neuropathol Exp Neurol , vol.70 , Issue.5 , pp. 349-359
    • Sasaki, S.1
  • 232
    • 41449113885 scopus 로고    scopus 로고
    • Altered macroautophagy in the spinal cord of SOD1 mutant mice
    • COI: 1:CAS:528:DC%2BD1cXltVKnt7k%3D, PID: 18196963
    • Li L, Zhang X, Le W (2008) Altered macroautophagy in the spinal cord of SOD1 mutant mice. Autophagy 4:290–293
    • (2008) Autophagy , vol.4 , pp. 290-293
    • Li, L.1    Zhang, X.2    Le, W.3
  • 233
    • 34548125010 scopus 로고    scopus 로고
    • Increased autophagy in transgenic mice with a G93A mutant SOD1 gene
    • COI: 1:CAS:528:DC%2BD2sXpvFKhtrw%3D, PID: 17689501
    • Morimoto N, Nagai M, Ohta Y et al (2007) Increased autophagy in transgenic mice with a G93A mutant SOD1 gene. Brain Res 1167:112–117
    • (2007) Brain Res , vol.1167 , pp. 112-117
    • Morimoto, N.1    Nagai, M.2    Ohta, Y.3
  • 234
    • 77955365630 scopus 로고    scopus 로고
    • The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)
    • COI: 1:CAS:528:DC%2BC3cXpvVGqu7Y%3D, PID: 20570967
    • Crippa V et al (2010) The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet 19:3440–3456
    • (2010) Hum Mol Genet , vol.19 , pp. 3440-3456
    • Crippa, V.1
  • 235
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • COI: 1:CAS:528:DC%2BD1MXht12qtbfP, PID: 19762508
    • Hetz C et al (2009) XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev 23:2294–2306
    • (2009) Genes Dev , vol.23 , pp. 2294-2306
    • Hetz, C.1
  • 236
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • COI: 1:CAS:528:DC%2BD2sXht12jsbzO, PID: 17984323
    • Filimonenko M, Stuffers S, Raiborg C et al (2007) Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J Cell Biol 179:485–500
    • (2007) J Cell Biol , vol.179 , pp. 485-500
    • Filimonenko, M.1    Stuffers, S.2    Raiborg, C.3
  • 237
    • 78649941297 scopus 로고    scopus 로고
    • Exome sequencing reveals VCP mutations as a cause of familial ALS
    • COI: 1:CAS:528:DC%2BC3cXhsFGhu73J, PID: 21145000
    • Johnson JO, Mandrioli J, Benatar M et al (2010) Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron 68:857–64. doi:10.1016/j.neuron.2010.11.036
    • (2010) Neuron , vol.68 , pp. 857-864
    • Johnson, J.O.1    Mandrioli, J.2    Benatar, M.3
  • 238
    • 0034849783 scopus 로고    scopus 로고
    • Autophagic cell death and its execution by lysosomal cathepsins
    • COI: 1:STN:280:DC%2BD3MrivFGksA%3D%3D, PID: 11575420
    • Uchiyama Y (2001) Autophagic cell death and its execution by lysosomal cathepsins. Arch Histol Cytol 64:233–246
    • (2001) Arch Histol Cytol , vol.64 , pp. 233-246
    • Uchiyama, Y.1
  • 239
    • 41049092706 scopus 로고    scopus 로고
    • Autophagic neuron death in neonatal brain ischemia/hypoxia
    • COI: 1:CAS:528:DC%2BD1cXntFyntLk%3D, PID: 18212531
    • Uchiyama Y, Koike M, Shibata M (2008) Autophagic neuron death in neonatal brain ischemia/hypoxia. Autophagy 4:404–408
    • (2008) Autophagy , vol.4 , pp. 404-408
    • Uchiyama, Y.1    Koike, M.2    Shibata, M.3
  • 240
    • 50249189191 scopus 로고    scopus 로고
    • Neuronal injury in rat model of permanent focal cerebral ischemia is associated with activation of autophagic and lysosomal pathways
    • COI: 1:CAS:528:DC%2BD1cXhtVynt7jE, PID: 18567942
    • Wen YD, Sheng R, Zhang LS et al (2008) Neuronal injury in rat model of permanent focal cerebral ischemia is associated with activation of autophagic and lysosomal pathways. Autophagy 4:762–769
    • (2008) Autophagy , vol.4 , pp. 762-769
    • Wen, Y.D.1    Sheng, R.2    Zhang, L.S.3
  • 241
    • 79953221421 scopus 로고    scopus 로고
    • Severe global cerebral ischemia-induced programmed necrosis of hippocampal CA1 neurons in rat is prevented by 3-methyladenine: a widely used inhibitor of autophagy
    • COI: 1:CAS:528:DC%2BC3MXjslKrt7o%3D, PID: 21412169
    • Wang JY, Xia Q, Chu KT et al (2011) Severe global cerebral ischemia-induced programmed necrosis of hippocampal CA1 neurons in rat is prevented by 3-methyladenine: a widely used inhibitor of autophagy. J Neuropathol Exp Neurol 70:314–322. doi:10.1097/NEN.0b013e31821352bd
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 314-322
    • Wang, J.Y.1    Xia, Q.2    Chu, K.T.3
  • 242
    • 82855169507 scopus 로고    scopus 로고
    • Accumulation of p62 in degenerated spinal cord under chronic mechanical compression: functional analysis of p62 and autophagy in hypoxic neuronal cells
    • COI: 1:CAS:528:DC%2BC38Xks1ygsrY%3D, PID: 22082874
    • Tanabe F, Yone K, Kawabata N et al (2011) Accumulation of p62 in degenerated spinal cord under chronic mechanical compression: functional analysis of p62 and autophagy in hypoxic neuronal cells. Autophagy 7:1462–1471
    • (2011) Autophagy , vol.7 , pp. 1462-1471
    • Tanabe, F.1    Yone, K.2    Kawabata, N.3
  • 243
    • 84863012215 scopus 로고    scopus 로고
    • Induction of autophagy contributes to the neuroprotection of nicotinamide phosphoribosyltransferase in cerebral ischemia
    • COI: 1:CAS:528:DC%2BC38XlsVWnt7c%3D, PID: 22113203
    • Wang P, Guan YF, Du H et al (2012) Induction of autophagy contributes to the neuroprotection of nicotinamide phosphoribosyltransferase in cerebral ischemia. Autophagy 8:77–87. doi:10.4161/auto.8.1.18274
    • (2012) Autophagy , vol.8 , pp. 77-87
    • Wang, P.1    Guan, Y.F.2    Du, H.3
  • 244
    • 0036236006 scopus 로고    scopus 로고
    • The mitochondrial-lysosomal axis theory of aging: accumulation of damaged mitochondria as a result of imperfect autophagocytosis
    • COI: 1:CAS:528:DC%2BD38XjsFWlt7w%3D, PID: 11985575
    • Brunk UT, Terman A (2002) The mitochondrial-lysosomal axis theory of aging: accumulation of damaged mitochondria as a result of imperfect autophagocytosis. Eur J Biochem 269:1996–2002
    • (2002) Eur J Biochem , vol.269 , pp. 1996-2002
    • Brunk, U.T.1    Terman, A.2
  • 245
    • 77956562189 scopus 로고    scopus 로고
    • Autophagy and protein aggregation after brain ischemia
    • COI: 1:CAS:528:DC%2BC3cXht1ejurrF, PID: 20633207
    • Liu C, Gao Y, Barrett J et al (2010) Autophagy and protein aggregation after brain ischemia. J Neurochem 115(1):68–78. doi:10.1111/j.1471-4159.2010.06905.x
    • (2010) J Neurochem , vol.115 , Issue.1 , pp. 68-78
    • Liu, C.1    Gao, Y.2    Barrett, J.3
  • 246
    • 77955887349 scopus 로고    scopus 로고
    • Autophagy was activated in injured astrocytes and mildly decreased cell survival following glucose and oxygen deprivation and focal cerebral ischemia
    • COI: 1:CAS:528:DC%2BC3cXhtFCqsrrN, PID: 20574158
    • Qin AP, Liu CF, Qin YY et al (2010) Autophagy was activated in injured astrocytes and mildly decreased cell survival following glucose and oxygen deprivation and focal cerebral ischemia. Autophagy 6(6):738–753
    • (2010) Autophagy , vol.6 , Issue.6 , pp. 738-753
    • Qin, A.P.1    Liu, C.F.2    Qin, Y.Y.3
  • 247
    • 84859622499 scopus 로고    scopus 로고
    • Propofol prevents autophagic cell death following oxygen and glucose deprivation in PC12 cells and cerebral ischemia-reperfusion injury in rats
    • COI: 1:CAS:528:DC%2BC38XmtVOlsr0%3D, PID: 22509406
    • Cui D, Wang L, Qi A et al (2012) Propofol prevents autophagic cell death following oxygen and glucose deprivation in PC12 cells and cerebral ischemia-reperfusion injury in rats. PLoS ONE 7(4):e35324
    • (2012) PLoS ONE , vol.7 , Issue.4 , pp. e35324
    • Cui, D.1    Wang, L.2    Qi, A.3
  • 248
    • 84866992233 scopus 로고    scopus 로고
    • Inhibition of autophagy contributes to ischemic postconditioning-induced neuroprotection against focal cerebral ischemia in rats
    • COI: 1:CAS:528:DC%2BC38XhsFShs7fJ, PID: 23029398
    • Gao L, Jiang T, Guo J et al (2012) Inhibition of autophagy contributes to ischemic postconditioning-induced neuroprotection against focal cerebral ischemia in rats. PLoS One 7(9):e46092. doi:10.1371/journal.pone.0046092
    • (2012) PLoS One , vol.7 , Issue.9 , pp. e46092
    • Gao, L.1    Jiang, T.2    Guo, J.3
  • 249
    • 79953221421 scopus 로고    scopus 로고
    • Severe global cerebral ischemia-induced programmed necrosis of hippocampal CA1 neurons in rat is prevented by 3-methyladenine: a widely used inhibitor of autophagy
    • COI: 1:CAS:528:DC%2BC3MXjslKrt7o%3D, PID: 21412169
    • Wang JY, Xia Q, Chu KT et al (2011) Severe global cerebral ischemia-induced programmed necrosis of hippocampal CA1 neurons in rat is prevented by 3-methyladenine: a widely used inhibitor of autophagy. J Neuropathol Exp Neurol 70:314–322
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 314-322
    • Wang, J.Y.1    Xia, Q.2    Chu, K.T.3
  • 250
    • 77953699438 scopus 로고    scopus 로고
    • Autophagy activation is associated with neuroprotection in a rat model of focal cerebral ischemic preconditioning
    • COI: 1:CAS:528:DC%2BC3cXpvFWitL0%3D, PID: 20400854
    • Sheng R, Zhang LS, Han R et al (2010) Autophagy activation is associated with neuroprotection in a rat model of focal cerebral ischemic preconditioning. Autophagy 6:482–494
    • (2010) Autophagy , vol.6 , pp. 482-494
    • Sheng, R.1    Zhang, L.S.2    Han, R.3
  • 251
    • 13544277142 scopus 로고    scopus 로고
    • The influence of age on apoptotic and other mechanisms of cell death after cerebral hypoxia-ischemia
    • Zhu C, Wang X, Xu F et al (2004) The influence of age on apoptotic and other mechanisms of cell death after cerebral hypoxia-ischemia. Cell Death Differ 12:162–176
    • (2004) Cell Death Differ , vol.12 , pp. 162-176
    • Zhu, C.1    Wang, X.2    Xu, F.3
  • 252
    • 0038060334 scopus 로고    scopus 로고
    • Ischemic tolerance and endogenous neuroprotection
    • COI: 1:CAS:528:DC%2BD3sXjs1Wks7g%3D, PID: 12744841
    • Dirnagl U, Simon RP, Hallenbeck JM (2003) Ischemic tolerance and endogenous neuroprotection. Trends Neurosci 26:248–254
    • (2003) Trends Neurosci , vol.26 , pp. 248-254
    • Dirnagl, U.1    Simon, R.P.2    Hallenbeck, J.M.3
  • 253
    • 79551532458 scopus 로고    scopus 로고
    • Autophagy aids membrane expansion by neuropathic Schwann cells
    • PID: 21135575
    • Rangaraju S, Notterpek L (2011) Autophagy aids membrane expansion by neuropathic Schwann cells. Autophagy 7:238–239
    • (2011) Autophagy , vol.7 , pp. 238-239
    • Rangaraju, S.1    Notterpek, L.2
  • 254
    • 62149126997 scopus 로고    scopus 로고
    • Intermittent fasting alleviates the neuropathic phenotype in a mouse model of Charcot-Marie-Tooth disease
    • COI: 1:CAS:528:DC%2BD1MXjsVOgu7w%3D, PID: 19320048
    • Madorsky I, Opalach K, Waber A et al (2009) Intermittent fasting alleviates the neuropathic phenotype in a mouse model of Charcot-Marie-Tooth disease. Neurobiol Dis 34:146–154
    • (2009) Neurobiol Dis , vol.34 , pp. 146-154
    • Madorsky, I.1    Opalach, K.2    Waber, A.3
  • 255
    • 84877144774 scopus 로고    scopus 로고
    • Autophagy promotes oligodendrocyte survival and function following dysmyelination in a long-lived myelin mutant
    • Smith CM, Mayer JA, Duncan ID (2013) Autophagy promotes oligodendrocyte survival and function following dysmyelination in a long-lived myelin mutant. J Neurosci 33nn:8088–8100. doi:10.1523/JNEUROSCI.0233-13.2013
    • (2013) J Neurosci , vol.33nn , pp. 8088-8100
    • Smith, C.M.1    Mayer, J.A.2    Duncan, I.D.3
  • 256
    • 33747816491 scopus 로고    scopus 로고
    • Glia-specific activation of all pathways of the unfolded protein response in vanishing white matter disease
    • PID: 16825957
    • van Kollenburg B, van Dijk J et al (2006) Glia-specific activation of all pathways of the unfolded protein response in vanishing white matter disease. J Neuropathol Exp Neurol 65:707–715
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 707-715
    • van Kollenburg, B.1    van Dijk, J.2
  • 257
    • 64849083774 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response as a potential therapeutic target in multiple sclerosis
    • PID: 20357912
    • Getts MT, Getts DR, Kohm AP et al (2008) Endoplasmic reticulum stress response as a potential therapeutic target in multiple sclerosis. Therapy 5:631–640
    • (2008) Therapy , vol.5 , pp. 631-640
    • Getts, M.T.1    Getts, D.R.2    Kohm, A.P.3
  • 258
    • 36749104299 scopus 로고    scopus 로고
    • A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease
    • COI: 1:CAS:528:DC%2BD2sXht12lurfI, PID: 17962415
    • Dhaunchak AS, Nave KA (2007) A common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease. Proc Natl Acad Sci U S A 104:17813–17818
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17813-17818
    • Dhaunchak, A.S.1    Nave, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.