메뉴 건너뛰기




Volumn 52, Issue 3, 2015, Pages 1284-1296

Crosstalk Between Macroautophagy and Chaperone-Mediated Autophagy: Implications for the Treatment of Neurological Diseases

Author keywords

Cell biology; Chaperone mediated autophagy; Interplay; Macroautophagy; Neurological disease

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; AUTOPHAGY PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK COGNATE PROTEIN 70; LEUCINE RICH REPEAT KINASE 2; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2A; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; PROTEIN AGGREGATE; VESICULAR TRANSPORT PROTEIN;

EID: 84942829952     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-014-8933-0     Document Type: Review
Times cited : (71)

References (167)
  • 1
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • COI: 1:CAS:528:DC%2BD1cXhtFehtb8%3D, PID: 18191218
    • Levine B, Kroemer G (2008) Autophagy in the pathogenesis of disease. Cell 132(1):27–42. doi:10.1016/j.cell.2007.12.018
    • (2008) Cell , vol.132 , Issue.1 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 2
    • 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, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451(7182):1069–1075. doi:10.1038/nature06639
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 3
    • 77956416339 scopus 로고    scopus 로고
    • Autophagy in mammalian development and differentiation
    • COI: 1:CAS:528:DC%2BC3cXhtFSju7zJ, PID: 20811354
    • Mizushima N, Levine B (2010) Autophagy in mammalian development and differentiation. Nat Cell Biol 12(9):823–830. doi:10.1038/ncb0910-823
    • (2010) Nat Cell Biol , vol.12 , Issue.9 , pp. 823-830
    • Mizushima, N.1    Levine, B.2
  • 4
    • 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, Han R, Zhang X, Zhang XD, Han F, Fukunaga K, Qin ZH (2008) Neuronal injury in rat model of permanent focal cerebral ischemia is associated with activation of autophagic and lysosomal pathways. Autophagy 4(6):762–769
    • (2008) Autophagy , vol.4 , Issue.6 , pp. 762-769
    • Wen, Y.D.1    Sheng, R.2    Zhang, L.S.3    Han, R.4    Zhang, X.5    Zhang, X.D.6    Han, F.7    Fukunaga, K.8    Qin, Z.H.9
  • 7
    • 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, Patrick C, Paulino A, Rockenstein E, Hansen L, Adame A, Galasko D, Masliah E (2010) Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS ONE 5(2):e9313. doi:10.1371/journal.pone.0009313
    • (2010) PLoS ONE , vol.5 , Issue.2 , pp. e9313
    • Crews, L.1    Spencer, B.2    Desplats, P.3    Patrick, C.4    Paulino, A.5    Rockenstein, E.6    Hansen, L.7    Adame, A.8    Galasko, D.9    Masliah, E.10
  • 10
    • 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
  • 11
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: a double-edged sword
    • COI: 1:CAS:528:DC%2BD2cXptFyju78%3D, PID: 15528435
    • Shintani T, Klionsky DJ (2004) Autophagy in health and disease: a double-edged sword. Science 306(5698):990–995. doi:10.1126/science.1099993
    • (2004) Science , vol.306 , Issue.5698 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 12
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • COI: 1:CAS:528:DC%2BD3cXovVOitbw%3D, PID: 11099404
    • Klionsky DJ, Emr SD (2000) Autophagy as a regulated pathway of cellular degradation. Science 290(5497):1717–1721
    • (2000) Science , vol.290 , Issue.5497 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 13
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: revisiting a 40-year-old conundrum
    • COI: 1:CAS:528:DC%2BC38XhtFCis70%3D, PID: 21646866
    • Mijaljica D, Prescott M, Devenish RJ (2011) Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 7(7):673–682
    • (2011) Autophagy , vol.7 , Issue.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 14
    • 1642329712 scopus 로고    scopus 로고
    • Determination of four sequential stages during microautophagy in vitro
    • COI: 1:CAS:528:DC%2BD2cXitlygsr0%3D, PID: 14679207
    • Kunz JB, Schwarz H, Mayer A (2004) Determination of four sequential stages during microautophagy in vitro. J Biol Chem 279(11):9987–9996. doi:10.1074/jbc.M307905200
    • (2004) J Biol Chem , vol.279 , Issue.11 , pp. 9987-9996
    • Kunz, J.B.1    Schwarz, H.2    Mayer, A.3
  • 15
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • COI: 1:CAS:528:DC%2BD2sXhtVGrtLbM, PID: 17404494
    • Dice JF (2007) Chaperone-mediated autophagy. Autophagy 3(4):295–299
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 295-299
    • Dice, J.F.1
  • 16
    • 79954422997 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in protein quality control
    • COI: 1:CAS:528:DC%2BC3MXkvFamtLc%3D, PID: 21094035
    • Arias E, Cuervo AM (2011) Chaperone-mediated autophagy in protein quality control. Curr Opin Cell Biol 23(2):184–189. doi:10.1016/j.ceb.2010.10.009
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 184-189
    • Arias, E.1    Cuervo, A.M.2
  • 17
    • 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, Kiffin R, Cuervo AM (2006) Consequences of the selective blockage of chaperone-mediated autophagy. Proc Natl Acad Sci U S A 103(15):5805–5810. doi:10.1073/pnas.0507436103
    • (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    Kiffin, R.4    Cuervo, A.M.5
  • 19
    • 84877628647 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • COI: 1:CAS:528:DC%2BC3sXivVWjsr0%3D, PID: 23406030
    • Choi AM, Ryter SW, Levine B (2013) Autophagy in human health and disease. N Engl J Med 368(7):651–662. doi:10.1056/NEJMra1205406
    • (2013) N Engl J Med , vol.368 , Issue.7 , pp. 651-662
    • Choi, A.M.1    Ryter, S.W.2    Levine, B.3
  • 20
    • 84863890450 scopus 로고    scopus 로고
    • Autophagy and neuronal cell death in neurological disorders
    • Nixon RA, Yang DS (2012) Autophagy and neuronal cell death in neurological disorders. Cold Spring Harbor perspectives in biology 4 (10). doi:10.1101/cshperspect.a008839
    • (2012) Cold Spring Harbor perspectives in biology , vol.4 , Issue.10
    • Nixon, R.A.1    Yang, D.S.2
  • 21
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: process and function
    • COI: 1:CAS:528:DC%2BD2sXhtlGmsrjP, PID: 18006683
    • Mizushima N (2007) Autophagy: process and function. Genes Dev 21(22):2861–2873. doi:10.1101/gad.1599207
    • (2007) Genes Dev , vol.21 , Issue.22 , pp. 2861-2873
    • Mizushima, N.1
  • 22
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • COI: 1:CAS:528:DC%2BD2sXhtF2qsL3I, PID: 17712358
    • Klionsky DJ (2007) Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 8(11):931–937. doi:10.1038/nrm2245
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.11 , pp. 931-937
    • Klionsky, D.J.1
  • 23
    • 80052303130 scopus 로고    scopus 로고
    • Autophagy and aging
    • COI: 1:CAS:528:DC%2BC3MXhtFakurzM, PID: 21884931
    • Rubinsztein DC, Marino G, Kroemer G (2011) Autophagy and aging. Cell 146(5):682–695. doi:10.1016/j.cell.2011.07.030
    • (2011) Cell , vol.146 , Issue.5 , pp. 682-695
    • Rubinsztein, D.C.1    Marino, G.2    Kroemer, G.3
  • 24
    • 35348886043 scopus 로고    scopus 로고
    • Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein
    • COI: 1:CAS:528:DC%2BD2sXhtFKitLnI, PID: 17893711
    • Cao Y, Klionsky DJ (2007) Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Cell Res 17(10):839–849. doi:10.1038/cr.2007.78
    • (2007) Cell Res , vol.17 , Issue.10 , pp. 839-849
    • Cao, Y.1    Klionsky, D.J.2
  • 25
    • 77953601881 scopus 로고    scopus 로고
    • Regulation of innate immune responses by autophagy-related proteins
    • COI: 1:CAS:528:DC%2BC3cXnvVantb8%3D, PID: 20548099
    • Saitoh T, Akira S (2010) Regulation of innate immune responses by autophagy-related proteins. J Cell Biol 189(6):925–935. doi:10.1083/jcb.201002021
    • (2010) J Cell Biol , vol.189 , Issue.6 , pp. 925-935
    • Saitoh, T.1    Akira, S.2
  • 26
    • 79960878784 scopus 로고    scopus 로고
    • Atg8: an autophagy-related ubiquitin-like protein family
    • COI: 1:CAS:528:DC%2BC3MXhtF2gu7vM, PID: 21867568
    • Shpilka T, Weidberg H, Pietrokovski S, Elazar Z (2011) Atg8: an autophagy-related ubiquitin-like protein family. Genome Biol 12(7):226. doi:10.1186/gb-2011-12-7-226
    • (2011) Genome Biol , vol.12 , Issue.7 , pp. 226
    • Shpilka, T.1    Weidberg, H.2    Pietrokovski, S.3    Elazar, Z.4
  • 27
    • 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, Kim YM, Otto NM, Cao J, Kundu M, Kim DH (2009) ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell 20(7):1992–2003. doi:10.1091/mbc.E08-12-1249
    • (2009) Mol Biol Cell , vol.20 , Issue.7 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6    Kundu, M.7    Kim, D.H.8
  • 28
    • 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, Ding X, Chen S, Jiang X (2009) ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. J Biol Chem 284(18):12297–12305. doi:10.1074/jbc.M900573200
    • (2009) J Biol Chem , vol.284 , Issue.18 , pp. 12297-12305
    • Ganley, I.G.1    du Lam, H.2    Wang, J.3    Ding, X.4    Chen, S.5    Jiang, X.6
  • 29
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • COI: 1:CAS:528:DC%2BC3MXhtlamtb0%3D, PID: 21258367
    • Kim J, Kundu M, Viollet B, Guan KL (2011) AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 13(2):132–141. doi:10.1038/ncb2152
    • (2011) Nat Cell Biol , vol.13 , Issue.2 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 30
    • 39049194057 scopus 로고    scopus 로고
    • The evolutionarily conserved domain of Beclin 1 is required for Vps34 binding, autophagy and tumor suppressor function
    • COI: 1:CAS:528:DC%2BD2MXos1ensLc%3D, PID: 16874027
    • Furuya N, Yu J, Byfield M, Pattingre S, Levine B (2005) The evolutionarily conserved domain of Beclin 1 is required for Vps34 binding, autophagy and tumor suppressor function. Autophagy 1(1):46–52
    • (2005) Autophagy , vol.1 , Issue.1 , pp. 46-52
    • Furuya, N.1    Yu, J.2    Byfield, M.3    Pattingre, S.4    Levine, B.5
  • 31
    • 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, Mizushima N (2008) Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 19(12):5360–5372. doi:10.1091/mbc.E08-01-0080
    • (2008) Mol Biol Cell , vol.19 , Issue.12 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 32
    • 77955895424 scopus 로고    scopus 로고
    • Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L
    • COI: 1:CAS:528:DC%2BC3cXhtFajtb3M, PID: 20713597
    • Matsunaga K, Morita E, Saitoh T, Akira S, Ktistakis NT, Izumi T, Noda T, Yoshimori T (2010) Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L. J Cell Biol 190(4):511–521. doi:10.1083/jcb.200911141
    • (2010) J Cell Biol , vol.190 , Issue.4 , pp. 511-521
    • Matsunaga, K.1    Morita, E.2    Saitoh, T.3    Akira, S.4    Ktistakis, N.T.5    Izumi, T.6    Noda, T.7    Yoshimori, T.8
  • 34
    • 34250900953 scopus 로고    scopus 로고
    • LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: caution in the interpretation of LC3 localization
    • COI: 1:CAS:528:DC%2BD2sXhtVGrtLbO, PID: 17387262
    • Kuma A, Matsui M, Mizushima N (2007) LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: caution in the interpretation of LC3 localization. Autophagy 3(4):323–328
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 323-328
    • Kuma, A.1    Matsui, M.2    Mizushima, N.3
  • 35
    • 84869210001 scopus 로고    scopus 로고
    • Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16 complex during autophagosome formation
    • COI: 1:CAS:528:DC%2BC38XhsV2rsb7F, PID: 23064152
    • Romanov J, Walczak M, Ibiricu I, Schuchner S, Ogris E, Kraft C, Martens S (2012) Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16 complex during autophagosome formation. EMBO J 31(22):4304–4317. doi:10.1038/emboj.2012.278
    • (2012) EMBO J , vol.31 , Issue.22 , pp. 4304-4317
    • Romanov, J.1    Walczak, M.2    Ibiricu, I.3    Schuchner, S.4    Ogris, E.5    Kraft, C.6    Martens, S.7
  • 36
    • 34248203863 scopus 로고    scopus 로고
    • Structure of Atg5.Atg16, a complex essential for autophagy
    • COI: 1:CAS:528:DC%2BD2sXitVCitL8%3D, PID: 17192262
    • Matsushita M, Suzuki NN, Obara K, Fujioka Y, Ohsumi Y, Inagaki F (2007) Structure of Atg5.Atg16, a complex essential for autophagy. J Biol Chem 282(9):6763–6772. doi:10.1074/jbc.M609876200
    • (2007) J Biol Chem , vol.282 , Issue.9 , pp. 6763-6772
    • Matsushita, M.1    Suzuki, N.N.2    Obara, K.3    Fujioka, Y.4    Ohsumi, Y.5    Inagaki, F.6
  • 37
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. ‘Protein modifications: beyond the usual suspects’ review series
    • COI: 1:CAS:528:DC%2BD1cXhtVGgt7jL, PID: 18704115
    • Geng J, Klionsky DJ (2008) The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. ‘Protein modifications: beyond the usual suspects’ review series. EMBO Rep 9(9):859–864. doi:10.1038/embor.2008.163
    • (2008) EMBO Rep , vol.9 , Issue.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 38
    • 0035971160 scopus 로고    scopus 로고
    • The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation
    • COI: 1:CAS:528:DC%2BD3MXis1Oksr8%3D, PID: 11139573
    • Komatsu M, Tanida I, Ueno T, Ohsumi M, Ohsumi Y, Kominami E (2001) The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation. J Biol Chem 276(13):9846–9854. doi:10.1074/jbc.M007737200
    • (2001) J Biol Chem , vol.276 , Issue.13 , pp. 9846-9854
    • Komatsu, M.1    Tanida, I.2    Ueno, T.3    Ohsumi, M.4    Ohsumi, Y.5    Kominami, E.6
  • 39
    • 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, Minematsu-Ikeguchi N, Yokota M, Ohsumi M, Ueno T, Kominami E (2003) The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification. J Biol Chem 278(41):39517–39526. doi:10.1074/jbc.C200334200
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 39517-39526
    • Nemoto, T.1    Tanida, I.2    Tanida-Miyake, E.3    Minematsu-Ikeguchi, N.4    Yokota, M.5    Ohsumi, M.6    Ueno, T.7    Kominami, E.8
  • 40
    • 84893500894 scopus 로고    scopus 로고
    • Molecular mechanism of autophagic membrane-scaffold assembly and disassembly
    • COI: 1:CAS:528:DC%2BC2cXhs1Knsbk%3D, PID: 24485455
    • Kaufmann A, Beier V, Franquelim HG, Wollert T (2014) Molecular mechanism of autophagic membrane-scaffold assembly and disassembly. Cell 156(3):469–481. doi:10.1016/j.cell.2013.12.022
    • (2014) Cell , vol.156 , Issue.3 , pp. 469-481
    • Kaufmann, A.1    Beier, V.2    Franquelim, H.G.3    Wollert, T.4
  • 41
    • 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, Ichimura Y, Fujioka Y, Takao T, Inagaki F, Ohsumi Y (2007) The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 282(52):37298–37302. doi:10.1074/jbc.C700195200
    • (2007) J Biol Chem , vol.282 , Issue.52 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6    Inagaki, F.7    Ohsumi, Y.8
  • 42
    • 84856487167 scopus 로고    scopus 로고
    • The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation
    • COI: 1:CAS:528:DC%2BC38XlsVWntL8%3D, PID: 22170151
    • Tanida I, Yamasaki M, Komatsu M, Ueno T (2012) The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation. Autophagy 8(1):88–97. doi:10.4161/auto.8.1.18339
    • (2012) Autophagy , vol.8 , Issue.1 , pp. 88-97
    • Tanida, I.1    Yamasaki, M.2    Komatsu, M.3    Ueno, T.4
  • 43
    • 34247237202 scopus 로고    scopus 로고
    • The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation
    • COI: 1:CAS:528:DC%2BD2sXis1Kgt7w%3D, PID: 17227760
    • Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F (2007) The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. J Biol Chem 282(11):8036–8043. doi:10.1074/jbc.M611473200
    • (2007) J Biol Chem , vol.282 , Issue.11 , pp. 8036-8043
    • Yamada, Y.1    Suzuki, N.N.2    Hanada, T.3    Ichimura, Y.4    Kumeta, H.5    Fujioka, Y.6    Ohsumi, Y.7    Inagaki, F.8
  • 44
    • 84857058225 scopus 로고    scopus 로고
    • Control of autophagy as a therapy for neurodegenerative disease
    • COI: 1:CAS:528:DC%2BC38XitFGru7c%3D
    • Harris H, Rubinsztein DC (2012) Control of autophagy as a therapy for neurodegenerative disease. Nat Rev Neurol 8(2):108–117. doi:10.1038/nrneurol.2011.200
    • (2012) Nat Rev Neurol , vol.8 , Issue.2 , pp. 108-117
    • Harris, H.1    Rubinsztein, D.C.2
  • 45
    • 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, Davies JE, Luo S, Oroz LG, Scaravilli F, Easton DF, Duden R, O'Kane CJ, Rubinsztein DC (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 36(6):585–595. doi:10.1038/ng1362
    • (2004) Nat Genet , vol.36 , Issue.6 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6    Scaravilli, F.7    Easton, D.F.8    Duden, R.9    O'Kane, C.J.10    Rubinsztein, D.C.11
  • 47
    • 84857802958 scopus 로고    scopus 로고
    • Molecules and their functions in autophagy
    • COI: 1:CAS:528:DC%2BC38Xmtlymt7k%3D, PID: 22257882
    • 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
    • (2012) Exp Mol Med , vol.44 , Issue.2 , pp. 73-80
    • Pyo, J.O.1    Nah, J.2    Jung, Y.K.3
  • 48
    • 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, Rubinsztein DC (2009) Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ 16(1):46–56. doi:10.1038/cdd.2008.110
    • (2009) Cell Death Differ , vol.16 , Issue.1 , pp. 46-56
    • Sarkar, S.1    Ravikumar, B.2    Floto, R.A.3    Rubinsztein, D.C.4
  • 49
    • 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
  • 50
    • 77955708390 scopus 로고    scopus 로고
    • Overview of macroautophagy regulation in mammalian cells
    • PID: 20548331
    • Mehrpour M, Esclatine A, Beau I, Codogno P (2010) Overview of macroautophagy regulation in mammalian cells. Cell Res 20(7):748–762. doi:10.1038/cr.2010.82
    • (2010) Cell Res , vol.20 , Issue.7 , pp. 748-762
    • Mehrpour, M.1    Esclatine, A.2    Beau, I.3    Codogno, P.4
  • 51
    • 53549113031 scopus 로고    scopus 로고
    • The role of TOR in autophagy regulation from yeast to plants and mammals
    • COI: 1:CAS:528:DC%2BD1cXht12rurvO, PID: 18670193
    • Diaz-Troya S, Perez-Perez ME, Florencio FJ, Crespo JL (2008) The role of TOR in autophagy regulation from yeast to plants and mammals. Autophagy 4(7):851–865
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 851-865
    • Diaz-Troya, S.1    Perez-Perez, M.E.2    Florencio, F.J.3    Crespo, J.L.4
  • 52
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: a unique way to enter the lysosome world
    • COI: 1:CAS:528:DC%2BC38XhtFaks7%2FI, PID: 22748206
    • Kaushik S, Cuervo AM (2012) Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol 22(8):407–417. doi:10.1016/j.tcb.2012.05.006
    • (2012) Trends Cell Biol , vol.22 , Issue.8 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 53
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • COI: 1:CAS:528:DyaK3cXivFei, PID: 2799391
    • Chiang HL, Terlecky SR, Plant CP, Dice JF (1989) A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246(4928):382–385
    • (1989) Science , vol.246 , Issue.4928 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 54
    • 79951580982 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: machinery, regulation and biological consequences
    • COI: 1:CAS:528:DC%2BC3MXhvVWhur0%3D
    • Li W, Yang Q, Mao Z (2011) Chaperone-mediated autophagy: machinery, regulation and biological consequences. Cell Mole Life Sci: CMLS 68(5):749–763. doi:10.1007/s00018-010-0565-6
    • (2011) Cell Mole Life Sci: CMLS , vol.68 , Issue.5 , pp. 749-763
    • Li, W.1    Yang, Q.2    Mao, Z.3
  • 55
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • COI: 1:CAS:528:DC%2BD1cXhtFCqsbvF, PID: 18644871
    • Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM (2008) The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 28(18):5747–5763. doi:10.1128/MCB.02070-07
    • (2008) Mol Cell Biol , vol.28 , Issue.18 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 56
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • COI: 1:CAS:528:DyaK2sXjtlenu7c%3D, PID: 9151685
    • Agarraberes FA, Terlecky SR, Dice JF (1997) An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 137(4):825–834
    • (1997) J Cell Biol , vol.137 , Issue.4 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 57
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • COI: 1:CAS:528:DyaK2sXhslalsL8%3D, PID: 9038169
    • Cuervo AM, Dice JF, Knecht E (1997) A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J Biol Chem 272(9):5606–5615
    • (1997) J Biol Chem , vol.272 , Issue.9 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 58
    • 33645812852 scopus 로고    scopus 로고
    • Effects of small molecules on chaperone-mediated autophagy
    • COI: 1:CAS:528:DC%2BD2MXht12lt7vF, PID: 16874031
    • Finn PF, Mesires NT, Vine M, Dice JF (2005) Effects of small molecules on chaperone-mediated autophagy. Autophagy 1(3):141–145
    • (2005) Autophagy , vol.1 , Issue.3 , pp. 141-145
    • Finn, P.F.1    Mesires, N.T.2    Vine, M.3    Dice, J.F.4
  • 59
    • 84884306536 scopus 로고    scopus 로고
    • Cerebral ischemia-reperfusion-induced autophagy protects against neuronal injury by mitochondrial clearance
    • COI: 1:CAS:528:DC%2BC2cXktF2rtLg%3D, PID: 23800795
    • Zhang X, Yan H, Yuan Y, Gao J, Shen Z, Cheng Y, Shen Y, Wang RR, Wang X, Hu WW, Wang G, Chen Z (2013) Cerebral ischemia-reperfusion-induced autophagy protects against neuronal injury by mitochondrial clearance. Autophagy 9(9):1321–1333. doi:10.4161/auto.25132
    • (2013) Autophagy , vol.9 , Issue.9 , pp. 1321-1333
    • Zhang, X.1    Yan, H.2    Yuan, Y.3    Gao, J.4    Shen, Z.5    Cheng, Y.6    Shen, Y.7    Wang, R.R.8    Wang, X.9    Hu, W.W.10    Wang, G.11    Chen, Z.12
  • 60
    • 84861679273 scopus 로고    scopus 로고
    • Autophagy activation is associated with neuroprotection against apoptosis via a mitochondrial pathway in a rat model of subarachnoid hemorrhage
    • COI: 1:CAS:528:DC%2BC38XotValsLk%3D, PID: 22521819
    • Jing CH, Wang L, Liu PP, Wu C, Ruan D, Chen G (2012) Autophagy activation is associated with neuroprotection against apoptosis via a mitochondrial pathway in a rat model of subarachnoid hemorrhage. Neuroscience 213:144–153. doi:10.1016/j.neuroscience.2012.03.055
    • (2012) Neuroscience , vol.213 , pp. 144-153
    • Jing, C.H.1    Wang, L.2    Liu, P.P.3    Wu, C.4    Ruan, D.5    Chen, G.6
  • 63
    • 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(5):719–731. doi:10.1083/jcb.200510065
    • (2006) J Cell Biol , vol.172 , Issue.5 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 64
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • Schaeffer V, Lavenir I, Ozcelik S, Tolnay M, Winkler DT, Goedert M (2012) Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy. Brain: J Neurol 135(Pt 7):2169–2177. doi:10.1093/brain/aws143
    • (2012) Brain : J Neurol , vol.135 , pp. 2169-2177
    • Schaeffer, V.1    Lavenir, I.2    Ozcelik, S.3    Tolnay, M.4    Winkler, D.T.5    Goedert, M.6
  • 65
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • COI: 1:CAS:528:DC%2BD3MXislCrsLc%3D, PID: 11274343
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81(2):741–766
    • (2001) Physiol Rev , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 70
    • 0034940160 scopus 로고    scopus 로고
    • Neurodegenerative tauopathies
    • COI: 1:CAS:528:DC%2BD3MXls1Shsbo%3D, PID: 11520930
    • Lee VM, Goedert M, Trojanowski JQ (2001) Neurodegenerative tauopathies. Annu Rev Neurosci 24:1121–1159. doi:10.1146/annurev.neuro.24.1.1121
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1121-1159
    • Lee, V.M.1    Goedert, M.2    Trojanowski, J.Q.3
  • 71
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • COI: 1:CAS:528:DC%2BD3cXmtVCrtbY%3D, PID: 10967355
    • Buee L, Bussiere T, Buee-Scherrer V, Delacourte A, Hof PR (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 33(1):95–130
    • (2000) Brain Res Brain Res Rev , vol.33 , Issue.1 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 74
    • 77956305343 scopus 로고    scopus 로고
    • Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease
    • PID: 20376313
    • Spilman P, Podlutskaya N, Hart MJ, Debnath J, Gorostiza O, Bredesen D, Richardson A, Strong R, Galvan V (2010) Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease. PLoS ONE 5(4):e9979. doi:10.1371/journal.pone.0009979
    • (2010) PLoS ONE , vol.5 , Issue.4 , pp. e9979
    • Spilman, P.1    Podlutskaya, N.2    Hart, M.J.3    Debnath, J.4    Gorostiza, O.5    Bredesen, D.6    Richardson, A.7    Strong, R.8    Galvan, V.9
  • 75
    • 79957917512 scopus 로고    scopus 로고
    • A small-molecule enhancer of autophagy decreases levels of Abeta and APP-CTF via Atg5-dependent autophagy pathway
    • COI: 1:CAS:528:DC%2BC3MXnsFyqt70%3D
    • Tian Y, Bustos V, Flajolet M, Greengard P (2011) A small-molecule enhancer of autophagy decreases levels of Abeta and APP-CTF via Atg5-dependent autophagy pathway. FASEB J: Off Publ Fed Am Soc Exp Biol 25(6):1934–1942. doi:10.1096/fj.10-175158
    • (2011) FASEB J: Off Publ Fed Am Soc Exp Biol , vol.25 , Issue.6 , pp. 1934-1942
    • Tian, Y.1    Bustos, V.2    Flajolet, M.3    Greengard, P.4
  • 78
    • 84862285881 scopus 로고    scopus 로고
    • Autophagic degradation of tau in primary neurons and its enhancement by trehalose
    • PID: 22169203
    • Kruger U, Wang Y, Kumar S, Mandelkow EM (2012) Autophagic degradation of tau in primary neurons and its enhancement by trehalose. Neurobiol Aging 33(10):2291–2305. doi:10.1016/j.neurobiolaging.2011.11.009
    • (2012) Neurobiol Aging , vol.33 , Issue.10 , pp. 2291-2305
    • Kruger, U.1    Wang, Y.2    Kumar, S.3    Mandelkow, E.M.4
  • 79
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • COI: 1:CAS:528:DyaK1cXntlakur0%3D, PID: 9809558
    • Conway KA, Harper JD, Lansbury PT (1998) Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat Med 4(11):1318–1320. doi:10.1038/3311
    • (1998) Nat Med , vol.4 , Issue.11 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 80
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset Parkinson's disease and mutations in the parkin gene
    • COI: 1:CAS:528:DC%2BD3cXktVCgtbs%3D, PID: 10824074
    • Lucking CB, Durr A, Bonifati V, Vaughan J, De Michele G, Gasser T, Harhangi BS, Meco G, Denefle P, Wood NW, Agid Y, Brice A, French Parkinson's Disease Genetics Study G, European Consortium on Genetic Susceptibility in Parkinson's D (2000) Association between early-onset Parkinson's disease and mutations in the parkin gene. N Engl J Med 342(21):1560–1567. doi:10.1056/NEJM200005253422103
    • (2000) N Engl J Med , vol.342 , Issue.21 , pp. 1560-1567
    • Lucking, C.B.1    Durr, A.2    Bonifati, V.3    Vaughan, J.4    De Michele, G.5    Gasser, T.6    Harhangi, B.S.7    Meco, G.8    Denefle, P.9    Wood, N.W.10    Agid, Y.11    Brice, A.12
  • 84
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • COI: 1:CAS:528:DC%2BD2MXht1KgsLrI, PID: 16269541
    • West AB, Moore DJ, Biskup S, Bugayenko A, Smith WW, Ross CA, Dawson VL, Dawson TM (2005) Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc Natl Acad Sci U S A 102(46):16842–16847. doi:10.1073/pnas.0507360102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.46 , pp. 16842-16847
    • West, A.B.1    Moore, D.J.2    Biskup, S.3    Bugayenko, A.4    Smith, W.W.5    Ross, C.A.6    Dawson, V.L.7    Dawson, T.M.8
  • 86
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease
    • COI: 1:CAS:528:DC%2BD3MXlt1yitL4%3D, PID: 11431533
    • Shimura H, Schlossmacher MG, Hattori N, Frosch MP, Trockenbacher A, Schneider R, Mizuno Y, Kosik KS, Selkoe DJ (2001) Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 293(5528):263–269. doi:10.1126/science.1060627
    • (2001) Science , vol.293 , Issue.5528 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6    Mizuno, Y.7    Kosik, K.S.8    Selkoe, D.J.9
  • 87
    • 29444437871 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
    • COI: 1:CAS:528:DC%2BD28Xpt12q, PID: 16352719
    • Smith WW, Pei Z, Jiang H, Moore DJ, Liang Y, West AB, Dawson VL, Dawson TM, Ross CA (2005) Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc Natl Acad Sci U S A 102(51):18676–18681. doi:10.1073/pnas.0508052102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.51 , pp. 18676-18681
    • Smith, W.W.1    Pei, Z.2    Jiang, H.3    Moore, D.J.4    Liang, Y.5    West, A.B.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9
  • 88
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
    • COI: 1:CAS:528:DC%2BD3MXns12kurg%3D, PID: 11590439
    • Chung KK, Zhang Y, Lim KL, Tanaka Y, Huang H, Gao J, Ross CA, Dawson VL, Dawson TM (2001) Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med 7(10):1144–1150. doi:10.1038/nm1001-1144
    • (2001) Nat Med , vol.7 , Issue.10 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 89
    • 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, Skepper JN, Rubinsztein DC (2003) Alpha-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 278(27):25009–25013. doi:10.1074/jbc.M300227200
    • (2003) J Biol Chem , vol.278 , Issue.27 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3    Skepper, J.N.4    Rubinsztein, D.C.5
  • 90
    • 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
    • Spencer B, Potkar R, Trejo M, Rockenstein E, Patrick C, Gindi R, Adame A, Wyss-Coray T, Masliah E (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: Off J Soc Neurosci 29(43):13578–13588. doi:10.1523/JNEUROSCI.4390-09.2009
    • (2009) J Neurosci : Off J Soc Neurosci , vol.29 , Issue.43 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 91
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72(6):971–983
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 93
    • 0029092340 scopus 로고
    • Expression of the Huntington's disease (IT15) protein product in HD patients
    • COI: 1:CAS:528:DyaK2MXnt1altrs%3D, PID: 7581375
    • Schilling G, Sharp AH, Loev SJ, Wagster MV, Li SH, Stine OC, Ross CA (1995) Expression of the Huntington's disease (IT15) protein product in HD patients. Hum Mol Genet 4(8):1365–1371
    • (1995) Hum Mol Genet , vol.4 , Issue.8 , pp. 1365-1371
    • Schilling, G.1    Sharp, A.H.2    Loev, S.J.3    Wagster, M.V.4    Li, S.H.5    Stine, O.C.6    Ross, C.A.7
  • 95
    • 84878934829 scopus 로고    scopus 로고
    • Inhibition of autophagy via p53-mediated disruption of ULK1 in a SCA7 polyglutamine disease model
    • COI: 1:CAS:528:DC%2BC3sXptVOnsb4%3D
    • Yu X, Munoz-Alarcon A, Ajayi A, Webling KE, Steinhof A, Langel U, Strom AL (2013) Inhibition of autophagy via p53-mediated disruption of ULK1 in a SCA7 polyglutamine disease model. J Mole Neurosci: MN 50(3):586–599. doi:10.1007/s12031-013-0012-x
    • (2013) J Mole Neurosci : MN , vol.50 , Issue.3 , pp. 586-599
    • Yu, X.1    Munoz-Alarcon, A.2    Ajayi, A.3    Webling, K.E.4    Steinhof, A.5    Langel, U.6    Strom, A.L.7
  • 97
    • 74249103961 scopus 로고    scopus 로고
    • Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3
    • Menzies FM, Huebener J, Renna M, Bonin M, Riess O, Rubinsztein DC (2010) Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3. Brain: J Neurol 133(Pt 1):93–104. doi:10.1093/brain/awp292
    • (2010) Brain : J Neurol , vol.133 , pp. 93-104
    • Menzies, F.M.1    Huebener, J.2    Renna, M.3    Bonin, M.4    Riess, O.5    Rubinsztein, D.C.6
  • 98
    • 33750089740 scopus 로고    scopus 로고
    • Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Zn-superoxide dismutase proteins by macroautophagy and the proteasome
    • COI: 1:CAS:528:DC%2BD28XhtVCrsL3E, PID: 16920710
    • Kabuta T, Suzuki Y, Wada K (2006) Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Zn-superoxide dismutase proteins by macroautophagy and the proteasome. J Biol Chem 281(41):30524–30533. doi:10.1074/jbc.M603337200
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 30524-30533
    • Kabuta, T.1    Suzuki, Y.2    Wada, K.3
  • 99
    • 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, Thielen P, Matus S, Nassif M, Court F, Kiffin R, Martinez G, Cuervo AM, Brown RH, Glimcher LH (2009) XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev 23(19):2294–2306. doi:10.1101/gad.1830709
    • (2009) Genes Dev , vol.23 , Issue.19 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3    Nassif, M.4    Court, F.5    Kiffin, R.6    Martinez, G.7    Cuervo, A.M.8    Brown, R.H.9    Glimcher, L.H.10
  • 103
    • 13944256602 scopus 로고    scopus 로고
    • Arsenic trioxide induces autophagic cell death in malignant glioma cells by upregulation of mitochondrial cell death protein BNIP3
    • COI: 1:CAS:528:DC%2BD2MXptlKhtQ%3D%3D, PID: 15592527
    • Kanzawa T, Zhang L, Xiao L, Germano IM, Kondo Y, Kondo S (2005) Arsenic trioxide induces autophagic cell death in malignant glioma cells by upregulation of mitochondrial cell death protein BNIP3. Oncogene 24(6):980–991. doi:10.1038/sj.onc.1208095
    • (2005) Oncogene , vol.24 , Issue.6 , pp. 980-991
    • Kanzawa, T.1    Zhang, L.2    Xiao, L.3    Germano, I.M.4    Kondo, Y.5    Kondo, S.6
  • 104
    • 34447132925 scopus 로고    scopus 로고
    • Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells
    • COI: 1:CAS:528:DC%2BD2sXnsVyqtL4%3D, PID: 17616690
    • Kim EH, Sohn S, Kwon HJ, Kim SU, Kim MJ, Lee SJ, Choi KS (2007) Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells. Cancer Res 67(13):6314–6324. doi:10.1158/0008-5472.CAN-06-4217
    • (2007) Cancer Res , vol.67 , Issue.13 , pp. 6314-6324
    • Kim, E.H.1    Sohn, S.2    Kwon, H.J.3    Kim, S.U.4    Kim, M.J.5    Lee, S.J.6    Choi, K.S.7
  • 105
    • 84862791828 scopus 로고    scopus 로고
    • Hypoxic stress activates chaperone-mediated autophagy and modulates neuronal cell survival
    • COI: 1:CAS:528:DC%2BC38XjsFOhsbo%3D, PID: 22306777
    • Dohi E, Tanaka S, Seki T, Miyagi T, Hide I, Takahashi T, Matsumoto M, Sakai N (2012) Hypoxic stress activates chaperone-mediated autophagy and modulates neuronal cell survival. Neurochem Int 60(4):431–442. doi:10.1016/j.neuint.2012.01.020
    • (2012) Neurochem Int , vol.60 , Issue.4 , pp. 431-442
    • Dohi, E.1    Tanaka, S.2    Seki, T.3    Miyagi, T.4    Hide, I.5    Takahashi, T.6    Matsumoto, M.7    Sakai, N.8
  • 107
    • 70349666552 scopus 로고    scopus 로고
    • Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways
    • COI: 1:CAS:528:DC%2BD1MXht1GjtLbI
    • Liu H, Wang P, Song W, Sun X (2009) Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways. FASEB J: Off Publ Fed Am Soc Exp Biol 23(10):3383–3392. doi:10.1096/fj.09-134296
    • (2009) FASEB J: Off Publ Fed Am Soc Exp Biol , vol.23 , Issue.10 , pp. 3383-3392
    • Liu, H.1    Wang, P.2    Song, W.3    Sun, X.4
  • 108
    • 84867427022 scopus 로고    scopus 로고
    • The role of chaperone-mediated autophagy in huntingtin degradation
    • COI: 1:CAS:528:DC%2BC38Xhs1Sitr7K, PID: 23071649
    • Qi L, Zhang XD, Wu JC, Lin F, Wang J, DiFiglia M, Qin ZH (2012) The role of chaperone-mediated autophagy in huntingtin degradation. PLoS ONE 7(10):e46834. doi:10.1371/journal.pone.0046834
    • (2012) PLoS ONE , vol.7 , Issue.10 , pp. e46834
    • Qi, L.1    Zhang, X.D.2    Wu, J.C.3    Lin, F.4    Wang, J.5    DiFiglia, M.6    Qin, Z.H.7
  • 109
    • 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, Lansbury PT, Sulzer D (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305(5688):1292–1295. doi:10.1126/science.1101738
    • (2004) Science , vol.305 , Issue.5688 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 110
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • COI: 1:CAS:528:DC%2BD1cXhtVWksbfE, PID: 18566453
    • Vogiatzi T, Xilouri M, Vekrellis K, Stefanis L (2008) Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem 283(35):23542–23556. doi:10.1074/jbc.M801992200
    • (2008) J Biol Chem , vol.283 , Issue.35 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 111
    • 77951541740 scopus 로고    scopus 로고
    • Lysosomal degradation of alpha-synuclein in vivo
    • COI: 1:CAS:528:DC%2BC3cXltFOgsb8%3D, PID: 20200163
    • Mak SK, McCormack AL, Manning-Bog AB, Cuervo AM, Di Monte DA (2010) Lysosomal degradation of alpha-synuclein in vivo. J Biol Chem 285(18):13621–13629. doi:10.1074/jbc.M109.074617
    • (2010) J Biol Chem , vol.285 , Issue.18 , pp. 13621-13629
    • Mak, S.K.1    McCormack, A.L.2    Manning-Bog, A.B.3    Cuervo, A.M.4    Di Monte, D.A.5
  • 112
    • 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, Park D, Stefanis L (2009) Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 4(5):e5515. doi:10.1371/journal.pone.0005515
    • (2009) PLoS ONE , vol.4 , Issue.5 , pp. e5515
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 116
    • 84875876495 scopus 로고    scopus 로고
    • Influence of microRNA deregulation on chaperone-mediated autophagy and alpha-synuclein pathology in Parkinson's disease
    • COI: 1:CAS:528:DC%2BC3sXhtVykt7nO, PID: 23492776
    • Alvarez-Erviti L, Seow Y, Schapira AH, Rodriguez-Oroz MC, Obeso JA, Cooper JM (2013) Influence of microRNA deregulation on chaperone-mediated autophagy and alpha-synuclein pathology in Parkinson's disease. Cell Death Dis 4:e545. doi:10.1038/cddis.2013.73
    • (2013) Cell Death Dis , vol.4 , pp. e545
    • Alvarez-Erviti, L.1    Seow, Y.2    Schapira, A.H.3    Rodriguez-Oroz, M.C.4    Obeso, J.A.5    Cooper, J.M.6
  • 117
    • 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, Kaushik S, Wong E, Mandelkow EM, Cuervo AM, Mandelkow E (2009) Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum Mol Genet 18(21):4153–4170. doi:10.1093/hmg/ddp367
    • (2009) Hum Mol Genet , vol.18 , Issue.21 , pp. 4153-4170
    • Wang, Y.1    Martinez-Vicente, M.2    Kruger, U.3    Kaushik, S.4    Wong, E.5    Mandelkow, E.M.6    Cuervo, A.M.7    Mandelkow, E.8
  • 118
    • 79951578639 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration
    • COI: 1:CAS:528:DC%2BC3MXmtFCktb4%3D, PID: 20643207
    • Koga H, Cuervo AM (2011) Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration. Neurobiol Dis 43(1):29–37. doi:10.1016/j.nbd.2010.07.006
    • (2011) Neurobiol Dis , vol.43 , Issue.1 , pp. 29-37
    • Koga, H.1    Cuervo, A.M.2
  • 120
    • 84880376355 scopus 로고    scopus 로고
    • Emerging regulation and functions of autophagy
    • COI: 1:CAS:528:DC%2BC3sXhtVehurzO, PID: 23817233
    • Boya P, Reggiori F, Codogno P (2013) Emerging regulation and functions of autophagy. Nat Cell Biol 15(7):713–720. doi:10.1038/ncb2788
    • (2013) Nat Cell Biol , vol.15 , Issue.7 , pp. 713-720
    • Boya, P.1    Reggiori, F.2    Codogno, P.3
  • 121
    • 33748433101 scopus 로고    scopus 로고
    • Lysosomal chat maintains the balance
    • COI: 1:CAS:528:DC%2BD28XhtVGisbjN, PID: 16874078
    • Massey AC, Kaushik S, Cuervo AM (2006) Lysosomal chat maintains the balance. Autophagy 2(4):325–327
    • (2006) Autophagy , vol.2 , Issue.4 , pp. 325-327
    • Massey, A.C.1    Kaushik, S.2    Cuervo, A.M.3
  • 122
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • COI: 1:CAS:528:DyaK2MXpslOiu7o%3D, PID: 7491910
    • Cuervo AM, Knecht E, Terlecky SR, Dice JF (1995) Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am J Physiol 269(5 Pt 1):C1200–C1208
    • (1995) Am J Physiol , vol.269 , pp. C1200-C1208
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 123
    • 77956178939 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: molecular mechanisms and physiological relevance
    • COI: 1:CAS:528:DC%2BC3cXhtVymur3J, PID: 20176123
    • Orenstein SJ, Cuervo AM (2010) Chaperone-mediated autophagy: molecular mechanisms and physiological relevance. Semin Cell Dev Biol 21(7):719–726. doi:10.1016/j.semcdb.2010.02.005
    • (2010) Semin Cell Dev Biol , vol.21 , Issue.7 , pp. 719-726
    • Orenstein, S.J.1    Cuervo, A.M.2
  • 124
    • 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, Cuervo AM (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    Cuervo, A.M.4
  • 125
    • 75149188760 scopus 로고    scopus 로고
    • Synergy and antagonism of macroautophagy and chaperone-mediated autophagy in a cell model of pathological tau aggregation
    • PID: 20023429
    • Wang Y, Martinez-Vicente M, Kruger U, Kaushik S, Wong E, Mandelkow EM, Cuervo AM, Mandelkow E (2010) Synergy and antagonism of macroautophagy and chaperone-mediated autophagy in a cell model of pathological tau aggregation. Autophagy 6(1):182–183
    • (2010) Autophagy , vol.6 , Issue.1 , pp. 182-183
    • Wang, Y.1    Martinez-Vicente, M.2    Kruger, U.3    Kaushik, S.4    Wong, E.5    Mandelkow, E.M.6    Cuervo, A.M.7    Mandelkow, E.8
  • 126
    • 84891741302 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: roles in disease and aging
    • COI: 1:CAS:528:DC%2BC3sXhvVOiurjL, PID: 24281265
    • Cuervo AM, Wong E (2014) Chaperone-mediated autophagy: roles in disease and aging. Cell Res 24(1):92–104. doi:10.1038/cr.2013.153
    • (2014) Cell Res , vol.24 , Issue.1 , pp. 92-104
    • Cuervo, A.M.1    Wong, E.2
  • 127
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • COI: 1:CAS:528:DC%2BD2cXpslKgu7w%3D, PID: 15331765
    • Kiffin R, Christian C, Knecht E, Cuervo AM (2004) Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell 15(11):4829–4840. doi:10.1091/mbc.E04-06-0477
    • (2004) Mol Biol Cell , vol.15 , Issue.11 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 128
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
    • COI: 1:CAS:528:DC%2BD1cXhtVyms7zL, PID: 18690243
    • Zhang C, Cuervo AM (2008) Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat Med 14(9):959–965. doi:10.1038/nm.1851
    • (2008) Nat Med , vol.14 , Issue.9 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 129
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • COI: 1:CAS:528:DC%2BD2MXht1Witb3L, PID: 16239905
    • Kroemer G, Jaattela M (2005) Lysosomes and autophagy in cell death control. Nat Rev Cancer 5(11):886–897. doi:10.1038/nrc1738
    • (2005) Nat Rev Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 130
    • 67749111834 scopus 로고    scopus 로고
    • Insulin-like growth factor-I prevents the accumulation of autophagic vesicles and cell death in Purkinje neurons by increasing the rate of autophagosome-to-lysosome fusion and degradation
    • COI: 1:CAS:528:DC%2BD1MXos1ensbc%3D, PID: 19509289
    • Bains M, Florez-McClure ML, Heidenreich KA (2009) Insulin-like growth factor-I prevents the accumulation of autophagic vesicles and cell death in Purkinje neurons by increasing the rate of autophagosome-to-lysosome fusion and degradation. J Biol Chem 284(30):20398–20407. doi:10.1074/jbc.M109.011791
    • (2009) J Biol Chem , vol.284 , Issue.30 , pp. 20398-20407
    • Bains, M.1    Florez-McClure, M.L.2    Heidenreich, K.A.3
  • 131
    • 43949117436 scopus 로고    scopus 로고
    • Early cellular changes after blockage of chaperone-mediated autophagy
    • COI: 1:CAS:528:DC%2BD1cXntFyntbY%3D, PID: 18253088
    • Massey AC, Follenzi A, Kiffin R, Zhang C, Cuervo AM (2008) Early cellular changes after blockage of chaperone-mediated autophagy. Autophagy 4(4):442–456
    • (2008) Autophagy , vol.4 , Issue.4 , pp. 442-456
    • Massey, A.C.1    Follenzi, A.2    Kiffin, R.3    Zhang, C.4    Cuervo, A.M.5
  • 132
    • 84868145847 scopus 로고    scopus 로고
    • The “Janus-faced role” of autophagy in neuronal sickness: focus on neurodegeneration
    • COI: 1:CAS:528:DC%2BC38XhsVeiurbP, PID: 22773113
    • Viscomi MT, D'Amelio M (2012) The “Janus-faced role” of autophagy in neuronal sickness: focus on neurodegeneration. Mol Neurobiol 46(2):513–521. doi:10.1007/s12035-012-8296-3
    • (2012) Mol Neurobiol , vol.46 , Issue.2 , pp. 513-521
    • Viscomi, M.T.1    D'Amelio, M.2
  • 133
    • 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
    • Boland B, Kumar A, Lee S, Platt FM, Wegiel J, Yu WH, Nixon RA (2008) Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J Neurosci: Off J Soc Neurosci 28(27):6926–6937. doi:10.1523/JNEUROSCI.0800-08.2008
    • (2008) J Neurosci : Off J Soc Neurosci , vol.28 , Issue.27 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 134
    • 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, Lucin K, Narasimhan R, Jaeger PA, Small S, Spencer B, Rockenstein E, Levine B, Wyss-Coray T (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(6):2190–2199. doi:10.1172/JCI33585
    • (2008) J Clin Invest , vol.118 , Issue.6 , pp. 2190-2199
    • Pickford, F.1    Masliah, E.2    Britschgi, M.3    Lucin, K.4    Narasimhan, R.5    Jaeger, P.A.6    Small, S.7    Spencer, B.8    Rockenstein, E.9    Levine, B.10    Wyss-Coray, T.11
  • 135
    • 83455169115 scopus 로고    scopus 로고
    • IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux
    • PID: 21954231
    • Lee H, Noh JY, Oh Y, Kim Y, Chang JW, Chung CW, Lee ST, Kim M, Ryu H, Jung YK (2012) IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux. Hum Mol Genet 21(1):101–114. doi:10.1093/hmg/ddr445
    • (2012) Hum Mol Genet , vol.21 , Issue.1 , pp. 101-114
    • Lee, H.1    Noh, J.Y.2    Oh, Y.3    Kim, Y.4    Chang, J.W.5    Chung, C.W.6    Lee, S.T.7    Kim, M.8    Ryu, H.9    Jung, Y.K.10
  • 136
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • COI: 1:CAS:528:DC%2BD1cXisVWjtbc%3D, PID: 18255062
    • Reijonen S, Putkonen N, Norremolle A, Lindholm D, Korhonen L (2008) Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp Cell Res 314(5):950–960. doi:10.1016/j.yexcr.2007.12.025
    • (2008) Exp Cell Res , vol.314 , Issue.5 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhonen, L.5
  • 138
    • 83455199097 scopus 로고    scopus 로고
    • Constitutive upregulation of chaperone-mediated autophagy in Huntington's disease
    • COI: 1:CAS:528:DC%2BC3MXhs1yktb%2FI
    • Koga H, Martinez-Vicente M, Arias E, Kaushik S, Sulzer D, Cuervo AM (2011) Constitutive upregulation of chaperone-mediated autophagy in Huntington's disease. J Neurosci: Off J Soc Neurosci 31(50):18492–18505. doi:10.1523/JNEUROSCI.3219-11.2011
    • (2011) J Neurosci : Off J Soc Neurosci , vol.31 , Issue.50 , pp. 18492-18505
    • Koga, H.1    Martinez-Vicente, M.2    Arias, E.3    Kaushik, S.4    Sulzer, D.5    Cuervo, A.M.6
  • 139
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to other lamp2 isoforms
    • COI: 1:CAS:528:DC%2BD3MXmsVKmtw%3D%3D, PID: 11082038
    • Cuervo AM, Dice JF (2000) Unique properties of lamp2a compared to other lamp2 isoforms. J Cell Sci 113(Pt 24):4441–4450
    • (2000) J Cell Sci , vol.113 , pp. 4441-4450
    • Cuervo, A.M.1    Dice, J.F.2
  • 140
    • 43949141438 scopus 로고    scopus 로고
    • Compensatory mechanisms and the type of injury determine the fate of cells with impaired macroautophagy
    • COI: 1:CAS:528:DC%2BD1cXntFynu7k%3D, PID: 18319638
    • Singh R, Czaja MJ (2008) Compensatory mechanisms and the type of injury determine the fate of cells with impaired macroautophagy. Autophagy 4(4):516–518
    • (2008) Autophagy , vol.4 , Issue.4 , pp. 516-518
    • Singh, R.1    Czaja, M.J.2
  • 141
    • 41949125675 scopus 로고    scopus 로고
    • Loss of macroautophagy promotes or prevents fibroblast apoptosis depending on the death stimulus
    • COI: 1:CAS:528:DC%2BD1cXhvFeksro%3D, PID: 18073215
    • Wang Y, Singh R, Massey AC, Kane SS, Kaushik S, Grant T, Xiang Y, Cuervo AM, Czaja MJ (2008) Loss of macroautophagy promotes or prevents fibroblast apoptosis depending on the death stimulus. J Biol Chem 283(8):4766–4777. doi:10.1074/jbc.M706666200
    • (2008) J Biol Chem , vol.283 , Issue.8 , pp. 4766-4777
    • Wang, Y.1    Singh, R.2    Massey, A.C.3    Kane, S.S.4    Kaushik, S.5    Grant, T.6    Xiang, Y.7    Cuervo, A.M.8    Czaja, M.J.9
  • 143
    • 77954230819 scopus 로고    scopus 로고
    • Macroautophagy and chaperone-mediated autophagy are required for hepatocyte resistance to oxidant stress
    • COI: 1:CAS:528:DC%2BC3cXpsFShtbw%3D, PID: 20578144
    • Wang Y, Singh R, Xiang Y, Czaja MJ (2010) Macroautophagy and chaperone-mediated autophagy are required for hepatocyte resistance to oxidant stress. Hepatology 52(1):266–277. doi:10.1002/hep.23645
    • (2010) Hepatology , vol.52 , Issue.1 , pp. 266-277
    • Wang, Y.1    Singh, R.2    Xiang, Y.3    Czaja, M.J.4
  • 144
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • COI: 1:CAS:528:DyaK1cXlsFOmsLc%3D, PID: 9759494
    • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425–479. doi:10.1146/annurev.biochem.67.1.425
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 145
    • 33847410541 scopus 로고    scopus 로고
    • Emerging roles for ubiquitin and protein degradation in neuronal function
    • COI: 1:CAS:528:DC%2BD2sXkt1WmtLc%3D, PID: 17329546
    • Yi JJ, Ehlers MD (2007) Emerging roles for ubiquitin and protein degradation in neuronal function. Pharmacol Rev 59(1):14–39. doi:10.1124/pr.59.1.4
    • (2007) Pharmacol Rev , vol.59 , Issue.1 , pp. 14-39
    • Yi, J.J.1    Ehlers, M.D.2
  • 146
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • COI: 1:CAS:528:DC%2BD1cXktFGisrg%3D, PID: 18362179
    • Wang J, Wang CE, Orr A, Tydlacka S, Li SH, Li XJ (2008) Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J Cell Biol 180(6):1177–1189. doi:10.1083/jcb.200709080
    • (2008) J Cell Biol , vol.180 , Issue.6 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3    Tydlacka, S.4    Li, S.H.5    Li, X.J.6
  • 149
    • 84890178991 scopus 로고    scopus 로고
    • Substrate recognition in selective autophagy and the ubiquitin-proteasome system
    • COI: 1:CAS:528:DC%2BC3sXmt1Cltro%3D, PID: 23545414
    • Schreiber A, Peter M (2014) Substrate recognition in selective autophagy and the ubiquitin-proteasome system. Biochim Biophys Acta 1843(1):163–181. doi:10.1016/j.bbamcr.2013.03.019
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.1 , pp. 163-181
    • Schreiber, A.1    Peter, M.2
  • 150
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection
    • COI: 1:CAS:528:DC%2BD1cXhsVCntb%2FN, PID: 18930136
    • Nedelsky NB, Todd PK, Taylor JP (2008) Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection. Biochim Biophys Acta 1782(12):691–699. doi:10.1016/j.bbadis.2008.10.002
    • (2008) Biochim Biophys Acta , vol.1782 , Issue.12 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 152
    • 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, Yoshimori T, Stolz DB, Ron D, Yin XM (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. doi:10.2353/ajpath.2007.070188
    • (2007) Am J Pathol , vol.171 , Issue.2 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 153
    • 75149175502 scopus 로고    scopus 로고
    • Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells
    • COI: 1:CAS:528:DC%2BD1MXhtlers7bK, PID: 19881538
    • Zhu K, Dunner K Jr, McConkey DJ (2010) Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells. Oncogene 29(3):451–462. doi:10.1038/onc.2009.343
    • (2010) Oncogene , vol.29 , Issue.3 , pp. 451-462
    • Zhu, K.1    Dunner, K.2    McConkey, D.J.3
  • 154
    • 84885593791 scopus 로고    scopus 로고
    • A novel crosstalk between two major protein degradation systems: regulation of proteasomal activity by autophagy
    • COI: 1:CAS:528:DC%2BC2cXjvFSgt7c%3D, PID: 23934082
    • Wang XJ, Yu J, Wong SH, Cheng AS, Chan FK, Ng SS, Cho CH, Sung JJ, Wu WK (2013) A novel crosstalk between two major protein degradation systems: regulation of proteasomal activity by autophagy. Autophagy 9(10):1500–1508. doi:10.4161/auto.25573
    • (2013) Autophagy , vol.9 , Issue.10 , pp. 1500-1508
    • Wang, X.J.1    Yu, J.2    Wong, S.H.3    Cheng, A.S.4    Chan, F.K.5    Ng, S.S.6    Cho, C.H.7    Sung, J.J.8    Wu, W.K.9
  • 156
    • 0037067678 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells
    • COI: 1:CAS:528:DC%2BD38XlsVWitLo%3D, PID: 11976344
    • Xiao C, Yang BF, Asadi N, Beguinot F, Hao C (2002) Tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells. J Biol Chem 277(28):25020–25025. doi:10.1074/jbc.M202946200
    • (2002) J Biol Chem , vol.277 , Issue.28 , pp. 25020-25025
    • Xiao, C.1    Yang, B.F.2    Asadi, N.3    Beguinot, F.4    Hao, C.5
  • 157
    • 84859385707 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy promotes tumor cell survival and adaptation to antiangiogenic treatment in glioblastoma
    • COI: 1:CAS:528:DC%2BC38XkvVelsbo%3D, PID: 22447568
    • Hu YL, DeLay M, Jahangiri A, Molinaro AM, Rose SD, Carbonell WS, Aghi MK (2012) Hypoxia-induced autophagy promotes tumor cell survival and adaptation to antiangiogenic treatment in glioblastoma. Cancer Res 72(7):1773–1783. doi:10.1158/0008-5472.CAN-11-3831
    • (2012) Cancer Res , vol.72 , Issue.7 , pp. 1773-1783
    • Hu, Y.L.1    DeLay, M.2    Jahangiri, A.3    Molinaro, A.M.4    Rose, S.D.5    Carbonell, W.S.6    Aghi, M.K.7
  • 158
    • 84877636823 scopus 로고    scopus 로고
    • Crosstalk between the proteasome system and autophagy in the clearance of alpha-synuclein
    • PID: 23603979
    • Yang F, Yang YP, Mao CJ, Liu L, Zheng HF, Hu LF, Liu CF (2013) Crosstalk between the proteasome system and autophagy in the clearance of alpha-synuclein. Acta Pharmacol Sin 34(5):674–680. doi:10.1038/aps.2013.29
    • (2013) Acta Pharmacol Sin , vol.34 , Issue.5 , pp. 674-680
    • Yang, F.1    Yang, Y.P.2    Mao, C.J.3    Liu, L.4    Zheng, H.F.5    Hu, L.F.6    Liu, C.F.7
  • 160
    • 59649110865 scopus 로고    scopus 로고
    • PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation
    • PID: 19148225
    • N'Diaye EN, Kajihara KK, Hsieh I, Morisaki H, Debnath J, Brown EJ (2009) PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation. EMBO Rep 10(2):173–179. doi:10.1038/embor.2008.238
    • (2009) EMBO Rep , vol.10 , Issue.2 , pp. 173-179
    • N'Diaye, E.N.1    Kajihara, K.K.2    Hsieh, I.3    Morisaki, H.4    Debnath, J.5    Brown, E.J.6
  • 161
    • 0037352279 scopus 로고    scopus 로고
    • Activated protein C blocks p53-mediated apoptosis in ischemic human brain endothelium and is neuroprotective
    • COI: 1:CAS:528:DC%2BD3sXhsFGgs7g%3D, PID: 12563316
    • Cheng T, Liu D, Griffin JH, Fernandez JA, Castellino F, Rosen ED, Fukudome K, Zlokovic BV (2003) Activated protein C blocks p53-mediated apoptosis in ischemic human brain endothelium and is neuroprotective. Nat Med 9(3):338–342. doi:10.1038/nm826
    • (2003) Nat Med , vol.9 , Issue.3 , pp. 338-342
    • Cheng, T.1    Liu, D.2    Griffin, J.H.3    Fernandez, J.A.4    Castellino, F.5    Rosen, E.D.6    Fukudome, K.7    Zlokovic, B.V.8
  • 163
    • 0026569818 scopus 로고
    • Clonal expansion of p53 mutant cells is associated with brain tumour progression
    • COI: 1:CAS:528:DyaK38XhslWhtL4%3D, PID: 1311419
    • Sidransky D, Mikkelsen T, Schwechheimer K, Rosenblum ML, Cavanee W, Vogelstein B (1992) Clonal expansion of p53 mutant cells is associated with brain tumour progression. Nature 355(6363):846–847. doi:10.1038/355846a0
    • (1992) Nature , vol.355 , Issue.6363 , pp. 846-847
    • Sidransky, D.1    Mikkelsen, T.2    Schwechheimer, K.3    Rosenblum, M.L.4    Cavanee, W.5    Vogelstein, B.6
  • 166
    • 65249125897 scopus 로고    scopus 로고
    • p53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum
    • COI: 1:CAS:528:DC%2BD1MXnvVyrsr4%3D, PID: 19305162
    • Zhang XD, Wang Y, Wang Y, Zhang X, Han R, Wu JC, Liang ZQ, Gu ZL, Han F, Fukunaga K, Qin ZH (2009) p53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum. Autophagy 5(3):339–350
    • (2009) Autophagy , vol.5 , Issue.3 , pp. 339-350
    • Zhang, X.D.1    Wang, Y.2    Wang, Y.3    Zhang, X.4    Han, R.5    Wu, J.C.6    Liang, Z.Q.7    Gu, Z.L.8    Han, F.9    Fukunaga, K.10    Qin, Z.H.11
  • 167
    • 84870549095 scopus 로고    scopus 로고
    • Astrocyte-specific overexpression of Nrf2 delays motor pathology and synuclein aggregation throughout the CNS in the alpha-synuclein mutant (A53T) mouse model
    • COI: 1:CAS:528:DC%2BC38XhvVCmu77E
    • Gan L, Vargas MR, Johnson DA, Johnson JA (2012) Astrocyte-specific overexpression of Nrf2 delays motor pathology and synuclein aggregation throughout the CNS in the alpha-synuclein mutant (A53T) mouse model. J Neurosci: Off J Soc Neurosci 32(49):17775–17787. doi:10.1523/JNEUROSCI.3049-12.2012
    • (2012) J Neurosci: Off J Soc Neurosci , vol.32 , Issue.49 , pp. 17775-17787
    • Gan, L.1    Vargas, M.R.2    Johnson, D.A.3    Johnson, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.