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Volumn 37, Issue 3, 2017, Pages 377-388

Autophagy and Alzheimer’s Disease

Author keywords

Alzheimer s disease; Autophagy; Tau; Amyloid

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CALPAIN; INOSITOL; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; PRESENILIN 1; PRESENILIN 2; PROTEIN AGGREGATE; TAU PROTEIN;

EID: 85013932885     PISSN: 02724340     EISSN: 15736830     Source Type: Journal    
DOI: 10.1007/s10571-016-0386-8     Document Type: Review
Times cited : (261)

References (105)
  • 1
    • 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
  • 2
    • 0041343303 scopus 로고    scopus 로고
    • Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD3sXmslSnsLY%3D, PID: 12875979
    • An WL, Cowburn RF, Li L, Braak H, Alafuzoff I, Iqbal K, Iqbal IG, Winblad B, Pei JJ (2003) Up-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer’s disease. Am J Pathol 163(2):591–607
    • (2003) Am J Pathol , vol.163 , Issue.2 , pp. 591-607
    • An, W.L.1    Cowburn, R.F.2    Li, L.3    Braak, H.4    Alafuzoff, I.5    Iqbal, K.6    Iqbal, I.G.7    Winblad, B.8    Pei, J.J.9
  • 3
    • 80053906347 scopus 로고    scopus 로고
    • Calcium channel blocking as a therapeutic strategy for Alzheimer’s disease: the case for isradipine
    • COI: 1:CAS:528:DC%2BC3MXhtl2htbnJ, PID: 21925266
    • Anekonda TS, Quinn JF (2011) Calcium channel blocking as a therapeutic strategy for Alzheimer’s disease: the case for isradipine. Biochim Biophys Acta 1812(12):1584–1590
    • (2011) Biochim Biophys Acta , vol.1812 , Issue.12 , pp. 1584-1590
    • Anekonda, T.S.1    Quinn, J.F.2
  • 4
    • 84906861963 scopus 로고    scopus 로고
    • Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin
    • COI: 1:CAS:528:DC%2BC2cXhsFantb%2FE, PID: 25154397
    • Ashrafi G, Schlehe JS, LaVoie MJ, Schwarz TL (2014) Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin. J Cell Biol 206(5):655–670
    • (2014) J Cell Biol , vol.206 , Issue.5 , pp. 655-670
    • Ashrafi, G.1    Schlehe, J.S.2    LaVoie, M.J.3    Schwarz, T.L.4
  • 5
    • 84872351818 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 ameliorates β-amyloid pathology and restores lysosomal acidification and mammalian target of rapamycin activity in the Alzheimer disease mouse model: in vivo and in vitro studies
    • COI: 1:CAS:528:DC%2BC3sXos1WisA%3D%3D, PID: 23155049
    • Avrahami L, Farfara D, Shaham Kol M, Vassar R, Frenkel D, Eldar-Finkelman H (2013) Inhibition of glycogen synthase kinase-3 ameliorates β-amyloid pathology and restores lysosomal acidification and mammalian target of rapamycin activity in the Alzheimer disease mouse model: in vivo and in vitro studies. J Biol Chem 288:1295–1306
    • (2013) J Biol Chem , vol.288 , pp. 1295-1306
    • Avrahami, L.1    Farfara, D.2    Shaham Kol, M.3    Vassar, R.4    Frenkel, D.5    Eldar-Finkelman, H.6
  • 6
    • 44649090171 scopus 로고    scopus 로고
    • Activation of the amyloid cascade in apolipoprotein E4 transgenic mice induces lysosomal activation and neurodegeneration resulting in marked cognitive deficits
    • COI: 1:CAS:528:DC%2BD1cXlvFWhtbw%3D, PID: 18448646
    • Belinson H, Lev D, Masliah E, Michaelson DM (2008) Activation of the amyloid cascade in apolipoprotein E4 transgenic mice induces lysosomal activation and neurodegeneration resulting in marked cognitive deficits. J Neurosci 28(18):4690–4701
    • (2008) J Neurosci , vol.28 , Issue.18 , pp. 4690-4701
    • Belinson, H.1    Lev, D.2    Masliah, E.3    Michaelson, D.M.4
  • 7
    • 33747130379 scopus 로고    scopus 로고
    • Altered synaptic function in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD28XotlWktbg%3D, PID: 16887118
    • Bell KF, Claudio CA (2006) Altered synaptic function in Alzheimer’s disease. Eur J Pharmacol 545(1):11–21
    • (2006) Eur J Pharmacol , vol.545 , Issue.1 , pp. 11-21
    • Bell, K.F.1    Claudio, C.A.2
  • 8
    • 84894491282 scopus 로고    scopus 로고
    • Defining the membrane precursor supporting the nucleation of the phagophore
    • COI: 1:CAS:528:DC%2BC2cXht1Gns7rP, PID: 24257021
    • Bernard A, Klionsky DJ (2014) Defining the membrane precursor supporting the nucleation of the phagophore. Autophagy 10(1):1–2
    • (2014) Autophagy , vol.10 , Issue.1 , pp. 1-2
    • Bernard, A.1    Klionsky, D.J.2
  • 9
    • 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, 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 28(27):6926–6937
    • (2008) J 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
  • 10
    • 84901745843 scopus 로고    scopus 로고
    • Genetic reduction of mammalian target of rapamycin ameliorates Alzheimer’s disease-like cognitive and pathological deficits by restoring hippocampal gene expression signature
    • COI: 1:CAS:528:DC%2BC2cXps12qtr8%3D, PID: 24899720
    • Caccamo A, De Pinto V, Messina A, Branca C, Oddo S (2014) Genetic reduction of mammalian target of rapamycin ameliorates Alzheimer’s disease-like cognitive and pathological deficits by restoring hippocampal gene expression signature. J Neurosci 34(23):7988–7998
    • (2014) J Neurosci , vol.34 , Issue.23 , pp. 7988-7998
    • Caccamo, A.1    De Pinto, V.2    Messina, A.3    Branca, C.4    Oddo, S.5
  • 12
    • 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
  • 13
    • 84907898151 scopus 로고    scopus 로고
    • Autophagy in microglia degrades extracellular β-amyloid fibrils and regulates the NLRP3 inflammasome
    • COI: 1:CAS:528:DC%2BC2MXjvFGjurc%3D, PID: 25126727
    • Cho MH, Cho K, Kang HJ, Jeon EY, Kim HS, Kwon HJ, Kim HM, Kim DH, Yoon SY (2014) Autophagy in microglia degrades extracellular β-amyloid fibrils and regulates the NLRP3 inflammasome. Autophagy 10(10):1761–1775
    • (2014) Autophagy , vol.10 , Issue.10 , pp. 1761-1775
    • Cho, M.H.1    Cho, K.2    Kang, H.J.3    Jeon, E.Y.4    Kim, H.S.5    Kwon, H.J.6    Kim, H.M.7    Kim, D.H.8    Yoon, S.Y.9
  • 15
    • 84862281225 scopus 로고    scopus 로고
    • Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
    • COI: 1:CAS:528:DC%2BC38Xht1art73N, PID: 22361619
    • Congdon EE, Wu JW, Myeku N, Figueroa YH, Herman M, Marinec PS, Gestwicki JE, Dickey CA, Yu WH (2012) Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo. Autophagy 8(4):609–622
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 609-622
    • Congdon, E.E.1    Wu, J.W.2    Myeku, N.3    Figueroa, Y.H.4    Herman, M.5    Marinec, P.S.6    Gestwicki, J.E.7    Dickey, C.A.8    Yu, W.H.9
  • 16
    • 84926636149 scopus 로고    scopus 로고
    • Pereira CM (2015) Alzheimer’s disease-related misfolded proteins and dysfunctional organelles on autophagy menu
    • COI: 1:CAS:528:DC%2BC2MXlvVehtrg%3D, PID: 25664381
    • Correia SC, Resende R, Moreira PI (2015) Pereira CM (2015) Alzheimer’s disease-related misfolded proteins and dysfunctional organelles on autophagy menu. DNA Cell Biol 34(4):261–273
    • (2015) DNA Cell Biol , vol.34 , Issue.4 , pp. 261-273
    • Correia, S.C.1    Resende, R.2    Moreira, P.I.3
  • 17
    • 77949328788 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: selectivity pays off
    • COI: 1:CAS:528:DC%2BC3cXis1ShtbY%3D, PID: 19857975
    • Cuervo AM (2010) Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol Metab 21(3):142–150
    • (2010) Trends Endocrinol Metab , vol.21 , Issue.3 , pp. 142-150
    • Cuervo, A.M.1
  • 18
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • COI: 1:CAS:528:DyaK28Xks1Wmu7o%3D, PID: 8662539
    • Cuervo AM, Dice JF (1996) A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273:501–503
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 19
    • 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
  • 20
    • 84881496428 scopus 로고    scopus 로고
    • Activity-induced convergence of APP and BACE-1 in acidic microdomains via an endocytosis-dependent pathway
    • COI: 1:CAS:528:DC%2BC3sXht1elurvF, PID: 23931995
    • Das U, Scott DA, Ganguly A, Koo EH, Tang Y, Roy S (2013) Activity-induced convergence of APP and BACE-1 in acidic microdomains via an endocytosis-dependent pathway. Neuron 79(3):447–460
    • (2013) Neuron , vol.79 , Issue.3 , pp. 447-460
    • Das, U.1    Scott, D.A.2    Ganguly, A.3    Koo, E.H.4    Tang, Y.5    Roy, S.6
  • 21
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • COI: 1:CAS:528:DC%2BD2sXhtVGrtLbM, PID: 17404494
    • Dice J (2007) Chaperone-mediated autophagy. Autophagy 3:295–299
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.1
  • 23
    • 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, Fukuda M, Noda T, Yoshimori T (2008) The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell 19(5):2092–2100
    • (2008) Mol Biol Cell , vol.19 , Issue.5 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 24
    • 41149085729 scopus 로고    scopus 로고
    • Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression
    • PID: 18294209
    • Hamano T, Gendron TF, Causevic E, Yen SH, Lin WL, Isidoro C, Deture M, Ko LW (2008) Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression. Eur J Neurosci 27(5):1119–1130
    • (2008) Eur J Neurosci , vol.27 , Issue.5 , pp. 1119-1130
    • Hamano, T.1    Gendron, T.F.2    Causevic, E.3    Yen, S.H.4    Lin, W.L.5    Isidoro, C.6    Deture, M.7    Ko, L.W.8
  • 26
    • 73949133110 scopus 로고    scopus 로고
    • Alzheimer disease-associated peptide, amyloid β40, inhibits vascular regeneration with induction of endothelial autophagy
    • COI: 1:CAS:528:DC%2BD1MXht1ymsr7I, PID: 19815818
    • Hayashi S, Sato N, Yamamoto A, Ikegame Y, Nakashima S, Ogihara T, Morishita R (2009) Alzheimer disease-associated peptide, amyloid β40, inhibits vascular regeneration with induction of endothelial autophagy. Arterioscler Thromb Vasc Biol 29(11):1909–1915
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , Issue.11 , pp. 1909-1915
    • Hayashi, S.1    Sato, N.2    Yamamoto, A.3    Ikegame, Y.4    Nakashima, S.5    Ogihara, T.6    Morishita, R.7
  • 28
    • 84866519178 scopus 로고    scopus 로고
    • Macroautophagy deficiency mediates age-dependent neurodegeneration through a phospho-tau pathway
    • COI: 1:CAS:528:DC%2BC3sXitVymsr0%3D, PID: 22998728
    • Inoue K, Rispoli J, Kaphzan H, Klann E, Chen EI, Kim J, Komatsu M, Abeliovich A (2012) Macroautophagy deficiency mediates age-dependent neurodegeneration through a phospho-tau pathway. Mol Neurodegener 7:48
    • (2012) Mol Neurodegener , vol.7 , pp. 48
    • Inoue, K.1    Rispoli, J.2    Kaphzan, H.3    Klann, E.4    Chen, E.I.5    Kim, J.6    Komatsu, M.7    Abeliovich, A.8
  • 29
    • 84875423993 scopus 로고    scopus 로고
    • Amino acid signalling upstream of mTOR
    • COI: 1:CAS:528:DC%2BC3sXhsFGjsr4%3D, PID: 23361334
    • Jewell JL, Russell RC, Guan KL (2013) Amino acid signalling upstream of mTOR. Nat Rev Mol Cell Biol 14(3):133–139
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.3 , pp. 133-139
    • Jewell, J.L.1    Russell, R.C.2    Guan, K.L.3
  • 30
    • 33645553416 scopus 로고    scopus 로고
    • Reactivity of apolipoprotein E4 and amyloid beta peptide: lysosomal stability and neurodegeneration
    • COI: 1:CAS:528:DC%2BD28XovVehsw%3D%3D, PID: 16298992
    • Ji ZS, Müllendorff K, Cheng IH, Miranda RD, Huang Y, Mahley RW (2006) Reactivity of apolipoprotein E4 and amyloid beta peptide: lysosomal stability and neurodegeneration. J Biol Chem 281(5):2683–2692
    • (2006) J Biol Chem , vol.281 , Issue.5 , pp. 2683-2692
    • Ji, Z.S.1    Müllendorff, K.2    Cheng, I.H.3    Miranda, R.D.4    Huang, Y.5    Mahley, R.W.6
  • 31
    • 84896338549 scopus 로고    scopus 로고
    • Temsirolimus promotes autophagic clearance of amyloid-β and provides protective effects in cellular and animal models of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC2cXltl2iurw%3D, PID: 24602800
    • Jiang T, Yu JT, Zhu XC, Tan MS, Wang HF, Cao L, Zhang QQ, Shi JQ, Gao L, Qin H, Zhang YD, Tan L (2014a) Temsirolimus promotes autophagic clearance of amyloid-β and provides protective effects in cellular and animal models of Alzheimer’s disease. Pharmacol Res 81:54–63
    • (2014) Pharmacol Res , vol.81 , pp. 54-63
    • Jiang, T.1    Yu, J.T.2    Zhu, X.C.3    Tan, M.S.4    Wang, H.F.5    Cao, L.6    Zhang, Q.Q.7    Shi, J.Q.8    Gao, L.9    Qin, H.10    Zhang, Y.D.11    Tan, L.12
  • 32
    • 84902273908 scopus 로고    scopus 로고
    • Temsirolimus attenuates tauopathy in vitro and in vivo by targeting tau hyperphosphorylation and autophagic clearance
    • COI: 1:CAS:528:DC%2BC2cXhtFyhtb%2FM, PID: 24880087
    • Jiang T, Yu JT, Zhu XC, Zhang QQ, Cao L, Wang HF, Tan MS, Gao Q, Qin H, Zhang YD, Tan L (2014b) Temsirolimus attenuates tauopathy in vitro and in vivo by targeting tau hyperphosphorylation and autophagic clearance. Neuropharmacology 85:121–130
    • (2014) Neuropharmacology , vol.85 , pp. 121-130
    • Jiang, T.1    Yu, J.T.2    Zhu, X.C.3    Zhang, Q.Q.4    Cao, L.5    Wang, H.F.6    Tan, M.S.7    Gao, Q.8    Qin, H.9    Zhang, Y.D.10    Tan, L.11
  • 33
    • 84897093101 scopus 로고    scopus 로고
    • Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52
    • PID: 24667209
    • Jo C, Gundemir S, Pritchard S, Jin YN, Rahman I, Johnson GV (2014) Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52. Nat Commun 5:3496
    • (2014) Nat Commun , vol.5 , pp. 3496
    • Jo, C.1    Gundemir, S.2    Pritchard, S.3    Jin, Y.N.4    Rahman, I.5    Johnson, G.V.6
  • 34
    • 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
    • (2012) Trends Cell Biol , vol.22 , Issue.8 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 35
    • 75249102415 scopus 로고    scopus 로고
    • Does lithium protect against dementia?
    • PID: 20148870
    • Kessing LV, Forman JL, Andersen PK (2010) Does lithium protect against dementia? Bipolar Disord 12(1):87–94
    • (2010) Bipolar Disord , vol.12 , Issue.1 , pp. 87-94
    • Kessing, L.V.1    Forman, J.L.2    Andersen, P.K.3
  • 36
    • 84921443304 scopus 로고    scopus 로고
    • mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation
    • COI: 1:CAS:528:DC%2BC2MXnslGrtQ%3D%3D, PID: 25533187
    • Kim YM, Jung CH, Seo M, Kim EK, Park JM, Bae SS, Kim DH (2015) mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation. Mol Cell 57(2):207–218
    • (2015) Mol Cell , vol.57 , Issue.2 , pp. 207-218
    • Kim, Y.M.1    Jung, C.H.2    Seo, M.3    Kim, E.K.4    Park, J.M.5    Bae, S.S.6    Kim, D.H.7
  • 37
    • 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
    • (2011) Neurobiol Dis , vol.43 , Issue.1 , pp. 29-37
    • Koga, H.1    Cuervo, A.M.2
  • 39
    • 84864471069 scopus 로고    scopus 로고
    • Inhibition of amyloid-beta peptide aggregation rescues the autophagic deficits in the TgCRND8 mouse model of Alzheimer disease
    • COI: 1:CAS:528:DC%2BC38XhtFKms7rL, PID: 22800931
    • Lai AY, McLaurin J (2012) Inhibition of amyloid-beta peptide aggregation rescues the autophagic deficits in the TgCRND8 mouse model of Alzheimer disease. Biochim Biophys Acta 1822(10):1629–1637
    • (2012) Biochim Biophys Acta , vol.1822 , Issue.10 , pp. 1629-1637
    • Lai, A.Y.1    McLaurin, J.2
  • 41
    • 84896465806 scopus 로고    scopus 로고
    • Neuronal autophagy and neurodevelopmental disorders
    • PID: 24167408
    • Lee KM, Hwang SK, Lee JA (2013) Neuronal autophagy and neurodevelopmental disorders. Exp Neurobiol 22(3):133–142
    • (2013) Exp Neurobiol , vol.22 , Issue.3 , pp. 133-142
    • Lee, K.M.1    Hwang, S.K.2    Lee, J.A.3
  • 42
    • 84905111905 scopus 로고    scopus 로고
    • Acid sphingomyelinase modulates the autophagic process by controlling lysosomal biogenesis in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC2cXht1KrtrnE, PID: 25049335
    • Lee JK, Jin HK, Park MH, Kim BR, Lee PH, Nakauchi H, Carter JE, He X, Schuchman EH, Bae JS (2014) Acid sphingomyelinase modulates the autophagic process by controlling lysosomal biogenesis in Alzheimer’s disease. J Exp Med 211(8):1551–1570
    • (2014) J Exp Med , vol.211 , Issue.8 , pp. 1551-1570
    • Lee, J.K.1    Jin, H.K.2    Park, M.H.3    Kim, B.R.4    Lee, P.H.5    Nakauchi, H.6    Carter, J.E.7    He, X.8    Schuchman, E.H.9    Bae, J.S.10
  • 43
    • 84941991917 scopus 로고    scopus 로고
    • Cilostazol upregulates autophagy via SIRT1 activation: reducing amyloid-β peptide and APP-CTFβ levels in neuronal cells
    • PID: 26244661
    • Lee HR, Shin HK, Park SY, Kim HY, Bae SS, Lee WS, Rhim BY, Hong KW, Kim CD (2015) Cilostazol upregulates autophagy via SIRT1 activation: reducing amyloid-β peptide and APP-CTFβ levels in neuronal cells. PLoS ONE 10(8):e0134486
    • (2015) PLoS ONE , vol.10 , Issue.8
    • Lee, H.R.1    Shin, H.K.2    Park, S.Y.3    Kim, H.Y.4    Bae, S.S.5    Lee, W.S.6    Rhim, B.Y.7    Hong, K.W.8    Kim, C.D.9
  • 44
    • 75149129707 scopus 로고    scopus 로고
    • Copper downregulates neprilysin activity through modulation of neprilysin degradation
    • COI: 1:CAS:528:DC%2BC3MXjtV2ru70%3D
    • Li M, Sun M, Liu Y, Yu J, Yang H, Fan D, Chui D (2010) Copper downregulates neprilysin activity through modulation of neprilysin degradation. J Alzheimer’s Dis 19(1):161–169
    • (2010) J Alzheimer’s Dis , vol.19 , Issue.1 , pp. 161-169
    • Li, M.1    Sun, M.2    Liu, Y.3    Yu, J.4    Yang, H.5    Fan, D.6    Chui, D.7
  • 45
    • 84878653069 scopus 로고    scopus 로고
    • Autophagy enhancer carbamazepine alleviates memory deficits and cerebral amyloid-β pathology in a mouse model of Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BC3sXotFagtbc%3D, PID: 23305067
    • Li L, Zhang S, Zhang X, Li T, Tang Y, Liu H, Yang W, Le W (2013) Autophagy enhancer carbamazepine alleviates memory deficits and cerebral amyloid-β pathology in a mouse model of Alzheimer’s disease. Curr Alzheimer Res 10:433–441
    • (2013) Curr Alzheimer Res , vol.10 , pp. 433-441
    • Li, L.1    Zhang, S.2    Zhang, X.3    Li, T.4    Tang, Y.5    Liu, H.6    Yang, W.7    Le, W.8
  • 46
    • 0035680685 scopus 로고    scopus 로고
    • FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and tau filaments in forebrain
    • COI: 1:CAS:528:DC%2BD3MXptFegtbk%3D, PID: 11749044
    • Lim F, Hernández F, Lucas JJ, Gómez-Ramos P, Morán MA, Avila J (2001) FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and tau filaments in forebrain. Mol Cell Neurosci 18(6):702–714
    • (2001) Mol Cell Neurosci , vol.18 , Issue.6 , pp. 702-714
    • Lim, F.1    Hernández, F.2    Lucas, J.J.3    Gómez-Ramos, P.4    Morán, M.A.5    Avila, J.6
  • 47
    • 3442884830 scopus 로고    scopus 로고
    • Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau
    • COI: 1:CAS:528:DC%2BD2cXisV2jsrk%3D, PID: 15044841
    • Lin WL, Lewis J, Yen SH, Hutton M, Dickson DW (2003) Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau. J Neurocytol 32(9):1091–1105
    • (2003) J Neurocytol , vol.32 , Issue.9 , pp. 1091-1105
    • Lin, W.L.1    Lewis, J.2    Yen, S.H.3    Hutton, M.4    Dickson, D.W.5
  • 48
    • 84896301845 scopus 로고    scopus 로고
    • Accumulation of amyloid-like Aβ1-42 in AEL (autophagy–endosomal–lysosomal) vesicles: potential implications for plaque biogenesis
    • Ling D, Magallanes M, Salvaterra PM (2014) Accumulation of amyloid-like Aβ1-42 in AEL (autophagy–endosomal–lysosomal) vesicles: potential implications for plaque biogenesis. ASN Neuro 6(2):95–109
    • (2014) ASN Neuro , vol.6 , Issue.2 , pp. 95-109
    • Ling, D.1    Magallanes, M.2    Salvaterra, P.M.3
  • 50
    • 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, Hu B (2010) Autophagy and protein aggregation after brain ischemia. J Neurochem 115(1):68–78
    • (2010) J Neurochem , vol.115 , Issue.1 , pp. 68-78
    • Liu, C.1    Gao, Y.2    Barrett, J.3    Hu, B.4
  • 52
    • 84904266112 scopus 로고    scopus 로고
    • Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway
    • COI: 1:CAS:528:DC%2BC2cXhtFGqu73M, PID: 25026034
    • Maday S, Holzbaur EL (2014) Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway. Dev Cell 30(1):71–85
    • (2014) Dev Cell , vol.30 , Issue.1 , pp. 71-85
    • Maday, S.1    Holzbaur, E.L.2
  • 53
    • 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 196:407–417
    • (2012) J Cell Biol , vol.196 , pp. 407-417
    • Maday, S.1    Wallace, K.E.2    Holzbaur, E.L.3
  • 54
    • 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, Oddo S (2011) Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits. PLoS ONE 6(9):e25416
    • (2011) PLoS ONE , vol.6 , Issue.9
    • Majumder, S.1    Richardson, A.2    Strong, R.3    Oddo, S.4
  • 55
    • 79954417611 scopus 로고    scopus 로고
    • Autophagy for tissue homeostasis and neuroprotection
    • PID: 21030235
    • Mariño G, Madeo F, Kroemer G (2011) Autophagy for tissue homeostasis and neuroprotection. Curr Opin Cell Biol 23(2):198–206
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 198-206
    • Mariño, G.1    Madeo, F.2    Kroemer, G.3
  • 56
    • 77951228508 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy: Cell death or cell survival?
    • COI: 1:CAS:528:DC%2BC3cXks1Srtb8%3D, PID: 20022734
    • Mazure NM, Pouysségur J (2010) Hypoxia-induced autophagy: Cell death or cell survival? Curr Opin Cell Biol 22(2):177–180
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 177-180
    • Mazure, N.M.1    Pouysségur, J.2
  • 57
    • 41149149615 scopus 로고    scopus 로고
    • Abeta-degrading enzymes in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD1cXmtFGqt7o%3D, PID: 18363935
    • Miners JS, Baig S, Palmer J, Palmer LE, Kehoe PG, Love S (2008) Abeta-degrading enzymes in Alzheimer’s disease. Brain Pathol 18(2):240–252
    • (2008) Brain Pathol , vol.18 , Issue.2 , pp. 240-252
    • Miners, J.S.1    Baig, S.2    Palmer, J.3    Palmer, L.E.4    Kehoe, P.G.5    Love, S.6
  • 58
    • 26444461505 scopus 로고    scopus 로고
    • A(beta) generation in autophagic vacuoles
    • COI: 1:CAS:528:DC%2BD2MXhtFWitrvL, PID: 16216920
    • Mizushima N (2005) A(beta) generation in autophagic vacuoles. J Cell Biol 171(1):15–17
    • (2005) J Cell Biol , vol.171 , Issue.1 , pp. 15-17
    • Mizushima, N.1
  • 59
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • COI: 1:CAS:528:DC%2BD2cXitlGhu7g%3D, PID: 14699058
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y (2004) In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 15(3):1101–1111
    • (2004) Mol Biol Cell , vol.15 , Issue.3 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 62
    • 70349188426 scopus 로고    scopus 로고
    • Sodium valproate: an old drug with new roles
    • COI: 1:CAS:528:DC%2BD1MXhtFyqtbzL, PID: 19762089
    • Nalivaeva NN, Belyaev ND, Turner AJ (2009) Sodium valproate: an old drug with new roles. Trends Pharmacol Sci 30(10):509–514
    • (2009) Trends Pharmacol Sci , vol.30 , Issue.10 , pp. 509-514
    • Nalivaeva, N.N.1    Belyaev, N.D.2    Turner, A.J.3
  • 63
    • 84900015351 scopus 로고    scopus 로고
    • Dual roles for autophagy: degradation and secretion of Alzheimer’s disease Aβ peptide
    • COI: 1:CAS:528:DC%2BC2cXnvV2gsb8%3D, PID: 24711225
    • Nilsson P, Saido TC (2014) Dual roles for autophagy: degradation and secretion of Alzheimer’s disease Aβ peptide. BioEssays 36(6):570–578
    • (2014) BioEssays , vol.36 , Issue.6 , pp. 570-578
    • Nilsson, P.1    Saido, T.C.2
  • 64
    • 84922276427 scopus 로고    scopus 로고
    • Autophagy-related protein 7 deficiency in amyloid β (Aβ) precursor protein transgenic mice decreases Aβ in the multivesicular bodies and induces Aβ accumulation in the Golgi
    • COI: 1:CAS:528:DC%2BC2cXitVSiu7nI, PID: 25433221
    • Nilsson P, Sekiguchi M, Akagi T, Izumi S, Komori T, Hui K, Sörgjerd K, Tanaka M, Saito T, Iwata N, Saido TC (2015) Autophagy-related protein 7 deficiency in amyloid β (Aβ) precursor protein transgenic mice decreases Aβ in the multivesicular bodies and induces Aβ accumulation in the Golgi. Am J Pathol 185:305–313
    • (2015) Am J Pathol , vol.185 , pp. 305-313
    • Nilsson, P.1    Sekiguchi, M.2    Akagi, T.3    Izumi, S.4    Komori, T.5    Hui, K.6    Sörgjerd, K.7    Tanaka, M.8    Saito, T.9    Iwata, N.10    Saido, T.C.11
  • 66
    • 34147210411 scopus 로고    scopus 로고
    • Lithium and risk for Alzheimer’s disease in elderly patients with bipolar disorder
    • PID: 17401045
    • Nunes PV, Forlenza OV, Gattaz WF (2007) Lithium and risk for Alzheimer’s disease in elderly patients with bipolar disorder. Br J Psychiatry 190:359–360
    • (2007) Br J Psychiatry , vol.190 , pp. 359-360
    • Nunes, P.V.1    Forlenza, O.V.2    Gattaz, W.F.3
  • 67
    • 84980052141 scopus 로고    scopus 로고
    • Age-induced reduction of autophagy-related gene expression is associated with onset of Alzheimer’s disease
    • PID: 25628964
    • Omata Y, Lim YM, Akao Y, Tsuda L (2014) Age-induced reduction of autophagy-related gene expression is associated with onset of Alzheimer’s disease. Am J Neurodegener Dis 3(3):134–142
    • (2014) Am J Neurodegener Dis , vol.3 , Issue.3 , pp. 134-142
    • Omata, Y.1    Lim, Y.M.2    Akao, Y.3    Tsuda, L.4
  • 69
    • 85013934254 scopus 로고    scopus 로고
    • Yoon SY: Regulation of amyloid precursor protein processing by its KFERQ motif. BMB Rep (Epub ahead of print
    • Park JS, Kim DH, Yoon SY (2016) Regulation of amyloid precursor protein processing by its KFERQ motif. BMB Rep (Epub ahead of print)
    • (2016) Kim DH
    • Park, J.S.1
  • 70
    • 58149463424 scopus 로고    scopus 로고
    • mTOR-dependent signalling in Alzheimer’s disease
    • COI: 1:CAS:528:DC%2BD1MXhvVGms7Y%3D, PID: 19210753
    • Pei JJ, Hugon J (2008) mTOR-dependent signalling in Alzheimer’s disease. J Cell Mol Med 12(6B):2525–2532
    • (2008) J Cell Mol Med , vol.12 , Issue.6B , pp. 2525-2532
    • Pei, J.J.1    Hugon, J.2
  • 71
    • 84925511980 scopus 로고    scopus 로고
    • Early etiology of Alzheimer’s disease: Tipping the balance toward autophagy or endosomal dysfunction?
    • COI: 1:CAS:528:DC%2BC2MXht12kt7Y%3D, PID: 25556159
    • Peric A, Annaert W (2015) Early etiology of Alzheimer’s disease: Tipping the balance toward autophagy or endosomal dysfunction? Acta Neuropathol 129(3):363–381
    • (2015) Acta Neuropathol , vol.129 , Issue.3 , pp. 363-381
    • Peric, A.1    Annaert, W.2
  • 75
    • 80052303130 scopus 로고    scopus 로고
    • Autophagy and aging
    • COI: 1:CAS:528:DC%2BC3MXhtFakurzM, PID: 21884931
    • Rubinsztein DC, Mariño G, Kroemer G (2011) Autophagy and aging. Cell 146(5):682–695
    • (2011) Cell , vol.146 , Issue.5 , pp. 682-695
    • Rubinsztein, D.C.1    Mariño, G.2    Kroemer, G.3
  • 78
    • 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(17):4263–4270
    • (2008) FEBS J , vol.275 , Issue.17 , pp. 4263-4270
    • Sarkar, S.1    Rubinsztein, D.C.2
  • 79
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, 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, Tunnacliffe A, Rubinsztein DC (2007a) Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 282(8):5641–5652
    • (2007) J Biol Chem , vol.282 , Issue.8 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 81
    • 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
    • (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
  • 82
    • 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, Shorer H, Gil L, Elazar Z (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26(7):1749–1760
    • (2007) EMBO J , vol.26 , Issue.7 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 84
    • 84858336588 scopus 로고    scopus 로고
    • Aβ-induced formation of autophagosomes is mediated by RAGE-CaMKKβ-AMPK signaling
    • Son SM, Jung ES, Shin HJ, Byun J, Mook-Jung I (2012) Aβ-induced formation of autophagosomes is mediated by RAGE-CaMKKβ-AMPK signaling. Neurobiol Aging 33(5):1006.e11–1006.e23
    • (2012) Neurobiol Aging , vol.33 , Issue.5 , pp. 1006.e11-1006.e23
    • Son, S.M.1    Jung, E.S.2    Shin, H.J.3    Byun, J.4    Mook-Jung, I.5
  • 85
    • 84879211357 scopus 로고    scopus 로고
    • Molecular mechanisms of neurodegeneration mediated by dysfunctional subcellular organelles in transmissible spongiform encephalopathies
    • COI: 1:CAS:528:DC%2BC3sXos12nsro%3D
    • Song Z, Zhao D, Yang L (2013) Molecular mechanisms of neurodegeneration mediated by dysfunctional subcellular organelles in transmissible spongiform encephalopathies. Acta Biochim Biophys Sin (Shanghai) 45(6):452–464
    • (2013) Acta Biochim Biophys Sin (Shanghai) , vol.45 , Issue.6 , pp. 452-464
    • Song, Z.1    Zhao, D.2    Yang, L.3
  • 86
    • 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
    • (2010) PLoS ONE , vol.5 , Issue.4
    • 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
  • 87
    • 0027364862 scopus 로고
    • Identification and distribution of axonal dystrophic neuritis in Alzheimer’s disease
    • COI: 1:STN:280:DyaK2c7gtFeqtA%3D%3D, PID: 8275305
    • Su JH, Cummings BJ, Cotman CW (1993) Identification and distribution of axonal dystrophic neuritis in Alzheimer’s disease. Brain Res 625(2):228–237
    • (1993) Brain Res , vol.625 , Issue.2 , pp. 228-237
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 89
    • 0014193263 scopus 로고
    • Fine structural localization of acid phosphatase in senile plaques in Alzheimer’s presenile dementia
    • COI: 1:STN:280:DyaF2s3kslanuw%3D%3D, PID: 6039977
    • Suzuki K, Terry RD (1967) Fine structural localization of acid phosphatase in senile plaques in Alzheimer’s presenile dementia. Acta Neuropathol 8:276–284
    • (1967) Acta Neuropathol , vol.8 , pp. 276-284
    • Suzuki, K.1    Terry, R.D.2
  • 90
    • 84858642778 scopus 로고    scopus 로고
    • Phase III CONCERT trial of latrepirdine. Negative results
    • Sweetlove M (2012) Phase III CONCERT trial of latrepirdine. Negative results. Pharm Med 26(2):113–115
    • (2012) Pharm Med , vol.26 , Issue.2 , pp. 113-115
    • Sweetlove, M.1
  • 91
    • 0038755598 scopus 로고    scopus 로고
    • Genetic studies in Alzheimer’s disease
    • Tang YP (2003) Genetic studies in Alzheimer’s disease. Dialog Clin Neurosci 5(1):17–26
    • (2003) Dialog Clin Neurosci , vol.5 , Issue.1 , pp. 17-26
    • Tang, Y.P.1
  • 92
    • 84898614697 scopus 로고    scopus 로고
    • The convergence of endosomal and autophagosomal pathways: implications for APP-CTF degradation
    • COI: 1:CAS:528:DC%2BC2cXitVOhtbvP, PID: 24447917
    • Tian Y, Chang JC, Greengard P, Flajolet M (2014) The convergence of endosomal and autophagosomal pathways: implications for APP-CTF degradation. Autophagy 10(4):694–696
    • (2014) Autophagy , vol.10 , Issue.4 , pp. 694-696
    • Tian, Y.1    Chang, J.C.2    Greengard, P.3    Flajolet, M.4
  • 97
    • 84949988536 scopus 로고    scopus 로고
    • Autophagy facilitates lung adenocarcinoma resistance to cisplatin treatment by activation of AMPK/mTOR signaling pathway
    • PID: 26715839
    • Wu T, Wang MC, Jing L, Liu ZY, Guo H, Liu Y, Bai YY, Cheng YZ, Nan KJ, Liang X (2015) Autophagy facilitates lung adenocarcinoma resistance to cisplatin treatment by activation of AMPK/mTOR signaling pathway. Drug Des Devel Ther 9:6421–6431
    • (2015) Drug Des Devel Ther , vol.9 , pp. 6421-6431
    • Wu, T.1    Wang, M.C.2    Jing, L.3    Liu, Z.Y.4    Guo, H.5    Liu, Y.6    Bai, Y.Y.7    Cheng, Y.Z.8    Nan, K.J.9    Liang, X.10
  • 98
    • 84947555603 scopus 로고    scopus 로고
    • Progressive endolysosomal deficits impair autophagic clearance beginning at early asymptomatic stages in fALS mice
    • COI: 1:CAS:528:DC%2BC2MXhvVWqtbbN, PID: 26290961
    • Xie Y, Zhou B, Lin MY, Sheng ZH (2015) Progressive endolysosomal deficits impair autophagic clearance beginning at early asymptomatic stages in fALS mice. Autophagy 11(10):1934–1936
    • (2015) Autophagy , vol.11 , Issue.10 , pp. 1934-1936
    • Xie, Y.1    Zhou, B.2    Lin, M.Y.3    Sheng, Z.H.4
  • 101
    • 77954561084 scopus 로고    scopus 로고
    • Magnesium modulates amyloid-beta protein precursor trafficking and processing
    • COI: 1:CAS:528:DC%2BC3cXovFKgtr4%3D, PID: 20413885
    • Yu J, Sun M, Chen Z, Lu J, Liu Y, Zhou L, Xu X, Fan D, Chui D (2010) Magnesium modulates amyloid-beta protein precursor trafficking and processing. J Alzheimers Dis 20(4):1091–1106
    • (2010) J Alzheimers Dis , vol.20 , Issue.4 , pp. 1091-1106
    • Yu, J.1    Sun, M.2    Chen, Z.3    Lu, J.4    Liu, Y.5    Zhou, L.6    Xu, X.7    Fan, D.8    Chui, D.9
  • 103
    • 84946748901 scopus 로고    scopus 로고
    • TFEB participates in the Aβ-induced pathogenesis of Alzheimer’s disease by regulating the autophagy-lysosome pathway
    • COI: 1:CAS:528:DC%2BC2MXhslOks7vI, PID: 26368054
    • Zhang YD, Zhao JJ (2015) TFEB participates in the Aβ-induced pathogenesis of Alzheimer’s disease by regulating the autophagy-lysosome pathway. DNA Cell Biol 34(11):661–668
    • (2015) DNA Cell Biol , vol.34 , Issue.11 , pp. 661-668
    • Zhang, Y.D.1    Zhao, J.J.2
  • 104
    • 80053087596 scopus 로고    scopus 로고
    • APP and APLP1 are degraded through autophagy in response to proteasome inhibition in neuronal cells
    • COI: 1:CAS:528:DC%2BC3MXntlahurw%3D, PID: 21626267
    • Zhou F, van Laar T, Huang H, Zhang L (2011) APP and APLP1 are degraded through autophagy in response to proteasome inhibition in neuronal cells. Protein Cell 2(5):377–383
    • (2011) Protein Cell , vol.2 , Issue.5 , pp. 377-383
    • Zhou, F.1    van Laar, T.2    Huang, H.3    Zhang, L.4
  • 105
    • 80555143078 scopus 로고    scopus 로고
    • mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • COI: 1:CAS:528:DC%2BC3MXhtlyqu7jE, PID: 22053050
    • Zoncu R, Bar-Peled L, Efeyan A, Wang S, Sancak Y, Sabatini DM (2011) mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 334(6056):678–683
    • (2011) Science , vol.334 , Issue.6056 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6


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