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Volumn 12, Issue 12, 2016, Pages 2467-2483

Autophagy flux in CA1 neurons of Alzheimer hippocampus: Increased induction overburdens failing lysosomes to propel neuritic dystrophy

Author keywords

Alzheimer disease; autophagosomes; autophagy; CA1 pyramidal neurons; dystrophic neurites; hippocampus; lysosomes; MTOR; TFE3; TFEB

Indexed keywords

AUTOPHAGY PROTEIN 12; AUTOPHAGY PROTEIN 3; AUTOPHAGY PROTEIN 5; AUTOPHAGY PROTEIN 8; CATHEPSIN D; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; MESSENGER RNA; MICROPHTHALMIA ASSOCIATED TRANSCRIPTION FACTOR; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN P62; RAB PROTEIN; RAB4A PROTEIN; RAB5A PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR BINDING TO IGHM ENHANCER 3 PROTEIN; TRANSCRIPTION FACTOR EB; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG; BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; LIGHT CHAIN 3, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; TFE3 PROTEIN, HUMAN; TFEB PROTEIN, HUMAN;

EID: 84994128006     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2016.1239003     Document Type: Article
Times cited : (255)

References (98)
  • 1
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • 23921753
    • Nixon RA. The role of autophagy in neurodegenerative disease. Nat Med 2013; 19:983-97; PMID:23921753; http://dx.doi.org/10.1038/nm.3232
    • (2013) Nat Med , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 2
    • 84863482530 scopus 로고    scopus 로고
    • Lysosomal function and dysfunction: mechanism and disease
    • 22098160
    • Boya P. Lysosomal function and dysfunction:mechanism and disease. Antioxid Redox Signal 2012; 17:766-74; PMID:22098160; http://dx.doi.org/10.1089/ars.2011.4405
    • (2012) Antioxid Redox Signal , vol.17 , pp. 766-774
    • Boya, P.1
  • 3
    • 79954425069 scopus 로고    scopus 로고
    • Protein misfolding disorders and macroautophagy
    • 21087849
    • Menzies FM, Moreau K, Rubinsztein DC. Protein misfolding disorders and macroautophagy. Curr Opin Cell Biol 2011; 23:190-7; PMID:21087849; http://dx.doi.org/10.1016/j.ceb.2010.10.010
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 190-197
    • Menzies, F.M.1    Moreau, K.2    Rubinsztein, D.C.3
  • 4
    • 38949099761 scopus 로고    scopus 로고
    • Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
    • 18059160
    • Simonsen A, Cumming RC, Brech A, Isakson P, Schubert DR, Finley KD. Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila. Autophagy 2008; 4:176-84; PMID:18059160; http://dx.doi.org/10.4161/auto.5269
    • (2008) Autophagy , vol.4 , pp. 176-184
    • Simonsen, A.1    Cumming, R.C.2    Brech, A.3    Isakson, P.4    Schubert, D.R.5    Finley, K.D.6
  • 5
    • 77956420489 scopus 로고    scopus 로고
    • Can autophagy promote longevity?
    • 20811357
    • Madeo F, Tavernarakis N, Kroemer G. Can autophagy promote longevity? Nat Cell Biol 2010; 12:842-6; PMID:20811357; http://dx.doi.org/10.1038/ncb0910-842
    • (2010) Nat Cell Biol , vol.12 , pp. 842-846
    • Madeo, F.1    Tavernarakis, N.2    Kroemer, G.3
  • 6
    • 84899766412 scopus 로고    scopus 로고
    • Identification of autophagy as a longevity-assurance mechanism in the aging model Podospora anserina
    • 24584154
    • Knuppertz L, Hamann A, Pampaloni F, Stelzer E, Osiewacz HD. Identification of autophagy as a longevity-assurance mechanism in the aging model Podospora anserina. Autophagy 2014; 10:822-34; PMID:24584154; http://dx.doi.org/10.4161/auto.28148
    • (2014) Autophagy , vol.10 , pp. 822-834
    • Knuppertz, L.1    Hamann, A.2    Pampaloni, F.3    Stelzer, E.4    Osiewacz, H.D.5
  • 8
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • 20811353
    • Yang Z, Klionsky DJ. Eaten alive:a history of macroautophagy. Nat Cell Biol 2010; 12:814-22; PMID:20811353; http://dx.doi.org/10.1038/ncb0910-814
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 9
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: a continuum from development to late age
    • 18497567
    • Nixon RA, Yang DS, Lee JH. Neurodegenerative lysosomal disorders:a continuum from development to late age. Autophagy 2008; 4:590-9; PMID:18497567; http://dx.doi.org/10.4161/auto.6259
    • (2008) Autophagy , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 11
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • 18552835
    • Liang C, Lee JS, Inn KS, Gack MU, Li Q, Roberts EA, Vergne I, Deretic V, Feng P, Akazawa C, et al. Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat Cell Biol 2008; 10:776-87; PMID:18552835; http://dx.doi.org/10.1038/ncb1740
    • (2008) Nat Cell Biol , vol.10 , pp. 776-787
    • Liang, C.1    Lee, J.S.2    Inn, K.S.3    Gack, M.U.4    Li, Q.5    Roberts, E.A.6    Vergne, I.7    Deretic, V.8    Feng, P.9    Akazawa, C.10
  • 12
    • 84876991846 scopus 로고    scopus 로고
    • Autophagosome formation: tracing the source
    • 23639440
    • Bernard A, Klionsky DJ. Autophagosome formation:tracing the source. Dev Cell 2013; 25:116-7; PMID:23639440; http://dx.doi.org/10.1016/j.devcel.2013.04.004
    • (2013) Dev Cell , vol.25 , pp. 116-117
    • Bernard, A.1    Klionsky, D.J.2
  • 13
    • 84865251228 scopus 로고    scopus 로고
    • The autophagy-related protein kinase Atg1 interacts with the ubiquitin-like protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation
    • 22778255
    • Nakatogawa H, Ohbayashi S, Sakoh-Nakatogawa M, Kakuta S, Suzuki SW, Kirisako H, Kondo-Kakuta C, Noda NN, Yamamoto H, Ohsumi Y. The autophagy-related protein kinase Atg1 interacts with the ubiquitin-like protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation. J Biol Chem 2012; 287:28503-7; PMID:22778255; http://dx.doi.org/10.1074/jbc.C112.387514
    • (2012) J Biol Chem , vol.287 , pp. 28503-28507
    • Nakatogawa, H.1    Ohbayashi, S.2    Sakoh-Nakatogawa, M.3    Kakuta, S.4    Suzuki, S.W.5    Kirisako, H.6    Kondo-Kakuta, C.7    Noda, N.N.8    Yamamoto, H.9    Ohsumi, Y.10
  • 14
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • 17632063
    • Nakatogawa H, Ichimura Y, Ohsumi Y. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 2007; 130:165-78; PMID:17632063; http://dx.doi.org/10.1016/j.cell.2007.05.021
    • (2007) Cell , vol.130 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 15
    • 84891461247 scopus 로고    scopus 로고
    • The LC3 interactome at a glance
    • 24345374
    • Wild P, McEwan DG, Dikic I. The LC3 interactome at a glance. J Cell Sci 2014; 127:3-9; PMID:24345374; http://dx.doi.org/10.1242/jcs.140426
    • (2014) J Cell Sci , vol.127 , pp. 3-9
    • Wild, P.1    McEwan, D.G.2    Dikic, I.3
  • 17
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • 22053050
    • Zoncu R, Bar-Peled L, Efeyan A, Wang S, Sancak Y, Sabatini DM. MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 2011; 334:678-83; PMID:22053050; http://dx.doi.org/10.1126/science.1207056
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6
  • 18
    • 48649085816 scopus 로고    scopus 로고
    • Regulation of TORC1 by Rag GTPases in nutrient response
    • 18604198
    • Kim E, Goraksha-Hicks P, Li L, Neufeld TP, Guan KL. Regulation of TORC1 by Rag GTPases in nutrient response. Nat Cell Biol 2008; 10:935-45; PMID:18604198; http://dx.doi.org/10.1038/ncb1753
    • (2008) Nat Cell Biol , vol.10 , pp. 935-945
    • Kim, E.1    Goraksha-Hicks, P.2    Li, L.3    Neufeld, T.P.4    Guan, K.L.5
  • 22
    • 80052716148 scopus 로고    scopus 로고
    • Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways
    • 21752829
    • Palmieri M, Impey S, Kang H, di Ronza A, Pelz C, Sardiello M, Ballabio A. Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways. Hum Mol Genet 2011; 20:3852-66; PMID:21752829; http://dx.doi.org/10.1093/hmg/ddr306
    • (2011) Hum Mol Genet , vol.20 , pp. 3852-3866
    • Palmieri, M.1    Impey, S.2    Kang, H.3    di Ronza, A.4    Pelz, C.5    Sardiello, M.6    Ballabio, A.7
  • 23
    • 84897414264 scopus 로고    scopus 로고
    • FOXO transcription factors: key regulators of cellular quality control
    • 24630600
    • Webb AE, Brunet A. FOXO transcription factors:key regulators of cellular quality control. Trends Biochem Sci 2014; 39:159-69; PMID:24630600; http://dx.doi.org/10.1016/j.tibs.2014.02.003
    • (2014) Trends Biochem Sci , vol.39 , pp. 159-169
    • Webb, A.E.1    Brunet, A.2
  • 24
    • 79955969705 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer's disease–locating the primary defect
    • 21296668
    • Nixon RA, Yang DS. Autophagy failure in Alzheimer's disease–locating the primary defect. Neurobiol Dis 2011; 43:38-45; PMID:21296668; http://dx.doi.org/10.1016/j.nbd.2011.01.021
    • (2011) Neurobiol Dis , vol.43 , pp. 38-45
    • Nixon, R.A.1    Yang, D.S.2
  • 25
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • 20541250
    • Lee JH, Yu WH, Kumar A, Lee S, Mohan PS, Peterhoff CM, Wolfe DM, Martinez-Vicente M, Massey AC, Sovak G, et al. Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell 2010; 141:1146-58; PMID:20541250; http://dx.doi.org/10.1016/j.cell.2010.05.008
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1    Yu, W.H.2    Kumar, A.3    Lee, S.4    Mohan, P.S.5    Peterhoff, C.M.6    Wolfe, D.M.7    Martinez-Vicente, M.8    Massey, A.C.9    Sovak, G.10
  • 26
    • 14844303381 scopus 로고    scopus 로고
    • Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study
    • 15751225
    • Nixon RA, Wegiel J, Kumar A, Yu WH, Peterhoff C, Cataldo A, Cuervo AM. Extensive involvement of autophagy in Alzheimer disease:an immuno-electron microscopy study. J Neuropathol Exp Neurol 2005; 64:113-22; PMID:15751225; http://dx.doi.org/10.1093/jnen/64.2.113
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 113-122
    • Nixon, R.A.1    Wegiel, J.2    Kumar, A.3    Yu, W.H.4    Peterhoff, C.5    Cataldo, A.6    Cuervo, A.M.7
  • 27
    • 0014193263 scopus 로고
    • Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia
    • 6039977
    • Suzuki K, Terry RD. Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia. Acta Neuropathol 1967; 8:276-84; PMID:6039977; http://dx.doi.org/10.1007/BF00688828
    • (1967) Acta Neuropathol , vol.8 , pp. 276-284
    • Suzuki, K.1    Terry, R.D.2
  • 29
    • 0024280247 scopus 로고
    • Alzheimer's disease. Paired helical filaments and the cytoskeleton
    • 3138546
    • Anderton BH. Alzheimer's disease. Paired helical filaments and the cytoskeleton. Nature 1988; 335:497-8; PMID:3138546; http://dx.doi.org/10.1038/335497a0
    • (1988) Nature , vol.335 , pp. 497-498
    • Anderton, B.H.1
  • 30
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • 6375662
    • Glenner GG, Wong CW. Alzheimer's disease:initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984; 120:885-90; PMID:6375662; http://dx.doi.org/10.1016/S0006-291X(84)80190-4
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 31
    • 84940796652 scopus 로고    scopus 로고
    • Presenilin 1 Maintains Lysosomal Ca(2+) Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification
    • 26299959
    • Lee JH, McBrayer MK, Wolfe DM, Haslett LJ, Kumar A, Sato Y, Lie PP, Mohan P, Coffey EE, Kompella U, et al. Presenilin 1 Maintains Lysosomal Ca(2+) Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification. Cell Rep 2015; 12:1430-44; PMID:26299959; http://dx.doi.org/10.1016/j.celrep.2015.07.050
    • (2015) Cell Rep , vol.12 , pp. 1430-1444
    • Lee, J.H.1    McBrayer, M.K.2    Wolfe, D.M.3    Haslett, L.J.4    Kumar, A.5    Sato, Y.6    Lie, P.P.7    Mohan, P.8    Coffey, E.E.9    Kompella, U.10
  • 32
    • 79959979604 scopus 로고    scopus 로고
    • Therapeutic effects of remediating autophagy failure in a mouse model of Alzheimer disease by enhancing lysosomal proteolysis
    • 21464620
    • Yang DS, Stavrides P, Mohan PS, Kaushik S, Kumar A, Ohno M, Schmidt SD, Wesson DW, Bandyopadhyay U, Jiang Y, et al. Therapeutic effects of remediating autophagy failure in a mouse model of Alzheimer disease by enhancing lysosomal proteolysis. Autophagy 2011; 7:788-9; PMID:21464620; http://dx.doi.org/10.4161/auto.7.7.15596
    • (2011) Autophagy , vol.7 , pp. 788-789
    • Yang, D.S.1    Stavrides, P.2    Mohan, P.S.3    Kaushik, S.4    Kumar, A.5    Ohno, M.6    Schmidt, S.D.7    Wesson, D.W.8    Bandyopadhyay, U.9    Jiang, Y.10
  • 33
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease
    • 18596167
    • Boland B, Kumar A, Lee S, Platt FM, Wegiel J, Yu WH, Nixon RA. Autophagy induction and autophagosome clearance in neurons:relationship to autophagic pathology in Alzheimer's disease. J Neurosci 2008; 28:6926-37; PMID:18596167; http://dx.doi.org/10.1523/JNEUROSCI.0800-08.2008
    • (2008) J Neurosci , vol.28 , 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
  • 35
    • 84928012290 scopus 로고    scopus 로고
    • Alteration of MTOR signaling occurs early in the progression of Alzheimer disease (AD): analysis of brain from subjects with pre-clinical AD, amnestic mild cognitive impairment and late-stage AD
    • 25645581
    • Tramutola A, Triplett JC, Di Domenico F, Niedowicz DM, Murphy MP, Coccia R, Perluigi M, Butterfield DA. Alteration of MTOR signaling occurs early in the progression of Alzheimer disease (AD):analysis of brain from subjects with pre-clinical AD, amnestic mild cognitive impairment and late-stage AD. J Neurochem 2015; 133:739-49; PMID:25645581; http://dx.doi.org/10.1111/jnc.13037
    • (2015) J Neurochem , vol.133 , pp. 739-749
    • Tramutola, A.1    Triplett, J.C.2    Di Domenico, F.3    Niedowicz, D.M.4    Murphy, M.P.5    Coccia, R.6    Perluigi, M.7    Butterfield, D.A.8
  • 36
    • 77956274584 scopus 로고    scopus 로고
    • Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer's disease
    • 20660724
    • Lipinski MM, Zheng B, Lu T, Yan Z, Py BF, Ng A, Xavier RJ, Li C, Yankner BA, Scherzer CR, et al. Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer's disease. Proc Natl Acad Sci U S A 2010; 107:14164-9; PMID:20660724; http://dx.doi.org/10.1073/pnas.1009485107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14164-14169
    • Lipinski, M.M.1    Zheng, B.2    Lu, T.3    Yan, Z.4    Py, B.F.5    Ng, A.6    Xavier, R.J.7    Li, C.8    Yankner, B.A.9    Scherzer, C.R.10
  • 37
    • 84889587250 scopus 로고    scopus 로고
    • Differential activation of MTOR complex 1 signaling in human brain with mild to severe Alzheimer's disease
    • 23979023
    • Sun YX, Ji X, Mao X, Xie L, Jia J, Galvan V, Greenberg DA, Jin K. Differential activation of MTOR complex 1 signaling in human brain with mild to severe Alzheimer's disease. J Alzheimers Dis 2014; 38:437-44; PMID:23979023
    • (2014) J Alzheimers Dis , vol.38 , pp. 437-444
    • Sun, Y.X.1    Ji, X.2    Mao, X.3    Xie, L.4    Jia, J.5    Galvan, V.6    Greenberg, D.A.7    Jin, K.8
  • 38
    • 78049427173 scopus 로고    scopus 로고
    • Microarray analysis of hippocampal CA1 neurons implicates early endosomal dysfunction during Alzheimer's disease progression
    • 20655510
    • Ginsberg SD, Alldred MJ, Counts SE, Cataldo AM, Neve RL, Jiang Y, Wuu J, Chao MV, Mufson EJ, Nixon RA, et al. Microarray analysis of hippocampal CA1 neurons implicates early endosomal dysfunction during Alzheimer's disease progression. Biol Psychiatry 2010; 68:885-93; PMID:20655510; http://dx.doi.org/10.1016/j.biopsych.2010.05.030
    • (2010) Biol Psychiatry , vol.68 , pp. 885-893
    • Ginsberg, S.D.1    Alldred, M.J.2    Counts, S.E.3    Cataldo, A.M.4    Neve, R.L.5    Jiang, Y.6    Wuu, J.7    Chao, M.V.8    Mufson, E.J.9    Nixon, R.A.10
  • 39
    • 84855798135 scopus 로고    scopus 로고
    • Microarray analysis of CA1 pyramidal neurons in a mouse model of tauopathy reveals progressive synaptic dysfunction
    • 22079237
    • Alldred MJ, Duff KE, Ginsberg SD. Microarray analysis of CA1 pyramidal neurons in a mouse model of tauopathy reveals progressive synaptic dysfunction. Neurobiol Dis 2012; 45:751-62; PMID:22079237; http://dx.doi.org/10.1016/j.nbd.2011.10.022
    • (2012) Neurobiol Dis , vol.45 , pp. 751-762
    • Alldred, M.J.1    Duff, K.E.2    Ginsberg, S.D.3
  • 40
    • 81955162957 scopus 로고    scopus 로고
    • Gene expression levels assessed by CA1 pyramidal neuron and regional hippocampal dissections in Alzheimer's disease
    • 21821124
    • Ginsberg SD, Alldred MJ, Che S. Gene expression levels assessed by CA1 pyramidal neuron and regional hippocampal dissections in Alzheimer's disease. Neurobiol Dis 2012; 45:99-107; PMID:21821124; http://dx.doi.org/10.1016/j.nbd.2011.07.013
    • (2012) Neurobiol Dis , vol.45 , pp. 99-107
    • Ginsberg, S.D.1    Alldred, M.J.2    Che, S.3
  • 43
    • 84896762116 scopus 로고    scopus 로고
    • HRES-1/Rab4 promotes the formation of LC3(+) autophagosomes and the accumulation of mitochondria during autophagy
    • 24404161
    • Talaber G, Miklossy G, Oaks Z, Liu Y, Tooze SA, Chudakov DM, Banki K, Perl A. HRES-1/Rab4 promotes the formation of LC3(+) autophagosomes and the accumulation of mitochondria during autophagy. PLoS One 2014; 9:e84392; PMID:24404161; http://dx.doi.org/10.1371/journal.pone.0084392
    • (2014) PLoS One , vol.9 , pp. e84392
    • Talaber, G.1    Miklossy, G.2    Oaks, Z.3    Liu, Y.4    Tooze, S.A.5    Chudakov, D.M.6    Banki, K.7    Perl, A.8
  • 44
    • 84893823338 scopus 로고    scopus 로고
    • Regulation of autophagy by the Rab GTPase network
    • 24440914
    • Ao X, Zou L, Wu Y. Regulation of autophagy by the Rab GTPase network. Cell Death Differ 2014; 21:348-58; PMID:24440914; http://dx.doi.org/10.1038/cdd.2013.187
    • (2014) Cell Death Differ , vol.21 , pp. 348-358
    • Ao, X.1    Zou, L.2    Wu, Y.3
  • 45
    • 84891014899 scopus 로고    scopus 로고
    • The return of the nucleus: transcriptional and epigenetic control of autophagy
    • 24326622
    • Fullgrabe J, Klionsky DJ, Joseph B. The return of the nucleus:transcriptional and epigenetic control of autophagy. Nat Rev Mol Cell Biol 2014; 15:65-74; PMID:24326622; http://dx.doi.org/10.1038/nrm3716
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 65-74
    • Fullgrabe, J.1    Klionsky, D.J.2    Joseph, B.3
  • 46
    • 0030045552 scopus 로고    scopus 로고
    • Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease
    • 8613784
    • Cataldo AM, Hamilton DJ, Barnett JL, Paskevich PA, Nixon RA. Properties of the endosomal-lysosomal system in the human central nervous system:disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J Neurosci 1996; 16:186-99; PMID:8613784
    • (1996) J Neurosci , vol.16 , pp. 186-199
    • Cataldo, A.M.1    Hamilton, D.J.2    Barnett, J.L.3    Paskevich, P.A.4    Nixon, R.A.5
  • 47
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system
    • 7695914
    • Cataldo AM, Barnett JL, Berman SA, Li J, Quarless S, Bursztajn S, Lippa C, Nixon RA. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain:evidence for early up-regulation of the endosomal-lysosomal system. Neuron 1995; 14:671-80; PMID:7695914; http://dx.doi.org/10.1016/0896-6273(95)90324-0
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 48
    • 0033933738 scopus 로고    scopus 로고
    • Expression profile of transcripts in Alzheimer's disease tangle-bearing CA1 neurons
    • 10894219
    • Ginsberg SD, Hemby SE, Lee VM, Eberwine JH, Trojanowski JQ. Expression profile of transcripts in Alzheimer's disease tangle-bearing CA1 neurons. Ann Neurol 2000; 48:77-87; PMID:10894219; http://dx.doi.org/10.1002/1531-8249(200007)48:1%3c77::AID-ANA12%3e3.0.CO;2-A
    • (2000) Ann Neurol , vol.48 , pp. 77-87
    • Ginsberg, S.D.1    Hemby, S.E.2    Lee, V.M.3    Eberwine, J.H.4    Trojanowski, J.Q.5
  • 49
    • 71149108056 scopus 로고    scopus 로고
    • Correlation of mRNA and protein in complex biological samples
    • 19850042
    • Maier T, Guell M, Serrano L. Correlation of mRNA and protein in complex biological samples. FEBS Lett 2009; 583:3966-73; PMID:19850042; http://dx.doi.org/10.1016/j.febslet.2009.10.036
    • (2009) FEBS Lett , vol.583 , pp. 3966-3973
    • Maier, T.1    Guell, M.2    Serrano, L.3
  • 50
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • 18032783
    • Nixon RA. Autophagy, amyloidogenesis and Alzheimer disease. J Cell Sci 2007; 120:4081-91; PMID:18032783; http://dx.doi.org/10.1242/jcs.019265
    • (2007) J Cell Sci , vol.120 , pp. 4081-4091
    • Nixon, R.A.1
  • 51
    • 79957663035 scopus 로고    scopus 로고
    • Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy
    • NOT_FOUND
    • Lee S, Sato Y, Nixon RA. Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy. J Neurosci 2010; 31:7817-30; PMID:NOT_FOUND; http://dx.doi.org/10.1523/JNEUROSCI.6412-10.2011
    • (2010) J Neurosci , vol.31 , pp. 7817-7830
    • Lee, S.1    Sato, Y.2    Nixon, R.A.3
  • 52
    • 0025327731 scopus 로고
    • Unbiased stereological estimation of the number of neurons in the human hippocampus
    • 2358525
    • West MJ, Gundersen HJ. Unbiased stereological estimation of the number of neurons in the human hippocampus. J Comp Neurol 1990; 296:1-22; PMID:2358525; http://dx.doi.org/10.1002/cne.902960102
    • (1990) J Comp Neurol , vol.296 , pp. 1-22
    • West, M.J.1    Gundersen, H.J.2
  • 53
    • 0028122463 scopus 로고
    • Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease
    • 7916070
    • West MJ, Coleman PD, Flood DG, Troncoso JC. Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease. Lancet 1994; 344:769-72; PMID:7916070; http://dx.doi.org/10.1016/S0140-6736(94)92338-8
    • (1994) Lancet , vol.344 , pp. 769-772
    • West, M.J.1    Coleman, P.D.2    Flood, D.G.3    Troncoso, J.C.4
  • 54
    • 84862667837 scopus 로고    scopus 로고
    • Abeta toxicity in Alzheimer's disease
    • 22415442
    • Cavallucci V, D'Amelio M, Cecconi F. Abeta toxicity in Alzheimer's disease. Mol Neurobiol 2012; 45:366-78; PMID:22415442; http://dx.doi.org/10.1007/s12035-012-8251-3
    • (2012) Mol Neurobiol , vol.45 , pp. 366-378
    • Cavallucci, V.1    D'Amelio, M.2    Cecconi, F.3
  • 55
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • 19131956
    • Huang da W, Sherman BT, Lempicki RA. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 2009; 4:44-57; PMID:19131956; http://dx.doi.org/10.1038/nprot.2008.211
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 57
    • 84893055506 scopus 로고    scopus 로고
    • The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis, and clearance of cellular debris
    • 24448649
    • Martina JA, Diab HI, Lishu L, Jeong AL, Patange S, Raben N, Puertollano R. The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis, and clearance of cellular debris. Sci Signal 2014; 7:ra9; PMID:24448649; http://dx.doi.org/10.1126/scisignal.2004754
    • (2014) Sci Signal , vol.7 , pp. ra9
    • Martina, J.A.1    Diab, H.I.2    Lishu, L.3    Jeong, A.L.4    Patange, S.5    Raben, N.6    Puertollano, R.7
  • 58
    • 84939820927 scopus 로고    scopus 로고
    • MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5
    • 26240184
    • Nezich CL, Wang C, Fogel AI, Youle RJ. MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5. J Cell Biol 2015; 210:435-50; PMID:26240184; http://dx.doi.org/10.1083/jcb.201501002
    • (2015) J Cell Biol , vol.210 , pp. 435-450
    • Nezich, C.L.1    Wang, C.2    Fogel, A.I.3    Youle, R.J.4
  • 60
    • 84887909793 scopus 로고    scopus 로고
    • Autophagic/lysosomal dysfunction in Alzheimer's disease
    • 24171818
    • Orr ME, Oddo S. Autophagic/lysosomal dysfunction in Alzheimer's disease. Alzheimers Res Ther 2013; 5:53; PMID:24171818; http://dx.doi.org/10.1186/alzrt217
    • (2013) Alzheimers Res Ther , vol.5 , pp. 53
    • Orr, M.E.1    Oddo, S.2
  • 61
    • 85015635987 scopus 로고    scopus 로고
    • Autophagic and lysosomal defects in human tauopathies: analysis of post-mortem brain from patients with familial Alzheimer disease, corticobasal degeneration and progressive supranuclear palsy
    • 26936765
    • Piras A, Collin L, Gruninger F, Graff C, Ronnback A. Autophagic and lysosomal defects in human tauopathies:analysis of post-mortem brain from patients with familial Alzheimer disease, corticobasal degeneration and progressive supranuclear palsy. Acta Neuropathol Commun 2016; 4:22; PMID:26936765; http://dx.doi.org/10.1186/s40478-016-0292-9
    • (2016) Acta Neuropathol Commun , vol.4 , pp. 22
    • Piras, A.1    Collin, L.2    Gruninger, F.3    Graff, C.4    Ronnback, A.5
  • 63
    • 21344459656 scopus 로고    scopus 로고
    • MTOR/p70S6k signalling alteration by Abeta exposure as well as in APP-PS1 transgenic models and in patients with Alzheimer's disease
    • 15953364
    • Lafay-Chebassier C, Paccalin M, Page G, Barc-Pain S, Perault-Pochat MC, Gil R, Pradier L, Hugon J. MTOR/p70S6k signalling alteration by Abeta exposure as well as in APP-PS1 transgenic models and in patients with Alzheimer's disease. J Neurochem 2005; 94:215-25; PMID:15953364; http://dx.doi.org/10.1111/j.1471-4159.2005.03187.x
    • (2005) J Neurochem , vol.94 , pp. 215-225
    • Lafay-Chebassier, C.1    Paccalin, M.2    Page, G.3    Barc-Pain, S.4    Perault-Pochat, M.C.5    Gil, R.6    Pradier, L.7    Hugon, J.8
  • 64
    • 77951227122 scopus 로고    scopus 로고
    • Molecular interplay between mammalian target of rapamycin (MTOR), amyloid-beta, and Tau: effects on cognitive impairments
    • 20178983
    • Caccamo A, Majumder S, Richardson A, Strong R, Oddo S. Molecular interplay between mammalian target of rapamycin (MTOR), amyloid-beta, and Tau:effects on cognitive impairments. J Biol Chem 2010; 285:13107-20; PMID:20178983; http://dx.doi.org/10.1074/jbc.M110.100420
    • (2010) J Biol Chem , vol.285 , pp. 13107-13120
    • Caccamo, A.1    Majumder, S.2    Richardson, A.3    Strong, R.4    Oddo, S.5
  • 65
    • 84914160024 scopus 로고    scopus 로고
    • Single-walled carbon nanotubes alleviate autophagic/lysosomal defects in primary glia from a mouse model of Alzheimer's disease
    • 25115676
    • Xue X, Wang LR, Sato Y, Jiang Y, Berg M, Yang DS, Nixon RA, Liang XJ. Single-walled carbon nanotubes alleviate autophagic/lysosomal defects in primary glia from a mouse model of Alzheimer's disease. Nano Lett 2014; 14:5110-7; PMID:25115676; http://dx.doi.org/10.1021/nl501839q
    • (2014) Nano Lett , vol.14 , pp. 5110-5117
    • Xue, X.1    Wang, L.R.2    Sato, Y.3    Jiang, Y.4    Berg, M.5    Yang, D.S.6    Nixon, R.A.7    Liang, X.J.8
  • 66
    • 23844457609 scopus 로고    scopus 로고
    • Levels of MTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain
    • 16098202
    • Li X, Alafuzoff I, Soininen H, Winblad B, Pei JJ. Levels of MTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain. FEBS J 2005; 272:4211-20; PMID:16098202; http://dx.doi.org/10.1111/j.1742-4658.2005.04833.x
    • (2005) FEBS J , vol.272 , pp. 4211-4220
    • Li, X.1    Alafuzoff, I.2    Soininen, H.3    Winblad, B.4    Pei, J.J.5
  • 67
    • 63849230729 scopus 로고    scopus 로고
    • The PI3K-Akt-MTOR pathway regulates Abeta oligomer induced neuronal cell cycle events
    • 19291319
    • Bhaskar K, Miller M, Chludzinski A, Herrup K, Zagorski M, Lamb BT. The PI3K-Akt-MTOR pathway regulates Abeta oligomer induced neuronal cell cycle events. Mol Neurodegener 2009; 4:14; PMID:19291319; http://dx.doi.org/10.1186/1750-1326-4-14
    • (2009) Mol Neurodegener , vol.4 , pp. 14
    • Bhaskar, K.1    Miller, M.2    Chludzinski, A.3    Herrup, K.4    Zagorski, M.5    Lamb, B.T.6
  • 68
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis
    • 9236226
    • Cataldo AM, Barnett JL, Pieroni C, Nixon RA. Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease:neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. J Neurosci 1997; 17:6142-51; PMID:9236226
    • (1997) J Neurosci , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 69
    • 78650716872 scopus 로고    scopus 로고
    • Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits
    • 21186265
    • Yang DS, Stavrides P, Mohan PS, Kaushik S, Kumar A, Ohno M, Schmidt SD, Wesson D, Bandyopadhyay U, Jiang Y, et al. Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits. Brain 2011; 134:258-77; PMID:21186265; http://dx.doi.org/10.1093/brain/awq341
    • (2011) Brain , vol.134 , pp. 258-277
    • Yang, D.S.1    Stavrides, P.2    Mohan, P.S.3    Kaushik, S.4    Kumar, A.5    Ohno, M.6    Schmidt, S.D.7    Wesson, D.8    Bandyopadhyay, U.9    Jiang, Y.10
  • 70
    • 84896730305 scopus 로고    scopus 로고
    • Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer's disease-linked presenilin 1 A246E mutation can be reversed with cAMP
    • 24418614
    • Coffey EE, Beckel JM, Laties AM, Mitchell CH. Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer's disease-linked presenilin 1 A246E mutation can be reversed with cAMP. Neuroscience 2014; 263:111-24; PMID:24418614; http://dx.doi.org/10.1016/j.neuroscience.2014.01.001
    • (2014) Neuroscience , vol.263 , pp. 111-124
    • Coffey, E.E.1    Beckel, J.M.2    Laties, A.M.3    Mitchell, C.H.4
  • 71
    • 84879232282 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification
    • 23773064
    • Wolfe DM, Lee JH, Kumar A, Lee S, Orenstein SJ, Nixon RA. Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification. Eur J Neurosci 2013; 37:1949-61; PMID:23773064; http://dx.doi.org/10.1111/ejn.12169
    • (2013) Eur J Neurosci , vol.37 , pp. 1949-1961
    • Wolfe, D.M.1    Lee, J.H.2    Kumar, A.3    Lee, S.4    Orenstein, S.J.5    Nixon, R.A.6
  • 72
    • 84887863225 scopus 로고    scopus 로고
    • Lysosome and calcium dysregulation in Alzheimer's disease: partners in crime
    • 24256243
    • McBrayer M, Nixon RA. Lysosome and calcium dysregulation in Alzheimer's disease:partners in crime. Biochem Soc Trans 2013; 41:1495-502; PMID:24256243; http://dx.doi.org/10.1042/BST20130201
    • (2013) Biochem Soc Trans , vol.41 , pp. 1495-1502
    • McBrayer, M.1    Nixon, R.A.2
  • 73
    • 84965071473 scopus 로고    scopus 로고
    • Lysosomal cathepsins and their regulation in aging and neurodegeneration
    • 27125852
    • Stoka V, Turk V, Turk B. Lysosomal cathepsins and their regulation in aging and neurodegeneration. Ageing Res Rev 2016; In press; PMID:27125852; http://dx.doi.org/10.1016/j.arr.2016.04.010
    • (2016) Ageing Res Rev
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 74
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • 20965422
    • Kroemer G, Marino G, Levine B. Autophagy and the integrated stress response. Mol Cell 2010; 40:280-93; PMID:20965422; http://dx.doi.org/10.1016/j.molcel.2010.09.023
    • (2010) Mol Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 75
    • 84937605093 scopus 로고    scopus 로고
    • Evidence that the rab5 effector APPL1 mediates APP-betaCTF-induced dysfunction of endosomes in Down syndrome and Alzheimer's disease
    • Kim S, Sato Y, Mohan PS, Peterhoff C, Pensalfini A, Rigoglioso A, Jiang Y, Nixon RA. Evidence that the rab5 effector APPL1 mediates APP-betaCTF-induced dysfunction of endosomes in Down syndrome and Alzheimer's disease. Mol Psychiatry 2015; 21:707-16; PMID:2619481.
    • (2015) Mol Psychiatry
    • Kim, S.1    Sato, Y.2    Mohan, P.S.3    Peterhoff, C.4    Pensalfini, A.5    Rigoglioso, A.6    Jiang, Y.7    Nixon, R.A.8
  • 77
    • 1242316279 scopus 로고    scopus 로고
    • Niemann-Pick Type C disease and Alzheimer's disease: the APP-endosome connection fattens up
    • 14982829
    • Nixon RA. Niemann-Pick Type C disease and Alzheimer's disease:the APP-endosome connection fattens up. Am J Pathol 2004; 164:757-61; PMID:14982829; http://dx.doi.org/10.1016/S0002-9440(10)63163-X
    • (2004) Am J Pathol , vol.164 , pp. 757-761
    • Nixon, R.A.1
  • 78
    • 84868102987 scopus 로고    scopus 로고
    • Impaired proteolysis underlies autophagic dysfunction in Niemann-Pick type C disease
    • 22872701
    • Elrick MJ, Yu T, Chung C, Lieberman AP. Impaired proteolysis underlies autophagic dysfunction in Niemann-Pick type C disease. Hum Mol Genet 2012; 21:4876-87; PMID:22872701; http://dx.doi.org/10.1093/hmg/dds324
    • (2012) Hum Mol Genet , vol.21 , pp. 4876-4887
    • Elrick, M.J.1    Yu, T.2    Chung, C.3    Lieberman, A.P.4
  • 79
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • 1759558
    • Braak H, Braak E. Neuropathological staging of Alzheimer-related changes. Acta Neuropathol 1991; 82:239-59; PMID:1759558; http://dx.doi.org/10.1007/BF00308809
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 80
    • 0031255112 scopus 로고    scopus 로고
    • Consensus recommendations for the postmortem diagnosis of Alzheimer disease from the National Institute on Aging and the Reagan Institute Working Group on diagnostic criteria for the neuropathological assessment of Alzheimer disease
    • 9329452
    • Hyman BT, Trojanowski JQ. Consensus recommendations for the postmortem diagnosis of Alzheimer disease from the National Institute on Aging and the Reagan Institute Working Group on diagnostic criteria for the neuropathological assessment of Alzheimer disease. J Neuropathol Exp Neurol 1997; 56:1095-7; PMID:9329452; http://dx.doi.org/10.1097/00005072-199710000-00002
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 1095-1097
    • Hyman, B.T.1    Trojanowski, J.Q.2
  • 81
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • 2011243
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, Vogel FS, Hughes JP, van Belle G, Berg L. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991; 41:479-86; PMID:2011243; http://dx.doi.org/10.1212/WNL.41.4.479
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6    Vogel, F.S.7    Hughes, J.P.8    van Belle, G.9    Berg, L.10
  • 83
    • 0033809884 scopus 로고    scopus 로고
    • Loss of nucleus basalis neurons containing trkA immunoreactivity in individuals with mild cognitive impairment and early Alzheimer's disease
    • 11042589
    • Mufson EJ, Ma SY, Cochran EJ, Bennett DA, Beckett LA, Jaffar S, Saragovi HU, Kordower JH. Loss of nucleus basalis neurons containing trkA immunoreactivity in individuals with mild cognitive impairment and early Alzheimer's disease. J Comp Neurol 2000; 427:19-30; PMID:11042589; http://dx.doi.org/10.1002/1096-9861(20001106)427:1%3c19::AID-CNE2%3e3.0.CO;2-A
    • (2000) J Comp Neurol , vol.427 , pp. 19-30
    • Mufson, E.J.1    Ma, S.Y.2    Cochran, E.J.3    Bennett, D.A.4    Beckett, L.A.5    Jaffar, S.6    Saragovi, H.U.7    Kordower, J.H.8
  • 86
    • 0025143937 scopus 로고
    • Cresyl violet: a red fluorescent Nissl stain
    • 2232864
    • Alvarez-Buylla A, Ling CY, Kirn JR. Cresyl violet:a red fluorescent Nissl stain. J Neurosci Methods 1990; 33:129-33; PMID:2232864; http://dx.doi.org/10.1016/0165-0270(90)90016-9
    • (1990) J Neurosci Methods , vol.33 , pp. 129-133
    • Alvarez-Buylla, A.1    Ling, C.Y.2    Kirn, J.R.3
  • 88
    • 18444384236 scopus 로고    scopus 로고
    • Expression profile analysis within the human hippocampus: comparison of CA1 and CA3 pyramidal neurons
    • 15861457
    • Ginsberg SD, Che S. Expression profile analysis within the human hippocampus:comparison of CA1 and CA3 pyramidal neurons. J Comp Neurol 2005; 487:107-18; PMID:15861457; http://dx.doi.org/10.1002/cne.20535
    • (2005) J Comp Neurol , vol.487 , pp. 107-118
    • Ginsberg, S.D.1    Che, S.2
  • 89
    • 80052102358 scopus 로고    scopus 로고
    • Upregulation of select rab GTPases in cholinergic basal forebrain neurons in mild cognitive impairment and Alzheimer's disease
    • 21669283
    • Ginsberg SD, Mufson EJ, Alldred MJ, Counts SE, Wuu J, Nixon RA, Che S. Upregulation of select rab GTPases in cholinergic basal forebrain neurons in mild cognitive impairment and Alzheimer's disease. J Chem Neuroanat 2011; 42:102-10; PMID:21669283; http://dx.doi.org/10.1016/j.jchemneu.2011.05.012
    • (2011) J Chem Neuroanat , vol.42 , pp. 102-110
    • Ginsberg, S.D.1    Mufson, E.J.2    Alldred, M.J.3    Counts, S.E.4    Wuu, J.5    Nixon, R.A.6    Che, S.7
  • 90
    • 84934436327 scopus 로고    scopus 로고
    • Transcriptional profiling of small samples in the central nervous system
    • 18370101
    • Ginsberg SD. Transcriptional profiling of small samples in the central nervous system. Methods Mol Biol 2008; 439:147-58; PMID:18370101; http://dx.doi.org/10.1007/978-1-59745-188-8_10
    • (2008) Methods Mol Biol , vol.439 , pp. 147-158
    • Ginsberg, S.D.1
  • 91
    • 84909599287 scopus 로고    scopus 로고
    • Expression profile analysis of vulnerable CA1 pyramidal neurons in young-Middle-Aged Ts65Dn mice
    • 25131634
    • Alldred MJ, Lee SH, Petkova E, Ginsberg SD. Expression profile analysis of vulnerable CA1 pyramidal neurons in young-Middle-Aged Ts65Dn mice. J Comp Neurol 2015; 523:61-74; PMID:25131634; http://dx.doi.org/10.1002/cne.23663
    • (2015) J Comp Neurol , vol.523 , pp. 61-74
    • Alldred, M.J.1    Lee, S.H.2    Petkova, E.3    Ginsberg, S.D.4
  • 92
    • 84940575866 scopus 로고    scopus 로고
    • Expression profile analysis of hippocampal CA1 pyramidal neurons in aged Ts65Dn mice, a model of Down syndrome (DS) and Alzheimer's disease (AD)
    • 25031177
    • Alldred MJ, Lee SH, Petkova E, Ginsberg SD. Expression profile analysis of hippocampal CA1 pyramidal neurons in aged Ts65Dn mice, a model of Down syndrome (DS) and Alzheimer's disease (AD). Brain Struct Funct 2015; 220:2983-96; PMID:25031177; http://dx.doi.org/10.1007/s00429-014-0839-0
    • (2015) Brain Struct Funct , vol.220 , pp. 2983-2996
    • Alldred, M.J.1    Lee, S.H.2    Petkova, E.3    Ginsberg, S.D.4
  • 93
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • 12184808
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 2002; 3:RESEARCH0034; PMID:12184808; http://dx.doi.org/10.1186/gb-2002-3-7-research0034
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 95
    • 22844438739 scopus 로고    scopus 로고
    • Tissue processing prior to protein analysis and amyloid-beta quantitation
    • 15980611
    • Schmidt SD, Jiang Y, Nixon RA, Mathews PM. Tissue processing prior to protein analysis and amyloid-beta quantitation. Methods Mol Biol 2005; 299:267-78; PMID:15980611
    • (2005) Methods Mol Biol , vol.299 , pp. 267-278
    • Schmidt, S.D.1    Jiang, Y.2    Nixon, R.A.3    Mathews, P.M.4
  • 97
    • 0028868307 scopus 로고
    • Purification and properties of high molecular weight calpastatin from bovine brain
    • 7830080
    • Mohan PS, Nixon RA. Purification and properties of high molecular weight calpastatin from bovine brain. J Neurochem 1995; 64:859-66; PMID:7830080; http://dx.doi.org/10.1046/j.1471-4159.1995.64020859.x
    • (1995) J Neurochem , vol.64 , pp. 859-866
    • Mohan, P.S.1    Nixon, R.A.2
  • 98
    • 0025355591 scopus 로고
    • Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin
    • 2350688
    • Cataldo AM, Thayer CY, Bird ED, Wheelock TR, Nixon RA. Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease:evidence for a neuronal origin. Brain Res 1990; 513:181-92; PMID:2350688; http://dx.doi.org/10.1016/0006-8993(90)90456-L
    • (1990) Brain Res , vol.513 , pp. 181-192
    • Cataldo, A.M.1    Thayer, C.Y.2    Bird, E.D.3    Wheelock, T.R.4    Nixon, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.