메뉴 건너뛰기




Volumn 4 S, Issue 3, 2012, Pages 941-952

The role of mTOR signaling in Alzheimer disease

Author keywords

Abeta; AD; Alzheimer's disease; Autophagy; Learning and memory; mTOR; Plaques; PS1; Rapamycin; Review; Tangles; Tau

Indexed keywords

AMYLOID BETA PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; TAU PROTEIN; TARGET OF RAPAMYCIN KINASE;

EID: 84869413374     PISSN: 19450516     EISSN: 19450524     Source Type: Journal    
DOI: 10.2741/s310     Document Type: Article
Times cited : (182)

References (122)
  • 1
    • 77949336151 scopus 로고    scopus 로고
    • 2010 Alzheimer's disease facts and figures
    • 2010 Alzheimer's disease facts and figures. Alzheimers Dement, 6, 158-94 (2010)
    • (2010) Alzheimers Dement , vol.6 , pp. 158-194
  • 3
    • 33846604242 scopus 로고    scopus 로고
    • How common are the "common" neurologic disorders?
    • DOI 10.1212/01.wnl.0000252807.38124.a3, PII 0000611420070130000006
    • D. Hirtz, D. J. Thurman, K. Gwinn-Hardy, M. Mohamed, A. R. Chaudhuri and R. Zalutsky: How common are the "common" neurologic disorders? Neurology, 68, 326-37 (2007) (Pubitemid 46188246)
    • (2007) Neurology , vol.68 , Issue.5 , pp. 326-337
    • Hirtz, D.1    Thurman, D.J.2    Gwinn-Hardy, K.3    Mohamed, M.4    Chaudhuri, A.R.5    Zalutsky, R.6
  • 5
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid betaprotein impair synaptic plasticity and behavior
    • D. J. Selkoe: Soluble oligomers of the amyloid betaprotein impair synaptic plasticity and behavior. Behav Brain Res, 192, 106-13 (2008)
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 6
    • 78651072485 scopus 로고    scopus 로고
    • CBP gene transfer increases BDNF levels and ameliorates learning and memory deficits in a mouse model of Alzheimer's disease
    • A. Caccamo, M. A. Maldonado, A. F. Bokov, S. Majumder and S. Oddo: CBP gene transfer increases BDNF levels and ameliorates learning and memory deficits in a mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A, 107, 22687-92 (2010)
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22687-22692
    • Caccamo, A.1    Maldonado, M.A.2    Bokov, A.F.3    Majumder, S.4    Oddo, S.5
  • 7
    • 77954132249 scopus 로고    scopus 로고
    • Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: From synapses toward neural networks
    • J. J. Palop and L. Mucke: Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks. Nat Neurosci, 13, 812-8 (2010)
    • (2010) Nat Neurosci , vol.13 , pp. 812-818
    • Palop, J.J.1    Mucke, L.2
  • 9
    • 27144530643 scopus 로고    scopus 로고
    • Vulnerability of dentate granule cells to disruption of Arc expression in human amyloid precursor protein transgenic mice
    • DOI 10.1523/JNEUROSCI.2829-05.2005
    • J. J. Palop, J. Chin, N. Bien-Ly, C. Massaro, B. Z. Yeung, G. Q. Yu and L. Mucke: Vulnerability of dentate granule cells to disruption of arc expression in human amyloid precursor protein transgenic mice. J Neurosci, 25, 9686-93 (2005) (Pubitemid 41510909)
    • (2005) Journal of Neuroscience , vol.25 , Issue.42 , pp. 9686-9693
    • Palop, J.J.1    Chin, J.2    Bien-Ly, N.3    Massaro, C.4    Yeung, B.Z.5    Yu, G.-Q.6    Mucke, L.7
  • 11
  • 12
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • DOI 10.1016/j.cell.2006.01.016, PII S0092867406001085
    • S. Wullschleger, R. Loewith and M. N. Hall: TOR signaling in growth and metabolism. Cell, 124, 471-84 (2006) (Pubitemid 43199434)
    • (2006) Cell , vol.124 , Issue.3 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 13
    • 77953014263 scopus 로고    scopus 로고
    • The role of mTOR signaling in controlling mammalian life span: What a fungicide teaches us about longevity
    • Z. D. Sharp and R. Strong: The role of mTOR signaling in controlling mammalian life span: what a fungicide teaches us about longevity. J Gerontol A Biol Sci Med Sci, 65, 580-9 (2010)
    • (2010) J Gerontol a Biol Sci Med Sci , vol.65 , pp. 580-589
    • Sharp, Z.D.1    Strong, R.2
  • 15
    • 30944458446 scopus 로고    scopus 로고
    • Extension of chronological life span in yeast by decreased TOR pathway signaling
    • DOI 10.1101/gad.1381406
    • R. W. Powers, 3rd. M. Kaeberlein, S. D. Caldwell, B. K. Kennedy and S. Fields: Extension of chronological life span in yeast by decreased TOR pathway signaling. Genes Dev, 20, 174-84 (2006) (Pubitemid 43112936)
    • (2006) Genes and Development , vol.20 , Issue.2 , pp. 174-184
    • Powers III, R.W.1    Kaeberlein, M.2    Caldwell, S.D.3    Kennedy, B.K.4    Fields, S.5
  • 16
    • 4544311861 scopus 로고    scopus 로고
    • The TOR pathway interacts with the insulin signaling pathway to regulate C. Elegans larval development, metabolism and life span
    • DOI 10.1242/dev.01255
    • K. Jia, D. Chen and D. L. Riddle: The TOR pathway interacts with the insulin signaling pathway to regulate C. elegans larval development, metabolism and life span. Development, 131, 3897-906 (2004) (Pubitemid 39232150)
    • (2004) Development , vol.131 , Issue.16 , pp. 3897-3906
    • Jia, K.1    Chen, D.2    Riddle, D.L.3
  • 17
    • 3042648746 scopus 로고    scopus 로고
    • Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway
    • DOI 10.1016/j.cub.2004.03.059, PII S0960982204002386
    • P. Kapahi, B. M. Zid, T. Harper, D. Koslover, V. Sapin and S. Benzer: Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway. Curr Biol, 14, 885-90 (2004) (Pubitemid 38800910)
    • (2004) Current Biology , vol.14 , Issue.10 , pp. 885-890
    • Kapahi, P.1    Zid, B.M.2    Harper, T.3    Koslover, D.4    Sapin, V.5    Benzer, S.6
  • 18
  • 22
    • 0037147666 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor-2α (eIF2α) is associated with neuronal degeneration in Alzheimer's disease
    • DOI 10.1097/00001756-200212200-00011
    • R. C. Chang, A. K. Wong, H. K. Ng and J. Hugon: Phosphorylation of eukaryotic initiation factor-2alpha (eIF2alpha) is associated with neuronal degeneration in Alzheimer's disease. Neuroreport, 13, 2429-32 (2002) (Pubitemid 36143538)
    • (2002) NeuroReport , vol.13 , Issue.18 , pp. 2429-2432
    • Chang, R.C.C.1    Wong, A.K.Y.2    Ng, H.-K.3    Hugon, J.4
  • 23
    • 16244391770 scopus 로고    scopus 로고
    • Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer's disease pathology
    • DOI 10.1111/j.1471-4159.2004.02949.x
    • R. J. Griffin, A. Moloney, M. Kelliher, J. A. Johnston, R. Ravid, P. Dockery, R. O'Connor and C. O'Neill: Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer's disease pathology. J Neurochem, 93, 105-17 (2005) (Pubitemid 40463520)
    • (2005) Journal of Neurochemistry , vol.93 , Issue.1 , pp. 105-117
    • Griffin, R.J.1    Moloney, A.2    Kelliher, M.3    Johnston, J.A.4    Ravid, R.5    Dockery, P.6    O'Connor, R.7    O'Neill, C.8
  • 24
    • 1842562209 scopus 로고    scopus 로고
    • An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer's disease
    • DOI 10.1038/sj.emboj.7600049
    • R. Onuki, Y. Bando, E. Suyama, T. Katayama, H. Kawasaki, T. Baba, M. Tohyama and K. Taira: An RNAdependent protein kinase is involved in tunicamycininduced apoptosis and Alzheimer's disease. Embo J, 23, 959-68 (2004) (Pubitemid 38418762)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 959-968
    • Onuki, R.1    Bando, Y.2    Suyama, E.3    Katayama, T.4    Kawasaki, H.5    Baba, T.6    Tohyama, M.7    Taira, K.8
  • 25
    • 0041833464 scopus 로고    scopus 로고
    • Activation of the cell stress kinase PKR in Alzheimer's disease and human amyloid precursor protein transgenic mice
    • DOI 10.1016/S0969-9961(03)00086-X
    • A. L. Peel and D. E. Bredesen: Activation of the cell stress kinase PKR in Alzheimer's disease and human amyloid precursor protein transgenic mice. Neurobiol Dis, 14, 52-62 (2003) (Pubitemid 37103179)
    • (2003) Neurobiology of Disease , vol.14 , Issue.1 , pp. 52-62
    • Peel, A.L.1    Bredesen, D.E.2
  • 27
    • 58149463424 scopus 로고    scopus 로고
    • Mtor-dependent signalling in Alzheimer's disease
    • J. J. Pei and J. Hugon: mTOR-dependent signalling in Alzheimer's disease. J Cell Mol Med, 12, 2525-32 (2008)
    • (2008) J Cell Mol Med , vol.12 , pp. 2525-2532
    • Pei, J.J.1    Hugon, J.2
  • 28
    • 6344269168 scopus 로고    scopus 로고
    • Phosphorylated eukaryotic translation factor 4E is elevated in Alzheimer brain
    • DOI 10.1097/00001756-200410050-00019
    • X. Li, W. L. An, I. Alafuzoff, H. Soininen, B. Winblad and J. J. Pei: Phosphorylated eukaryotic translation factor 4E is elevated in Alzheimer brain. Neuroreport, 15, 2237-40 (2004) (Pubitemid 39392247)
    • (2004) NeuroReport , vol.15 , Issue.14 , pp. 2237-2240
    • Li, X.1    An, W.-L.2    Alafuzoff, I.3    Soininen, H.4    Winblad, B.5    Pei, J.-J.6
  • 29
    • 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
    • DOI 10.1111/j.1742-4658.2005.04833.x
    • X. Li, I. Alafuzoff, H. Soininen, B. Winblad and J. J. Pei: Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain. FEBS J, 272, 4211-20 (2005) (Pubitemid 41160927)
    • (2005) FEBS Journal , vol.272 , Issue.16 , pp. 4211-4220
    • Li, X.1    Alafuzoff, I.2    Soininen, H.3    Winblad, B.4    Pei, J.-J.5
  • 30
    • 0034839145 scopus 로고    scopus 로고
    • Effect of the Alzheimer amyloid fragment Aβ(25-35) on Akt/PKB kinase and survival of PC12 cells
    • DOI 10.1046/j.1471-4159.2001.00472.x
    • D. Martin, M. Salinas, R. Lopez-Valdaliso, E. Serrano, M. Recuero and A. Cuadrado: Effect of the Alzheimer amyloid fragment Abeta (25-35) on Akt/PKB kinase and survival of PC12 cells. J Neurochem, 78, 1000-8 (2001) (Pubitemid 32823149)
    • (2001) Journal of Neurochemistry , vol.78 , Issue.5 , pp. 1000-1008
    • Martin, D.1    Salinas, M.2    Lopez-Valdaliso, R.3    Serrano, E.4    Recuero, M.5    Cuadrado, A.6
  • 31
    • 33847397874 scopus 로고    scopus 로고
    • Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40
    • DOI 10.1038/ncb1547, PII NCB1547
    • E. Vander Haar, S. I. Lee, S. Bandhakavi, T. J. Griffin and D. H. Kim: Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40. Nat Cell Biol, 9, 316-23 (2007) (Pubitemid 46344611)
    • (2007) Nature Cell Biology , vol.9 , Issue.3 , pp. 316-323
    • Haar, E.V.1    Lee, S.2    Bandhakavi, S.3    Griffin, T.J.4    Kim, D.-H.5
  • 32
    • 34248592575 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinases (MMP3, MMP12 and MMP13) expression in the microglia by amyloid-β stimulation via the PI3K/Akt pathway
    • DOI 10.1016/j.exger.2006.11.012, PII S0531556506004062
    • S. Ito, K. Kimura, M. Haneda, Y. Ishida, M. Sawada and K. Isobe: Induction of matrix metalloproteinases (MMP3, MMP12 and MMP13) expression in the microglia by amyloid-beta stimulation via the PI3K/Akt pathway. Exp Gerontol, 42, 532-7 (2007) (Pubitemid 46756086)
    • (2007) Experimental Gerontology , vol.42 , Issue.6 , pp. 532-537
    • Ito, S.1    Kimura, K.2    Haneda, M.3    Ishida, Y.4    Sawada, M.5    Isobe, K.-i.6
  • 33
    • 33750079297 scopus 로고    scopus 로고
    • Amyloid-β peptides induce several chemokine mRNA expressions in the primary microglia and Ra2 cell line via the PI3K/Akt and/or ERK pathway
    • DOI 10.1016/j.neures.2006.07.009, PII S0168010206001842
    • S. Ito, M. Sawada, M. Haneda, Y. Ishida and K. Isobe: Amyloid-beta peptides induce several chemokine mRNA expressions in the primary microglia and Ra2 cell line via the PI3K/Akt and/or ERK pathway. Neurosci Res, 56, 294-9 (2006) (Pubitemid 44574518)
    • (2006) Neuroscience Research , vol.56 , Issue.3 , pp. 294-299
    • Ito, S.1    Sawada, M.2    Haneda, M.3    Ishida, Y.4    Isobe, K.-i.5
  • 36
    • 21344459656 scopus 로고    scopus 로고
    • mTOR/p70S6k signalling alteration by Aβ exposure as well as in APP-PS1 transgenic models and in patients with Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2005.03187.x
    • C. Lafay-Chebassier, M. Paccalin, G. Page, S. Barc-Pain, M. C. Perault-Pochat, R. Gil, L. Pradier and J. Hugon: mTOR/p70S6k signalling alteration by Abeta exposure as well as in APP-PS1 transgenic models and in patients with Alzheimer's disease. J Neurochem, 94, 215-25 (2005) (Pubitemid 40911407)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.1 , 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
  • 37
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • E. H. Koo and S. L. Squazzo: Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J Biol Chem, 269, 17386-9 (1994) (Pubitemid 24218009)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.26 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 39
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture
    • M. B. Podlisny, B. L. Ostaszewski, S. L. Squazzo, E. H. Koo, R. E. Rydell, D. B. Teplow and D. J. Selkoe: Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture. J Biol Chem, 270, 9564-70 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 9564-9570
    • Podlisny, M.B.1    Ostaszewski, B.L.2    Squazzo, S.L.3    Koo, E.H.4    Rydell, R.E.5    Teplow, D.B.6    Selkoe, D.J.7
  • 40
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • D. M. Walsh, I. Klyubin, J. V. Fadeeva, W. K. Cullen, R. Anwyl, M. S. Wolfe, M. J. Rowan and D. J. Selkoe: Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature, 416, 535-9 (2002) (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 41
    • 77951227122 scopus 로고    scopus 로고
    • Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: Effects on cognitive impairments
    • A. Caccamo, S. Majumder, A. Richardson, R. Strong and S. Oddo: Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: effects on cognitive impairments. J Biol Chem, 285, 13107-20 (2010)
    • (2010) J Biol Chem , vol.285 , pp. 13107-13120
    • Caccamo, A.1    Majumder, S.2    Richardson, A.3    Strong, R.4    Oddo, S.5
  • 42
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • DOI 10.1016/j.neuron.2005.01.040
    • L. M. Billings, S. Oddo, K. N. Green, J. L. McGaugh and F. M. LaFerla: Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron, 45, 675-88 (2005) (Pubitemid 40320703)
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 43
    • 34547464672 scopus 로고    scopus 로고
    • Genetically augmenting tau levels does not modulate the onset or progression of Aβ pathology in transgenic mice
    • DOI 10.1111/j.1471-4159.2007.04607.x
    • S. Oddo, A. Caccamo, D. Cheng, B. Jouleh, R. Torp and F. M. LaFerla: Genetically augmenting tau levels does not modulate the onset or progression of Abeta pathology in transgenic mice. J Neurochem, 102, 1053-63 (2007) (Pubitemid 47174220)
    • (2007) Journal of Neurochemistry , vol.102 , Issue.4 , pp. 1053-1063
    • Oddo, S.1    Caccamo, A.2    Cheng, D.3    Jouleh, B.4    Torp, R.5    LaFerla, F.M.6
  • 44
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's Disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • DOI 10.1016/S0896-6273(03)00434-3
    • S. Oddo, A. Caccamo, J. D. Shepherd, M. P. Murphy, T. E. Golde, R. Kayed, R. Metherate, M. P. Mattson, Y. Akbari and F. M. LaFerla: Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Abeta and synaptic dysfunction. Neuron, 39, 409-21 (2003) (Pubitemid 36937044)
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    LaFerla, F.M.10
  • 45
    • 58149388879 scopus 로고    scopus 로고
    • Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: A mechanistic link between Abeta and tau pathology
    • S. Oddo, A. Caccamo, B. Tseng, D. Cheng, V. Vasilevko, D. H. Cribbs and F. M. LaFerla: Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: a mechanistic link between Abeta and tau pathology. J Neurosci, 28, 12163-75 (2008)
    • (2008) J Neurosci , vol.28 , pp. 12163-12175
    • Oddo, S.1    Caccamo, A.2    Tseng, B.3    Cheng, D.4    Vasilevko, V.5    Cribbs, D.H.6    La Ferla, F.M.7
  • 46
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2003.08.012
    • S. Oddo, A. Caccamo, M. Kitazawa, B. P. Tseng and F. M. LaFerla: Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol Aging, 24, 1063-70 (2003) (Pubitemid 37487883)
    • (2003) Neurobiology of Aging , vol.24 , Issue.8 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 47
    • 65649106997 scopus 로고    scopus 로고
    • Genetically altering Abeta distribution from the brain to the vasculature ameliorates tau pathology
    • S. Oddo, A. Caccamo, D. Cheng and F. M. LaFerla: Genetically altering Abeta distribution from the brain to the vasculature ameliorates tau pathology. Brain Pathol, 19, 421-30 (2009)
    • (2009) Brain Pathol , vol.19 , pp. 421-430
    • Oddo, S.1    Caccamo, A.2    Cheng, D.3    La Ferla, F.M.4
  • 48
    • 33144487701 scopus 로고    scopus 로고
    • Temporal profile of amyloid-beta (Abeta) oligomerization in an in vivo model of Alzheimer disease. A link between Abeta and tau pathology
    • S. Oddo, A. Caccamo, L. Tran, M. P. Lambert, C. G. Glabe, W. L. Klein and F. M. LaFerla: Temporal profile of amyloid-beta (Abeta) oligomerization in an in vivo model of Alzheimer disease. A link between Abeta and tau pathology. J Biol Chem, 281, 1599-604 (2006)
    • (2006) J Biol Chem , vol.281 , pp. 1599-1604
    • Oddo, S.1    Caccamo, A.2    Tran, L.3    Lambert, M.P.4    Glabe, C.G.5    Klein, W.L.6    La Ferla, F.M.7
  • 51
    • 34547099855 scopus 로고    scopus 로고
    • PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding
    • DOI 10.1074/jbc.M702376200
    • L. Wang, T. E. Harris, R. A. Roth and J. C. Lawrence, Jr.: PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding. J Biol Chem, 282, 20036-44 (2007) (Pubitemid 47100127)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 20036-20044
    • Wang, L.1    Harris, T.E.2    Roth, R.A.3    Lawrence Jr., J.C.4
  • 53
    • 0032692620 scopus 로고    scopus 로고
    • A transient, neuron-wide form of CREB-mediated long-term facilitation can be stabilized at specific synapses by local protein synthesis
    • DOI 10.1016/S0092-8674(00)81653-0
    • A. Casadio, K. C. Martin, M. Giustetto, H. Zhu, M. Chen, D. Bartsch, C. H. Bailey and E. R. Kandel: A transient, neuron-wide form of CREB-mediated long-term facilitation can be stabilized at specific synapses by local protein synthesis. Cell, 99, 221-37 (1999) (Pubitemid 29491788)
    • (1999) Cell , vol.99 , Issue.2 , pp. 221-237
    • Casadio, A.1    Martin, K.C.2    Giustetto, M.3    Zhu, H.4    Chen, M.5    Bartsch, D.6    Bailey, C.H.7    Kandel, E.R.8
  • 57
    • 33748128950 scopus 로고    scopus 로고
    • Spatial memory formation and memory-enhancing effect of glucose involves activation of the tuberous sclerosis complex-mammalian target of rapamycin pathway
    • DOI 10.1523/JNEUROSCI.0671-06.2006
    • P. K. Dash, S. A. Orsi and A. N. Moore: Spatial memory formation and memory-enhancing effect of glucose involves activation of the tuberous sclerosis complex-Mammalian target of rapamycin pathway. J Neurosci, 26, 8048-56 (2006) (Pubitemid 44315129)
    • (2006) Journal of Neuroscience , vol.26 , Issue.31 , pp. 8048-8056
    • Dash, P.K.1    Orsi, S.A.2    Moore, A.N.3
  • 58
    • 33845606405 scopus 로고    scopus 로고
    • Translational control via the mammalian target of rapamycin pathway is critical for the formation and stability of long-term fear memory in amygdala neurons
    • DOI 10.1523/JNEUROSCI.4209-06.2006
    • R. G. Parsons, G. M. Gafford and F. J. Helmstetter: Translational control via the mammalian target of rapamycin pathway is critical for the formation and stability of long-term fear memory in amygdala neurons. J Neurosci, 26, 12977-83 (2006) (Pubitemid 44954616)
    • (2006) Journal of Neuroscience , vol.26 , Issue.50 , pp. 12977-12983
    • Parsons, R.G.1    Gafford, G.M.2    Helmstetter, F.J.3
  • 59
    • 0141918785 scopus 로고    scopus 로고
    • Compartmentalized synthesis and degradation of proteins in neurons
    • DOI 10.1016/S0896-6273(03)00635-4
    • O. Steward and E. M. Schuman: Compartmentalized synthesis and degradation of proteins in neurons. Neuron, 40, 347-59 (2003) (Pubitemid 37244100)
    • (2003) Neuron , vol.40 , Issue.2 , pp. 347-359
    • Steward, O.1    Schuman, E.M.2
  • 60
    • 7744224557 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor induces mammalian target of rapamycin-dependent local activation of translation machinery and protein synthesis in neuronal dendrites
    • DOI 10.1523/JNEUROSCI.1427-04.2004
    • N. Takei, N. Inamura, M. Kawamura, H. Namba, K. Hara, K. Yonezawa and H. Nawa: Brain-derived neurotrophic factor induces mammalian target of rapamycin-dependent local activation of translation machinery and protein synthesis in neuronal dendrites. J Neurosci, 24, 9760-9 (2004) (Pubitemid 39463557)
    • (2004) Journal of Neuroscience , vol.24 , Issue.44 , pp. 9760-9769
    • Takei, N.1    Inamura, N.2    Kawamura, M.3    Namba, H.4    Hara, K.5    Yonezawa, K.6    Nawa, H.7
  • 62
    • 70349865087 scopus 로고    scopus 로고
    • Mtor signaling in epileptogenesis: Too much of a good thing?
    • R. Cao, A. Li and H. Y. Cho: mTOR signaling in epileptogenesis: too much of a good thing? J Neurosci, 29, 12372-3 (2009)
    • (2009) J Neurosci , vol.29 , pp. 12372-12373
    • Cao, R.1    Li, A.2    Cho, H.Y.3
  • 63
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSC-mTOR pathway in human disease
    • DOI 10.1038/ng1494
    • K. Inoki, M. N. Corradetti and K. L. Guan: Dysregulation of the TSC-mTOR pathway in human disease. Nat Genet, 37, 19-24 (2005) (Pubitemid 40070934)
    • (2005) Nature Genetics , vol.37 , Issue.1 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.-L.3
  • 64
    • 66149169973 scopus 로고    scopus 로고
    • The mammalian target of rapamycin signaling pathway mediates epileptogenesis in a model of temporal lobe epilepsy
    • L. H. Zeng, N. R. Rensing and M. Wong: The mammalian target of rapamycin signaling pathway mediates epileptogenesis in a model of temporal lobe epilepsy. J Neurosci, 29, 6964-72 (2009)
    • (2009) J Neurosci , vol.29 , pp. 6964-6972
    • Zeng, L.H.1    Rensing, N.R.2    Wong, M.3
  • 66
    • 0346362997 scopus 로고    scopus 로고
    • Rapamycins: Mechanism of action and cellular resistance
    • S. Huang, M. A. Bjornsti and P. J. Houghton: Rapamycins: mechanism of action and cellular resistance. Cancer Biol Ther, 2, 222-32 (2003)
    • (2003) Cancer Biol Ther , vol.2 , pp. 222-232
    • Huang, S.1    Bjornsti, M.A.2    Houghton, P.J.3
  • 68
    • 0034881393 scopus 로고    scopus 로고
    • Sirolimus, but not the structurally related RAD (everolimus), enhances the negative effects of cyclosporine on mitochondrial metabolism in the rat brain
    • N. Serkova, W. Jacobsen, C. U. Niemann, L. Litt, L. Z. Benet, D. Leibfritz and U. Christians: Sirolimus, but not the structurally related RAD (everolimus), enhances the negative effects of cyclosporine on mitochondrial metabolism in the rat brain. Br J Pharmacol, 133, 875-85 (2001) (Pubitemid 32751797)
    • (2001) British Journal of Pharmacology , vol.133 , Issue.6 , pp. 875-885
    • Serkova, N.1    Jacobsen, W.2    Niemann, C.U.3    Litt, L.4    Benet, L.Z.5    Leibfritz, D.6    Christians, U.7
  • 69
    • 0028115928 scopus 로고
    • Dose-dependent pharmacokinetics of rapamycin-28-N,N-dimethylglycinate in the mouse
    • DOI 10.1007/s002800050061
    • J. G. Supko and L. Malspeis: Dose-dependent pharmacokinetics of rapamycin-28-N, N-dimethylglycinate in the mouse. Cancer Chemother Pharmacol, 33, 325-30 (1994) (Pubitemid 24033058)
    • (1994) Cancer Chemotherapy and Pharmacology , vol.33 , Issue.4 , pp. 325-330
    • Supko, J.G.1    Malspeis, L.2
  • 71
    • 70350412265 scopus 로고    scopus 로고
    • From mTOR to cognition: Molecular and cellular mechanisms of cognitive impairments in tuberous sclerosis
    • D. Ehninger, P. J. de Vries and A. J. Silva: From mTOR to cognition: molecular and cellular mechanisms of cognitive impairments in tuberous sclerosis. J Intellect Disabil Res, 53, 838-51 (2009)
    • (2009) J Intellect Disabil Res , vol.53 , pp. 838-851
    • Ehninger, D.1    De Vries, P.J.2    Silva, A.J.3
  • 72
    • 75749127850 scopus 로고    scopus 로고
    • Rapamycin protects against neuron death in in vitro and in vivo models of Parkinson's disease
    • C. Malagelada, Z. H. Jin, V. Jackson-Lewis, S. Przedborski and L. A. Greene: Rapamycin protects against neuron death in in vitro and in vivo models of Parkinson's disease. J Neurosci, 30, 1166-75 (2010)
    • (2010) J Neurosci , vol.30 , pp. 1166-1175
    • Malagelada, C.1    Jin, Z.H.2    Jackson-Lewis, V.3    Przedborski, S.4    Greene, L.A.5
  • 73
    • 61449235398 scopus 로고    scopus 로고
    • Not all substrates are treated equally: Implications for mTOR, rapamycin-resistance and cancer therapy
    • A. Y. Choo and J. Blenis: Not all substrates are treated equally: implications for mTOR, rapamycin-resistance and cancer therapy. Cell Cycle, 8, 567-72 (2009)
    • (2009) Cell Cycle , vol.8 , pp. 567-572
    • Choo, A.Y.1    Blenis, J.2
  • 75
    • 67650228579 scopus 로고    scopus 로고
    • Rapamycin inhibits mTORC1, but not completely
    • C. C. Thoreen and D. M. Sabatini: Rapamycin inhibits mTORC1, but not completely. Autophagy, 5, 725-6 (2009)
    • (2009) Autophagy , vol.5 , pp. 725-726
    • Thoreen, C.C.1    Sabatini, D.M.2
  • 76
    • 56249147509 scopus 로고    scopus 로고
    • Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-type-specific repression of mRNA translation
    • A. Y. Choo, S. O. Yoon, S. G. Kim, P. P. Roux and J. Blenis: Rapamycin differentially inhibits S6Ks and 4E-BP1 to mediate cell-type-specific repression of mRNA translation. Proc Natl Acad Sci U S A, 105, 17414-9 (2008)
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 17414-17419
    • Choo, A.Y.1    Yoon, S.O.2    Kim, S.G.3    Roux, P.P.4    Blenis, J.5
  • 78
    • 70350455151 scopus 로고    scopus 로고
    • Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway
    • T. Morita and K. Sobue: Specification of neuronal polarity regulated by local translation of CRMP2 and Tau via the mTOR-p70S6K pathway. J Biol Chem, 284, 27734-45 (2009)
    • (2009) J Biol Chem , vol.284 , pp. 27734-27745
    • Morita, T.1    Sobue, K.2
  • 79
    • 38049170722 scopus 로고    scopus 로고
    • Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2Aand glycogen synthase kinase-3-dependent phosphorylation of Tau
    • V. Meske, F. Albert and T. G. Ohm: Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2Aand glycogen synthase kinase-3-dependent phosphorylation of Tau. J Biol Chem, 283, 100-9 (2008)
    • (2008) J Biol Chem , vol.283 , pp. 100-109
    • Meske, V.1    Albert, F.2    Ohm, T.G.3
  • 80
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • DOI 10.1042/0264-6021:3530417
    • V. Janssens and J. Goris: Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J, 353, 417-39 (2001) (Pubitemid 32158309)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 82
    • 36348950449 scopus 로고    scopus 로고
    • Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells
    • DOI 10.1158/0008-5472.CAN-07-2310
    • R. J. Dowling, M. Zakikhani, I. G. Fantus, M. Pollak and N. Sonenberg: Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells. Cancer Res, 67, 10804-12 (2007) (Pubitemid 350145909)
    • (2007) Cancer Research , vol.67 , Issue.22 , pp. 10804-10812
    • Dowling, R.J.O.1    Zakikhani, M.2    Fantus, I.G.3    Pollak, M.4    Sonenberg, N.5
  • 83
    • 60749108023 scopus 로고    scopus 로고
    • The antidiabetic drug metformin suppresses HER2 (erbB-2) oncoprotein overexpression via inhibition of the mTOR effector p70S6K1 in human breast carcinoma cells
    • A. Vazquez-Martin, C. Oliveras-Ferraros and J. A. Menendez: The antidiabetic drug metformin suppresses HER2 (erbB-2) oncoprotein overexpression via inhibition of the mTOR effector p70S6K1 in human breast carcinoma cells. Cell Cycle, 8, 88-96 (2009)
    • (2009) Cell Cycle , vol.8 , pp. 88-96
    • Vazquez-Martin, A.1    Oliveras-Ferraros, C.2    Menendez, J.A.3
  • 86
    • 31944434543 scopus 로고    scopus 로고
    • TOR-mediated cell-cycle activation causes neurodegeneration in a Drosophila tauopathy model
    • DOI 10.1016/j.cub.2005.12.042, PII S0960982206010256
    • V. Khurana, Y. Lu, M. L. Steinhilb, S. Oldham, J. M. Shulman and M. B. Feany: TOR-mediated cell-cycle activation causes neurodegeneration in a Drosophila tauopathy model. Curr Biol, 16, 230-41 (2006) (Pubitemid 43190222)
    • (2006) Current Biology , vol.16 , Issue.3 , pp. 230-241
    • Khurana, V.1    Lu, Y.2    Steinhilb, M.L.3    Oldham, S.4    Shulman, J.M.5    Feany, M.B.6
  • 88
    • 70349638299 scopus 로고    scopus 로고
    • Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
    • K. R. Brunden, J. Q. Trojanowski and V. M. Lee: Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies. Nat Rev Drug Discov, 8, 783-93 (2009)
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 783-793
    • Brunden, K.R.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 89
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • DOI 10.1023/B:MCBI.0000041848.57020.57
    • A. M. Cuervo: Autophagy: many paths to the same end. Mol Cell Biochem, 263, 55-72 (2004) (Pubitemid 39256145)
    • (2004) Molecular and Cellular Biochemistry , vol.263 , Issue.1 , pp. 55-72
    • Cuervo, A.M.1
  • 90
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • DOI 10.1126/science.290.5497.1717
    • D. J. Klionsky and S. D. Emr: Autophagy as a regulated pathway of cellular degradation. Science, 290, 1717-21 (2000) (Pubitemid 32004796)
    • (2000) Science , vol.290 , Issue.5497 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 95
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • I. Tanida, N. Minematsu-Ikeguchi, T. Ueno and E. Kominami: Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy, 1, 84-91 (2005)
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 96
    • 53549113031 scopus 로고    scopus 로고
    • The role of TOR in autophagy regulation from yeast to plants and mammals
    • S. Diaz-Troya, M. E. Perez-Perez, F. J. Florencio and J. L. Crespo: The role of TOR in autophagy regulation from yeast to plants and mammals. Autophagy, 4, 851-65 (2008)
    • (2008) Autophagy , vol.4 , pp. 851-865
    • Diaz-Troya, S.1    Perez-Perez, M.E.2    Florencio, F.J.3    Crespo, J.L.4
  • 97
    • 37349003177 scopus 로고    scopus 로고
    • The role of autophagy in age-related neurodegeneration
    • DOI 10.1159/000109761
    • B. A. McCray and J. P. Taylor: The role of autophagy in age-related neurodegeneration. Neurosignals, 16, 75-84 (2008) (Pubitemid 350308323)
    • (2008) NeuroSignals , vol.16 , Issue.1 , pp. 75-84
    • McCray, B.A.1    Taylor, J.P.2
  • 98
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitin-proteasome system: Collaborators in neuroprotection
    • N. B. Nedelsky, P. K. Todd and J. P. Taylor: Autophagy and the ubiquitin-proteasome system: collaborators in neuroprotection. Biochim Biophys Acta, 1782, 691-9 (2008)
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 99
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • DOI 10.1038/nature05291, PII NATURE05291
    • D. C. Rubinsztein: The roles of intracellular proteindegradation pathways in neurodegeneration. Nature, 443, 780-6 (2006) (Pubitemid 44622682)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 100
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Alzheimer's disease
    • DOI 10.1111/j.1582-4934.2008.00276.x
    • S. Oddo: The ubiquitin-proteasome system in Alzheimer's disease. J Cell Mol Med, 12, 363-73 (2008) (Pubitemid 351555121)
    • (2008) Journal of Cellular and Molecular Medicine , vol.12 , Issue.2 , pp. 363-373
    • Oddo, S.1
  • 101
    • 53749088439 scopus 로고    scopus 로고
    • Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases
    • X. Li, H. Li and X. J. Li: Intracellular degradation of misfolded proteins in polyglutamine neurodegenerative diseases. Brain Res Rev, 59, 245-52 (2008)
    • (2008) Brain Res Rev , vol.59 , pp. 245-252
    • Li, X.1    Li, H.2    Li, X.J.3
  • 102
    • 70350454798 scopus 로고    scopus 로고
    • Rapamycin rescues TDP-43 mislocalization and the associated low molecular weight neurofilament instability
    • A. Caccamo, S. Majumder, J. J. Deng, Y. Bai, F. B. Thornton and S. Oddo: Rapamycin rescues TDP-43 mislocalization and the associated low molecular weight neurofilament instability. J Biol Chem (2009)
    • (2009) J Biol Chem
    • Caccamo, A.1    Majumder, S.2    Deng, J.J.3    Bai, Y.4    Thornton, F.B.5    Oddo, S.6
  • 103
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: When the cleaning crew goes on strike
    • DOI 10.1016/S1474-4422(07)70076-5, PII S1474442207700765
    • M. Martinez-Vicente and A. M. Cuervo: Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol, 6, 352-61 (2007) (Pubitemid 46367949)
    • (2007) Lancet Neurology , vol.6 , Issue.4 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 108
    • 37849030901 scopus 로고    scopus 로고
    • Polyglutamine diseases: Emerging concepts in pathogenesis and therapy
    • J. Shao and M. I. Diamond: Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum Mol Genet, 16 Spec No. 2, R115-23 (2007)
    • (2007) Hum Mol Genet , vol.16 , Issue.2
    • Shao, J.1    Diamond, M.I.2
  • 109
    • 69349087207 scopus 로고    scopus 로고
    • Diffusion of docosahexaenoic and eicosapentaenoic acids through the blood-brain barrier: An in situ cerebral perfusion study
    • M. Ouellet, V. Emond, C. T. Chen, C. Julien, F. Bourasset, S. Oddo, F. LaFerla, R. P. Bazinet and F. Calon: Diffusion of docosahexaenoic and eicosapentaenoic acids through the blood-brain barrier: An in situ cerebral perfusion study. Neurochem Int, 55, 476-82 (2009)
    • (2009) Neurochem Int , vol.55 , pp. 476-482
    • Ouellet, M.1    Emond, V.2    Chen, C.T.3    Julien, C.4    Bourasset, F.5    Oddo, S.6    La Ferla, F.7    Bazinet, R.P.8    Calon, F.9
  • 113
    • 68449089023 scopus 로고    scopus 로고
    • Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein
    • W. H. Yu, B. Dorado, H. Y. Figueroa, L. Wang, E. Planel, M. R. Cookson, L. N. Clark and K. E. Duff: Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein. Am J Pathol, 175, 736-47 (2009)
    • (2009) Am J Pathol , vol.175 , pp. 736-747
    • Yu, W.H.1    Dorado, B.2    Figueroa, H.Y.3    Wang, L.4    Planel, E.5    Cookson, M.R.6    Clark, L.N.7    Duff, K.E.8
  • 114
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • B. Boland, A. Kumar, S. Lee, F. M. Platt, J. Wegiel, W. H. Yu and R. A. Nixon: Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J Neurosci, 28, 6926-37 (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
  • 116
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from Abeta-induced cytotoxicity
    • S. Y. Hung, W. P. Huang, H. C. Liou and W. M. Fu: Autophagy protects neuron from Abeta-induced cytotoxicity. Autophagy, 5, 502-10 (2009)
    • (2009) Autophagy , vol.5 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3    Fu, W.M.4
  • 117
    • 67650264904 scopus 로고    scopus 로고
    • A central role for autophagy in Alzheimer-type neurodegeneration
    • D. Ling and P. M. Salvaterra: A central role for autophagy in Alzheimer-type neurodegeneration. Autophagy, 5, 738-40 (2009)
    • (2009) Autophagy , vol.5 , pp. 738-740
    • Ling, D.1    Salvaterra, P.M.2
  • 118
    • 58449101589 scopus 로고    scopus 로고
    • Abeta42-induced neurodegeneration via an agedependent autophagic-lysosomal injury in Drosophila
    • D. Ling, H. J. Song, D. Garza, T. P. Neufeld and P. M. Salvaterra: Abeta42-induced neurodegeneration via an agedependent autophagic-lysosomal injury in Drosophila. PLoS One, 4, e4201 (2009)
    • (2009) PLoS One , vol.4
    • Ling, D.1    Song, H.J.2    Garza, D.3    Neufeld, T.P.4    Salvaterra, P.M.5
  • 120
    • 79956048660 scopus 로고    scopus 로고
    • Parkin mediates beclindependent autophagic clearance of defective mitochondria and ubiquitinated A{beta} in AD models
    • P. J. Khandelwal, A. M. Herman, H. S. Hoe, G. W. Rebeck and C. E. Moussa: Parkin mediates beclindependent autophagic clearance of defective mitochondria and ubiquitinated A{beta} in AD models. Hum Mol Genet (2011)
    • (2011) Hum Mol Genet
    • Khandelwal, P.J.1    Herman, A.M.2    Hoe, H.S.3    Rebeck, G.W.4    Moussa, C.E.5
  • 121
    • 79957917512 scopus 로고    scopus 로고
    • A small-molecule enhancer of autophagy decreases levels of A{beta} and APP-CTF via Atg5-dependent autophagy pathway
    • Y. Tian, V. Bustos, M. Flajolet and P. Greengard: A small-molecule enhancer of autophagy decreases levels of A{beta} and APP-CTF via Atg5-dependent autophagy pathway. Faseb J (2011)
    • (2011) Faseb J
    • Tian, Y.1    Bustos, V.2    Flajolet, M.3    Greengard, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.