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Volumn 35, Issue 11, 2014, Pages 583-591

Targeting autophagy in neurodegenerative diseases

Author keywords

aggregation; autophagy; Beclin 1; mTOR; neurodegenerative disease; rapamycin

Indexed keywords

BECLIN 1; RAPAMYCIN; TREHALOSE; APOPTOSIS REGULATORY PROTEIN;

EID: 84908386761     PISSN: 01656147     EISSN: 18733735     Source Type: Journal    
DOI: 10.1016/j.tips.2014.09.002     Document Type: Review
Times cited : (136)

References (104)
  • 1
    • 84894539428 scopus 로고    scopus 로고
    • Systemic stress signalling: Understanding the cell non-autonomous control of proteostasis
    • R.C. Taylor Systemic stress signalling: understanding the cell non-autonomous control of proteostasis Nat. Rev. Mol. Cell Biol. 15 2014 211 217
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 211-217
    • Taylor, R.C.1
  • 2
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • A. Aguzzi Protein aggregation diseases: pathogenicity and therapeutic perspectives Nat. Rev. Drug Discov. 9 2000 237 248
    • (2000) Nat. Rev. Drug Discov. , vol.9 , pp. 237-248
    • Aguzzi, A.1
  • 3
    • 84861559058 scopus 로고    scopus 로고
    • Transmissible proteins: Expanding the prion heresy
    • C. Soto Transmissible proteins: expanding the prion heresy Cell 149 2012 968 977
    • (2012) Cell , vol.149 , pp. 968-977
    • Soto, C.1
  • 4
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • C. Soto Unfolding the role of protein misfolding in neurodegenerative diseases Nat. Rev. Neurosci. 4 2003 49 60
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 5
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • C. Hetz Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases Nat. Rev. Neurosci. 15 2014 233 249
    • (2014) Nat. Rev. Neurosci. , vol.15 , pp. 233-249
    • Hetz, C.1
  • 6
    • 79954425069 scopus 로고    scopus 로고
    • Protein misfolding disorders and macroautophagy
    • F.M. Menzies Protein misfolding disorders and macroautophagy Curr. Opin. Cell Biol. 23 2011 190 197
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 190-197
    • Menzies, F.M.1
  • 7
    • 84884634690 scopus 로고    scopus 로고
    • Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: Autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers
    • S. Sarkar Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers Biochem. Soc. Trans. 41 2013 1103 1130
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1103-1130
    • Sarkar, S.1
  • 8
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • D.C. Rubinsztein Autophagy modulation as a potential therapeutic target for diverse diseases Nat. Rev. Drug Discov. 11 2012 709 730
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1
  • 9
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded Huntingtin and related proteinopathies
    • S. Sarkar Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded Huntingtin and related proteinopathies Cell Death Differ. 16 2009 46 56
    • (2009) Cell Death Differ. , vol.16 , pp. 46-56
    • Sarkar, S.1
  • 10
    • 79954417611 scopus 로고    scopus 로고
    • Autophagy for tissue homeostasis and neuroprotection
    • G. Marino Autophagy for tissue homeostasis and neuroprotection Curr. Opin. Cell Biol. 23 2011 198 206
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 198-206
    • Marino, G.1
  • 11
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • C. Haass Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8 2007 101 112
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1
  • 12
    • 3142596164 scopus 로고    scopus 로고
    • Molecular pathways to neurodegeneration
    • E. Bossy-Wetzel Molecular pathways to neurodegeneration Nat. Med. 10 Suppl. 2004 S2 S9
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL. , pp. 2-S9
    • Bossy-Wetzel, E.1
  • 13
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • W. Dauer Parkinson's disease: mechanisms and models Neuron 39 2003 889 909
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1
  • 14
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • A.J. Williams Polyglutamine neurodegeneration: protein misfolding revisited Trends Neurosci. 31 2008 521 528
    • (2008) Trends Neurosci. , vol.31 , pp. 521-528
    • Williams, A.J.1
  • 15
    • 44449131447 scopus 로고    scopus 로고
    • Huntington's disease: From pathology and genetics to potential therapies
    • S. Imarisio Huntington's disease: from pathology and genetics to potential therapies Biochem. J. 412 2008 191 209
    • (2008) Biochem. J. , vol.412 , pp. 191-209
    • Imarisio, S.1
  • 16
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • P. Pasinelli Molecular biology of amyotrophic lateral sclerosis: insights from genetics Nat. Rev. Neurosci. 7 2006 710 723
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1
  • 17
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: What do we really know?
    • P.M. Andersen Clinical genetics of amyotrophic lateral sclerosis: what do we really know? Nat. Rev. Neurol. 7 2011 603 615
    • (2011) Nat. Rev. Neurol. , vol.7 , pp. 603-615
    • Andersen, P.M.1
  • 18
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • N. Mizushima Autophagy fights disease through cellular self-digestion Nature 451 2008 1069 1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1
  • 19
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • M.C. Maiuri Self-eating and self-killing: crosstalk between autophagy and apoptosis Nat. Rev. Mol. Cell Biol. 8 2007 741 752
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 741-752
    • Maiuri, M.C.1
  • 20
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • C. He Regulation mechanisms and signaling pathways of autophagy Annu. Rev. Genet. 43 2009 67 93
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 67-93
    • He, C.1
  • 21
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • C. He The Beclin 1 interactome Curr. Opin. Cell Biol. 22 2010 140 149
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 140-149
    • He, C.1
  • 22
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • S. Pattingre Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy Cell 122 2005 927 939
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1
  • 23
    • 70349687405 scopus 로고    scopus 로고
    • Discovery of Atg5/Atg7-independent alternative macroautophagy
    • Y. Nishida Discovery of Atg5/Atg7-independent alternative macroautophagy Nature 461 2009 654 658
    • (2009) Nature , vol.461 , pp. 654-658
    • Nishida, Y.1
  • 24
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • D.J. Klionsky Guidelines for the use and interpretation of assays for monitoring autophagy Autophagy 8 2012 445 544
    • (2012) Autophagy , vol.8 , pp. 445-544
    • Klionsky, D.J.1
  • 25
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • A. Williams Novel targets for Huntington's disease in an mTOR-independent autophagy pathway Nat. Chem. Biol. 4 2008 295 305
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 295-305
    • Williams, A.1
  • 26
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant Huntingtin and alpha-synuclein
    • S. Sarkar Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant Huntingtin and alpha-synuclein J Biol. Chem. 282 2007 5641 5652
    • (2007) J Biol. Chem. , vol.282 , pp. 5641-5652
    • Sarkar, S.1
  • 27
    • 84875753542 scopus 로고    scopus 로고
    • Chemical screening platforms for autophagy drug discovery to identify therapeutic candidates for Huntington's disease and other neurodegenerative disorders
    • S. Sarkar Chemical screening platforms for autophagy drug discovery to identify therapeutic candidates for Huntington's disease and other neurodegenerative disorders Drug Discov. Today Technol. 10 2013 e137 e144
    • (2013) Drug Discov. Today Technol. , vol.10 , pp. 137-e144
    • Sarkar, S.1
  • 28
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • S. Sarkar Lithium induces autophagy by inhibiting inositol monophosphatase J. Cell Biol. 170 2005 1101 1111
    • (2005) J. Cell Biol. , vol.170 , pp. 1101-1111
    • Sarkar, S.1
  • 29
    • 79951889242 scopus 로고    scopus 로고
    • Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome
    • E. Morselli Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome J. Cell Biol. 192 2011 615 629
    • (2011) J. Cell Biol. , vol.192 , pp. 615-629
    • Morselli, E.1
  • 30
    • 80052303130 scopus 로고    scopus 로고
    • Autophagy and aging
    • D.C. Rubinsztein Autophagy and aging Cell 146 2011 682 695
    • (2011) Cell , vol.146 , pp. 682-695
    • Rubinsztein, D.C.1
  • 31
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • G. Kroemer Autophagy and the integrated stress response Mol. Cell 40 2010 280 293
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1
  • 32
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • M. Ogata Autophagy is activated for cell survival after endoplasmic reticulum stress Mol. Cell. Biol. 26 2006 9220 9231
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9220-9231
    • Ogata, M.1
  • 33
    • 34247380330 scopus 로고    scopus 로고
    • Regulation of autophagy by the inositol trisphosphate receptor
    • A. Criollo Regulation of autophagy by the inositol trisphosphate receptor Cell Death Differ. 14 2007 1029 1039
    • (2007) Cell Death Differ. , vol.14 , pp. 1029-1039
    • Criollo, A.1
  • 34
    • 80455173839 scopus 로고    scopus 로고
    • BAX inhibitor-1 regulates autophagy by controlling the IRE1alpha branch of the unfolded protein response
    • K. Castillo BAX inhibitor-1 regulates autophagy by controlling the IRE1alpha branch of the unfolded protein response EMBO J. 30 2011 4465 4478
    • (2011) EMBO J. , vol.30 , pp. 4465-4478
    • Castillo, K.1
  • 35
    • 84891748139 scopus 로고    scopus 로고
    • A current perspective of autophagosome biogenesis
    • S.T. Shibutani A current perspective of autophagosome biogenesis Cell Res. 24 2014 58 68
    • (2014) Cell Res. , vol.24 , pp. 58-68
    • Shibutani, S.T.1
  • 36
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • E.L. Axe Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum J. Cell Biol. 182 2008 685 701
    • (2008) J. Cell Biol. , vol.182 , pp. 685-701
    • Axe, E.L.1
  • 37
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • T. Hara Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice Nature 441 2006 885 889
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1
  • 38
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • M. Komatsu Loss of autophagy in the central nervous system causes neurodegeneration in mice Nature 441 2006 880 884
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1
  • 39
    • 82755161734 scopus 로고    scopus 로고
    • Autophagy and disease: Always two sides to a problem
    • S. Sridhar Autophagy and disease: always two sides to a problem J. Pathol. 226 2012 255 273
    • (2012) J. Pathol. , vol.226 , pp. 255-273
    • Sridhar, S.1
  • 40
    • 79953665568 scopus 로고    scopus 로고
    • Targeting autophagy in ALS: A complex mission
    • M. Nassif Targeting autophagy in ALS: a complex mission Autophagy 7 2011 450 453
    • (2011) Autophagy , vol.7 , pp. 450-453
    • Nassif, M.1
  • 41
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • E. Wong Autophagy gone awry in neurodegenerative diseases Nat. Neurosci. 13 2010 805 811
    • (2010) Nat. Neurosci. , vol.13 , pp. 805-811
    • Wong, E.1
  • 42
    • 77957565855 scopus 로고    scopus 로고
    • Age at onset in Huntington's disease is modified by the autophagy pathway: Implication of the V471A polymorphism in Atg7
    • S. Metzger Age at onset in Huntington's disease is modified by the autophagy pathway: implication of the V471A polymorphism in Atg7 Hum. Genet. 128 2010 453 459
    • (2010) Hum. Genet. , vol.128 , pp. 453-459
    • Metzger, S.1
  • 43
    • 45749114895 scopus 로고    scopus 로고
    • The autophagy-related protein Beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice
    • F. Pickford The autophagy-related protein Beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice J. Clin. Invest. 118 2008 2190 2199
    • (2008) J. Clin. Invest. , vol.118 , pp. 2190-2199
    • Pickford, F.1
  • 44
    • 33744916798 scopus 로고    scopus 로고
    • Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
    • M. Shibata Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1 J. Biol. Chem. 281 2006 14474 14485
    • (2006) J. Biol. Chem. , vol.281 , pp. 14474-14485
    • Shibata, M.1
  • 45
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • C. Hetz XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy Genes Dev. 23 2009 2294 2306
    • (2009) Genes Dev. , vol.23 , pp. 2294-2306
    • Hetz, C.1
  • 46
    • 84856189081 scopus 로고    scopus 로고
    • Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways
    • J. Wills Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways PLoS ONE 7 2012 e30745
    • (2012) PLoS ONE , vol.7 , pp. 30745
    • Wills, J.1
  • 47
    • 79957458183 scopus 로고    scopus 로고
    • Overexpression of the autophagic Beclin-1 protein clears mutant ataxin-3 and alleviates Machado-Joseph disease
    • I. Nascimento-Ferreira Overexpression of the autophagic Beclin-1 protein clears mutant ataxin-3 and alleviates Machado-Joseph disease Brain 134 2011 1400 1415
    • (2011) Brain , vol.134 , pp. 1400-1415
    • Nascimento-Ferreira, I.1
  • 48
    • 84862547657 scopus 로고    scopus 로고
    • The regulation of N-terminal Huntingtin (Htt552) accumulation by Beclin1
    • J.C. Wu The regulation of N-terminal Huntingtin (Htt552) accumulation by Beclin1 Acta Pharmacol. Sin. 33 2012 743 751
    • (2012) Acta Pharmacol. Sin. , vol.33 , pp. 743-751
    • Wu, J.C.1
  • 49
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • B. Spencer Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases J. Neurosci. 29 2009 13578 13588
    • (2009) J. Neurosci. , vol.29 , pp. 13578-13588
    • Spencer, B.1
  • 50
    • 84881490638 scopus 로고    scopus 로고
    • Tyrosine kinase inhibition increases functional Parkin-Beclin-1 interaction and enhances amyloid clearance and cognitive performance
    • I. Lonskaya Tyrosine kinase inhibition increases functional Parkin-Beclin-1 interaction and enhances amyloid clearance and cognitive performance EMBO Mol. Med. 5 2013 1247 1262
    • (2013) EMBO Mol. Med. , vol.5 , pp. 1247-1262
    • Lonskaya, I.1
  • 51
    • 84898463603 scopus 로고    scopus 로고
    • Pathogenic role of BECN1/Beclin 1 in the development of amyotrophic lateral sclerosis
    • M. Nassif Pathogenic role of BECN1/Beclin 1 in the development of amyotrophic lateral sclerosis Autophagy 10 2014 1256 1271
    • (2014) Autophagy , vol.10 , pp. 1256-1271
    • Nassif, M.1
  • 52
    • 84893690813 scopus 로고    scopus 로고
    • Rhes, a striatal-selective protein implicated in Huntington disease, binds Beclin-1 and activates autophagy
    • R.G. Mealer Rhes, a striatal-selective protein implicated in Huntington disease, binds Beclin-1 and activates autophagy J. Biol. Chem. 289 2014 3547 3554
    • (2014) J. Biol. Chem. , vol.289 , pp. 3547-3554
    • Mealer, R.G.1
  • 53
    • 77952242572 scopus 로고    scopus 로고
    • The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy
    • S. Michiorri The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy Cell Death Differ. 17 2010 962 974
    • (2010) Cell Death Differ. , vol.17 , pp. 962-974
    • Michiorri, S.1
  • 54
    • 84880303306 scopus 로고    scopus 로고
    • PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage
    • G. Arena PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage Cell Death Differ. 20 2013 920 930
    • (2013) Cell Death Differ. , vol.20 , pp. 920-930
    • Arena, G.1
  • 55
    • 77951665859 scopus 로고    scopus 로고
    • Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease
    • M. Martinez-Vicente Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease Nat. Neurosci. 13 2010 567 576
    • (2010) Nat. Neurosci. , vol.13 , pp. 567-576
    • Martinez-Vicente, M.1
  • 56
    • 80855150639 scopus 로고    scopus 로고
    • SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis
    • F. Fecto SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis Arch. Neurol. 68 2011 1440 1446
    • (2011) Arch. Neurol. , vol.68 , pp. 1440-1446
    • Fecto, F.1
  • 57
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • J. Gal Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism J. Neurochem. 111 2009 1062 1073
    • (2009) J. Neurochem. , vol.111 , pp. 1062-1073
    • Gal, J.1
  • 58
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • O.A. Brady Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1 J. Neurochem. 116 2011 248 259
    • (2011) J. Neurochem. , vol.116 , pp. 248-259
    • Brady, O.A.1
  • 59
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • H.X. Deng Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia Nature 477 2011 211 215
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1
  • 60
    • 78149339310 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis pathogenesis: A journey through the secretory pathway
    • M. Nassif Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway Antioxid. Redox Signal. 13 2010 1955 1989
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1955-1989
    • Nassif, M.1
  • 62
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • J.H. Lee Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations Cell 141 2010 1146 1158
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1
  • 63
    • 78650716872 scopus 로고    scopus 로고
    • Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits
    • D.S. Yang Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits Brain 134 2011 258 277
    • (2011) Brain , vol.134 , pp. 258-277
    • Yang, D.S.1
  • 64
    • 77956855813 scopus 로고    scopus 로고
    • Pathogenic lysosomal depletion in Parkinson's disease
    • B. Dehay Pathogenic lysosomal depletion in Parkinson's disease J. Neurosci. 30 2010 12535 12544
    • (2010) J. Neurosci. , vol.30 , pp. 12535-12544
    • Dehay, B.1
  • 65
    • 84862189804 scopus 로고    scopus 로고
    • Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration
    • B. Dehay Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration Proc. Natl. Acad. Sci. U.S.A. 109 2012 9611 9616
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 9611-9616
    • Dehay, B.1
  • 66
    • 84875640261 scopus 로고    scopus 로고
    • Interplay of LRRK2 with chaperone-mediated autophagy
    • S.J. Orenstein Interplay of LRRK2 with chaperone-mediated autophagy Nat. Neurosci. 16 2013 394 406
    • (2013) Nat. Neurosci. , vol.16 , pp. 394-406
    • Orenstein, S.J.1
  • 67
    • 38849174979 scopus 로고    scopus 로고
    • Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy
    • M. Martinez-Vicente Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy J. Clin. Invest. 118 2008 777 788
    • (2008) J. Clin. Invest. , vol.118 , pp. 777-788
    • Martinez-Vicente, M.1
  • 68
    • 77957189194 scopus 로고    scopus 로고
    • Alpha-synuclein impairs macroautophagy: Implications for Parkinson's disease
    • A.R. Winslow Alpha-synuclein impairs macroautophagy: implications for Parkinson's disease J. Cell Biol. 190 2010 1023 1037
    • (2010) J. Cell Biol. , vol.190 , pp. 1023-1037
    • Winslow, A.R.1
  • 69
    • 84900460616 scopus 로고    scopus 로고
    • Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy
    • E. Zavodszky Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy Nat. Commun. 5 2014 3828
    • (2014) Nat. Commun. , vol.5 , pp. 3828
    • Zavodszky, E.1
  • 71
    • 84903635313 scopus 로고    scopus 로고
    • BECN1 is involved in the initiation of mitophagy: It facilitates PARK2 translocation to mitochondria
    • V. Choubey BECN1 is involved in the initiation of mitophagy: it facilitates PARK2 translocation to mitochondria Autophagy 10 2014 1105 1119
    • (2014) Autophagy , vol.10 , pp. 1105-1119
    • Choubey, V.1
  • 72
    • 78650448754 scopus 로고    scopus 로고
    • Chemical modulators of autophagy as biological probes and potential therapeutics
    • A. Fleming Chemical modulators of autophagy as biological probes and potential therapeutics Nat. Chem. Biol. 7 2011 9 17
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 9-17
    • Fleming, A.1
  • 73
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • B. Ravikumar Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease Nat. Genet. 36 2004 585 595
    • (2004) Nat. Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1
  • 74
    • 80053243942 scopus 로고    scopus 로고
    • Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits
    • S. Majumder Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits PLoS ONE 6 2011 e25416
    • (2011) PLoS ONE , vol.6 , pp. 25416
    • Majumder, S.1
  • 75
    • 77951227122 scopus 로고    scopus 로고
    • Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and tau: Effects on cognitive impairments
    • A. Caccamo Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and tau: effects on cognitive impairments J. Biol. Chem. 285 2010 13107 13120
    • (2010) J. Biol. Chem. , vol.285 , pp. 13107-13120
    • Caccamo, A.1
  • 76
    • 79953208952 scopus 로고    scopus 로고
    • Naturally secreted amyloid-beta increases mammalian target of rapamycin (mTOR) activity via a PRAS40-mediated mechanism
    • A. Caccamo Naturally secreted amyloid-beta increases mammalian target of rapamycin (mTOR) activity via a PRAS40-mediated mechanism J. Biol. Chem. 286 2011 8924 8932
    • (2011) J. Biol. Chem. , vol.286 , pp. 8924-8932
    • Caccamo, A.1
  • 77
    • 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
    • P. Spilman Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease PLoS ONE 5 2010 e9979
    • (2010) PLoS ONE , vol.5 , pp. 9979
    • Spilman, P.1
  • 78
    • 75749127850 scopus 로고    scopus 로고
    • Rapamycin protects against neuron death in in vitro and in vivo models of Parkinson's disease
    • C. Malagelada Rapamycin protects against neuron death in in vitro and in vivo models of Parkinson's disease J. Neurosci. 30 2010 1166 1175
    • (2010) J. Neurosci. , vol.30 , pp. 1166-1175
    • Malagelada, C.1
  • 79
    • 49749096430 scopus 로고    scopus 로고
    • Small molecule enhancers of autophagy for neurodegenerative diseases
    • S. Sarkar Small molecule enhancers of autophagy for neurodegenerative diseases Mol. Biosyst. 4 2008 895 901
    • (2008) Mol. Biosyst. , vol.4 , pp. 895-901
    • Sarkar, S.1
  • 80
    • 84861898911 scopus 로고    scopus 로고
    • Dietary restriction but not rapamycin extends disease onset and survival of the H46R/H48Q mouse model of ALS
    • A. Bhattacharya Dietary restriction but not rapamycin extends disease onset and survival of the H46R/H48Q mouse model of ALS Neurobiol. Aging 33 2012 1829 1832
    • (2012) Neurobiol. Aging , vol.33 , pp. 1829-1832
    • Bhattacharya, A.1
  • 81
    • 84883637335 scopus 로고    scopus 로고
    • Rapamycin increases survival in ALS mice lacking mature lymphocytes
    • K.A. Staats Rapamycin increases survival in ALS mice lacking mature lymphocytes Mol. Neurodegener. 8 2013 31
    • (2013) Mol. Neurodegener. , vol.8 , pp. 31
    • Staats, K.A.1
  • 82
    • 79953647105 scopus 로고    scopus 로고
    • Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • X. Zhang Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis Autophagy 7 2011 412 425
    • (2011) Autophagy , vol.7 , pp. 412-425
    • Zhang, X.1
  • 83
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • I.F. Wang Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43 Proc. Natl. Acad. Sci. U.S.A. 109 2012 15024 15029
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 15024-15029
    • Wang, I.F.1
  • 84
    • 84874529071 scopus 로고    scopus 로고
    • MTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy
    • J.K. Ching mTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy Hum. Mol. Genet. 22 2013 1167 1179
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1167-1179
    • Ching, J.K.1
  • 85
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • M. Tanaka Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease Nat. Med. 10 2004 148 154
    • (2004) Nat. Med. , vol.10 , pp. 148-154
    • Tanaka, M.1
  • 86
    • 84860296702 scopus 로고    scopus 로고
    • Trehalose protects from aggravation of amyloid pathology induced by isoflurane anesthesia in APP(swe) mutant mice
    • J. Perucho Trehalose protects from aggravation of amyloid pathology induced by isoflurane anesthesia in APP(swe) mutant mice Curr. Alzheimer Res. 9 2012 334 343
    • (2012) Curr. Alzheimer Res. , vol.9 , pp. 334-343
    • Perucho, J.1
  • 87
    • 77954955573 scopus 로고    scopus 로고
    • Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation
    • J.A. Rodriguez-Navarro Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation Neurobiol. Dis. 39 2010 423 438
    • (2010) Neurobiol. Dis. , vol.39 , pp. 423-438
    • Rodriguez-Navarro, J.A.1
  • 88
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • V. Schaeffer Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy Brain 135 2012 2169 2177
    • (2012) Brain , vol.135 , pp. 2169-2177
    • Schaeffer, V.1
  • 89
    • 29644437591 scopus 로고    scopus 로고
    • Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
    • J.E. Davies Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy Hum. Mol. Genet. 15 2006 23 31
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 23-31
    • Davies, J.E.1
  • 90
    • 84884294596 scopus 로고    scopus 로고
    • Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons
    • K. Castillo Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons Autophagy 9 2013 1308 1320
    • (2013) Autophagy , vol.9 , pp. 1308-1320
    • Castillo, K.1
  • 91
    • 84898486403 scopus 로고    scopus 로고
    • A new method to measure autophagy flux in the nervous system
    • S. Matus A new method to measure autophagy flux in the nervous system Autophagy 10 2014 710 714
    • (2014) Autophagy , vol.10 , pp. 710-714
    • Matus, S.1
  • 92
    • 84898465382 scopus 로고    scopus 로고
    • MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis
    • X. Zhang mTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis Autophagy 10 2014 588 602
    • (2014) Autophagy , vol.10 , pp. 588-602
    • Zhang, X.1
  • 93
    • 84876410429 scopus 로고    scopus 로고
    • Unspliced XBP1 controls autophagy through FoxO1
    • R.L. Vidal Unspliced XBP1 controls autophagy through FoxO1 Cell Res. 23 2014 463 464
    • (2014) Cell Res. , vol.23 , pp. 463-464
    • Vidal, R.L.1
  • 94
    • 84862281225 scopus 로고    scopus 로고
    • Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
    • E.E. Congdon Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo Autophagy 8 2012 609 622
    • (2012) Autophagy , vol.8 , pp. 609-622
    • Congdon, E.E.1
  • 95
    • 79959886743 scopus 로고    scopus 로고
    • Complex inhibitory effects of nitric oxide on autophagy
    • S. Sarkar Complex inhibitory effects of nitric oxide on autophagy Mol. Cell 43 2011 19 32
    • (2011) Mol. Cell , vol.43 , pp. 19-32
    • Sarkar, S.1
  • 96
    • 79551543554 scopus 로고    scopus 로고
    • Rescue of progranulin deficiency associated with frontotemporal lobar degeneration by alkalizing reagents and inhibition of vacuolar ATPase
    • A. Capell Rescue of progranulin deficiency associated with frontotemporal lobar degeneration by alkalizing reagents and inhibition of vacuolar ATPase J. Neurosci. 31 2011 1885 1894
    • (2011) J. Neurosci. , vol.31 , pp. 1885-1894
    • Capell, A.1
  • 97
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • W.E. Balch Adapting proteostasis for disease intervention Science 319 2008 916 919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1
  • 98
    • 84918547483 scopus 로고    scopus 로고
    • Control of systemic proteostasis by the nervous system
    • P. Mardones Control of systemic proteostasis by the nervous system Trends Cell Biol. 2014 10.1016/j.tcb.2014.08.001
    • (2014) Trends Cell Biol.
    • Mardones, P.1
  • 99
    • 84862303631 scopus 로고    scopus 로고
    • ER stress inhibits neuronal death by promoting autophagy
    • A. Fouillet ER stress inhibits neuronal death by promoting autophagy Autophagy 8 2013 915 926
    • (2013) Autophagy , vol.8 , pp. 915-926
    • Fouillet, A.1
  • 100
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy
    • R.L. Vidal Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy Hum. Mol. Genet. 21 2012 2245 2262
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2245-2262
    • Vidal, R.L.1
  • 101
    • 84885456003 scopus 로고    scopus 로고
    • The ire-1 ER stress-response pathway is required for normal secretory-protein metabolism in C. Elegans
    • M. Safra The ire-1 ER stress-response pathway is required for normal secretory-protein metabolism in C. elegans J. Cell Sci. 126 2013 4136 4146
    • (2013) J. Cell Sci. , vol.126 , pp. 4136-4146
    • Safra, M.1
  • 102
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • C. Hetz Targeting the unfolded protein response in disease Nat. Rev. Drug Discov. 12 2014 703 719
    • (2014) Nat. Rev. Drug Discov. , vol.12 , pp. 703-719
    • Hetz, C.1
  • 103
    • 84879899999 scopus 로고    scopus 로고
    • Beclin 1 mitigates motor and neuropathological deficits in genetic mouse models of Machado-Joseph disease
    • I. Nascimento-Ferreira Beclin 1 mitigates motor and neuropathological deficits in genetic mouse models of Machado-Joseph disease Brain 136 2013 2173 2188
    • (2013) Brain , vol.136 , pp. 2173-2188
    • Nascimento-Ferreira, I.1
  • 104
    • 77956215864 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein processing by the Beclin 1 complex
    • P.A. Jaeger Regulation of amyloid precursor protein processing by the Beclin 1 complex PLoS ONE 5 2010 e11102
    • (2010) PLoS ONE , vol.5 , pp. 11102
    • Jaeger, P.A.1


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