메뉴 건너뛰기




Volumn 93, Issue 5, 2017, Pages 1015-1034

Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities

Author keywords

Alzheimer's disease; autophagy; dementia; Huntington's disease; lysosome; motor neuron disease; neurodegeneration; Parkinson's disease; tau

Indexed keywords

EVEROLIMUS; POLYGLUTAMINE; RAPAMYCIN; RAPAMYCIN DERIVATIVE; PROTEIN;

EID: 85014799386     PISSN: 08966273     EISSN: 10974199     Source Type: Journal    
DOI: 10.1016/j.neuron.2017.01.022     Document Type: Review
Times cited : (857)

References (285)
  • 6
    • 84973879571 scopus 로고    scopus 로고
    • Level of PICALM, a key component of clathrin-mediated endocytosis, is correlated with levels of phosphotau and autophagy-related proteins and is associated with tau inclusions in AD, PSP and Pick disease
    • Ando, K., Tomimura, K., Sazdovitch, V., Suain, V., Yilmaz, Z., Authelet, M., Ndjim, M., Vergara, C., Belkouch, M., Potier, M.C., et al. Level of PICALM, a key component of clathrin-mediated endocytosis, is correlated with levels of phosphotau and autophagy-related proteins and is associated with tau inclusions in AD, PSP and Pick disease. Neurobiol. Dis. 94 (2016), 32–43.
    • (2016) Neurobiol. Dis. , vol.94 , pp. 32-43
    • Ando, K.1    Tomimura, K.2    Sazdovitch, V.3    Suain, V.4    Yilmaz, Z.5    Authelet, M.6    Ndjim, M.7    Vergara, C.8    Belkouch, M.9    Potier, M.C.10
  • 7
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E.L., Walker, S.A., Manifava, M., Chandra, P., Roderick, H.L., Habermann, A., Griffiths, G., Ktistakis, N.T., 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    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 8
    • 62949116803 scopus 로고    scopus 로고
    • Lysosomal disorders: from storage to cellular damage
    • Ballabio, A., Gieselmann, V., Lysosomal disorders: from storage to cellular damage. Biochim. Biophys. Acta 1793 (2009), 684–696.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 684-696
    • Ballabio, A.1    Gieselmann, V.2
  • 10
    • 84973596577 scopus 로고    scopus 로고
    • The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate autophagy via a common pathway
    • Bento, C.F., Ashkenazi, A., Jimenez-Sanchez, M., Rubinsztein, D.C., The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate autophagy via a common pathway. Nat. Commun., 7, 2016, 11803.
    • (2016) Nat. Commun. , vol.7 , pp. 11803
    • Bento, C.F.1    Ashkenazi, A.2    Jimenez-Sanchez, M.3    Rubinsztein, D.C.4
  • 14
    • 33745922994 scopus 로고
    • Charcot-Marie-Tooth Hereditary Neuropathy Overview
    • R.A. Pagon M.P. Adam H.H. Ardinger S.E. Wallace A. Amemiya L.J.H. Bean T.D. Bird C.T. Fong H.C. Mefford R.J.H. Smith K. Stephens University of Washington Seattle, WA
    • Bird, T.D., Charcot-Marie-Tooth Hereditary Neuropathy Overview. Pagon, R.A., Adam, M.P., Ardinger, H.H., Wallace, S.E., Amemiya, A., Bean, L.J.H., Bird, T.D., Fong, C.T., Mefford, H.C., Smith, R.J.H., Stephens, K., (eds.) GeneReviews(R), 1993, University of Washington, Seattle, WA.
    • (1993) GeneReviews(R)
    • Bird, T.D.1
  • 15
    • 84871351575 scopus 로고
    • Charcot-Marie-Tooth Neuropathy Type 1
    • R.A. Pagon M.P. Adam H.H. Ardinger S.E. Wallace A. Amemiya L.J.H. Bean T.D. Bird C.T. Fong H.C. Mefford R.J.H. Smith K. Stephens University of Washington Seattle, WA
    • Bird, T.D., Charcot-Marie-Tooth Neuropathy Type 1. Pagon, R.A., Adam, M.P., Ardinger, H.H., Wallace, S.E., Amemiya, A., Bean, L.J.H., Bird, T.D., Fong, C.T., Mefford, H.C., Smith, R.J.H., Stephens, K., (eds.) GeneReviews(R), 1993, University of Washington, Seattle, WA.
    • (1993) GeneReviews(R)
    • Bird, T.D.1
  • 16
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H., Johansen, T., p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171 (2005), 603–614.
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 17
    • 77950360086 scopus 로고    scopus 로고
    • Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase
    • Blanz, J., Groth, J., Zachos, C., Wehling, C., Saftig, P., Schwake, M., Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase. Hum. Mol. Genet. 19 (2010), 563–572.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 563-572
    • Blanz, J.1    Groth, J.2    Zachos, C.3    Wehling, C.4    Saftig, P.5    Schwake, M.6
  • 19
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease
    • Boland, B., Kumar, A., Lee, S., Platt, F.M., Wegiel, J., Yu, W.H., Nixon, R.A., Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J. Neurosci. 28 (2008), 6926–6937.
    • (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
  • 23
    • 84915793059 scopus 로고    scopus 로고
    • Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation
    • Chang, J., Lee, S., Blackstone, C., Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation. J. Clin. Invest. 124 (2014), 5249–5262.
    • (2014) J. Clin. Invest. , vol.124 , pp. 5249-5262
    • Chang, J.1    Lee, S.2    Blackstone, C.3
  • 26
    • 84921456454 scopus 로고    scopus 로고
    • A53T human α-synuclein overexpression in transgenic mice induces pervasive mitochondria macroautophagy defects preceding dopamine neuron degeneration
    • Chen, L., Xie, Z., Turkson, S., Zhuang, X., A53T human α-synuclein overexpression in transgenic mice induces pervasive mitochondria macroautophagy defects preceding dopamine neuron degeneration. J. Neurosci. 35 (2015), 890–905.
    • (2015) J. Neurosci. , vol.35 , pp. 890-905
    • Chen, L.1    Xie, Z.2    Turkson, S.3    Zhuang, X.4
  • 27
    • 84989284335 scopus 로고    scopus 로고
    • Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
    • Ciechanover, A., Kwon, Y.T., Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. Exp Mol Med., 47, 2015, e147.
    • (2015) Exp Mol Med. , vol.47 , pp. e147
    • Ciechanover, A.1    Kwon, Y.T.2
  • 29
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice
    • Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-Wood, K., Lee, M., Seubert, P., Davis, A., et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells and transgenic mice. Nat. Med. 3 (1997), 67–72.
    • (1997) Nat. Med. , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3    Carlson, G.4    Diehl, T.5    Levesque, G.6    Johnson-Wood, K.7    Lee, M.8    Seubert, P.9    Davis, A.10
  • 30
    • 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
    • Coffey, E.E., Beckel, J.M., Laties, A.M., Mitchell, C.H., Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer's disease-linked presenilin 1 A246E mutation can be reversed with cAMP. Neuroscience 263 (2014), 111–124.
    • (2014) Neuroscience , vol.263 , pp. 111-124
    • Coffey, E.E.1    Beckel, J.M.2    Laties, A.M.3    Mitchell, C.H.4
  • 31
    • 84971643966 scopus 로고    scopus 로고
    • Disorders of lysosomal acidification-the emerging role of v-ATPase in aging and neurodegenerative disease
    • Colacurcio, D.J., Nixon, R.A., Disorders of lysosomal acidification-the emerging role of v-ATPase in aging and neurodegenerative disease. Ageing Res. Rev. 32 (2016), 75–88.
    • (2016) Ageing Res. Rev. , vol.32 , pp. 75-88
    • Colacurcio, D.J.1    Nixon, R.A.2
  • 32
    • 84908377705 scopus 로고    scopus 로고
    • Neuronal uptake of tau/pS422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer's disease
    • Collin, L., Bohrmann, B., Göpfert, U., Oroszlan-Szovik, K., Ozmen, L., Grüninger, F., Neuronal uptake of tau/pS422 antibody and reduced progression of tau pathology in a mouse model of Alzheimer's disease. Brain 137 (2014), 2834–2846.
    • (2014) Brain , vol.137 , pp. 2834-2846
    • Collin, L.1    Bohrmann, B.2    Göpfert, U.3    Oroszlan-Szovik, K.4    Ozmen, L.5    Grüninger, F.6
  • 35
    • 84865749298 scopus 로고    scopus 로고
    • Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Sträussler-Scheinker disease
    • Cortes, C.J., Qin, K., Cook, J., Solanki, A., Mastrianni, J.A., Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Sträussler-Scheinker disease. J. Neurosci. 32 (2012), 12396–12405.
    • (2012) J. Neurosci. , vol.32 , pp. 12396-12405
    • Cortes, C.J.1    Qin, K.2    Cook, J.3    Solanki, A.4    Mastrianni, J.A.5
  • 38
    • 84968928647 scopus 로고    scopus 로고
    • Caloric restriction blocks neuropathology and motor deficits in Machado-Joseph disease mouse models through SIRT1 pathway
    • Cunha-Santos, J., Duarte-Neves, J., Carmona, V., Guarente, L., Pereira de Almeida, L., Cavadas, C., Caloric restriction blocks neuropathology and motor deficits in Machado-Joseph disease mouse models through SIRT1 pathway. Nat. Commun., 7, 2016, 11445.
    • (2016) Nat. Commun. , vol.7 , pp. 11445
    • Cunha-Santos, J.1    Duarte-Neves, J.2    Carmona, V.3    Guarente, L.4    Pereira de Almeida, L.5    Cavadas, C.6
  • 39
    • 29644437591 scopus 로고    scopus 로고
    • Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
    • Davies, J.E., Sarkar, S., Rubinsztein, D.C., 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    Sarkar, S.2    Rubinsztein, D.C.3
  • 44
    • 62949163223 scopus 로고    scopus 로고
    • Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - Lysosomal storage disorders caused by defects of non-lysosomal proteins
    • Dierks, T., Schlotawa, L., Frese, M.A., Radhakrishnan, K., von Figura, K., Schmidt, B., Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - Lysosomal storage disorders caused by defects of non-lysosomal proteins. Biochim. Biophys. Acta 1793 (2009), 710–725.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 710-725
    • Dierks, T.1    Schlotawa, L.2    Frese, M.A.3    Radhakrishnan, K.4    von Figura, K.5    Schmidt, B.6
  • 45
    • 84904575441 scopus 로고    scopus 로고
    • WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1
    • Dooley, H.C., Razi, M., Polson, H.E., Girardin, S.E., Wilson, M.I., Tooze, S.A., WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1. Mol. Cell 55 (2014), 238–252.
    • (2014) Mol. Cell , vol.55 , pp. 238-252
    • Dooley, H.C.1    Razi, M.2    Polson, H.E.3    Girardin, S.E.4    Wilson, M.I.5    Tooze, S.A.6
  • 46
    • 84887984325 scopus 로고    scopus 로고
    • Trehalose rescues Alzheimer's disease phenotypes in APP/PS1 transgenic mice
    • Du, J., Liang, Y., Xu, F., Sun, B., Wang, Z., Trehalose rescues Alzheimer's disease phenotypes in APP/PS1 transgenic mice. J. Pharm. Pharmacol. 65 (2013), 1753–1756.
    • (2013) J. Pharm. Pharmacol. , vol.65 , pp. 1753-1756
    • Du, J.1    Liang, Y.2    Xu, F.3    Sun, B.4    Wang, Z.5
  • 49
    • 80053476420 scopus 로고    scopus 로고
    • The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR
    • Egan, D., Kim, J., Shaw, R.J., Guan, K.L., The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR. Autophagy 7 (2011), 643–644.
    • (2011) Autophagy , vol.7 , pp. 643-644
    • Egan, D.1    Kim, J.2    Shaw, R.J.3    Guan, K.L.4
  • 50
    • 84925521323 scopus 로고    scopus 로고
    • Danon disease: a phenotypic expression of LAMP-2 deficiency
    • Endo, Y., Furuta, A., Nishino, I., Danon disease: a phenotypic expression of LAMP-2 deficiency. Acta Neuropathol. 129 (2015), 391–398.
    • (2015) Acta Neuropathol. , vol.129 , pp. 391-398
    • Endo, Y.1    Furuta, A.2    Nishino, I.3
  • 55
    • 84883461543 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia: clinico-pathologic features and emerging molecular mechanisms
    • Fink, J.K., Hereditary spastic paraplegia: clinico-pathologic features and emerging molecular mechanisms. Acta Neuropathol. 126 (2013), 307–328.
    • (2013) Acta Neuropathol. , vol.126 , pp. 307-328
    • Fink, J.K.1
  • 56
    • 78650448754 scopus 로고    scopus 로고
    • Chemical modulators of autophagy as biological probes and potential therapeutics
    • Fleming, A., Noda, T., Yoshimori, T., Rubinsztein, D.C., 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    Noda, T.2    Yoshimori, T.3    Rubinsztein, D.C.4
  • 59
    • 84891014899 scopus 로고    scopus 로고
    • The return of the nucleus: transcriptional and epigenetic control of autophagy
    • Füllgrabe, J., Klionsky, D.J., Joseph, B., The return of the nucleus: transcriptional and epigenetic control of autophagy. Nat. Rev. Mol. Cell Biol. 15 (2014), 65–74.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 65-74
    • Füllgrabe, J.1    Klionsky, D.J.2    Joseph, B.3
  • 60
    • 0034712047 scopus 로고    scopus 로고
    • Mammalian neural stem cells
    • Gage, F.H., Mammalian neural stem cells. Science 287 (2000), 1433–1438.
    • (2000) Science , vol.287 , pp. 1433-1438
    • Gage, F.H.1
  • 61
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • Gal, J., Ström, A.L., Kwinter, D.M., Kilty, R., Zhang, J., Shi, P., Fu, W., Wooten, M.W., Zhu, H., 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    Ström, A.L.2    Kwinter, D.M.3    Kilty, R.4    Zhang, J.5    Shi, P.6    Fu, W.7    Wooten, M.W.8    Zhu, H.9
  • 62
    • 66449083078 scopus 로고    scopus 로고
    • ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy
    • Ganley, I.G., Lam, H., Wang, J., Ding, X., Chen, S., Jiang, X., ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. J. Biol. Chem. 284 (2009), 12297–12305.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam, H.2    Wang, J.3    Ding, X.4    Chen, S.5    Jiang, X.6
  • 63
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • Ganley, I.G., Wong, P.M., Gammoh, N., Jiang, X., Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol. Cell 42 (2011), 731–743.
    • (2011) Mol. Cell , vol.42 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 64
    • 84905365244 scopus 로고    scopus 로고
    • Protein degradation and quality control in cells from laforin and malin knockout mice
    • Garyali, P., Segvich, D.M., DePaoli-Roach, A.A., Roach, P.J., Protein degradation and quality control in cells from laforin and malin knockout mice. J. Biol. Chem. 289 (2014), 20606–20614.
    • (2014) J. Biol. Chem. , vol.289 , pp. 20606-20614
    • Garyali, P.1    Segvich, D.M.2    DePaoli-Roach, A.A.3    Roach, P.J.4
  • 65
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier, C.A., Kitada, T., Shen, J., Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc. Natl. Acad. Sci. USA 105 (2008), 11364–11369.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 66
    • 84881506338 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment is a key membrane source for the LC3 lipidation step of autophagosome biogenesis
    • Ge, L., Melville, D., Zhang, M., Schekman, R., The ER-Golgi intermediate compartment is a key membrane source for the LC3 lipidation step of autophagosome biogenesis. eLife, 2, 2013, e00947.
    • (2013) eLife , vol.2 , pp. e00947
    • Ge, L.1    Melville, D.2    Zhang, M.3    Schekman, R.4
  • 67
    • 84927720203 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and COPII generate LC3 lipidation vesicles from the ER-Golgi intermediate compartment
    • Ge, L., Zhang, M., Schekman, R., Phosphatidylinositol 3-kinase and COPII generate LC3 lipidation vesicles from the ER-Golgi intermediate compartment. eLife, 3, 2014, e04135.
    • (2014) eLife , vol.3 , pp. e04135
    • Ge, L.1    Zhang, M.2    Schekman, R.3
  • 68
    • 84940751095 scopus 로고    scopus 로고
    • A Genome Scale Screen for Mutants with Delayed Exit from Mitosis: Ire1-Independent Induction of Autophagy Integrates ER Homeostasis into Mitotic Lifespan
    • Ghavidel, A., Baxi, K., Ignatchenko, V., Prusinkiewicz, M., Arnason, T.G., Kislinger, T., Carvalho, C.E., Harkness, T.A., A Genome Scale Screen for Mutants with Delayed Exit from Mitosis: Ire1-Independent Induction of Autophagy Integrates ER Homeostasis into Mitotic Lifespan. PLoS Genet., 11, 2015, e1005429.
    • (2015) PLoS Genet. , vol.11 , pp. e1005429
    • Ghavidel, A.1    Baxi, K.2    Ignatchenko, V.3    Prusinkiewicz, M.4    Arnason, T.G.5    Kislinger, T.6    Carvalho, C.E.7    Harkness, T.A.8
  • 72
    • 84966713295 scopus 로고    scopus 로고
    • Defective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD
    • Goode, A., Butler, K., Long, J., Cavey, J., Scott, D., Shaw, B., Sollenberger, J., Gell, C., Johansen, T., Oldham, N.J., et al. Defective recognition of LC3B by mutant SQSTM1/p62 implicates impairment of autophagy as a pathogenic mechanism in ALS-FTLD. Autophagy 12 (2016), 1094–1104.
    • (2016) Autophagy , vol.12 , pp. 1094-1104
    • Goode, A.1    Butler, K.2    Long, J.3    Cavey, J.4    Scott, D.5    Shaw, B.6    Sollenberger, J.7    Gell, C.8    Johansen, T.9    Oldham, N.J.10
  • 73
    • 84863109266 scopus 로고    scopus 로고
    • AP1 is essential for generation of autophagosomes from the trans-Golgi network
    • Guo, Y., Chang, C., Huang, R., Liu, B., Bao, L., Liu, W., AP1 is essential for generation of autophagosomes from the trans-Golgi network. J. Cell Sci. 125 (2012), 1706–1715.
    • (2012) J. Cell Sci. , vol.125 , pp. 1706-1715
    • Guo, Y.1    Chang, C.2    Huang, R.3    Liu, B.4    Bao, L.5    Liu, W.6
  • 76
    • 40149105890 scopus 로고    scopus 로고
    • A role for autophagy in the extension of lifespan by dietary restriction in C. elegans
    • Hansen, M., Chandra, A., Mitic, L.L., Onken, B., Driscoll, M., Kenyon, C., A role for autophagy in the extension of lifespan by dietary restriction in C. elegans. PLoS Genet., 4, 2008, e24.
    • (2008) PLoS Genet. , vol.4 , pp. e24
    • Hansen, M.1    Chandra, A.2    Mitic, L.L.3    Onken, B.4    Driscoll, M.5    Kenyon, C.6
  • 81
    • 84983734366 scopus 로고    scopus 로고
    • Tyrosine Kinase Inhibition Regulates Early Systemic Immune Changes and Modulates the Neuroimmune Response in α-Synucleinopathy
    • Hebron, M.L., Lonskaya, I., Olopade, P., Selby, S.T., Pagan, F., Moussa, C.E., Tyrosine Kinase Inhibition Regulates Early Systemic Immune Changes and Modulates the Neuroimmune Response in α-Synucleinopathy. J. Clin. Cell. Immunol., 5, 2014, 259.
    • (2014) J. Clin. Cell. Immunol. , vol.5 , pp. 259
    • Hebron, M.L.1    Lonskaya, I.2    Olopade, P.3    Selby, S.T.4    Pagan, F.5    Moussa, C.E.6
  • 88
    • 40449139980 scopus 로고    scopus 로고
    • The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes
    • Jahreiss, L., Menzies, F.M., Rubinsztein, D.C., The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes. Traffic 9 (2008), 574–587.
    • (2008) Traffic , vol.9 , pp. 574-587
    • Jahreiss, L.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 89
    • 84920837013 scopus 로고    scopus 로고
    • Autophagy is involved in the reduction of myelinating Schwann cell cytoplasm during myelin maturation of the peripheral nerve
    • Jang, S.Y., Shin, Y.K., Park, S.Y., Park, J.Y., Rha, S.H., Kim, J.K., Lee, H.J., Park, H.T., Autophagy is involved in the reduction of myelinating Schwann cell cytoplasm during myelin maturation of the peripheral nerve. PLoS ONE, 10, 2015, e0116624.
    • (2015) PLoS ONE , vol.10 , pp. e0116624
    • Jang, S.Y.1    Shin, Y.K.2    Park, S.Y.3    Park, J.Y.4    Rha, S.H.5    Kim, J.K.6    Lee, H.J.7    Park, H.T.8
  • 90
    • 84952685679 scopus 로고    scopus 로고
    • Autophagic myelin destruction by Schwann cells during Wallerian degeneration and segmental demyelination
    • Jang, S.Y., Shin, Y.K., Park, S.Y., Park, J.Y., Lee, H.J., Yoo, Y.H., Kim, J.K., Park, H.T., Autophagic myelin destruction by Schwann cells during Wallerian degeneration and segmental demyelination. Glia 64 (2016), 730–742.
    • (2016) Glia , vol.64 , pp. 730-742
    • Jang, S.Y.1    Shin, Y.K.2    Park, S.Y.3    Park, J.Y.4    Lee, H.J.5    Yoo, Y.H.6    Kim, J.K.7    Park, H.T.8
  • 92
  • 93
    • 84941985443 scopus 로고    scopus 로고
    • Therapeutic effect of barberine on Huntington's disease transgenic mouse model
    • Jiang, W., Wei, W., Gaertig, M.A., Li, X.J., Therapeutic effect of barberine on Huntington's disease transgenic mouse model. PLoS One., 10, 2015, e0134142.
    • (2015) PLoS One. , vol.10 , pp. e0134142
    • Jiang, W.1    Wei, W.2    Gaertig, M.A.3    Li, X.J.4
  • 95
    • 77957909886 scopus 로고    scopus 로고
    • Meta-analysis confirms CR1, CLU, and PICALM as alzheimer disease risk loci and reveals interactions with APOE genotypes
    • Jun, G., Naj, A.C., Beecham, G.W., Wang, L.S., Buros, J., Gallins, P.J., Buxbaum, J.D., Ertekin-Taner, N., Fallin, M.D., Friedland, R., et al., Alzheimer's Disease Genetics Consortium. Meta-analysis confirms CR1, CLU, and PICALM as alzheimer disease risk loci and reveals interactions with APOE genotypes. Arch. Neurol. 67 (2010), 1473–1484.
    • (2010) Arch. Neurol. , vol.67 , pp. 1473-1484
    • Jun, G.1    Naj, A.C.2    Beecham, G.W.3    Wang, L.S.4    Buros, J.5    Gallins, P.J.6    Buxbaum, J.D.7    Ertekin-Taner, N.8    Fallin, M.D.9    Friedland, R.10
  • 97
    • 80052364474 scopus 로고    scopus 로고
    • Metformin treatment has no beneficial effect in a dose-response survival study in the SOD1(G93A) mouse model of ALS and is harmful in female mice
    • Kaneb, H.M., Sharp, P.S., Rahmani-Kondori, N., Wells, D.J., Metformin treatment has no beneficial effect in a dose-response survival study in the SOD1(G93A) mouse model of ALS and is harmful in female mice. PLoS ONE, 6, 2011, e24189.
    • (2011) PLoS ONE , vol.6 , pp. e24189
    • Kaneb, H.M.1    Sharp, P.S.2    Rahmani-Kondori, N.3    Wells, D.J.4
  • 99
    • 84884331483 scopus 로고    scopus 로고
    • TRP53 activates a global autophagy program to promote tumor suppression
    • Kenzelmann Broz, D., Attardi, L.D., TRP53 activates a global autophagy program to promote tumor suppression. Autophagy 9 (2013), 1440–1442.
    • (2013) Autophagy , vol.9 , pp. 1440-1442
    • Kenzelmann Broz, D.1    Attardi, L.D.2
  • 100
    • 84955242756 scopus 로고    scopus 로고
    • Ubiquitin-Dependent And Independent Signals In Selective Autophagy
    • Khaminets, A., Behl, C., Dikic, I., Ubiquitin-Dependent And Independent Signals In Selective Autophagy. Trends Cell Biol. 26 (2016), 6–16.
    • (2016) Trends Cell Biol. , vol.26 , pp. 6-16
    • Khaminets, A.1    Behl, C.2    Dikic, I.3
  • 101
    • 79956048660 scopus 로고    scopus 로고
    • Parkin mediates beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models
    • Khandelwal, P.J., Herman, A.M., Hoe, H.S., Rebeck, G.W., Moussa, C.E., Parkin mediates beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models. Hum. Mol. Genet. 20 (2011), 2091–2102.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2091-2102
    • Khandelwal, P.J.1    Herman, A.M.2    Hoe, H.S.3    Rebeck, G.W.4    Moussa, C.E.5
  • 102
    • 84920504512 scopus 로고    scopus 로고
    • mTOR: a pharmacologic target for autophagy regulation
    • Kim, Y.C., Guan, K.L., mTOR: a pharmacologic target for autophagy regulation. J. Clin. Invest. 125 (2015), 25–32.
    • (2015) J. Clin. Invest. , vol.125 , pp. 25-32
    • Kim, Y.C.1    Guan, K.L.2
  • 103
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J., Kundu, M., Viollet, B., Guan, K.L., AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13 (2011), 132–141.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 106
    • 84960354182 scopus 로고    scopus 로고
    • Precision autophagy directed by receptor regulators - emerging examples within the TRIM family
    • Kimura, T., Mandell, M., Deretic, V., Precision autophagy directed by receptor regulators - emerging examples within the TRIM family. J. Cell Sci. 129 (2016), 881–891.
    • (2016) J. Cell Sci. , vol.129 , pp. 881-891
    • Kimura, T.1    Mandell, M.2    Deretic, V.3
  • 111
    • 84964294603 scopus 로고    scopus 로고
    • Autophagosome closure requires membrane scission
    • Knorr, R.L., Lipowsky, R., Dimova, R., Autophagosome closure requires membrane scission. Autophagy 11 (2015), 2134–2137.
    • (2015) Autophagy , vol.11 , pp. 2134-2137
    • Knorr, R.L.1    Lipowsky, R.2    Dimova, R.3
  • 113
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu, M., Waguri, S., Koike, M., Sou, Y.S., Ueno, T., Hara, T., Mizushima, N., Iwata, J., Ezaki, J., Murata, S., et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131 (2007), 1149–1163.
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5    Hara, T.6    Mizushima, N.7    Iwata, J.8    Ezaki, J.9    Murata, S.10
  • 115
    • 15444378335 scopus 로고    scopus 로고
    • AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif
    • Kyttälä, A., Yliannala, K., Schu, P., Jalanko, A., Luzio, J.P., AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif. J. Biol. Chem. 280 (2005), 10277–10283.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10277-10283
    • Kyttälä, A.1    Yliannala, K.2    Schu, P.3    Jalanko, A.4    Luzio, J.P.5
  • 116
    • 84888380983 scopus 로고    scopus 로고
    • The autophagosome: origins unknown, biogenesis complex
    • Lamb, C.A., Yoshimori, T., Tooze, S.A., The autophagosome: origins unknown, biogenesis complex. Nat. Rev. Mol. Cell Biol. 14 (2013), 759–774.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 759-774
    • Lamb, C.A.1    Yoshimori, T.2    Tooze, S.A.3
  • 118
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • Laplante, M., Sabatini, D.M., mTOR signaling in growth control and disease. Cell 149 (2012), 274–293.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 121
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • Lee, J.A., Beigneux, A., Ahmad, S.T., Young, S.G., Gao, F.B., ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr. Biol. 17 (2007), 1561–1567.
    • (2007) Curr. Biol. , vol.17 , pp. 1561-1567
    • Lee, J.A.1    Beigneux, A.2    Ahmad, S.T.3    Young, S.G.4    Gao, F.B.5
  • 124
    • 84920407208 scopus 로고    scopus 로고
    • Development of autophagy inducers in clinical medicine
    • Levine, B., Packer, M., Codogno, P., Development of autophagy inducers in clinical medicine. J. Clin. Invest. 125 (2015), 14–24.
    • (2015) J. Clin. Invest. , vol.125 , pp. 14-24
    • Levine, B.1    Packer, M.2    Codogno, P.3
  • 126
    • 84928325579 scopus 로고    scopus 로고
    • Trehalose decreases mutant SOD1 expression and alleviates motor deficiency in early but not end-stage amyotrophic lateral sclerosis in a SOD1-G93A mouse model
    • Li, Y., Guo, Y., Wang, X., Yu, X., Duan, W., Hong, K., Wang, J., Han, H., Li, C., Trehalose decreases mutant SOD1 expression and alleviates motor deficiency in early but not end-stage amyotrophic lateral sclerosis in a SOD1-G93A mouse model. Neuroscience 298 (2015), 12–25.
    • (2015) Neuroscience , vol.298 , pp. 12-25
    • Li, Y.1    Guo, Y.2    Wang, X.3    Yu, X.4    Duan, W.5    Hong, K.6    Wang, J.7    Han, H.8    Li, C.9
  • 127
    • 77449094358 scopus 로고    scopus 로고
    • Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration
    • Liang, C.C., Wang, C., Peng, X., Gan, B., Guan, J.L., Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration. J. Biol. Chem. 285 (2010), 3499–3509.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3499-3509
    • Liang, C.C.1    Wang, C.2    Peng, X.3    Gan, B.4    Guan, J.L.5
  • 128
    • 77951727293 scopus 로고    scopus 로고
    • Lipids on trial: the search for the offending metabolite in Niemann-Pick type C disease
    • Lloyd-Evans, E., Platt, F.M., Lipids on trial: the search for the offending metabolite in Niemann-Pick type C disease. Traffic 11 (2010), 419–428.
    • (2010) Traffic , vol.11 , pp. 419-428
    • Lloyd-Evans, E.1    Platt, F.M.2
  • 130
    • 84862611041 scopus 로고    scopus 로고
    • TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
    • Longatti, A., Lamb, C.A., Razi, M., Yoshimura, S., Barr, F.A., Tooze, S.A., TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes. J. Cell Biol. 197 (2012), 659–675.
    • (2012) J. Cell Biol. , vol.197 , pp. 659-675
    • Longatti, A.1    Lamb, C.A.2    Razi, M.3    Yoshimura, S.4    Barr, F.A.5    Tooze, S.A.6
  • 131
    • 84938841739 scopus 로고    scopus 로고
    • Nilotinib and bosutinib modulate pre-plaque alterations of blood immune markers and neuro-inflammation in Alzheimer's disease models
    • Lonskaya, I., Hebron, M.L., Selby, S.T., Turner, R.S., Moussa, C.E., Nilotinib and bosutinib modulate pre-plaque alterations of blood immune markers and neuro-inflammation in Alzheimer's disease models. Neuroscience 304 (2015), 316–327.
    • (2015) Neuroscience , vol.304 , pp. 316-327
    • Lonskaya, I.1    Hebron, M.L.2    Selby, S.T.3    Turner, R.S.4    Moussa, C.E.5
  • 132
    • 84905491871 scopus 로고    scopus 로고
    • Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family
    • Lu, K., Psakhye, I., Jentsch, S., Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family. Cell 158 (2014), 549–563.
    • (2014) Cell , vol.158 , pp. 549-563
    • Lu, K.1    Psakhye, I.2    Jentsch, S.3
  • 133
    • 84905907209 scopus 로고    scopus 로고
    • The crucial role of Atg5 in cortical neurogenesis during early brain development
    • Lv, X., Jiang, H., Li, B., Liang, Q., Wang, S., Zhao, Q., Jiao, J., The crucial role of Atg5 in cortical neurogenesis during early brain development. Sci. Rep., 4, 2014, 6010.
    • (2014) Sci. Rep. , vol.4 , pp. 6010
    • Lv, X.1    Jiang, H.2    Li, B.3    Liang, Q.4    Wang, S.5    Zhao, Q.6    Jiao, J.7
  • 137
    • 84937574462 scopus 로고    scopus 로고
    • Autophagic Degradation of the 26S Proteasome Is Mediated by the Dual ATG8/Ubiquitin Receptor RPN10 in Arabidopsis
    • Marshall, R.S., Li, F., Gemperline, D.C., Book, A.J., Vierstra, R.D., Autophagic Degradation of the 26S Proteasome Is Mediated by the Dual ATG8/Ubiquitin Receptor RPN10 in Arabidopsis. Mol. Cell 58 (2015), 1053–1066.
    • (2015) Mol. Cell , vol.58 , pp. 1053-1066
    • Marshall, R.S.1    Li, F.2    Gemperline, D.C.3    Book, A.J.4    Vierstra, R.D.5
  • 138
    • 84903314885 scopus 로고    scopus 로고
    • Novel roles for the MiTF/TFE family of transcription factors in organelle biogenesis, nutrient sensing, and energy homeostasis
    • Martina, J.A., Diab, H.I., Li, H., Puertollano, R., Novel roles for the MiTF/TFE family of transcription factors in organelle biogenesis, nutrient sensing, and energy homeostasis. Cell. Mol. Life Sci. 71 (2014), 2483–2497.
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 2483-2497
    • Martina, J.A.1    Diab, H.I.2    Li, H.3    Puertollano, R.4
  • 141
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C.A., Sou, Y.S., Saiki, S., Kawajiri, S., Sato, F., et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 189 (2010), 211–221.
    • (2010) J. Cell Biol. , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6    Sou, Y.S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 143
    • 84893690813 scopus 로고    scopus 로고
    • Rhes, a striatal-selective protein implicated in Huntington disease, binds beclin-1 and activates autophagy
    • Mealer, R.G., Murray, A.J., Shahani, N., Subramaniam, S., Snyder, S.H., 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    Murray, A.J.2    Shahani, N.3    Subramaniam, S.4    Snyder, S.H.5
  • 145
    • 74249103961 scopus 로고    scopus 로고
    • Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3
    • Menzies, F.M., Huebener, J., Renna, M., Bonin, M., Riess, O., Rubinsztein, D.C., Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3. Brain 133 (2010), 93–104.
    • (2010) Brain , vol.133 , pp. 93-104
    • Menzies, F.M.1    Huebener, J.2    Renna, M.3    Bonin, M.4    Riess, O.5    Rubinsztein, D.C.6
  • 146
  • 148
    • 84968764106 scopus 로고    scopus 로고
    • Understanding Dopaminergic Cell Death Pathways in Parkinson Disease
    • Michel, P.P., Hirsch, E.C., Hunot, S., Understanding Dopaminergic Cell Death Pathways in Parkinson Disease. Neuron 90 (2016), 675–691.
    • (2016) Neuron , vol.90 , pp. 675-691
    • Michel, P.P.1    Hirsch, E.C.2    Hunot, S.3
  • 149
    • 84974815636 scopus 로고    scopus 로고
    • Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy
    • Moore, A.S., Holzbaur, E.L., Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy. Proc. Natl. Acad. Sci. USA 113 (2016), E3349–E3358.
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. E3349-E3358
    • Moore, A.S.1    Holzbaur, E.L.2
  • 150
    • 79960774898 scopus 로고    scopus 로고
    • Autophagosome precursor maturation requires homotypic fusion
    • Moreau, K., Ravikumar, B., Renna, M., Puri, C., Rubinsztein, D.C., Autophagosome precursor maturation requires homotypic fusion. Cell 146 (2011), 303–317.
    • (2011) Cell , vol.146 , pp. 303-317
    • Moreau, K.1    Ravikumar, B.2    Renna, M.3    Puri, C.4    Rubinsztein, D.C.5
  • 154
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D.F., Youle, R.J., Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183 (2008), 795–803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 156
    • 84870527124 scopus 로고    scopus 로고
    • TBK1 kinase addiction in lung cancer cells is mediated via autophagy of Tax1bp1/Ndp52 and non-canonical NF-κB signalling
    • Newman, A.C., Scholefield, C.L., Kemp, A.J., Newman, M., McIver, E.G., Kamal, A., Wilkinson, S., TBK1 kinase addiction in lung cancer cells is mediated via autophagy of Tax1bp1/Ndp52 and non-canonical NF-κB signalling. PLoS ONE, 7, 2012, e50672.
    • (2012) PLoS ONE , vol.7 , pp. e50672
    • Newman, A.C.1    Scholefield, C.L.2    Kemp, A.J.3    Newman, M.4    McIver, E.G.5    Kamal, A.6    Wilkinson, S.7
  • 157
    • 84991826660 scopus 로고    scopus 로고
    • Deciphering the Molecular Signals of PINK1/Parkin Mitophagy
    • Nguyen, T.N., Padman, B.S., Lazarou, M., Deciphering the Molecular Signals of PINK1/Parkin Mitophagy. Trends Cell Biol. 26 (2016), 733–744.
    • (2016) Trends Cell Biol. , vol.26 , pp. 733-744
    • Nguyen, T.N.1    Padman, B.S.2    Lazarou, M.3
  • 159
    • 35848944122 scopus 로고    scopus 로고
    • Aberrant membranes and double-membrane structures accumulate in the axons of Atg5-null Purkinje cells before neuronal death
    • Nishiyama, J., Miura, E., Mizushima, N., Watanabe, M., Yuzaki, M., Aberrant membranes and double-membrane structures accumulate in the axons of Atg5-null Purkinje cells before neuronal death. Autophagy 3 (2007), 591–596.
    • (2007) Autophagy , vol.3 , pp. 591-596
    • Nishiyama, J.1    Miura, E.2    Mizushima, N.3    Watanabe, M.4    Yuzaki, M.5
  • 162
    • 84861158462 scopus 로고    scopus 로고
    • Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy
    • Orsi, A., Razi, M., Dooley, H.C., Robinson, D., Weston, A.E., Collinson, L.M., Tooze, S.A., Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy. Mol. Biol. Cell 23 (2012), 1860–1873.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1860-1873
    • Orsi, A.1    Razi, M.2    Dooley, H.C.3    Robinson, D.4    Weston, A.E.5    Collinson, L.M.6    Tooze, S.A.7
  • 163
    • 79952317005 scopus 로고    scopus 로고
    • Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation
    • Otomo, A., Kunita, R., Suzuki-Utsunomiya, K., Ikeda, J.E., Hadano, S., Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation. FEBS Lett. 585 (2011), 730–736.
    • (2011) FEBS Lett. , vol.585 , pp. 730-736
    • Otomo, A.1    Kunita, R.2    Suzuki-Utsunomiya, K.3    Ikeda, J.E.4    Hadano, S.5
  • 166
    • 51849116835 scopus 로고    scopus 로고
    • The pathogenesis of Niemann-Pick type C disease: a role for autophagy?
    • Pacheco, C.D., Lieberman, A.P., The pathogenesis of Niemann-Pick type C disease: a role for autophagy?. Expert Rev. Mol. Med., 10, 2008, e26.
    • (2008) Expert Rev. Mol. Med. , vol.10 , pp. e26
    • Pacheco, C.D.1    Lieberman, A.P.2
  • 168
    • 84930632378 scopus 로고    scopus 로고
    • Coordination of mitophagy and mitochondrial biogenesis during ageing in C. elegans
    • Palikaras, K., Lionaki, E., Tavernarakis, N., Coordination of mitophagy and mitochondrial biogenesis during ageing in C. elegans. Nature 521 (2015), 525–528.
    • (2015) Nature , vol.521 , pp. 525-528
    • Palikaras, K.1    Lionaki, E.2    Tavernarakis, N.3
  • 170
    • 13844313915 scopus 로고    scopus 로고
    • Parkin-deficient mice are not a robust model of parkinsonism
    • Perez, F.A., Palmiter, R.D., Parkin-deficient mice are not a robust model of parkinsonism. Proc. Natl. Acad. Sci. USA 102 (2005), 2174–2179.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2174-2179
    • Perez, F.A.1    Palmiter, R.D.2
  • 171
    • 84925849144 scopus 로고    scopus 로고
    • Hippocampal endosomal, lysosomal, and autophagic dysregulation in mild cognitive impairment: correlation with aβ and tau pathology
    • Perez, S.E., He, B., Nadeem, M., Wuu, J., Ginsberg, S.D., Ikonomovic, M.D., Mufson, E.J., Hippocampal endosomal, lysosomal, and autophagic dysregulation in mild cognitive impairment: correlation with aβ and tau pathology. J. Neuropathol. Exp. Neurol. 74 (2015), 345–358.
    • (2015) J. Neuropathol. Exp. Neurol. , vol.74 , pp. 345-358
    • Perez, S.E.1    He, B.2    Nadeem, M.3    Wuu, J.4    Ginsberg, S.D.5    Ikonomovic, M.D.6    Mufson, E.J.7
  • 173
    • 84921369563 scopus 로고    scopus 로고
    • The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease
    • Pickrell, A.M., Youle, R.J., The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. Neuron 85 (2015), 257–273.
    • (2015) Neuron , vol.85 , pp. 257-273
    • Pickrell, A.M.1    Youle, R.J.2
  • 174
  • 176
    • 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
    • Piras, A., Collin, L., Grüninger, F., Graff, C., Rönnbäck, 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., 4, 2016, 22.
    • (2016) Acta Neuropathol. Commun. , vol.4 , pp. 22
    • Piras, A.1    Collin, L.2    Grüninger, F.3    Graff, C.4    Rönnbäck, A.5
  • 177
    • 84871960929 scopus 로고    scopus 로고
    • The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction
    • Platt, F.M., Boland, B., van der Spoel, A.C., The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction. J. Cell Biol. 199 (2012), 723–734.
    • (2012) J. Cell Biol. , vol.199 , pp. 723-734
    • Platt, F.M.1    Boland, B.2    van der Spoel, A.C.3
  • 179
    • 77956060447 scopus 로고    scopus 로고
    • The birth prevalence of lysosomal storage disorders in the Czech Republic: comparison with data in different populations
    • Poupetová, H., Ledvinová, J., Berná, L., Dvoráková, L., Kozich, V., Elleder, M., The birth prevalence of lysosomal storage disorders in the Czech Republic: comparison with data in different populations. J. Inherit. Metab. Dis. 33 (2010), 387–396.
    • (2010) J. Inherit. Metab. Dis. , vol.33 , pp. 387-396
    • Poupetová, H.1    Ledvinová, J.2    Berná, L.3    Dvoráková, L.4    Kozich, V.5    Elleder, M.6
  • 180
    • 11244289333 scopus 로고    scopus 로고
    • WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy
    • Proikas-Cezanne, T., Waddell, S., Gaugel, A., Frickey, T., Lupas, A., Nordheim, A., WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy. Oncogene 23 (2004), 9314–9325.
    • (2004) Oncogene , vol.23 , pp. 9314-9325
    • Proikas-Cezanne, T.1    Waddell, S.2    Gaugel, A.3    Frickey, T.4    Lupas, A.5    Nordheim, A.6
  • 182
    • 84922793541 scopus 로고    scopus 로고
    • Exome Sequencing Identifies DYNC1H1 Variant Associated With Vertebral Abnormality and Spinal Muscular Atrophy With Lower Extremity Predominance
    • Punetha, J., Monges, S., Franchi, M.E., Hoffman, E.P., Cirak, S., Tesi-Rocha, C., Exome Sequencing Identifies DYNC1H1 Variant Associated With Vertebral Abnormality and Spinal Muscular Atrophy With Lower Extremity Predominance. Pediatr. Neurol. 52 (2015), 239–244.
    • (2015) Pediatr. Neurol. , vol.52 , pp. 239-244
    • Punetha, J.1    Monges, S.2    Franchi, M.E.3    Hoffman, E.P.4    Cirak, S.5    Tesi-Rocha, C.6
  • 183
    • 84884220705 scopus 로고    scopus 로고
    • Diverse autophagosome membrane sources coalesce in recycling endosomes
    • Puri, C., Renna, M., Bento, C.F., Moreau, K., Rubinsztein, D.C., Diverse autophagosome membrane sources coalesce in recycling endosomes. Cell 154 (2013), 1285–1299.
    • (2013) Cell , vol.154 , pp. 1285-1299
    • Puri, C.1    Renna, M.2    Bento, C.F.3    Moreau, K.4    Rubinsztein, D.C.5
  • 186
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar, B., Duden, R., Rubinsztein, D.C., Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11 (2002), 1107–1117.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 190
    • 46249127490 scopus 로고    scopus 로고
    • Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease
    • Ravikumar, B., Imarisio, S., Sarkar, S., O'Kane, C.J., Rubinsztein, D.C., Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease. J. Cell Sci. 121 (2008), 1649–1660.
    • (2008) J. Cell Sci. , vol.121 , pp. 1649-1660
    • Ravikumar, B.1    Imarisio, S.2    Sarkar, S.3    O'Kane, C.J.4    Rubinsztein, D.C.5
  • 191
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., Rubinsztein, D.C., Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat. Cell Biol. 12 (2010), 747–757.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 198
    • 79955964504 scopus 로고    scopus 로고
    • Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer's disease brain
    • Rohn, T.T., Wirawan, E., Brown, R.J., Harris, J.R., Masliah, E., Vandenabeele, P., Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer's disease brain. Neurobiol. Dis. 43 (2011), 68–78.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 68-78
    • Rohn, T.T.1    Wirawan, E.2    Brown, R.J.3    Harris, J.R.4    Masliah, E.5    Vandenabeele, P.6
  • 200
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein, D.C., Codogno, P., Levine, B., 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    Codogno, P.2    Levine, B.3
  • 201
    • 84940457605 scopus 로고    scopus 로고
    • Therapeutic targeting of autophagy in neurodegenerative and infectious diseases
    • Rubinsztein, D.C., Bento, C.F., Deretic, V., Therapeutic targeting of autophagy in neurodegenerative and infectious diseases. J. Exp. Med. 212 (2015), 979–990.
    • (2015) J. Exp. Med. , vol.212 , pp. 979-990
    • Rubinsztein, D.C.1    Bento, C.F.2    Deretic, V.3
  • 205
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar, S., Davies, J.E., Huang, Z., Tunnacliffe, A., Rubinsztein, D.C., 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    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 206
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • Sarkar, S., Krishna, G., Imarisio, S., Saiki, S., O'Kane, C.J., Rubinsztein, D.C., A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum. Mol. Genet. 17 (2008), 170–178.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5    Rubinsztein, D.C.6
  • 207
    • 84869386716 scopus 로고    scopus 로고
    • Stimulation of autophagy is neuroprotective in a mouse model of human tauopathy
    • Schaeffer, V., Goedert, M., Stimulation of autophagy is neuroprotective in a mouse model of human tauopathy. Autophagy 8 (2012), 1686–1687.
    • (2012) Autophagy , vol.8 , pp. 1686-1687
    • Schaeffer, V.1    Goedert, M.2
  • 208
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D.T., Goedert, M., 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    Lavenir, I.2    Ozcelik, S.3    Tolnay, M.4    Winkler, D.T.5    Goedert, M.6
  • 210
    • 84977573474 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization in cell death: new evidence and implications for health and disease
    • Serrano-Puebla, A., Boya, P., Lysosomal membrane permeabilization in cell death: new evidence and implications for health and disease. Ann. N Y Acad. Sci. 1371 (2016), 30–44.
    • (2016) Ann. N Y Acad. Sci. , vol.1371 , pp. 30-44
    • Serrano-Puebla, A.1    Boya, P.2
  • 211
    • 84892644388 scopus 로고    scopus 로고
    • Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages
    • Seto, S., Sugaya, K., Tsujimura, K., Nagata, T., Horii, T., Koide, Y., Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages. PLoS ONE, 8, 2013, e83324.
    • (2013) PLoS ONE , vol.8 , pp. e83324
    • Seto, S.1    Sugaya, K.2    Tsujimura, K.3    Nagata, T.4    Horii, T.5    Koide, Y.6
  • 215
    • 84940751065 scopus 로고    scopus 로고
    • Mutations in the ubiquitin-binding domain of OPTN/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism
    • Shen, W.C., Li, H.Y., Chen, G.C., Chern, Y., Tu, P.H., Mutations in the ubiquitin-binding domain of OPTN/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism. Autophagy 11 (2015), 685–700.
    • (2015) Autophagy , vol.11 , pp. 685-700
    • Shen, W.C.1    Li, H.Y.2    Chen, G.C.3    Chern, Y.4    Tu, P.H.5
  • 217
    • 79961207215 scopus 로고    scopus 로고
    • The antioxidant Trolox helps recovery from the familial Parkinson's disease-specific mitochondrial deficits caused by PINK1- and DJ-1-deficiency in dopaminergic neuronal cells
    • Shim, J.H., Yoon, S.H., Kim, K.H., Han, J.Y., Ha, J.Y., Hyun, D.H., Paek, S.H., Kang, U.J., Zhuang, X., Son, J.H., The antioxidant Trolox helps recovery from the familial Parkinson's disease-specific mitochondrial deficits caused by PINK1- and DJ-1-deficiency in dopaminergic neuronal cells. Mitochondrion 11 (2011), 707–715.
    • (2011) Mitochondrion , vol.11 , pp. 707-715
    • Shim, J.H.1    Yoon, S.H.2    Kim, K.H.3    Han, J.Y.4    Ha, J.Y.5    Hyun, D.H.6    Paek, S.H.7    Kang, U.J.8    Zhuang, X.9    Son, J.H.10
  • 218
    • 84893697774 scopus 로고    scopus 로고
    • SIRT1 activation by methylene blue, a repurposed drug, leads to AMPK-mediated inhibition of steatosis and steatohepatitis
    • Shin, S.Y., Kim, T.H., Wu, H., Choi, Y.H., Kim, S.G., SIRT1 activation by methylene blue, a repurposed drug, leads to AMPK-mediated inhibition of steatosis and steatohepatitis. Eur. J. Pharmacol. 727 (2014), 115–124.
    • (2014) Eur. J. Pharmacol. , vol.727 , pp. 115-124
    • Shin, S.Y.1    Kim, T.H.2    Wu, H.3    Choi, Y.H.4    Kim, S.G.5
  • 220
    • 84867616698 scopus 로고    scopus 로고
    • The link between the GBA gene and parkinsonism
    • Sidransky, E., Lopez, G., The link between the GBA gene and parkinsonism. Lancet Neurol. 11 (2012), 986–998.
    • (2012) Lancet Neurol. , vol.11 , pp. 986-998
    • Sidransky, E.1    Lopez, G.2
  • 221
    • 38949099761 scopus 로고    scopus 로고
    • Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
    • Simonsen, A., Cumming, R.C., Brech, A., Isakson, P., Schubert, D.R., Finley, K.D., Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila. Autophagy 4 (2008), 176–184.
    • (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
  • 223
    • 84964854975 scopus 로고    scopus 로고
    • Metformin Facilitates Amyloid-β Generation by β- and γ-Secretases via Autophagy Activation
    • Son, S.M., Shin, H.J., Byun, J., Kook, S.Y., Moon, M., Chang, Y.J., Mook-Jung, I., Metformin Facilitates Amyloid-β Generation by β- and γ-Secretases via Autophagy Activation. J. Alzheimers Dis. 51 (2016), 1197–1208.
    • (2016) J. Alzheimers Dis. , vol.51 , pp. 1197-1208
    • Son, S.M.1    Shin, H.J.2    Byun, J.3    Kook, S.Y.4    Moon, M.5    Chang, Y.J.6    Mook-Jung, I.7
  • 224
    • 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
    • Spencer, B., Potkar, R., Trejo, M., Rockenstein, E., Patrick, C., Gindi, R., Adame, A., Wyss-Coray, T., Masliah, E., 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    Potkar, R.2    Trejo, M.3    Rockenstein, E.4    Patrick, C.5    Gindi, R.6    Adame, A.7    Wyss-Coray, T.8    Masliah, E.9
  • 225
    • 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
    • Spilman, P., Podlutskaya, N., Hart, M.J., Debnath, J., Gorostiza, O., Bredesen, D., Richardson, A., Strong, R., Galvan, V., 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. e9979
    • Spilman, P.1    Podlutskaya, N.2    Hart, M.J.3    Debnath, J.4    Gorostiza, O.5    Bredesen, D.6    Richardson, A.7    Strong, R.8    Galvan, V.9
  • 226
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease
    • Spinosa, M.R., Progida, C., De Luca, A., Colucci, A.M., Alifano, P., Bucci, C., Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 28 (2008), 1640–1648.
    • (2008) J. Neurosci. , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1    Progida, C.2    De Luca, A.3    Colucci, A.M.4    Alifano, P.5    Bucci, C.6
  • 229
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz, A., Ernst, A., Dikic, I., Cargo recognition and trafficking in selective autophagy. Nat. Cell Biol. 16 (2014), 495–501.
    • (2014) Nat. Cell Biol. , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 230
    • 85000814397 scopus 로고    scopus 로고
    • The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway
    • Sullivan, P.M., Zhou, X., Robins, A.M., Paushter, D.H., Kim, D., Smolka, M.B., Hu, F., The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway. Acta Neuropathol. Commun., 4, 2016, 51.
    • (2016) Acta Neuropathol. Commun. , vol.4 , pp. 51
    • Sullivan, P.M.1    Zhou, X.2    Robins, A.M.3    Paushter, D.H.4    Kim, D.5    Smolka, M.B.6    Hu, F.7
  • 234
  • 237
    • 79957917512 scopus 로고    scopus 로고
    • A small-molecule enhancer of autophagy decreases levels of Abeta and APP-CTF via Atg5-dependent autophagy pathway
    • Tian, Y., Bustos, V., Flajolet, M., Greengard, P., A small-molecule enhancer of autophagy decreases levels of Abeta and APP-CTF via Atg5-dependent autophagy pathway. FASEB J. 25 (2011), 1934–1942.
    • (2011) FASEB J. , vol.25 , pp. 1934-1942
    • Tian, Y.1    Bustos, V.2    Flajolet, M.3    Greengard, P.4
  • 238
    • 84885736277 scopus 로고    scopus 로고
    • Adaptor complex AP2/PICALM, through interaction with LC3, targets Alzheimer's APP-CTF for terminal degradation via autophagy
    • Tian, Y., Chang, J.C., Fan, E.Y., Flajolet, M., Greengard, P., Adaptor complex AP2/PICALM, through interaction with LC3, targets Alzheimer's APP-CTF for terminal degradation via autophagy. Proc. Natl. Acad. Sci. USA 110 (2013), 17071–17076.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 17071-17076
    • Tian, Y.1    Chang, J.C.2    Fan, E.Y.3    Flajolet, M.4    Greengard, P.5
  • 239
    • 27144550841 scopus 로고    scopus 로고
    • Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase
    • Tiede, S., Storch, S., Lübke, T., Henrissat, B., Bargal, R., Raas-Rothschild, A., Braulke, T., Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase. Nat. Med. 11 (2005), 1109–1112.
    • (2005) Nat. Med. , vol.11 , pp. 1109-1112
    • Tiede, S.1    Storch, S.2    Lübke, T.3    Henrissat, B.4    Bargal, R.5    Raas-Rothschild, A.6    Braulke, T.7
  • 240
    • 84981276961 scopus 로고    scopus 로고
    • Insights into the pathogenic mechanisms of Chromosome 9 open reading frame 72 (C9orf72) repeat expansions
    • Todd, T.W., Petrucelli, L., Insights into the pathogenic mechanisms of Chromosome 9 open reading frame 72 (C9orf72) repeat expansions. J. Neurochem. 138:Suppl 1 (2016), 145–162.
    • (2016) J. Neurochem. , vol.138 , pp. 145-162
    • Todd, T.W.1    Petrucelli, L.2
  • 241
    • 2642536202 scopus 로고    scopus 로고
    • Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor
    • Topp, J.D., Gray, N.W., Gerard, R.D., Horazdovsky, B.F., Alsin is a Rab5 and Rac1 guanine nucleotide exchange factor. J. Biol. Chem. 279 (2004), 24612–24623.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24612-24623
    • Topp, J.D.1    Gray, N.W.2    Gerard, R.D.3    Horazdovsky, B.F.4
  • 243
    • 84867103427 scopus 로고    scopus 로고
    • Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome
    • Tumbarello, D.A., Waxse, B.J., Arden, S.D., Bright, N.A., Kendrick-Jones, J., Buss, F., Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome. Nat. Cell Biol. 14 (2012), 1024–1035.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1024-1035
    • Tumbarello, D.A.1    Waxse, B.J.2    Arden, S.D.3    Bright, N.A.4    Kendrick-Jones, J.5    Buss, F.6
  • 244
    • 84907393377 scopus 로고    scopus 로고
    • AMPK modulates tissue and organismal aging in a non-cell-autonomous manner
    • Ulgherait, M., Rana, A., Rera, M., Graniel, J., Walker, D.W., AMPK modulates tissue and organismal aging in a non-cell-autonomous manner. Cell Rep. 8 (2014), 1767–1780.
    • (2014) Cell Rep. , vol.8 , pp. 1767-1780
    • Ulgherait, M.1    Rana, A.2    Rera, M.3    Graniel, J.4    Walker, D.W.5
  • 245
    • 84858403126 scopus 로고    scopus 로고
    • Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity
    • Usenovic, M., Tresse, E., Mazzulli, J.R., Taylor, J.P., Krainc, D., Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity. J. Neurosci. 32 (2012), 4240–4246.
    • (2012) J. Neurosci. , vol.32 , pp. 4240-4246
    • Usenovic, M.1    Tresse, E.2    Mazzulli, J.R.3    Taylor, J.P.4    Krainc, D.5
  • 249
    • 84857844643 scopus 로고    scopus 로고
    • Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets
    • Velikkakath, A.K., Nishimura, T., Oita, E., Ishihara, N., Mizushima, N., Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets. Mol. Biol. Cell 23 (2012), 896–909.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 896-909
    • Velikkakath, A.K.1    Nishimura, T.2    Oita, E.3    Ishihara, N.4    Mizushima, N.5
  • 250
    • 79251556232 scopus 로고    scopus 로고
    • Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-β peptide degradation
    • Vingtdeux, V., Chandakkar, P., Zhao, H., d'Abramo, C., Davies, P., Marambaud, P., Novel synthetic small-molecule activators of AMPK as enhancers of autophagy and amyloid-β peptide degradation. FASEB J. 25 (2011), 219–231.
    • (2011) FASEB J. , vol.25 , pp. 219-231
    • Vingtdeux, V.1    Chandakkar, P.2    Zhao, H.3    d'Abramo, C.4    Davies, P.5    Marambaud, P.6
  • 251
    • 84919468220 scopus 로고    scopus 로고
    • Formation of α-synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomes
    • Volpicelli-Daley, L.A., Gamble, K.L., Schultheiss, C.E., Riddle, D.M., West, A.B., Lee, V.M., Formation of α-synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomes. Mol. Biol. Cell 25 (2014), 4010–4023.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 4010-4023
    • Volpicelli-Daley, L.A.1    Gamble, K.L.2    Schultheiss, C.E.3    Riddle, D.M.4    West, A.B.5    Lee, V.M.6
  • 253
    • 79953298958 scopus 로고    scopus 로고
    • Next-generation mTOR inhibitors in clinical oncology: how pathway complexity informs therapeutic strategy
    • Wander, S.A., Hennessy, B.T., Slingerland, J.M., Next-generation mTOR inhibitors in clinical oncology: how pathway complexity informs therapeutic strategy. J. Clin. Invest. 121 (2011), 1231–1241.
    • (2011) J. Clin. Invest. , vol.121 , pp. 1231-1241
    • Wander, S.A.1    Hennessy, B.T.2    Slingerland, J.M.3
  • 255
    • 84876893671 scopus 로고    scopus 로고
    • FIP200 is required for maintenance and differentiation of postnatal neural stem cells
    • Wang, C., Liang, C.C., Bian, Z.C., Zhu, Y., Guan, J.L., FIP200 is required for maintenance and differentiation of postnatal neural stem cells. Nat. Neurosci. 16 (2013), 532–542.
    • (2013) Nat. Neurosci. , vol.16 , pp. 532-542
    • Wang, C.1    Liang, C.C.2    Bian, Z.C.3    Zhu, Y.4    Guan, J.L.5
  • 256
    • 84873628557 scopus 로고    scopus 로고
    • Autophagy activation ameliorates neuronal pathogenesis of FTLD-U mice: a new light for treatment of TARDBP/TDP-43 proteinopathies
    • Wang, I.F., Tsai, K.J., Shen, C.K., Autophagy activation ameliorates neuronal pathogenesis of FTLD-U mice: a new light for treatment of TARDBP/TDP-43 proteinopathies. Autophagy 9 (2013), 239–240.
    • (2013) Autophagy , vol.9 , pp. 239-240
    • Wang, I.F.1    Tsai, K.J.2    Shen, C.K.3
  • 260
    • 84928252437 scopus 로고    scopus 로고
    • Rab8, POSH, and TAK1 regulate synaptic growth in a Drosophila model of frontotemporal dementia
    • West, R.J., Lu, Y., Marie, B., Gao, F.B., Sweeney, S.T., Rab8, POSH, and TAK1 regulate synaptic growth in a Drosophila model of frontotemporal dementia. J. Cell Biol. 208 (2015), 931–947.
    • (2015) J. Cell Biol. , vol.208 , pp. 931-947
    • West, R.J.1    Lu, Y.2    Marie, B.3    Gao, F.B.4    Sweeney, S.T.5
  • 265
    • 84879232282 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification
    • Wolfe, D.M., Lee, J.H., Kumar, A., Lee, S., Orenstein, S.J., Nixon, R.A., Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification. Eur. J. Neurosci. 37 (2013), 1949–1961.
    • (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
  • 266
    • 84892755229 scopus 로고    scopus 로고
    • The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation
    • Wong, Y.C., Holzbaur, E.L., The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation. J. Neurosci. 34 (2014), 1293–1305.
    • (2014) J. Neurosci. , vol.34 , pp. 1293-1305
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 267
    • 84908065760 scopus 로고    scopus 로고
    • Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
    • Wong, Y.C., Holzbaur, E.L., Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc. Natl. Acad. Sci. USA 111 (2014), E4439–E4448.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E4439-E4448
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 268
    • 0036303882 scopus 로고    scopus 로고
    • Lysosomal disorders
    • Wraith, J.E., Lysosomal disorders. Semin. Neonatol 7 (2002), 75–83.
    • (2002) Semin. Neonatol , vol.7 , pp. 75-83
    • Wraith, J.E.1
  • 270
    • 85014783987 scopus 로고    scopus 로고
    • Knockout of Atg5 delays the maturation and reduces the survival of adult-generated neurons in the hippocampus
    • Xi, Y., Dhaliwal, J.S., Ceizar, M., Vaculik, M., Kumar, K.L., Lagace, D.C., Knockout of Atg5 delays the maturation and reduces the survival of adult-generated neurons in the hippocampus. Cell Death Dis., 7, 2016, e2127.
    • (2016) Cell Death Dis. , vol.7 , pp. e2127
    • Xi, Y.1    Dhaliwal, J.S.2    Ceizar, M.3    Vaculik, M.4    Kumar, K.L.5    Lagace, D.C.6
  • 271
    • 84964378661 scopus 로고    scopus 로고
    • CNS involvement in CMTX1 caused by a novel connexin 32 mutation: a 6-year follow-up in neuroimaging and nerve conduction
    • Xie, C., Zhou, X., Zhu, D., Liu, W., Wang, X., Yang, H., Li, Z., Hao, Y., Zhang, G.X., Guan, Y., CNS involvement in CMTX1 caused by a novel connexin 32 mutation: a 6-year follow-up in neuroimaging and nerve conduction. Neurol. Sci. 37 (2016), 1063–1070.
    • (2016) Neurol. Sci. , vol.37 , pp. 1063-1070
    • Xie, C.1    Zhou, X.2    Zhu, D.3    Liu, W.4    Wang, X.5    Yang, H.6    Li, Z.7    Hao, Y.8    Zhang, G.X.9    Guan, Y.10
  • 272
    • 0034785509 scopus 로고    scopus 로고
    • The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis
    • Yang, Y., Hentati, A., Deng, H.X., Dabbagh, O., Sasaki, T., Hirano, M., Hung, W.Y., Ouahchi, K., Yan, J., Azim, A.C., et al. The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis. Nat. Genet. 29 (2001), 160–165.
    • (2001) Nat. Genet. , vol.29 , pp. 160-165
    • Yang, Y.1    Hentati, A.2    Deng, H.X.3    Dabbagh, O.4    Sasaki, T.5    Hirano, M.6    Hung, W.Y.7    Ouahchi, K.8    Yan, J.9    Azim, A.C.10
  • 273
    • 84921792662 scopus 로고    scopus 로고
    • The autophagy regulators Ambra1 and Beclin 1 are required for adult neurogenesis in the brain subventricular zone
    • Yazdankhah, M., Farioli-Vecchioli, S., Tonchev, A.B., Stoykova, A., Cecconi, F., The autophagy regulators Ambra1 and Beclin 1 are required for adult neurogenesis in the brain subventricular zone. Cell Death Dis., 5, 2014, e1403.
    • (2014) Cell Death Dis. , vol.5 , pp. e1403
    • Yazdankhah, M.1    Farioli-Vecchioli, S.2    Tonchev, A.B.3    Stoykova, A.4    Cecconi, F.5
  • 277
    • 84880070521 scopus 로고    scopus 로고
    • Nilotinib induces autophagy in hepatocellular carcinoma through AMPK activation
    • Yu, H.C., Lin, C.S., Tai, W.T., Liu, C.Y., Shiau, C.W., Chen, K.F., Nilotinib induces autophagy in hepatocellular carcinoma through AMPK activation. J. Biol. Chem. 288 (2013), 18249–18259.
    • (2013) J. Biol. Chem. , vol.288 , pp. 18249-18259
    • Yu, H.C.1    Lin, C.S.2    Tai, W.T.3    Liu, C.Y.4    Shiau, C.W.5    Chen, K.F.6
  • 278
    • 84903785419 scopus 로고    scopus 로고
    • Berberine-induced apoptotic and autophagic death of HepG2 cells requires AMPK activation
    • Yu, R., Zhang, Z.Q., Wang, B., Jiang, H.X., Cheng, L., Shen, L.M., Berberine-induced apoptotic and autophagic death of HepG2 cells requires AMPK activation. Cancer Cell Int., 14, 2014, 49.
    • (2014) Cancer Cell Int. , vol.14 , pp. 49
    • Yu, R.1    Zhang, Z.Q.2    Wang, B.3    Jiang, H.X.4    Cheng, L.5    Shen, L.M.6
  • 280
    • 79953647105 scopus 로고    scopus 로고
    • Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Zhang, X., Li, L., Chen, S., Yang, D., Wang, Y., Zhang, X., Wang, Z., Le, W., 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    Li, L.2    Chen, S.3    Yang, D.4    Wang, Y.5    Zhang, X.6    Wang, Z.7    Le, W.8
  • 281
    • 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
    • Zhang, X., Chen, S., Song, L., Tang, Y., Shen, Y., Jia, L., Le, W., 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    Chen, S.2    Song, L.3    Tang, Y.4    Shen, Y.5    Jia, L.6    Le, W.7
  • 284
    • 77649219699 scopus 로고    scopus 로고
    • Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice
    • Zheng, S., Clabough, E.B., Sarkar, S., Futter, M., Rubinsztein, D.C., Zeitlin, S.O., Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice. PLoS Genet., 6, 2010, e1000838.
    • (2010) PLoS Genet. , vol.6 , pp. e1000838
    • Zheng, S.1    Clabough, E.B.2    Sarkar, S.3    Futter, M.4    Rubinsztein, D.C.5    Zeitlin, S.O.6
  • 285
    • 84922516098 scopus 로고    scopus 로고
    • Autophagy supports survival and phototransduction protein levels in rod photoreceptors
    • Zhou, Z., Doggett, T.A., Sene, A., Apte, R.S., Ferguson, T.A., Autophagy supports survival and phototransduction protein levels in rod photoreceptors. Cell Death Differ. 22 (2015), 488–498.
    • (2015) Cell Death Differ. , vol.22 , pp. 488-498
    • Zhou, Z.1    Doggett, T.A.2    Sene, A.3    Apte, R.S.4    Ferguson, T.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.