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Volumn 4, Issue 10, 2012, Pages

Autophagy and neuronal cell death in neurological disorders

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; ARTICLE; AUTOPHAGY; DEGENERATIVE DISEASE; HUMAN; NERVE CELL; PATHOLOGY; PHYSIOLOGY;

EID: 84863890450     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a008839     Document Type: Article
Times cited : (148)

References (220)
  • 1
    • 76749098103 scopus 로고    scopus 로고
    • Parkinson's disease: Mitochondrial damage control
    • Abeliovich A. 2010. Parkinson's disease: Mitochondrial damage control. Nature 463: 744-745.
    • (2010) Nature , vol.463 , pp. 744-745
    • Abeliovich, A.1
  • 3
    • 77955282380 scopus 로고    scopus 로고
    • Curcuminoids enhance memory in an amyloid-infused rat model of Alzheimer's disease
    • Ahmed T, Enam SA, Gilani AH. 2010. Curcuminoids enhance memory in an amyloid-infused rat model of Alzheimer's disease. Neuroscience 169: 1296-1306.
    • (2010) Neuroscience , vol.169 , pp. 1296-1306
    • Ahmed, T.1    Enam, S.A.2    Gilani, A.H.3
  • 5
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. 2004. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 6
    • 0000730374 scopus 로고
    • Cytoplasmic components in hepatic cell lysosomes
    • Ashford TP, Porter KR. 1962. Cytoplasmic components in hepatic cell lysosomes. J Cell Biol 12: 198-202.
    • (1962) J Cell Biol , vol.12 , pp. 198-202
    • Ashford, T.P.1    Porter, K.R.2
  • 7
    • 20344387475 scopus 로고    scopus 로고
    • Autophagy: Dual roles in life and death?
    • Baehrecke EH. 2005. Autophagy: Dual roles in life and death? Nat Rev Mol Cell Biol 6: 505-510.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 505-510
    • Baehrecke, E.H.1
  • 8
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM. 2008. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 28: 5747-5763.
    • (2008) Mol Cell Biol , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 10
    • 0030905260 scopus 로고    scopus 로고
    • Suppression of cathepsins B and L causes a proliferation of lysosomes and the formation of meganeurites in hippocampus
    • Bednarski E, Ribak CE, Lynch G. 1997. Suppression of cathepsins B and L causes a proliferation of lysosomes and the formation of meganeurites in hippocampus. J Neurosci 17: 4006-4021.
    • (1997) J Neurosci , vol.17 , pp. 4006-4021
    • Bednarski, E.1    Ribak, C.E.2    Lynch, G.3
  • 11
    • 44649090171 scopus 로고    scopus 로고
    • Activation of the amyloid cascade in apolipoprotein E4 transgenic mice induces lysosomal activation and neurodegeneration resulting in marked cognitive deficits
    • Belinson H, Lev D, Masliah E, Michaelson DM. 2008. Activation of the amyloid cascade in apolipoprotein E4 transgenic mice induces lysosomal activation and neurodegeneration resulting in marked cognitive deficits. J Neurosci 28: 4690-4701.
    • (2008) J Neurosci , vol.28 , pp. 4690-4701
    • Belinson, H.1    Lev, D.2    Masliah, E.3    Michaelson, D.M.4
  • 12
    • 79957608284 scopus 로고    scopus 로고
    • A tale on animal models o Parkinson's disease
    • Bezard E, Przedborski S. 2011. A tale on animal models o Parkinson's disease. Mov Disord 26: 993-1002.
    • (2011) Mov Disord , vol.26 , pp. 993-1002
    • Bezard, E.1    Przedborski, S.2
  • 14
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N, Lorenzo HK, Carmona S, Laforge M, Harper F, Dumont C, Senik A. 2003. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J Biol Chem 278: 31401-31411.
    • (2003) J Biol Chem , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 15
    • 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 FM, Wegiel J, Yu WH, Nixon RA. 2008. Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease. J Neurosci 28: 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
  • 16
    • 84863482530 scopus 로고    scopus 로고
    • Lysosomal function and dysfunction: Mechanism and disease
    • Boya P. 2011. Lysosomal function and dysfunction: Mechanism and disease. Antioxid Redox Signal 17: 766-774.
    • (2011) Antioxid Redox Signal , vol.17 , pp. 766-774
    • Boya, P.1
  • 17
    • 54949137644 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization in cell death
    • Boya P, Kroemer G. 2008. Lysosomal membrane permeabilization in cell death. Oncogene 27: 6434-6451.
    • (2008) Oncogene , vol.27 , pp. 6434-6451
    • Boya, P.1    Kroemer, G.2
  • 18
    • 0015274335 scopus 로고
    • The effect of aging on lysosomal permeability in nerve cells of the central nervous system. An enzyme histochemical study in rat
    • Brunk U, Brun A. 1972. The effect of aging on lysosomal permeability in nerve cells of the central nervous system. An enzyme histochemical study in rat. Histochemie 30: 315-324.
    • (1972) Histochemie , vol.30 , pp. 315-324
    • Brunk, U.1    Brun, A.2
  • 19
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • Brunk UT, Svensson I. 1999. Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak. Redox Rep 4: 3-11.
    • (1999) Redox Rep , vol.4 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 20
    • 77951227122 scopus 로고    scopus 로고
    • Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-b, and Tau: Effects on cognitive impairments
    • Caccamo A, Majumder S, Richardson A, Strong R, Oddo S. 2010. Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-b, and Tau: Effects on cognitive impairments. J Biol Chem 285: 13107-13120.
    • (2010) J Biol Chem , vol.285 , pp. 13107-13120
    • Caccamo, A.1    Majumder, S.2    Richardson, A.3    Strong, R.4    Oddo, S.5
  • 21
    • 14844310312 scopus 로고    scopus 로고
    • Role of the autophagic-lysosomal system on low potassium-induced apoptosis in cultured cerebellar granule cells
    • Canu N, Tufi R, Serafino AL, Amadoro G, Ciotti MT, Calissano P. 2005. Role of the autophagic-lysosomal system on low potassium-induced apoptosis in cultured cerebellar granule cells. J Neurochem 92: 1228-1242.
    • (2005) J Neurochem , vol.92 , pp. 1228-1242
    • Canu, N.1    Tufi, R.2    Serafino, A.L.3    Amadoro, G.4    Ciotti, M.T.5    Calissano, P.6
  • 22
    • 0028220243 scopus 로고
    • Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease
    • Cataldo AM, Hamilton DJ, Nixon RA. 1994. Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer disease. Brain Res 640: 68-80.
    • (1994) Brain Res , vol.640 , pp. 68-80
    • Cataldo, A.M.1    Hamilton, D.J.2    Nixon, R.A.3
  • 23
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsinDin Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • Cataldo AM, Barnett JL, Berman SA, Li J, Quarless S, Bursztajn S, Lippa C, Nixon RA. 1995. Gene expression and cellular content of cathepsinDin Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system. Neuron 14: 671-680.
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 24
    • 0030045552 scopus 로고    scopus 로고
    • Properties of the endosomal-lysosomal system in the human central nervous system: Disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease
    • Cataldo AM, Hamilton DJ, Barnett JL, Paskevich PA, Nixon RA. 1996. Properties of the endosomal-lysosomal system in the human central nervous system: Disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J Neurosci 16: 186-199.
    • (1996) J Neurosci , vol.16 , pp. 186-199
    • Cataldo, A.M.1    Hamilton, D.J.2    Barnett, J.L.3    Paskevich, P.A.4    Nixon, R.A.5
  • 25
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased bamyloidogenesis
    • Cataldo AM, Barnett JL, Pieroni C, Nixon RA. 1997. Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased bamyloidogenesis. J Neurosci 17: 6142-6151.
    • (1997) J Neurosci , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 26
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid b deposition in sporadic Alzheimer's disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations
    • Cataldo AM, Peterhoff CM, Troncoso JC, Gomez-Isla T, Hyman BT, Nixon RA. 2000. Endocytic pathway abnormalities precede amyloid b deposition in sporadic Alzheimer's disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations. AmJ Pathol 157: 277-286.
    • (2000) AmJ Pathol , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 28
    • 77449098426 scopus 로고    scopus 로고
    • Towards an understanding of the anti-aging mechanism of caloric restriction
    • Cavallini G, Donati A, Gori Z, Bergamini E. 2008. Towards an understanding of the anti-aging mechanism of caloric restriction. Curr Aging Sci 1: 4-9.
    • (2008) Curr Aging Sci , vol.1 , pp. 4-9
    • Cavallini, G.1    Donati, A.2    Gori, Z.3    Bergamini, E.4
  • 29
    • 0017928013 scopus 로고
    • Cell death of motoneurons in the chick embryo spinal cord. I. A light and electron microscopic study of naturally occurring and induced cell loss during development
    • Chu-Wang IW, Oppenheim RW. 1978. Cell death of motoneurons in the chick embryo spinal cord. I. A light and electron microscopic study of naturally occurring and induced cell loss during development. J Comp Neurol 177: 33-57.
    • (1978) J Comp Neurol , vol.177 , pp. 33-57
    • Chu-Wang, I.W.1    Oppenheim, R.W.2
  • 30
    • 0000189281 scopus 로고
    • Cellular differentiation in the kidneys of newborn mice studies with the electron microscope
    • Clark SL Jr. 1957. Cellular differentiation in the kidneys of newborn mice studies with the electron microscope. J Biophys Biochem Cytol 3: 349-362.
    • (1957) J Biophys Biochem Cytol , vol.3 , pp. 349-362
    • Clark Jr., S.L.1
  • 31
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke PG. 1990. Developmental cell death: Morphological diversity and multiple mechanisms. Anat Embryol 181: 195-213.
    • (1990) Anat Embryol , vol.181 , pp. 195-213
    • Clarke, P.G.1
  • 32
    • 27644591304 scopus 로고    scopus 로고
    • Axon degeneration mechanisms: Commonality amid diversity
    • Coleman M. 2005. Axon degeneration mechanisms: Commonality amid diversity. Nat Rev Neurosci 6: 889-898.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 889-898
    • Coleman, M.1
  • 33
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant a-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. 2004. Impaired degradation of mutant a-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 34
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1a by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L, Jeong H, Borovecki F, Parkhurst CN, Tanese N, Krainc D. 2006. Transcriptional repression of PGC-1a by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127: 59-69.
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 35
    • 77149132129 scopus 로고    scopus 로고
    • Autophagy protects the rotenone-induced cell death in a-synuclein overexpressing SHSY5Y cells
    • Dadakhujaev S, Noh HS, Jung EJ, Cha JY, Baek SM, Ha JH, Kim DR. 2010. Autophagy protects the rotenone-induced cell death in a-synuclein overexpressing SHSY5Y cells. Neurosci Lett 472: 47-52.
    • (2010) Neurosci Lett , vol.472 , pp. 47-52
    • Dadakhujaev, S.1    Noh, H.S.2    Jung, E.J.3    Cha, J.Y.4    Baek, S.M.5    Ha, J.H.6    Kim, D.R.7
  • 36
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda RK, Cherra SJ 3rd, Kulich SM, Tandon A, Park D, Chu CT. 2009. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem 284: 13843-13855.
    • (2009) J Biol Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra III, S.J.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 37
    • 84863954409 scopus 로고    scopus 로고
    • Regulation and function of autophagy during cell survival and cell death
    • doi: 10.1101/cshperspect. a008813
    • Das G, Shravage BV, Baehrecke EH. 2012. Regulation and function of autophagy during cell survival and cell death. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect. a008813.
    • (2012) Cold Spring Harb Perspect Biol
    • Das, G.1    Shravage, B.V.2    Baehrecke, E.H.3
  • 38
    • 0002549377 scopus 로고
    • The lysosome
    • de Duve C. 1963. The lysosome. Sci Am 208: 64-72.
    • (1963) Sci Am , vol.208 , pp. 64-72
    • de Duve, C.1
  • 42
    • 77951750296 scopus 로고    scopus 로고
    • Selective autophagy in cancer development and therapy
    • Dikic I, Johansen T, Kirkin V. 2010. Selective autophagy in cancer development and therapy. Cancer Res 70: 3431-3434.
    • (2010) Cancer Res , vol.70 , pp. 3431-3434
    • Dikic, I.1    Johansen, T.2    Kirkin, V.3
  • 44
    • 11844294713 scopus 로고    scopus 로고
    • Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis
    • Erdal H, Berndtsson M, Castro J, Brunk U, Shoshan MC, Linder S. 2005. Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis. Proc Natl Acad Sci 102: 192-197.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 192-197
    • Erdal, H.1    Berndtsson, M.2    Castro, J.3    Brunk, U.4    Shoshan, M.C.5    Linder, S.6
  • 45
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in Mammalian cells
    • Eskelinen EL. 2005. Maturation of autophagic vacuoles in Mammalian cells. Autophagy 1: 1-10.
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 46
    • 62949091373 scopus 로고    scopus 로고
    • Autophagy: A lysosomal degradation pathway with a central role in health and disease
    • Eskelinen EL, Saftig P. 2009. Autophagy: A lysosomal degradation pathway with a central role in health and disease. Biochim Biophys Acta 1793: 664-673.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 664-673
    • Eskelinen, E.L.1    Saftig, P.2
  • 47
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies:Twoclosely related partners
    • Fader CM, Colombo MI. 2009. Autophagy and multivesicular bodies:Twoclosely related partners. Cell Death Differ 16: 70-78.
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 49
    • 0344874551 scopus 로고    scopus 로고
    • Emerging role for autophagy in the removal of aggresomes i Schwann cells
    • Fortun J, DunnWA Jr, Joy S, Li J, Notterpek L. 2003. Emerging role for autophagy in the removal of aggresomes i Schwann cells. J Neurosci 23: 10672-10680.
    • (2003) J Neurosci , vol.23 , pp. 10672-10680
    • Fortun, J.1    Dunn Jr., W.A.2    Joy, S.3    Li, J.4    Notterpek, L.5
  • 50
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • Gafni J, Ellerby LM. 2002. Calpain activation in Huntington's disease. J Neurosci 22: 4842-4849.
    • (2002) J Neurosci , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 51
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease: Insights from genetic studies
    • Gasser T. 2009. Molecular pathogenesis of Parkinson disease: Insights from genetic studies. Expert Rev Mol Med 11: e22.
    • (2009) Expert Rev Mol Med , vol.11
    • Gasser, T.1
  • 54
    • 77949897022 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies
    • Geser F, Lee VM, Trojanowski JQ. 2010. Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: A spectrum of TDP-43 proteinopathies. Neuropathology 30: 103-112.
    • (2010) Neuropathology , vol.30 , pp. 103-112
    • Geser, F.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 55
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • Gil JM, Rego AC. 2008. Mechanisms of neurodegeneration in Huntington's disease. Eur J Neurosci 27: 2803-2820.
    • (2008) Eur J Neurosci , vol.27 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 57
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • Glabe C. 2001. Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease. J Mol Neurosci 17: 137-145.
    • (2001) J Mol Neurosci , vol.17 , pp. 137-145
    • Glabe, C.1
  • 58
    • 0024299286 scopus 로고
    • Prelysosomal convergence of autophagic and endocytic pathways
    • Gordon PB, Seglen PO. 1988. Prelysosomal convergence of autophagic and endocytic pathways. Biochem Biophys Res Commun 151: 40-47.
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 63
    • 0017646340 scopus 로고
    • Anterior horn cell degeneration and Bunina-type inclusions associatedwith dementia
    • Hart MN, Cancilla PA, Frommes S, Hirano A. 1977. Anterior horn cell degeneration and Bunina-type inclusions associatedwith dementia. ActaNeuropathol 38: 225-228.
    • (1977) ActaNeuropathol , vol.38 , pp. 225-228
    • Hart, M.N.1    Cancilla, P.A.2    Frommes, S.3    Hirano, A.4
  • 65
    • 0027538111 scopus 로고
    • An early cytoplasmic change before Lewy body maturation: An ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism
    • Hayashida K, Oyanagi S, Mizutani Y, Yokochi M. 1993. An early cytoplasmic change before Lewy body maturation: An ultrastructural study of the substantia nigra from an autopsy case of juvenile parkinsonism. Acta Neuropathol 85: 445-448.
    • (1993) Acta Neuropathol , vol.85 , pp. 445-448
    • Hayashida, K.1    Oyanagi, S.2    Mizutani, Y.3    Yokochi, M.4
  • 66
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C, Klionsky DJ. 2009. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 43: 67-93.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 69
    • 0029838035 scopus 로고    scopus 로고
    • Neuropathology of ALS: An overview
    • Hirano A. 1996. Neuropathology of ALS: An overview. Neurology 47: S63-S66.
    • (1996) Neurology , vol.47
    • Hirano, A.1
  • 70
    • 0013832794 scopus 로고
    • Lysomes in the rat sciatic nerve following crush
    • Holtzman E, Novikoff AB. 1965. Lysomes in the rat sciatic nerve following crush. J Cell Biol 27: 651-669.
    • (1965) J Cell Biol , vol.27 , pp. 651-669
    • Holtzman, E.1    Novikoff, A.B.2
  • 71
    • 0014085531 scopus 로고
    • Lysosomes and GERL in normal and chromatolytic neurons of the rat ganglion nodosum
    • Holtzman E, Novikoff AB, Villaverde H. 1967. Lysosomes and GERL in normal and chromatolytic neurons of the rat ganglion nodosum. J Cell Biol 33: 419-435.
    • (1967) J Cell Biol , vol.33 , pp. 419-435
    • Holtzman, E.1    Novikoff, A.B.2    Villaverde, H.3
  • 72
    • 0024370374 scopus 로고
    • Endocytosis and autophagy in dying neurons: An ultrastructural study in chick embryos
    • Hornung JP, Koppel H, Clarke PG. 1989. Endocytosis and autophagy in dying neurons: An ultrastructural study in chick embryos. J Comp Neurol 283: 425-437.
    • (1989) J Comp Neurol , vol.283 , pp. 425-437
    • Hornung, J.P.1    Koppel, H.2    Clarke, P.G.3
  • 73
    • 0021675999 scopus 로고
    • Inhibitors of lysosomal enzymes: Accumulation of lipofuscin-like dense bodies in the brain
    • Ivy GO, Schottler F, Wenzel J, Baudry M, Lynch G. 1984. Inhibitors of lysosomal enzymes: Accumulation of lipofuscin-like dense bodies in the brain. Science 226: 985-987.
    • (1984) Science , vol.226 , pp. 985-987
    • Ivy, G.O.1    Schottler, F.2    Wenzel, J.3    Baudry, M.4    Lynch, G.5
  • 75
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana NR, Zemskov EA, Wang G, Nukina N. 2001. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 10: 1049-1059.
    • (2001) Hum Mol Genet , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 77
    • 0037077284 scopus 로고    scopus 로고
    • Apolipoprotein E4 potentiates amyloid b peptide-induced lysosomal leakage and apoptosis in neuronal cells
    • Ji ZS, Miranda RD, Newhouse YM, Weisgraber KH, Huan Y, Mahley RW. 2002. Apolipoprotein E4 potentiates amyloid b peptide-induced lysosomal leakage and apoptosis in neuronal cells. J Biol Chem 277: 21821-21828.
    • (2002) J Biol Chem , vol.277 , pp. 21821-21828
    • Ji, Z.S.1    Miranda, R.D.2    Newhouse, Y.M.3    Weisgraber, K.H.4    Huan, Y.5    Mahley, R.W.6
  • 78
    • 33645553416 scopus 로고    scopus 로고
    • Reactivity of apolipoprotein E4 and amyloid b peptide: Lysosomal stability and neurodegeneration
    • Ji ZS, Mullendorff K, Cheng IH, Miranda RD, Huang Y, Mahley RW. 2006. Reactivity of apolipoprotein E4 and amyloid b peptide: Lysosomal stability and neurodegeneration. J Biol Chem 281: 2683-2692.
    • (2006) J Biol Chem , vol.281 , pp. 2683-2692
    • Ji, Z.S.1    Mullendorff, K.2    Cheng, I.H.3    Miranda, R.D.4    Huang, Y.5    Mahley, R.W.6
  • 80
    • 25844434838 scopus 로고    scopus 로고
    • Up-regulation of lysosomal cathepsin L and autophagy during neuronal death induced by reduced serum and potassium
    • Kaasik A, Rikk T, Piirsoo A, Zharkovsky T, Zharkovsky A. 2005. Up-regulation of lysosomal cathepsin L and autophagy during neuronal death induced by reduced serum and potassium. Eur J Neurosci 22: 1023-1031.
    • (2005) Eur J Neurosci , vol.22 , pp. 1023-1031
    • Kaasik, A.1    Rikk, T.2    Piirsoo, A.3    Zharkovsky, T.4    Zharkovsky, A.5
  • 81
    • 60249098801 scopus 로고    scopus 로고
    • Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease
    • Karuppagounder SS, Pinto JT, Xu H, Chen HL, Beal MF, Gibson GE. 2009. Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease. Neurochem Int 54: 111-118.
    • (2009) Neurochem Int , vol.54 , pp. 111-118
    • Karuppagounder, S.S.1    Pinto, J.T.2    Xu, H.3    Chen, H.L.4    Beal, M.F.5    Gibson, G.E.6
  • 82
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev AG, Thompson LM. 2008. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat Rev Drug Discov 7: 854-868.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 83
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castano JG, Aronin N, DiFiglia M. 2000. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 20: 7268-7278.
    • (2000) J Neurosci , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6    DiFiglia, M.7
  • 84
    • 77955845955 scopus 로고    scopus 로고
    • Lysosomal rupture, necroapoptotic interactions and potential crosstalk between cysteine proteases in neurons shortly after focal ischemia
    • Kilinc M, Gursoy-Ozdemir Y, Gurer G, Erdener SE, Erdemli E, Can A, Dalkara T. 2010. Lysosomal rupture, necroapoptotic interactions and potential crosstalk between cysteine proteases in neurons shortly after focal ischemia. Neurobiol Dis 40: 293-302.
    • (2010) Neurobiol Dis , vol.40 , pp. 293-302
    • Kilinc, M.1    Gursoy-Ozdemir, Y.2    Gurer, G.3    Erdener, S.E.4    Erdemli, E.5    Can, A.6    Dalkara, T.7
  • 86
    • 36148991943 scopus 로고    scopus 로고
    • Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease
    • Ko DC, Milenkovic L, Beier SM, Manuel H, Buchanan J, Scott MP. 2005. Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease. PLoS Genet 1: 81-95.
    • (2005) PLoS Genet , vol.1 , pp. 81-95
    • Ko, D.C.1    Milenkovic, L.2    Beier, S.M.3    Manuel, H.4    Buchanan, J.5    Scott, M.P.6
  • 91
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk VI, Mansilla A, Menzies FM, Rubinsztein DC. 2009. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 33: 517-527.
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 92
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G, Jaattela M. 2005. Lysosomes and autophagy in cell death control. Nat Rev Cancer 5: 886-897.
    • (2005) Nat Rev Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 96
    • 77949775195 scopus 로고    scopus 로고
    • Repeat expansion disease: Progress and puzzles in disease pathogenesis
    • La Spada AR, Taylor JP. 2010. Repeat expansion disease: Progress and puzzles in disease pathogenesis. Nat Rev Genet 11: 247-258.
    • (2010) Nat Rev Genet , vol.11 , pp. 247-258
    • la Spada, A.R.1    Taylor, J.P.2
  • 97
    • 67649996222 scopus 로고    scopus 로고
    • Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRTIII in frontotemporal dementia
    • Lee JA, Gao FB. 2009. Inhibition of autophagy induction delays neuronal cell loss caused by dysfunctional ESCRTIII in frontotemporal dementia. J Neurosci 29: 8506-8511.
    • (2009) J Neurosci , vol.29 , pp. 8506-8511
    • Lee, J.A.1    Gao, F.B.2
  • 98
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • Lee JA, Beigneux A, Ahmad ST, Young SG, Gao FB. 2007. ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr Biol 17: 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
  • 100
    • 79957663035 scopus 로고    scopus 로고
    • Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy
    • Lee S, Sato Y, Nixon RA. 2011. Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy. J Neurosci 31: 7817-7830.
    • (2011) J Neurosci , vol.31 , pp. 7817-7830
    • Lee, S.1    Sato, Y.2    Nixon, R.A.3
  • 101
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: An innocent convict?
    • Levine B, Yuan J. 2005. Autophagy in cell death: An innocent convict? J Clin Invest 115: 2679-2688.
    • (2005) J Clin Invest , vol.115 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 102
    • 41449113885 scopus 로고    scopus 로고
    • Altered macroautophagy in the spinal cord of SOD1 mutant mice
    • Li L, Zhang X, Le W. 2008. Altered macroautophagy in the spinal cord of SOD1 mutant mice. Autophagy 4: 290-293.
    • (2008) Autophagy , vol.4 , pp. 290-293
    • Li, L.1    Zhang, X.2    Le, W.3
  • 103
    • 78650824020 scopus 로고    scopus 로고
    • Parkinson's disease involves autophagy and abnormal distribution of cathepsin L
    • Li L, Wang X, Fei X, Xia L, Qin Z, Liang Z. 2011. Parkinson's disease involves autophagy and abnormal distribution of cathepsin L. Neurosci Lett 489: 62-67.
    • (2011) Neurosci Lett , vol.489 , pp. 62-67
    • Li, L.1    Wang, X.2    Fei, X.3    Xia, L.4    Qin, Z.5    Liang, Z.6
  • 104
    • 77449094358 scopus 로고    scopus 로고
    • Neuralspecific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration
    • Liang CC, Wang C, Peng X, Gan B, Guan JL. 2010. Neuralspecific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration. J Biol Chem 285: 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
  • 105
    • 0029079332 scopus 로고
    • Neuroaxonal dystrophy in experimental Creutzfeldt-Jakob disease: Electron microscopical and immunohistochemical demonstration of neurofilament accumulations within affected neurites
    • Liberski PP, Budka H, Yanagihara R, Gajdusek DC. 1995. Neuroaxonal dystrophy in experimental Creutzfeldt-Jakob disease: Electron microscopical and immunohistochemical demonstration of neurofilament accumulations within affected neurites. J Comp Pathol 112: 243-255.
    • (1995) J Comp Pathol , vol.112 , pp. 243-255
    • Liberski, P.P.1    Budka, H.2    Yanagihara, R.3    Gajdusek, D.C.4
  • 106
    • 58449101589 scopus 로고    scopus 로고
    • Ab42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila
    • Ling D, Song HJ, Garza D, Neufeld TP, Salvaterra PM. 2009. Ab42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila. PLoS ONE 4: e4201.
    • (2009) PLoS ONE , vol.4
    • Ling, D.1    Song, H.J.2    Garza, D.3    Neufeld, T.P.4    Salvaterra, P.M.5
  • 107
    • 0031031041 scopus 로고    scopus 로고
    • The autophagic and endocytic pathways converge at the nascent autophagic vacuoles
    • LiouW, Geuze HJ, Geelen MJ, Slot JW. 1997. The autophagic and endocytic pathways converge at the nascent autophagic vacuoles. J Cell Biol 136: 61-70.
    • (1997) J Cell Biol , vol.136 , pp. 61-70
    • Liou, W.1    Geuze, H.J.2    Geelen, M.J.3    Slot, J.W.4
  • 111
    • 37349063722 scopus 로고    scopus 로고
    • The neuropathology of FTD associated with ALS
    • Mackenzie IR. 2007. The neuropathology of FTD associated with ALS. Alzheimer Dis Assoc Disord 21: S44-S49.
    • (2007) Alzheimer Dis Assoc Disord , vol.21
    • McKenzie, I.R.1
  • 112
    • 33745740540 scopus 로고    scopus 로고
    • Apolipoprotein (apo) E4 and Alzheimer's disease: Unique conformational and biophysical properties of apoE4 can modulate neuropathology
    • Mahley RW, Huang Y. 2006. Apolipoprotein (apo) E4 and Alzheimer's disease: Unique conformational and biophysical properties of apoE4 can modulate neuropathology. Acta Neurol Scand Suppl 185: 8-14.
    • (2006) Acta Neurol Scand Suppl , vol.185 , pp. 8-14
    • Mahley, R.W.1    Huang, Y.2
  • 113
    • 34548188741 scopus 로고    scopus 로고
    • Selfeating and self-killing: Crosstalk between autophagy and apoptosis
    • Maiuri MC, Zalckvar E, Kimchi A, Kroemer G. 2007. Selfeating and self-killing: Crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 8: 741-752.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 114
    • 80053243942 scopus 로고    scopus 로고
    • Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits
    • Majumder S, Richardson A, Strong R, Oddo S. 2011. Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits. PLoS ONE 6: e25416.
    • (2011) PLoS ONE , vol.6
    • Majumder, S.1    Richardson, A.2    Strong, R.3    Oddo, S.4
  • 118
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y. 2004. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Bio Cell 15: 1101-1111.
    • (2004) Mol Bio Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 122
    • 0034030313 scopus 로고    scopus 로고
    • Frontotemporal dementiawith motor neuron disease (amyotrophic lateral sclerosis with dementia)
    • Nakano I. 2000. Frontotemporal dementiawith motor neuron disease (amyotrophic lateral sclerosis with dementia). Neuropathology 20: 68-75.
    • (2000) Neuropathology , vol.20 , pp. 68-75
    • Nakano, I.1
  • 123
    • 0027742029 scopus 로고
    • On the possibility of autolysosomal processing of skein-like inclusions. Electron microscopic observation in a case of amyotrophic lateral sclerosis
    • Nakano I, Shibata T, Uesaka Y. 1993. On the possibility of autolysosomal processing of skein-like inclusions. Electron microscopic observation in a case of amyotrophic lateral sclerosis. J Neurol Sci 120: 54-59.
    • (1993) J Neurol Sci , vol.120 , pp. 54-59
    • Nakano, I.1    Shibata, T.2    Uesaka, Y.3
  • 124
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, Youle RJ. 2008. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 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
  • 127
    • 33747881231 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative disease: Friend, foe or turncoat?
    • Nixon RA. 2006. Autophagy in neurodegenerative disease: Friend, foe or turncoat? Trends Neurosci 29: 528-535.
    • (2006) Trends Neurosci , vol.29 , pp. 528-535
    • Nixon, R.A.1
  • 128
    • 0028806557 scopus 로고
    • The endosomal-lysosomal system of neurons: New roles
    • Nixon RA, Cataldo AM. 1995. The endosomal-lysosomal system of neurons: New roles. Trends Neurosci 18: 489-496.
    • (1995) Trends Neurosci , vol.18 , pp. 489-496
    • Nixon, R.A.1    Cataldo, A.M.2
  • 129
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease
    • Nixon RA, Cataldo AM. 2006. Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease. JAlzheimers Dis 9: 277-289.
    • (2006) JAlzheimers Dis , vol.9 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 130
    • 79955969705 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer's disease-Locating the primary defect
    • Nixon RA, Yang DS. 2011. Autophagy failure in Alzheimer's disease-Locating the primary defect. Neurobiol Dis 43: 38-45.
    • (2011) Neurobiol Dis , vol.43 , pp. 38-45
    • Nixon, R.A.1    Yang, D.S.2
  • 131
    • 0034304390 scopus 로고    scopus 로고
    • The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: A review
    • Nixon RA, Cataldo AM, Mathews PM. 2000. The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: A review. Neurochem Res 25: 1161-1172.
    • (2000) Neurochem Res , vol.25 , pp. 1161-1172
    • Nixon, R.A.1    Cataldo, A.M.2    Mathews, P.M.3
  • 133
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: A continuum from development to late age
    • Nixon RA, Yang DS, Lee JH. 2008. Neurodegenerative lysosomal disorders: A continuum from development to late age. Autophagy 4: 590-599.
    • (2008) Autophagy , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 134
    • 67549132527 scopus 로고    scopus 로고
    • The late stages of autophagy: How does the end begin?
    • Noda T, Fujita N, Yoshimori T. 2009. The late stages of autophagy: How does the end begin? Cell Death Differ 16: 984-990.
    • (2009) Cell Death Differ , vol.16 , pp. 984-990
    • Noda, T.1    Fujita, N.2    Yoshimori, T.3
  • 135
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a nove BH3-only protein
    • Oberstein A, Jeffrey PD, Shi Y. 2007. Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a nove BH3-only protein. J Biol Chem 282: 13123-13132.
    • (2007) J Biol Chem , vol.282 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 136
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi Y. 2001. Molecular dissection of autophagy: Two ubiquitin-like systems. Nat RevMol Cell Biol 2: 211-216.
    • (2001) Nat RevMol Cell Biol , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 138
    • 80052716148 scopus 로고    scopus 로고
    • Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways
    • Palmieri M, Impey S, Kang H, di Ronza A, Pelz C, Sardiello M, Ballabio A. 2011. Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways. Hum Mol Genet 20: 3852-3866.
    • (2011) Hum Mol Genet , vol.20 , pp. 3852-3866
    • Palmieri, M.1    Impey, S.2    Kang, H.3    di Ronza, A.4    Pelz, C.5    Sardiello, M.6    Ballabio, A.7
  • 139
    • 0030946503 scopus 로고    scopus 로고
    • Mechanisms of cell death induced by the mitochondrial toxin 3-nitropropionic acid: Acute excitotoxic necrosis and delayed apoptosis
    • Pang Z, Geddes JW. 1997. Mechanisms of cell death induced by the mitochondrial toxin 3-nitropropionic acid: Acute excitotoxic necrosis and delayed apoptosis. J Neurosci 17: 3064-3073.
    • (1997) J Neurosci , vol.17 , pp. 3064-3073
    • Pang, Z.1    Geddes, J.W.2
  • 140
    • 0038279765 scopus 로고    scopus 로고
    • Calpain facilitates the neuron death induced by 3-nitropropionic acid and contributes to the necrotic morphology
    • Pang Z, Bondada V, Sengoku T, Siman R, Geddes JW. 2003. Calpain facilitates the neuron death induced by 3-nitropropionic acid and contributes to the necrotic morphology. J Neuropathol Exp Neurol 62: 633-643.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 633-643
    • Pang, Z.1    Bondada, V.2    Sengoku, T.3    Siman, R.4    Geddes, J.W.5
  • 145
    • 79960664223 scopus 로고    scopus 로고
    • Activation of autophagy in a rat model of retinal ischemia following high intraocular pressure
    • Piras A, Gianetto D, Conte D, Bosone A, Vercelli A. 2011. Activation of autophagy in a rat model of retinal ischemia following high intraocular pressure. PLoS ONE 6: e22514.
    • (2011) PLoS ONE , vol.6
    • Piras, A.1    Gianetto, D.2    Conte, D.3    Bosone, A.4    Vercelli, A.5
  • 146
    • 70350059677 scopus 로고    scopus 로고
    • Postischemic treatment of neonatal cerebral ischemia should target autophagy
    • Puyal J, Vaslin A, Mottier V, Clarke PG. 2009. Postischemic treatment of neonatal cerebral ischemia should target autophagy. Ann Neurol 66: 378-389.
    • (2009) Ann Neurol , vol.66 , pp. 378-389
    • Puyal, J.1    Vaslin, A.2    Mottier, V.3    Clarke, P.G.4
  • 147
    • 20144381544 scopus 로고    scopus 로고
    • Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death
    • Pyo JO, Jang MH, Kwon YK, Lee HJ, Jun JI, Woo HN, Cho DH, Choi B, Lee H, Kim JH, et al. 2005. Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death. J Biol Chem 280: 20722-20729.
    • (2005) J Biol Chem , vol.280 , pp. 20722-20729
    • Pyo, J.O.1    Jang, M.H.2    Kwon, Y.K.3    Lee, H.J.4    Jun, J.I.5    Woo, H.N.6    Cho, D.H.7    Choi, B.8    Lee, H.9    Kim, J.H.10
  • 149
    • 58149397537 scopus 로고    scopus 로고
    • Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: Neuroprotection by CAST overexpression
    • Rao MV, Mohan PS, Peterhoff CM, Yang DS, Schmidt SD, Stavrides PH, Campbell J, Chen Y, Jiang Y, Paskevich PA, et al. 2008. Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: Neuroprotection by CAST overexpression. J Neurosci 28: 12241-12254.
    • (2008) J Neurosci , vol.28 , pp. 12241-12254
    • Rao, M.V.1    Mohan, P.S.2    Peterhoff, C.M.3    Yang, D.S.4    Schmidt, S.D.5    Stavrides, P.H.6    Campbell, J.7    Chen, Y.8    Jiang, Y.9    Paskevich, P.A.10
  • 153
  • 154
    • 0022369964 scopus 로고
    • Neuronal nuclear membrane indentation and astrocyte/neuron ratio in Huntington's disease. A quantitative electron microscopic study
    • Roos RA, Bots GT, Hermans J. 1985. Neuronal nuclear membrane indentation and astrocyte/neuron ratio in Huntington's disease. A quantitative electron microscopic study. J Hirnforsch 26: 689-693.
    • (1985) J Hirnforsch , vol.26 , pp. 689-693
    • Roos, R.A.1    Bots, G.T.2    Hermans, J.3
  • 159
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I, Xu CJ, Juo P, Kakizaka A, Blenis J, Yuan J. 1999. Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22: 623-633.
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 161
    • 79955522014 scopus 로고    scopus 로고
    • Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis
    • Sasaki S. 2011. Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 70: 349-359.
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 349-359
    • Sasaki, S.1
  • 162
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • Schweichel JU, Merker HJ. 1973. The morphology of various types of cell death in prenatal tissues. Teratology 7: 253-266.
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 167
    • 77953858790 scopus 로고    scopus 로고
    • TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy
    • Shi CS, Kehrl JH. 2010. TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy. Sci Signal 3: ra42.
    • (2010) Sci Signal , vol.3
    • Shi, C.S.1    Kehrl, J.H.2
  • 172
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in a-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. 2009. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in a-synuclein models of Parkinson's and Lewy body diseases. J Neurosci 29: 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
  • 174
    • 13544273998 scopus 로고    scopus 로고
    • Caspase-dependent and-independent neuronal death: Twodistinct pathways to neuronal injury
    • Stefanis L. 2005. Caspase-dependent and-independent neuronal death: Twodistinct pathways to neuronal injury. Neuroscientist 11: 50-62.
    • (2005) Neuroscientist , vol.11 , pp. 50-62
    • Stefanis, L.1
  • 175
    • 54049140363 scopus 로고    scopus 로고
    • The syndromes of frontotemporal dysfunction in amyotrophic lateral sclerosis
    • Strong MJ. 2008. The syndromes of frontotemporal dysfunction in amyotrophic lateral sclerosis. Amyotroph Lateral Scler 9: 323-338.
    • (2008) Amyotroph Lateral Scler , vol.9 , pp. 323-338
    • Strong, M.J.1
  • 177
    • 53849106834 scopus 로고    scopus 로고
    • Cystatin Ccathepsin B axis regulates amyloid b levels and associated neuronal deficits in an animal model of Alzheimer's disease
    • Sun B, Zhou Y, Halabisky B, Lo I, Cho SH, Mueller-Steiner S, Devidze N, Wang X, Grubb A, Gan L. 2008. Cystatin Ccathepsin B axis regulates amyloid b levels and associated neuronal deficits in an animal model of Alzheimer's disease. Neuron 60: 247-257.
    • (2008) Neuron , vol.60 , pp. 247-257
    • Sun, B.1    Zhou, Y.2    Halabisky, B.3    Lo, I.4    Cho, S.H.5    Mueller-Steiner, S.6    Devidze, N.7    Wang, X.8    Grubb, A.9    Gan, L.10
  • 178
    • 0036023937 scopus 로고    scopus 로고
    • Death by necrosis. Uncontrollable catastrophe, or is there order behind the chaos?
    • Syntichaki P, Tavernarakis N. 2002. Death by necrosis. Uncontrollable catastrophe, or is there order behind the chaos? EMBO Rep 3: 604-609.
    • (2002) EMBO Rep , vol.3 , pp. 604-609
    • Syntichaki, P.1    Tavernarakis, N.2
  • 181
    • 33644641768 scopus 로고    scopus 로고
    • Oxidative stress, accumulation of biological "garbage, " and aging
    • Terman A, Brunk UT. 2006. Oxidative stress, accumulation of biological "garbage, " and aging. Antioxid Redox Signal 8: 197-204.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 197-204
    • Terman, A.1    Brunk, U.T.2
  • 182
    • 79957917512 scopus 로고    scopus 로고
    • A smallmolecule enhancer of autophagy decreases levels of Ab and APP-CTF via Atg5-dependent autophagy pathway
    • Tian Y, Bustos V, Flajolet M, Greengard P. 2011. A smallmolecule enhancer of autophagy decreases levels of Ab and APP-CTF via Atg5-dependent autophagy pathway. FASEB J 25: 1934-1942.
    • (2011) FASEB J , vol.25 , pp. 1934-1942
    • Tian, Y.1    Bustos, V.2    Flajolet, M.3    Greengard, P.4
  • 183
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E, Salomons FA, Vesa J, Bott LC, Kimonis V, Yao TP, Dantuma NP, Taylor JP. 2010. VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6: 217-227.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 184
    • 0034659833 scopus 로고    scopus 로고
    • A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration
    • Tyynela J, Sohar I, Sleat DE, Gin RM, Donnelly RJ, Baumann M, Haltia M, Lobel P. 2000. A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. Emb J 19: 2786-2792.
    • (2000) Emb J , vol.19 , pp. 2786-2792
    • Tyynela, J.1    Sohar, I.2    Sleat, D.E.3    Gin, R.M.4    Donnelly, R.J.5    Baumann, M.6    Haltia, M.7    Lobel, P.8
  • 185
    • 0034849783 scopus 로고    scopus 로고
    • Autophagic cell death and its execution by lysosomal cathepsins
    • Uchiyama Y. 2001. Autophagic cell death and its execution by lysosomal cathepsins. Arch Histol Cytol 64: 233-246.
    • (2001) Arch Histol Cytol , vol.64 , pp. 233-246
    • Uchiyama, Y.1
  • 186
    • 41649086378 scopus 로고    scopus 로고
    • Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria
    • Vande Velde C, Miller TM, Cashman NR, Cleveland DW. 2008. Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria. Proc Natl Acad Sci 105: 4022-4027.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 4022-4027
    • Vande Velde, C.1    Miller, T.M.2    Cashman, N.R.3    Cleveland, D.W.4
  • 187
    • 56349119573 scopus 로고    scopus 로고
    • Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells
    • Venkatachalam K, Long AA, Elsaesser R, Nikolaeva D, Broadie K, Montell C. 2008. Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells. Cell 135: 838-851.
    • (2008) Cell , vol.135 , pp. 838-851
    • Venkatachalam, K.1    Long, A.A.2    Elsaesser, R.3    Nikolaeva, D.4    Broadie, K.5    Montell, C.6
  • 188
    • 79953221421 scopus 로고    scopus 로고
    • Severe global cerebral ischemia-induced programmed necrosis of hippocampal CA1 neurons in rat is prevented by 3-methyladenine: A widely used inhibitor of autophagy
    • Wang JY, Xia Q, Chu KT, Pan J, Sun LN, Zeng B, Zhu YJ, Wang Q, Wang K, Luo BY. 2011. Severe global cerebral ischemia-induced programmed necrosis of hippocampal CA1 neurons in rat is prevented by 3-methyladenine: A widely used inhibitor of autophagy. J Neuropathol Exp Neurol 70: 314-322.
    • (2011) J Neuropathol Exp Neurol , vol.70 , pp. 314-322
    • Wang, J.Y.1    Xia, Q.2    Chu, K.T.3    Pan, J.4    Sun, L.N.5    Zeng, B.6    Zhu, Y.J.7    Wang, Q.8    Wang, K.9    Luo, B.Y.10
  • 190
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvationinduced autophagy
    • Wei Y, Pattingre S, Sinha S, Bassik M, Levine B. 2008. JNK1-mediated phosphorylation of Bcl-2 regulates starvationinduced autophagy. Mol Cell 30: 678-688.
    • (2008) Mol Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 191
    • 79959415069 scopus 로고    scopus 로고
    • Biogenesis and cargo selectivity of autophagosomes
    • Weidberg H, Shvets E, Elazar Z. 2011. Biogenesis and cargo selectivity of autophagosomes. Annu Rev Biochem 80: 125-156.
    • (2011) Annu Rev Biochem , vol.80 , pp. 125-156
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 192
    • 50249189191 scopus 로고    scopus 로고
    • Neuronal injury in rat model of permanent focal cerebral ischemia is associated with activation of autophagic and lysosomal pathways
    • Wen YD, Sheng R, Zhang LS, Han R, Zhang X, Zhang XD, Han F, Fukunaga K, Qin ZH. 2008. Neuronal injury in rat model of permanent focal cerebral ischemia is associated with activation of autophagic and lysosomal pathways. Autophagy 4: 762-769.
    • (2008) Autophagy , vol.4 , pp. 762-769
    • Wen, Y.D.1    Sheng, R.2    Zhang, L.S.3    Han, R.4    Zhang, X.5    Zhang, X.D.6    Han, F.7    Fukunaga, K.8    Qin, Z.H.9
  • 194
    • 35348948380 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosisinducing ligand activates a lysosomal pathway of apoptosis that is regulated by Bcl-2 proteins
    • Werneburg NW, Guicciardi ME, Bronk SF, Kaufmann SH, Gores GJ. 2007. Tumor necrosis factor-related apoptosisinducing ligand activates a lysosomal pathway of apoptosis that is regulated by Bcl-2 proteins. J Biol Chem 282: 28960-28970.
    • (2007) J Biol Chem , vol.282 , pp. 28960-28970
    • Werneburg, N.W.1    Guicciardi, M.E.2    Bronk, S.F.3    Kaufmann, S.H.4    Gores, G.J.5
  • 195
    • 75949104449 scopus 로고    scopus 로고
    • Mitochondria get a Parkin' ticket
    • Wild P, Dikic I. 2010. Mitochondria get a Parkin' ticket. Nat Cell Biol 12: 104-106.
    • (2010) Nat Cell Biol , vol.12 , pp. 104-106
    • Wild, P.1    Dikic, I.2
  • 197
    • 84971325184 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer's disease and lysosomal storage disorders: A common pathway to neurodegeneration
    • (ed. Yue Z, Chu CT)., World Scientific, Hackensack*N.J
    • Wolfe DM, Nixon RA. 2012. Autophagy failure in Alzheimer's disease and lysosomal storage disorders: A common pathway to neurodegeneration. In Autophagy of the nervous system: Cellular self-digestion in neurons and neurological diseases (ed. Yue Z, Chu CT). World Scientific, Hackensack*N.J.
    • (2012) Autophagy of the nervous system: Cellular self-digestion in neurons and neurological diseases
    • Wolfe, D.M.1    Nixon, R.A.2
  • 198
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • World Scientific, Hackensack, NJ. Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, Price DL. 1995. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14: 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 200
    • 65849127844 scopus 로고    scopus 로고
    • Abberant a-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M, Vogiatzi T, Vekrellis K, Park D, Stefanis L. 2009. Abberant a-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 4: e5515.
    • (2009) PLoS ONE , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 202
    • 70450222302 scopus 로고    scopus 로고
    • The role of lysosomal rupture in neuronal death
    • Yamashima T, Oikawa S. 2009. The role of lysosomal rupture in neuronal death. Prog Neurobiol 89: 343-358.
    • (2009) Prog Neurobiol , vol.89 , pp. 343-358
    • Yamashima, T.1    Oikawa, S.2
  • 203
    • 0032526652 scopus 로고    scopus 로고
    • Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Ab1-42 pathogenesis
    • Yang AJ, Chandswangbhuvana D, Margol L, Glabe CG. 1998. Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Ab1-42 pathogenesis. J Neurosci Res 52: 691-698.
    • (1998) J Neurosci Res , vol.52 , pp. 691-698
    • Yang, A.J.1    Chandswangbhuvana, D.2    Margol, L.3    Glabe, C.G.4
  • 205
    • 78650716872 scopus 로고    scopus 로고
    • Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits
    • Yang DS, Stavrides P, Mohan PS, Kaushik S, Kumar A, Ohno M, Schmidt SD, Wesson D, Bandyopadhyay U, Jiang Y, et al. 2011. Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits. Brain 134: 258-277.
    • (2011) Brain , vol.134 , pp. 258-277
    • Yang, D.S.1    Stavrides, P.2    Mohan, P.S.3    Kaushik, S.4    Kumar, A.5    Ohno, M.6    Schmidt, S.D.7    Wesson, D.8    Bandyopadhyay, U.9    Jiang, Y.10
  • 206
    • 68949209958 scopus 로고    scopus 로고
    • Cell death pathways in Parkinson's disease: Role of mitochondria
    • Yao Z, Wood NW. 2009. Cell death pathways in Parkinson's disease: Role of mitochondria. Antioxid Redox Signal 11: 2135-2149.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2135-2149
    • Yao, Z.1    Wood, N.W.2
  • 207
    • 55649106830 scopus 로고    scopus 로고
    • Targeting reactive oxygen species, reactive nitrogen species and inflammation in MPTP neurotoxicity and Parkinson's disease
    • Yokoyama H, Kuroiwa H, Yano R, Araki T. 2008. Targeting reactive oxygen species, reactive nitrogen species and inflammation in MPTP neurotoxicity and Parkinson's disease. Neurol Sci 29: 293-301.
    • (2008) Neurol Sci , vol.29 , pp. 293-301
    • Yokoyama, H.1    Kuroiwa, H.2    Yano, R.3    Araki, T.4
  • 208
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii SR, Kishi C, Ishihara N, Mizushima N. 2011. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J Biol Chem 286: 19630-19640.
    • (2011) J Biol Chem , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 211
    • 33749162486 scopus 로고    scopus 로고
    • Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis
    • Yousefi S. 2006. Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis. Nat Cell Biol 8: 1124-1132.
    • (2006) Nat Cell Biol , vol.8 , pp. 1124-1132
    • Yousefi, S.1
  • 213
  • 215
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J, Yankner BA. 2000. Apoptosis in the nervous system. Nature 407: 802-809.
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 216
    • 0037194894 scopus 로고    scopus 로고
    • A novel protein complex linking the d2 glutamate receptor and autophagy: Implications for neurodegeneration in lurcher mice
    • Yue Z, Horton A, Bravin M, DeJager PL, Selimi F, Heintz N. 2002. A novel protein complex linking the d2 glutamate receptor and autophagy: Implications for neurodegeneration in lurcher mice. Neuron 35: 921-933.
    • (2002) Neuron , vol.35 , pp. 921-933
    • Yue, Z.1    Horton, A.2    Bravin, M.3    DeJager, P.L.4    Selimi, F.5    Heintz, N.6
  • 217
  • 219
    • 84855937149 scopus 로고    scopus 로고
    • Autophagosomes accumulation is associated with b-amyloid deposits and secondary damage in the thalamus after focal cortical infarction in hypertensive rats
    • Zhang J, Zhang Y, Li J, Xing S, Li C, Li Y, Dang C, Fan Y, Yu J, Pei Z, et al. 2012. Autophagosomes accumulation is associated with b-amyloid deposits and secondary damage in the thalamus after focal cortical infarction in hypertensive rats. J Neurochem 120: 564-573.
    • (2012) J Neurochem , vol.120 , pp. 564-573
    • Zhang, J.1    Zhang, Y.2    Li, J.3    Xing, S.4    Li, C.5    Li, Y.6    Dang, C.7    Fan, Y.8    Yu, J.9    Pei, Z.10
  • 220
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death
    • Zhu JH, Horbinski C, Guo F, Watkins S, Uchiyama Y, Chu CT. 2007. Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death. Am J Pathol 170: 75-86.
    • (2007) Am J Pathol , vol.170 , pp. 75-86
    • Zhu, J.H.1    Horbinski, C.2    Guo, F.3    Watkins, S.4    Uchiyama, Y.5    Chu, C.T.6


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