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Volumn 697, Issue , 2019, Pages 49-58

Alzheimer's disease and the autophagic-lysosomal system

Author keywords

Alzheimer's disease; Amyloid; Autophagic lysosomal system; Protein clearance; Proteinopathy; Tau

Indexed keywords

AMYLOID BETA PROTEIN; LIPID; TAU PROTEIN;

EID: 85047197943     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2018.05.017     Document Type: Review
Times cited : (42)

References (164)
  • 3
    • 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
  • 5
    • 84937148634 scopus 로고    scopus 로고
    • Axonal autophagosomes recruit dynein for retrograde transport through fusion with late endosomes
    • Cheng, X.T., Zhou, B., Lin, M.Y., Cai, Q., Sheng, Z.H., Axonal autophagosomes recruit dynein for retrograde transport through fusion with late endosomes. J. Cell Biol. 209 (2015), 377–386.
    • (2015) J. Cell Biol. , vol.209 , pp. 377-386
    • Cheng, X.T.1    Zhou, B.2    Lin, M.Y.3    Cai, Q.4    Sheng, Z.H.5
  • 7
    • 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, R.A., Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy. J. Neurosci. 31 (2011), 7817–7830.
    • (2011) J. Neurosci. , vol.31 , pp. 7817-7830
    • Lee, S.1    Sato, Y.2    Nixon, R.A.3
  • 8
    • 84905721968 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in glia and its role in neurodegenerative diseases
    • Jansen, A.H., Reits, E.A., Hol, E.M., The ubiquitin proteasome system in glia and its role in neurodegenerative diseases. Front. Mol. Neurosci., 7, 2014, 73.
    • (2014) Front. Mol. Neurosci. , vol.7 , pp. 73
    • Jansen, A.H.1    Reits, E.A.2    Hol, E.M.3
  • 12
    • 84956686151 scopus 로고    scopus 로고
    • Glial alterations from early to late stages in a model of Alzheimer's disease: evidence of autophagy involvement in Abeta internalization
    • Pomilio, C., Pavia, P., Gorojod, R.M., Vinuesa, A., Alaimo, A., Galvan, V., Kotler, M.L., Beauquis, J., Saravia, F., Glial alterations from early to late stages in a model of Alzheimer's disease: evidence of autophagy involvement in Abeta internalization. Hippocampus 26 (2016), 194–210.
    • (2016) Hippocampus , vol.26 , pp. 194-210
    • Pomilio, C.1    Pavia, P.2    Gorojod, R.M.3    Vinuesa, A.4    Alaimo, A.5    Galvan, V.6    Kotler, M.L.7    Beauquis, J.8    Saravia, F.9
  • 13
    • 84907898151 scopus 로고    scopus 로고
    • Autophagy in microglia degrades extracellular beta-amyloid fibrils and regulates the NLRP3 inflammasome
    • Cho, M.H., Cho, K., Kang, H.J., Jeon, E.Y., Kim, H.S., Kwon, H.J., Kim, H.M., Kim, D.H., Yoon, S.Y., Autophagy in microglia degrades extracellular beta-amyloid fibrils and regulates the NLRP3 inflammasome. Autophagy 10 (2014), 1761–1775.
    • (2014) Autophagy , vol.10 , pp. 1761-1775
    • Cho, M.H.1    Cho, K.2    Kang, H.J.3    Jeon, E.Y.4    Kim, H.S.5    Kwon, H.J.6    Kim, H.M.7    Kim, D.H.8    Yoon, S.Y.9
  • 16
    • 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
  • 18
    • 80052646443 scopus 로고    scopus 로고
    • Presenilins function in ER calcium leak and Alzheimer's disease pathogenesis
    • Supnet, C., Bezprozvanny, I., Presenilins function in ER calcium leak and Alzheimer's disease pathogenesis. Cell Calcium 50 (2011), 303–309.
    • (2011) Cell Calcium , vol.50 , pp. 303-309
    • Supnet, C.1    Bezprozvanny, I.2
  • 21
    • 84994128006 scopus 로고    scopus 로고
    • Autophagy flux in CA1 neurons of Alzheimer hippocampus: increased induction overburdens failing lysosomes to propel neuritic dystrophy
    • Bordi, M., Berg, M.J., Mohan, P.S., Peterhoff, C.M., Alldred, M.J., Che, S., Ginsberg, S.D., Nixon, R.A., Autophagy flux in CA1 neurons of Alzheimer hippocampus: increased induction overburdens failing lysosomes to propel neuritic dystrophy. Autophagy 12 (2016), 2467–2483.
    • (2016) Autophagy , vol.12 , pp. 2467-2483
    • Bordi, M.1    Berg, M.J.2    Mohan, P.S.3    Peterhoff, C.M.4    Alldred, M.J.5    Che, S.6    Ginsberg, S.D.7    Nixon, R.A.8
  • 22
    • 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., Inducing autophagy by rapamycin before, but not after, the formation of plaques and tangles ameliorates cognitive deficits. PLoS One, 6, 2011, e25416.
    • (2011) PLoS One , vol.6
    • Majumder, S.1    Richardson, A.2    Strong, R.3    Oddo, S.4
  • 23
  • 24
    • 84929502727 scopus 로고    scopus 로고
    • How to control self-digestion: transcriptional, post-transcriptional, and post-translational regulation of autophagy
    • Feng, Y., Yao, Z., Klionsky, D.J., How to control self-digestion: transcriptional, post-transcriptional, and post-translational regulation of autophagy. Trends Cell Biol. 25 (2015), 354–363.
    • (2015) Trends Cell Biol. , vol.25 , pp. 354-363
    • Feng, Y.1    Yao, Z.2    Klionsky, D.J.3
  • 25
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K.L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., Goldberg, A.L., Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78 (1994), 761–771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 26
    • 84876050570 scopus 로고    scopus 로고
    • Relationship between the proteasomal system and autophagy
    • Lilienbaum, A., Relationship between the proteasomal system and autophagy. Int. J. Biochem. Mol. Biol. 4 (2013), 1–26.
    • (2013) Int. J. Biochem. Mol. Biol. , vol.4 , pp. 1-26
    • Lilienbaum, A.1
  • 27
    • 84954291382 scopus 로고    scopus 로고
    • Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling
    • Myeku, N., Clelland, C.L., Emrani, S., Kukushkin, N.V., Yu, W.H., Goldberg, A.L., Duff, K.E., Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling. Nat. Med. 22 (2016), 46–53.
    • (2016) Nat. Med. , vol.22 , pp. 46-53
    • Myeku, N.1    Clelland, C.L.2    Emrani, S.3    Kukushkin, N.V.4    Yu, W.H.5    Goldberg, A.L.6    Duff, K.E.7
  • 28
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo, A.M., Dice, J.F., Lysosomes, a meeting point of proteins, chaperones, and proteases. J. Mol. Med. (Berl.) 76 (1998), 6–12.
    • (1998) J. Mol. Med. (Berl.) , vol.76 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 29
    • 0033919992 scopus 로고    scopus 로고
    • Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using alpha-synuclein immunohistochemistry
    • Hamilton, R.L., Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using alpha-synuclein immunohistochemistry. Brain Pathol. 10 (2000), 378–384.
    • (2000) Brain Pathol. , vol.10 , pp. 378-384
    • Hamilton, R.L.1
  • 30
    • 84869493355 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation and neurodegeneration: lessons from transgenic models
    • Wirths, O., Bayer, T.A., Intraneuronal Abeta accumulation and neurodegeneration: lessons from transgenic models. Life Sci. 91 (2012), 1148–1152.
    • (2012) Life Sci. , vol.91 , pp. 1148-1152
    • Wirths, O.1    Bayer, T.A.2
  • 31
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla, F.M., Green, K.N., Oddo, S., Intracellular amyloid-beta in Alzheimer's disease. Nat. Rev. Neurosci. 8 (2007), 499–509.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 32
    • 77951227122 scopus 로고    scopus 로고
    • Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: effects on cognitive impairments
    • Caccamo, A., Majumder, S., Richardson, A., Strong, R., Oddo, S., Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: effects on cognitive impairments. J. Biol. Chem. 285 (2010), 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
  • 34
    • 82855181494 scopus 로고    scopus 로고
    • Macroautophagy-generated increase of lysosomal amyloid beta-protein mediates oxidant-induced apoptosis of cultured neuroblastoma cells
    • Zheng, L., Terman, A., Hallbeck, M., Dehvari, N., Cowburn, R.F., Benedikz, E., Kagedal, K., Cedazo-Minguez, A., Marcusson, J., Macroautophagy-generated increase of lysosomal amyloid beta-protein mediates oxidant-induced apoptosis of cultured neuroblastoma cells. Autophagy 7 (2011), 1528–1545.
    • (2011) Autophagy , vol.7 , pp. 1528-1545
    • Zheng, L.1    Terman, A.2    Hallbeck, M.3    Dehvari, N.4    Cowburn, R.F.5    Benedikz, E.6    Kagedal, K.7    Cedazo-Minguez, A.8    Marcusson, J.9
  • 37
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex–at the crossroads of autophagy and beyond
    • Funderburk, S.F., Wang, Q.J., Yue, Z., The Beclin 1-VPS34 complex–at the crossroads of autophagy and beyond. Trends Cell Biol. 20 (2010), 355–362.
    • (2010) Trends Cell Biol. , vol.20 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 38
    • 85021679704 scopus 로고    scopus 로고
    • Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease
    • Nixon, R.A., Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease. FASEB J. 31 (2017), 2729–2743.
    • (2017) FASEB J. , vol.31 , pp. 2729-2743
    • Nixon, R.A.1
  • 39
    • 84905110102 scopus 로고    scopus 로고
    • Transport and diffusion of Tau protein in neurons
    • Scholz, T., Mandelkow, E., Transport and diffusion of Tau protein in neurons. Cell. Mol. Life Sci. 71 (2014), 3139–3150.
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 3139-3150
    • Scholz, T.1    Mandelkow, E.2
  • 43
    • 65249116483 scopus 로고    scopus 로고
    • Tau mutations in neurodegenerative diseases
    • Wolfe, M.S., Tau mutations in neurodegenerative diseases. J. Biol. Chem. 284 (2009), 6021–6025.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6021-6025
    • Wolfe, M.S.1
  • 44
    • 79960325654 scopus 로고    scopus 로고
    • The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics
    • Pritchard, S.M., Dolan, P.J., Vitkus, A., Johnson, G.V., The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics. J. Cell. Mol. Med. 15 (2011), 1621–1635.
    • (2011) J. Cell. Mol. Med. , vol.15 , pp. 1621-1635
    • Pritchard, S.M.1    Dolan, P.J.2    Vitkus, A.3    Johnson, G.V.4
  • 46
    • 84878114130 scopus 로고    scopus 로고
    • Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system
    • Lee, M.J., Lee, J.H., Rubinsztein, D.C., Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog. Neurobiol. 105 (2013), 49–59.
    • (2013) Prog. Neurobiol. , vol.105 , pp. 49-59
    • Lee, M.J.1    Lee, J.H.2    Rubinsztein, D.C.3
  • 47
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A.M., Dice, J.F., A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273 (1996), 501–503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 49
    • 67349216078 scopus 로고    scopus 로고
    • Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover
    • Waters, S., Marchbank, K., Solomon, E., Whitehouse, C., Gautel, M., Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover. FEBS Lett. 583 (2009), 1846–1852.
    • (2009) FEBS Lett. , vol.583 , pp. 1846-1852
    • Waters, S.1    Marchbank, K.2    Solomon, E.3    Whitehouse, C.4    Gautel, M.5
  • 50
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen, T., Lamark, T., Selective autophagy mediated by autophagic adapter proteins. Autophagy 7 (2011), 279–296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 51
    • 67650517556 scopus 로고    scopus 로고
    • NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets
    • Lamark, T., Kirkin, V., Dikic, I., Johansen, T., NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets. ABBV Cell Cycle 8 (2009), 1986–1990.
    • (2009) ABBV Cell Cycle , vol.8 , pp. 1986-1990
    • Lamark, T.1    Kirkin, V.2    Dikic, I.3    Johansen, T.4
  • 52
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of NBR1 a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • D'Agostino, C., Nogalska, A., Cacciottolo, M., Engel, W.K., Askanas, V., Abnormalities of NBR1 a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol. 122 (2011), 627–636.
    • (2011) Acta Neuropathol. , vol.122 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3    Engel, W.K.4    Askanas, V.5
  • 53
    • 84877803859 scopus 로고    scopus 로고
    • mTOR regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies
    • Caccamo, A., Magri, A., Medina, D.X., Wisely, E.V., Lopez-Aranda, M.F., Silva, A.J., Oddo, S., mTOR regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies. Aging Cell 12 (2013), 370–380.
    • (2013) Aging Cell , vol.12 , pp. 370-380
    • Caccamo, A.1    Magri, A.2    Medina, D.X.3    Wisely, E.V.4    Lopez-Aranda, M.F.5    Silva, A.J.6    Oddo, S.7
  • 59
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells
    • Rideout, H.J., Larsen, K.E., Sulzer, D., Stefanis, L., Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J. Neurochem. 78 (2001), 899–908.
    • (2001) J. Neurochem. , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.E.2    Sulzer, D.3    Stefanis, L.4
  • 60
    • 0034640160 scopus 로고    scopus 로고
    • Alpha-synuclein and the Parkinson's disease-related mutant Ala53Thr-alpha-synuclein do not undergo proteasomal degradation in HEK293 and neuronal cells
    • Ancolio, K., Alves da Costa, C., Ueda, K., Checler, F., Alpha-synuclein and the Parkinson's disease-related mutant Ala53Thr-alpha-synuclein do not undergo proteasomal degradation in HEK293 and neuronal cells. Neurosci. Lett. 285 (2000), 79–82.
    • (2000) Neurosci. Lett. , vol.285 , pp. 79-82
    • Ancolio, K.1    Alves da Costa, C.2    Ueda, K.3    Checler, F.4
  • 61
    • 0035976835 scopus 로고    scopus 로고
    • alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris, G.K., Layfield, R., Spillantini, M.G., alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509 (2001), 22–26.
    • (2001) FEBS Lett. , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 63
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • Lee, H.J., Khoshaghideh, F., Patel, S., Lee, S.J., Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. J. Neurosci. 24 (2004), 1888–1896.
    • (2004) J. Neurosci. , vol.24 , pp. 1888-1896
    • Lee, H.J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.J.4
  • 64
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo, A.M., Stefanis, L., Fredenburg, R., Lansbury, P.T., Sulzer, D., Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305 (2004), 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
  • 73
    • 77953235753 scopus 로고    scopus 로고
    • Lipids in Alzheimer's disease: a century-old story
    • Foley, P., Lipids in Alzheimer's disease: a century-old story. Biochim. Biophys. Acta 1801 (2010), 750–753.
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 750-753
    • Foley, P.1
  • 74
    • 79955051063 scopus 로고    scopus 로고
    • Linking lipids to Alzheimer's disease: cholesterol and beyond
    • Di Paolo, G., Kim, T.W., Linking lipids to Alzheimer's disease: cholesterol and beyond. Nat. Rev. Neurosci. 12 (2011), 284–296.
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 284-296
    • Di Paolo, G.1    Kim, T.W.2
  • 75
    • 84886874221 scopus 로고    scopus 로고
    • Cross-talk of membrane lipids and Alzheimer-related proteins
    • Walter, J., van Echten-Deckert, G., Cross-talk of membrane lipids and Alzheimer-related proteins. Mol. Neurodegener., 8, 2013, 34.
    • (2013) Mol. Neurodegener. , vol.8 , pp. 34
    • Walter, J.1    van Echten-Deckert, G.2
  • 76
    • 84873436219 scopus 로고
    • Autophagy Emerging roles in lipid homeostasis and metabolic control
    • Christian, P., Sacco, J., Adeli, K., Autophagy Emerging roles in lipid homeostasis and metabolic control. Biochim. Biophys. Acta 2013 (1831), 819–824.
    • (1831) Biochim. Biophys. Acta , vol.2013 , pp. 819-824
    • Christian, P.1    Sacco, J.2    Adeli, K.3
  • 77
    • 52449089987 scopus 로고    scopus 로고
    • Thirty years of Alzheimer's disease genetics: the implications of systematic meta-analyses
    • Bertram, L., Tanzi, R.E., Thirty years of Alzheimer's disease genetics: the implications of systematic meta-analyses. Nat. Rev. Neurosci. 9 (2008), 768–778.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 768-778
    • Bertram, L.1    Tanzi, R.E.2
  • 80
    • 74149083982 scopus 로고    scopus 로고
    • Deregulation of sphingolipid metabolism in Alzheimer's disease
    • He, X., Huang, Y., Li, B., Gong, C.X., Schuchman, E.H., Deregulation of sphingolipid metabolism in Alzheimer's disease. Neurobiol. Aging 31 (2010), 398–408.
    • (2010) Neurobiol. Aging , vol.31 , pp. 398-408
    • He, X.1    Huang, Y.2    Li, B.3    Gong, C.X.4    Schuchman, E.H.5
  • 83
    • 33748746505 scopus 로고    scopus 로고
    • Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids
    • Gellermann, G.P., Appel, T.R., Davies, P., Diekmann, S., Paired helical filaments contain small amounts of cholesterol, phosphatidylcholine and sphingolipids. Biol. Chem. 387 (2006), 1267–1274.
    • (2006) Biol. Chem. , vol.387 , pp. 1267-1274
    • Gellermann, G.P.1    Appel, T.R.2    Davies, P.3    Diekmann, S.4
  • 84
    • 0023187131 scopus 로고
    • Alzheimer's disease: paired helical filaments and cytomembranes
    • Gray, E.G., Paula-Barbosa, M., Roher, A., Alzheimer's disease: paired helical filaments and cytomembranes. Neuropathol. Appl. Neurobiol. 13 (1987), 91–110.
    • (1987) Neuropathol. Appl. Neurobiol. , vol.13 , pp. 91-110
    • Gray, E.G.1    Paula-Barbosa, M.2    Roher, A.3
  • 85
    • 77953004116 scopus 로고    scopus 로고
    • The role of the lipid bilayer in tau aggregation
    • Elbaum-Garfinkle, S., Ramlall, T., Rhoades, E., The role of the lipid bilayer in tau aggregation. Biophys. J. 98 (2010), 2722–2730.
    • (2010) Biophys. J. , vol.98 , pp. 2722-2730
    • Elbaum-Garfinkle, S.1    Ramlall, T.2    Rhoades, E.3
  • 86
    • 84909606592 scopus 로고    scopus 로고
    • Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats
    • Georgieva, E.R., Xiao, S., Borbat, P.P., Freed, J.H., Eliezer, D., Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats. Biophys. J. 107 (2014), 1441–1452.
    • (2014) Biophys. J. , vol.107 , pp. 1441-1452
    • Georgieva, E.R.1    Xiao, S.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 95
    • 0142124232 scopus 로고    scopus 로고
    • Heterogeneity of endocytic proteins: distribution of clathrin adaptor proteins in neurons and glia
    • Yao, P.J., Zhang, P., Mattson, M.P., Furukawa, K., Heterogeneity of endocytic proteins: distribution of clathrin adaptor proteins in neurons and glia. Neuroscience 121 (2003), 25–37.
    • (2003) Neuroscience , vol.121 , pp. 25-37
    • Yao, P.J.1    Zhang, P.2    Mattson, M.P.3    Furukawa, K.4
  • 96
    • 55249094404 scopus 로고    scopus 로고
    • Clathrin assembly protein AP180 and CALM differentially control axogenesis and dendrite outgrowth in embryonic hippocampal neurons
    • Bushlin, I., Petralia, R.S., Wu, F., Harel, A., Mughal, M.R., Mattson, M.P., Yao, P.J., Clathrin assembly protein AP180 and CALM differentially control axogenesis and dendrite outgrowth in embryonic hippocampal neurons. J. Neurosci. 28 (2008), 10257–10271.
    • (2008) J. Neurosci. , vol.28 , pp. 10257-10271
    • Bushlin, I.1    Petralia, R.S.2    Wu, F.3    Harel, A.4    Mughal, M.R.5    Mattson, M.P.6    Yao, P.J.7
  • 98
    • 84862270067 scopus 로고    scopus 로고
    • Role of phosphatidylinositol clathrin assembly lymphoid-myeloid leukemia (PICALM) in intracellular amyloid precursor protein (APP) processing and amyloid plaque pathogenesis
    • Xiao, Q., Gil, S.C., Yan, P., Wang, Y., Han, S., Gonzales, E., Perez, R., Cirrito, J.R., Lee, J.M., Role of phosphatidylinositol clathrin assembly lymphoid-myeloid leukemia (PICALM) in intracellular amyloid precursor protein (APP) processing and amyloid plaque pathogenesis. J. Biol. Chem. 287 (2012), 21279–21289.
    • (2012) J. Biol. Chem. , vol.287 , pp. 21279-21289
    • Xiao, Q.1    Gil, S.C.2    Yan, P.3    Wang, Y.4    Han, S.5    Gonzales, E.6    Perez, R.7    Cirrito, J.R.8    Lee, J.M.9
  • 99
    • 84983433846 scopus 로고    scopus 로고
    • Partial loss of CALM function reduces Abeta42 production and amyloid deposition in vivo
    • Kanatsu, K., Hori, Y., Takatori, S., Watanabe, T., Iwatsubo, T., Tomita, T., Partial loss of CALM function reduces Abeta42 production and amyloid deposition in vivo. Hum. Mol. Genet. 25 (2016), 3988–3997.
    • (2016) Hum. Mol. Genet. , vol.25 , pp. 3988-3997
    • Kanatsu, K.1    Hori, Y.2    Takatori, S.3    Watanabe, T.4    Iwatsubo, T.5    Tomita, T.6
  • 100
    • 84896898403 scopus 로고    scopus 로고
    • Decreased CALM expression reduces Abeta42 to total Abeta ratio through clathrin-mediated endocytosis of gamma-secretase
    • Kanatsu, K., Morohashi, Y., Suzuki, M., Kuroda, H., Watanabe, T., Tomita, T., Iwatsubo, T., Decreased CALM expression reduces Abeta42 to total Abeta ratio through clathrin-mediated endocytosis of gamma-secretase. Nat. Commun., 5, 2014, 3386.
    • (2014) Nat. Commun. , vol.5 , pp. 3386
    • Kanatsu, K.1    Morohashi, Y.2    Suzuki, M.3    Kuroda, H.4    Watanabe, T.5    Tomita, T.6    Iwatsubo, T.7
  • 106
    • 84885708163 scopus 로고    scopus 로고
    • TREM2 and neurodegenerative disease
    • Jonsson, T., Stefansson, K., TREM2 and neurodegenerative disease. N. Engl. J. Med. 369 (2013), 1568–1569.
    • (2013) N. Engl. J. Med. , vol.369 , pp. 1568-1569
    • Jonsson, T.1    Stefansson, K.2
  • 111
    • 84996956254 scopus 로고    scopus 로고
    • Vps35-dependent recycling of Trem2 regulates microglial function
    • Yin, J., Liu, X., He, Q., Zhou, L., Yuan, Z., Zhao, S., Vps35-dependent recycling of Trem2 regulates microglial function. Traffic 17 (2016), 1286–1296.
    • (2016) Traffic , vol.17 , pp. 1286-1296
    • Yin, J.1    Liu, X.2    He, Q.3    Zhou, L.4    Yuan, Z.5    Zhao, S.6
  • 112
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino, J.S., Rojas, R., Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7 (2006), 568–579.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 114
    • 84954377019 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutant VPS35 causes mitochondrial dysfunction by recycling DLP1 complexes
    • Wang, W., Wang, X., Fujioka, H., Hoppel, C., Whone, A.L., Caldwell, M.A., Cullen, P.J., Liu, J., Zhu, X., Parkinson's disease-associated mutant VPS35 causes mitochondrial dysfunction by recycling DLP1 complexes. Nat. Med. 22 (2016), 54–63.
    • (2016) Nat. Med. , vol.22 , pp. 54-63
    • Wang, W.1    Wang, X.2    Fujioka, H.3    Hoppel, C.4    Whone, A.L.5    Caldwell, M.A.6    Cullen, P.J.7    Liu, J.8    Zhu, X.9
  • 119
    • 58149373433 scopus 로고    scopus 로고
    • Loss of LR11/SORLA enhances early pathology in a mouse model of amyloidosis: evidence for a proximal role in Alzheimer's disease
    • Dodson, S.E., Andersen, O.M., Karmali, V., Fritz, J.J., Cheng, D., Peng, J., Levey, A.I., Willnow, T.E., Lah, J.J., Loss of LR11/SORLA enhances early pathology in a mouse model of amyloidosis: evidence for a proximal role in Alzheimer's disease. J. Neurosci. 28 (2008), 12877–12886.
    • (2008) J. Neurosci. , vol.28 , pp. 12877-12886
    • Dodson, S.E.1    Andersen, O.M.2    Karmali, V.3    Fritz, J.J.4    Cheng, D.5    Peng, J.6    Levey, A.I.7    Willnow, T.E.8    Lah, J.J.9
  • 121
    • 3042806534 scopus 로고    scopus 로고
    • A. mitochondrial cascade hypothesis for sporadic Alzheimer's disease
    • Swerdlow, R.H., Khan, S.M., A. mitochondrial cascade hypothesis for sporadic Alzheimer's disease. Med. Hypotheses 63 (2004), 8–20.
    • (2004) Med. Hypotheses , vol.63 , pp. 8-20
    • Swerdlow, R.H.1    Khan, S.M.2
  • 122
    • 78751566697 scopus 로고    scopus 로고
    • Disrupted energy metabolism and neuronal circuit dysfunction in cognitive impairment and Alzheimer's disease
    • Kapogiannis, D., Mattson, M.P., Disrupted energy metabolism and neuronal circuit dysfunction in cognitive impairment and Alzheimer's disease. Lancet Neurol. 10 (2011), 187–198.
    • (2011) Lancet Neurol. , vol.10 , pp. 187-198
    • Kapogiannis, D.1    Mattson, M.P.2
  • 123
    • 70149093436 scopus 로고    scopus 로고
    • Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease
    • Yao, J., Irwin, R.W., Zhao, L., Nilsen, J., Hamilton, R.T., Brinton, R.D., Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 14670–14675.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14670-14675
    • Yao, J.1    Irwin, R.W.2    Zhao, L.3    Nilsen, J.4    Hamilton, R.T.5    Brinton, R.D.6
  • 124
    • 84862325005 scopus 로고    scopus 로고
    • Mitochondria-targeted catalase reduces abnormal APP processing, amyloid beta production and BACE1 in a mouse model of Alzheimer's disease: implications for neuroprotection and lifespan extension
    • Mao, P., Manczak, M., Calkins, M.J., Truong, Q., Reddy, T.P., Reddy, A.P., Shirendeb, U., Lo, H.H., Rabinovitch, P.S., Reddy, P.H., Mitochondria-targeted catalase reduces abnormal APP processing, amyloid beta production and BACE1 in a mouse model of Alzheimer's disease: implications for neuroprotection and lifespan extension. Hum. Mol. Genet. 21 (2012), 2973–2990.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2973-2990
    • Mao, P.1    Manczak, M.2    Calkins, M.J.3    Truong, Q.4    Reddy, T.P.5    Reddy, A.P.6    Shirendeb, U.7    Lo, H.H.8    Rabinovitch, P.S.9    Reddy, P.H.10
  • 126
    • 84927917189 scopus 로고    scopus 로고
    • Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer's disease patient brains
    • Ye, X., Sun, X., Starovoytov, V., Cai, Q., Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer's disease patient brains. Hum. Mol. Genet. 24 (2015), 2938–2951.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 2938-2951
    • Ye, X.1    Sun, X.2    Starovoytov, V.3    Cai, Q.4
  • 128
    • 84905706814 scopus 로고    scopus 로고
    • Knock-in of human BACE1 cleaves murine APP and reiterates Alzheimer-like phenotypes
    • Plucinska, K., Crouch, B., Koss, D., Robinson, L., Siebrecht, M., Riedel, G., Platt, B., Knock-in of human BACE1 cleaves murine APP and reiterates Alzheimer-like phenotypes. J. Neurosci. 34 (2014), 10710–10728.
    • (2014) J. Neurosci. , vol.34 , pp. 10710-10728
    • Plucinska, K.1    Crouch, B.2    Koss, D.3    Robinson, L.4    Siebrecht, M.5    Riedel, G.6    Platt, B.7
  • 129
    • 2942611429 scopus 로고    scopus 로고
    • Transgenic mice overexpressing amyloid beta protein are an incomplete model of Alzheimer disease
    • Schwab, C., Hosokawa, M., McGeer, P.L., Transgenic mice overexpressing amyloid beta protein are an incomplete model of Alzheimer disease. Exp. Neurol. 188 (2004), 52–64.
    • (2004) Exp. Neurol. , vol.188 , pp. 52-64
    • Schwab, C.1    Hosokawa, M.2    McGeer, P.L.3
  • 130
    • 84943361972 scopus 로고    scopus 로고
    • Being human: the role of pluripotent stem cells in regenerative medicine and humanizing Alzheimer's disease models
    • Sproul, A.A., Being human: the role of pluripotent stem cells in regenerative medicine and humanizing Alzheimer's disease models. Mol. Aspects Med. 43-44 (2015), 54–65.
    • (2015) Mol. Aspects Med. , vol.43-44 , pp. 54-65
    • Sproul, A.A.1
  • 136
    • 85020697469 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis patient iPSC-derived astrocytes impair autophagy via non-cell autonomous mechanisms
    • Madill, M., McDonagh, K., Ma, J., Vajda, A., McLoughlin, P., O'Brien, T., Hardiman, O., Shen, S., Amyotrophic lateral sclerosis patient iPSC-derived astrocytes impair autophagy via non-cell autonomous mechanisms. Mol. Brain, 10, 2017, 22.
    • (2017) Mol. Brain , vol.10 , pp. 22
    • Madill, M.1    McDonagh, K.2    Ma, J.3    Vajda, A.4    McLoughlin, P.5    O'Brien, T.6    Hardiman, O.7    Shen, S.8
  • 139
    • 84941795152 scopus 로고    scopus 로고
    • Mitochondrial quality control via the PGC1alpha-TFEB signaling pathway is compromised by parkin Q311X mutation but independently restored by rapamycin
    • Siddiqui, A., Bhaumik, D., Chinta, S.J., Rane, A., Rajagopalan, S., Lieu, C.A., Lithgow, G.J., Andersen, J.K., Mitochondrial quality control via the PGC1alpha-TFEB signaling pathway is compromised by parkin Q311X mutation but independently restored by rapamycin. J. Neurosci. 35 (2015), 12833–12844.
    • (2015) J. Neurosci. , vol.35 , pp. 12833-12844
    • Siddiqui, A.1    Bhaumik, D.2    Chinta, S.J.3    Rane, A.4    Rajagopalan, S.5    Lieu, C.A.6    Lithgow, G.J.7    Andersen, J.K.8
  • 142
    • 84887004639 scopus 로고    scopus 로고
    • Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation
    • Su, Y.C., Qi, X., Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation. Hum. Mol. Genet. 22 (2013), 4545–4561.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 4545-4561
    • Su, Y.C.1    Qi, X.2
  • 147
    • 84902161379 scopus 로고    scopus 로고
    • Genetic and chemical correction of cholesterol accumulation and impaired autophagy in hepatic and neural cells derived from Niemann-Pick type C patient-specific iPS cells
    • Maetzel, D., Sarkar, S., Wang, H., Abi-Mosleh, L., Xu, P., Cheng, A.W., Gao, Q., Mitalipova, M., Jaenisch, R., Genetic and chemical correction of cholesterol accumulation and impaired autophagy in hepatic and neural cells derived from Niemann-Pick type C patient-specific iPS cells. Stem cell reports 2 (2014), 866–880.
    • (2014) Stem cell reports , vol.2 , pp. 866-880
    • Maetzel, D.1    Sarkar, S.2    Wang, H.3    Abi-Mosleh, L.4    Xu, P.5    Cheng, A.W.6    Gao, Q.7    Mitalipova, M.8    Jaenisch, R.9
  • 157
    • 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
  • 158
    • 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
  • 160
    • 85018803247 scopus 로고    scopus 로고
    • The cytoskeleton-autophagy connection
    • Kast, D.J., Dominguez, R., The cytoskeleton-autophagy connection. Curr. Biol. 27 (2017), R318–R326.
    • (2017) Curr. Biol. , vol.27 , pp. R318-R326
    • Kast, D.J.1    Dominguez, R.2
  • 161
    • 33646881921 scopus 로고    scopus 로고
    • Beta-Amyloid and endoplasmic reticulum stress responses in primary neurons: effects of drugs that interact with the cytoskeleton
    • Seyb, K.I., Ansar, S., Bean, J., Michaelis, M.L., Beta-Amyloid and endoplasmic reticulum stress responses in primary neurons: effects of drugs that interact with the cytoskeleton. J. Mol. Neurosci. 28 (2006), 111–123.
    • (2006) J. Mol. Neurosci. , vol.28 , pp. 111-123
    • Seyb, K.I.1    Ansar, S.2    Bean, J.3    Michaelis, M.L.4
  • 162
    • 77958065504 scopus 로고    scopus 로고
    • 3rd, V.M., Lee, J.Q., Trojanowski, Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy
    • Brunden, K.R., Zhang, B., Carroll, J., Yao, Y., Potuzak, J.S., Hogan, A.M., Iba, M., James, M.J., Xie, S.X., Ballatore, C., Smith, A.B., 3rd, V.M., Lee, J.Q., Trojanowski, Epothilone D improves microtubule density, axonal integrity, and cognition in a transgenic mouse model of tauopathy. J. Neurosci. 30 (2010), 13861–13866.
    • (2010) J. Neurosci. , vol.30 , pp. 13861-13866
    • Brunden, K.R.1    Zhang, B.2    Carroll, J.3    Yao, Y.4    Potuzak, J.S.5    Hogan, A.M.6    Iba, M.7    James, M.J.8    Xie, S.X.9    Ballatore, C.10    Smith, A.B.11
  • 163
    • 84962628366 scopus 로고    scopus 로고
    • Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases
    • Bourdenx, M., Daniel, J., Genin, E., Soria, F.N., Blanchard-Desce, M., Bezard, E., Dehay, B., Nanoparticles restore lysosomal acidification defects: Implications for Parkinson and other lysosomal-related diseases. Autophagy 12 (2016), 472–483.
    • (2016) Autophagy , vol.12 , pp. 472-483
    • Bourdenx, M.1    Daniel, J.2    Genin, E.3    Soria, F.N.4    Blanchard-Desce, M.5    Bezard, E.6    Dehay, B.7
  • 164
    • 84928377926 scopus 로고    scopus 로고
    • Increasing the efficiency of Parkinson's disease treatment using a poly(lactic-co-glycolic acid) (PLGA) based L-DOPA delivery system
    • Gambaryan, P.Y., Kondrasheva, I.G., Severin, E.S., Guseva, A.A., Kamensky, A.A., Increasing the efficiency of Parkinson's disease treatment using a poly(lactic-co-glycolic acid) (PLGA) based L-DOPA delivery system. Exp. Neurobiol. 23 (2014), 246–252.
    • (2014) Exp. Neurobiol. , vol.23 , pp. 246-252
    • Gambaryan, P.Y.1    Kondrasheva, I.G.2    Severin, E.S.3    Guseva, A.A.4    Kamensky, A.A.5


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