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Volumn 24, Issue 11, 2014, Pages 3058-3081

NH2-truncated human tau induces deregulated mitophagy in neurons by aberrant recruitment of Parkin and UCHL-1: Implications in Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; PARKIN; SHORT HAIRPIN RNA; TAU PROTEIN; UBIQUITIN CARBOXY TERMINAL ESTERASE 1; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG; MAPT PROTEIN, HUMAN; MITOCHONDRIAL PROTEIN; UBIQUITIN PROTEIN LIGASE; UCHL1 PROTEIN, HUMAN;

EID: 84930729049     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv059     Document Type: Article
Times cited : (97)

References (162)
  • 2
    • 49149098756 scopus 로고    scopus 로고
    • Truncation of tau protein and its pathological significance in Alzheimer's disease
    • García-Sierra, F., Mondragón-Rodríguez, S. and Basurto-Islas, G. (2008) Truncation of tau protein and its pathological significance in Alzheimer's disease. J. Alzheimers Dis., 14, 401-409.
    • (2008) J. Alzheimers Dis. , vol.14 , pp. 401-409
    • García-Sierra, F.1    Mondragón-Rodríguez, S.2    Basurto-Islas, G.3
  • 5
    • 80052846665 scopus 로고    scopus 로고
    • Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease
    • Reddy, P.H. (2011) Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease. Brain Res., 1415, 136-148.
    • (2011) Brain Res. , vol.1415 , pp. 136-148
    • Reddy, P.H.1
  • 6
    • 84869012777 scopus 로고    scopus 로고
    • Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease
    • Manczak, M. and Reddy, P.H. (2012) Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease. Hum. Mol. Genet., 21, 5131-5146.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 5131-5146
    • Manczak, M.1    Reddy, P.H.2
  • 7
    • 78649815388 scopus 로고    scopus 로고
    • Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
    • Du, H., Guo, L., Yan, S., Sosunov, A.A., McKhann, G.M. and Yan, S.S. (2010) Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model. Proc. Natl. Acad. Sci. USA, 107, 18670-18675.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18670-18675
    • Du, H.1    Guo, L.2    Yan, S.3    Sosunov, A.A.4    McKhann, G.M.5    Yan, S.S.6
  • 8
    • 84860176236 scopus 로고    scopus 로고
    • Synaptic mitochondrial pathology in Alzheimer's disease
    • Du, H., Guo, L. and Yan, S.S. (2012) Synaptic mitochondrial pathology in Alzheimer's disease. Antioxid. Redox. Signal., 16, 1467-1475.
    • (2012) Antioxid. Redox. Signal. , vol.16 , pp. 1467-1475
    • Du, H.1    Guo, L.2    Yan, S.S.3
  • 9
    • 84886509822 scopus 로고    scopus 로고
    • A role for tau at the synapse in Alzheimer's disease pathogenesis
    • Pooler, A.M., Noble,W. and Hanger, D.P. (2014) A role for tau at the synapse in Alzheimer's disease pathogenesis. Neuropharmacology, 76(Pt A), 1-8.
    • (2014) Neuropharmacology , vol.76 , pp. 1-8
    • Pooler, A.M.1    Noble, W.2    Hanger, D.P.3
  • 10
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai, H.C., Serrano-Pozo, A., Hashimoto, T., Frosch, M.P., Spires-Jones, T.L. and Hyman, B.T. (2012) The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am. J. Pathol., 181, 1426-1435.
    • (2012) Am. J. Pathol. , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3    Frosch, M.P.4    Spires-Jones, T.L.5    Hyman, B.T.6
  • 11
    • 38449094180 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in Alzheimer's disease
    • Upadhya, S.C. and Hegde, A.N. (2007) Role of the ubiquitin proteasome system in Alzheimer's disease. BMC Biochem., 8(Suppl 1), S12.
    • (2007) BMC Biochem. , vol.8 , pp. S12
    • Upadhya, S.C.1    Hegde, A.N.2
  • 13
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck, S., Nitsch, R., Grune, T. and Ullrich, O. (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem., 85, 115-122.
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 14
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment
    • Terry, R.D., Masliah, E., Salmon, D.P., Butters, N., DeTeresa, R., Hill, R., Hansen, L.A. and Katzman, R. (1991) Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Ann. Neurol., 30, 572-580.
    • (1991) Ann. Neurol. , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    DeTeresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 15
    • 0025269152 scopus 로고
    • Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity
    • DeKosky, S.T. and Scheff, S.W. (1990) Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity. Ann. Neurol., 27, 457-464.
    • (1990) Ann. Neurol. , vol.27 , pp. 457-464
    • DeKosky, S.T.1    Scheff, S.W.2
  • 17
    • 84856953764 scopus 로고    scopus 로고
    • Interaction between NH(2)-tau fragment and Aβ in Alzheimer's disease mitochondria contributes to the synaptic deterioration
    • 833.e1-833S25
    • Amadoro, G., Corsetti, V., Atlante, A., Florenzano, F., Capsoni, S., Bussani, R., Mercanti, D. and Calissano, P. (2012) Interaction between NH(2)-tau fragment and Aβ in Alzheimer's disease mitochondria contributes to the synaptic deterioration. Neurobiol. Aging., 33, 833.e1-833S25.
    • (2012) Neurobiol. Aging. , vol.33
    • Amadoro, G.1    Corsetti, V.2    Atlante, A.3    Florenzano, F.4    Capsoni, S.5    Bussani, R.6    Mercanti, D.7    Calissano, P.8
  • 18
    • 84861130196 scopus 로고    scopus 로고
    • Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons:implications for mitochondrial dysfunction and neuronal damage
    • Manczak, M. and Reddy, P.H. (2012) Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons:implications for mitochondrial dysfunction and neuronal damage. Hum. Mol. Genet., 21, 2538-2547.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2538-2547
    • Manczak, M.1    Reddy, P.H.2
  • 19
    • 67650556426 scopus 로고    scopus 로고
    • Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease
    • Quintanilla, R.A., Matthews-Roberson, T.A., Dolan, P.J. and Johnson, G.V. (2009) Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: implications for the pathogenesis of Alzheimer disease. J. Biol. Chem., 284, 18754-18766.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18754-18766
    • Quintanilla, R.A.1    Matthews-Roberson, T.A.2    Dolan, P.J.3    Johnson, G.V.4
  • 20
    • 84855761078 scopus 로고    scopus 로고
    • Truncated tau and Aβ cooperatively impair mitochondria in primary neurons
    • 619.e25-635.e25
    • Quintanilla, R.A., Dolan, P.J., Jin, Y.N. and Johnson, G.V. (2012) Truncated tau and Aβ cooperatively impair mitochondria in primary neurons. Neurobiol. Aging., 33, 619.e25-35.
    • (2012) Neurobiol. Aging. , vol.33
    • Quintanilla, R.A.1    Dolan, P.J.2    Jin, Y.N.3    Johnson, G.V.4
  • 21
    • 81455157378 scopus 로고    scopus 로고
    • Mitochondrial dysfunction-the beginning of the end in Alzheimer's disease? Separate and synergistic modes of tau and amyloid-β toxicity
    • Eckert, A., Schmitt, K. and Götz, J. (2011) Mitochondrial dysfunction-the beginning of the end in Alzheimer's disease? Separate and synergistic modes of tau and amyloid-β toxicity. Alzheimers Res. Ther., 3, 15. doi:10.1186/ alzrt74.
    • (2011) Alzheimers Res. Ther. , vol.3 , pp. 15
    • Eckert, A.1    Schmitt, K.2    Götz, J.3
  • 22
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang, X., Su, B., Siedlak, S.L., Moreira, P.I., Fujioka, H.,Wang, Y., Casadesus, G. and Zhu, X. (2008) Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc. Natl Acad. Sci. USA, 105, 19318-19323.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 23
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang, X., Su, B., Lee, H.G., Li, X., Perry, G., Smith, M.A. and Zhu, X. (2009) Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J. Neurosci., 29, 9090-9103.
    • (2009) J. Neurosci. , vol.29 , pp. 9090-9103
    • Wang, X.1    Su, B.2    Lee, H.G.3    Li, X.4    Perry, G.5    Smith, M.A.6    Zhu, X.7
  • 24
    • 84857030799 scopus 로고    scopus 로고
    • Neurodegeneration as a consequence of failed mitochondrial maintenance
    • Karbowski, M. and Neutzner, A. (2012) Neurodegeneration as a consequence of failed mitochondrial maintenance. Acta Neuropathol., 123, 157-171.
    • (2012) Acta Neuropathol. , vol.123 , pp. 157-171
    • Karbowski, M.1    Neutzner, A.2
  • 25
    • 84878586555 scopus 로고    scopus 로고
    • Why size matters- balancing mitochondrial dynamics in Alzheimer's disease
    • DuBoff, B., Feany, M. and Götz, J. (2013) Why size matters- balancing mitochondrial dynamics in Alzheimer's disease. Trends Neurosci., 36, 325-335.
    • (2013) Trends Neurosci. , vol.36 , pp. 325-335
    • DuBoff, B.1    Feany, M.2    Götz, J.3
  • 26
    • 84872532360 scopus 로고    scopus 로고
    • Abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease
    • Zhu, X., Perry, G., Smith, M.A. andWang, X. (2013) Abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis., 33(Suppl 1), S253-S262.
    • (2013) J. Alzheimers Dis. , vol.33 , pp. S253-S262
    • Zhu, X.1    Perry, G.2    Smith, M.A.3    Wang, X.4
  • 27
    • 64349099993 scopus 로고    scopus 로고
    • The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease
    • Wang, X., Su, B., Zheng, L., Perry, G., Smith, M.A. and Zhu, X. (2009) The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J. Neurochem., 109 (Suppl 1), 153-159.
    • (2009) J. Neurochem. , vol.109 , pp. 153-159
    • Wang, X.1    Su, B.2    Zheng, L.3    Perry, G.4    Smith, M.A.5    Zhu, X.6
  • 30
    • 84858018995 scopus 로고    scopus 로고
    • The dying of the light: mitochondrial failure in Alzheimer's disease
    • Young-Collier, K.J., McArdle, M. and Bennett, J.P. (2012) The dying of the light: mitochondrial failure in Alzheimer's disease. J. Alzheimers Dis., 28, 771-781.
    • (2012) J. Alzheimers Dis. , vol.28 , pp. 771-781
    • Young-Collier, K.J.1    McArdle, M.2    Bennett, J.P.3
  • 31
    • 33746256557 scopus 로고    scopus 로고
    • Mitochondrial alterations in Alzheimer's disease
    • Baloyannis, S.J. (2006) Mitochondrial alterations in Alzheimer's disease. J. Alzheimers Dis., 9, 119-126.
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 119-126
    • Baloyannis, S.J.1
  • 32
    • 81555195711 scopus 로고    scopus 로고
    • Mitochondria are related to synaptic pathology in Alzheimer's disease
    • Baloyannis, S.J. (2011) Mitochondria are related to synaptic pathology in Alzheimer's disease. Int. J. Alzheimers Dis., 2011, 305395.
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 305395
    • Baloyannis, S.J.1
  • 33
    • 0033903441 scopus 로고    scopus 로고
    • Mitochondrial DNA damage as a mechanism of cell loss in Alzheimer's disease
    • de la Monte, S.M., Luong, T., Neely, T.R., Robinson, D. and Wands, J.R. (2000) Mitochondrial DNA damage as a mechanism of cell loss in Alzheimer's disease. Lab. Invest., 80, 1323-1335.
    • (2000) Lab. Invest. , vol.80 , pp. 1323-1335
    • de la Monte, S.M.1    Luong, T.2    Neely, T.R.3    Robinson, D.4    Wands, J.R.5
  • 34
    • 84886925692 scopus 로고    scopus 로고
    • Mitochondrial alterations near amyloid plaques in an Alzheimer's disease mouse model
    • Xie, H., Guan, J., Borrelli, L.A., Xu, J., Serrano-Pozo, A. and Bacskai, B.J. (2013) Mitochondrial alterations near amyloid plaques in an Alzheimer's disease mouse model. J. Neurosci., 33, 17042-17051.
    • (2013) J. Neurosci. , vol.33 , pp. 17042-17051
    • Xie, H.1    Guan, J.2    Borrelli, L.A.3    Xu, J.4    Serrano-Pozo, A.5    Bacskai, B.J.6
  • 35
    • 77749326636 scopus 로고    scopus 로고
    • Mitochondrial dynamics in Alzheimer's disease:opportunities for future treatment strategies
    • Bonda, D.J., Wang, X., Perry, G., Smith, M.A. and Zhu, X. (2010) Mitochondrial dynamics in Alzheimer's disease:opportunities for future treatment strategies. Drugs Aging, 27, 181-192.
    • (2010) Drugs Aging , vol.27 , pp. 181-192
    • Bonda, D.J.1    Wang, X.2    Perry, G.3    Smith, M.A.4    Zhu, X.5
  • 36
    • 84964313038 scopus 로고    scopus 로고
    • Autophagy of mitochondria: a promising therapeutic target for neurodegenerative disease
    • Kamat, P.K., Kalani, A., Kyles, P., Tyagi, S.C. and Tyagi, N. (2014) Autophagy of mitochondria: a promising therapeutic target for neurodegenerative disease. Cell Biochem Biophys., 70, 707-719.
    • (2014) Cell Biochem Biophys. , vol.70 , pp. 707-719
    • Kamat, P.K.1    Kalani, A.2    Kyles, P.3    Tyagi, S.C.4    Tyagi, N.5
  • 37
    • 84901826020 scopus 로고    scopus 로고
    • Mitochondrial homeostasis: the interplay between mitophagy and mitochondrial biogenesis
    • Palikaras, K. and Tavernarakis, N. (2014) Mitochondrial homeostasis: the interplay between mitophagy and mitochondrial biogenesis. Exp. Gerontol., 56, 182-188.
    • (2014) Exp. Gerontol. , vol.56 , pp. 182-188
    • Palikaras, K.1    Tavernarakis, N.2
  • 38
    • 84887387419 scopus 로고    scopus 로고
    • After the banquet:mitochondrial biogenesis, mitophagy, and cell survival
    • Zhu, J., Wang, K.Z. and Chu, C.T. (2013) After the banquet:mitochondrial biogenesis, mitophagy, and cell survival. Autophagy, 9, 1663-1676.
    • (2013) Autophagy , vol.9 , pp. 1663-1676
    • Zhu, J.1    Wang, K.Z.2    Chu, C.T.3
  • 39
    • 84898622934 scopus 로고    scopus 로고
    • .Roles of autophagy in MPP+-induced neurotoxicity in vivo: the involvement of mitochondria and α-synuclein aggregation
    • Hung, K.C., Huang, H.J., Lin, M.W., Lei, Y.P. and Lin, A.M. (2014) .Roles of autophagy in MPP+-induced neurotoxicity in vivo: the involvement of mitochondria and α-synuclein aggregation. PLoS One, 9, e91074.
    • (2014) PLoS One , vol.9 , pp. e91074
    • Hung, K.C.1    Huang, H.J.2    Lin, M.W.3    Lei, Y.P.4    Lin, A.M.5
  • 40
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenyl pyridinium -induced cell death
    • Zhu, J.H., Horbinski, C., Guo, F.,Watkins, S., Uchiyama, Y. and Chu, C.T. (2000) Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenyl pyridinium -induced cell death. Am. J. Pathol., 170, 75-86.
    • (2000) 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
  • 42
    • 84858748850 scopus 로고    scopus 로고
    • Melatonin attenuates kainic acid-induced neurotoxicity in mouse hippocampus via inhibition of autophagy and α-synuclein aggregation
    • Chang, C.F., Huang, H.J., Lee, H.C., Hung, K.C., Wu, R.T. and Lin, A.M. (2012) Melatonin attenuates kainic acid-induced neurotoxicity in mouse hippocampus via inhibition of autophagy and α-synuclein aggregation. J. Pineal. Res., 52, 312-321.
    • (2012) J. Pineal. Res. , vol.52 , pp. 312-321
    • Chang, C.F.1    Huang, H.J.2    Lee, H.C.3    Hung, K.C.4    Wu, R.T.5    Lin, A.M.6
  • 43
    • 77955095337 scopus 로고    scopus 로고
    • Role of autophagy in protection afforded by hypoxic preconditioning against MPP+-induced neurotoxicity in SH-SY5Y cells
    • Tzeng, Y.W., Lee, L.Y., Chao, P.L., Lee, H.C., Wu, R.T. and Lin, A.M. (2010) Role of autophagy in protection afforded by hypoxic preconditioning against MPP+-induced neurotoxicity in SH-SY5Y cells. Free Radic. Biol. Med., 49, 839-846.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 839-846
    • Tzeng, Y.W.1    Lee, L.Y.2    Chao, P.L.3    Lee, H.C.4    Wu, R.T.5    Lin, A.M.6
  • 44
    • 84898612040 scopus 로고    scopus 로고
    • Dynamic survey of mitochondria by ubiquitin
    • Escobar-Henriques, M. and Langer, T. (2014) Dynamic survey of mitochondria by ubiquitin. EMBO Rep., 15, 231-243.
    • (2014) EMBO Rep. , vol.15 , pp. 231-243
    • Escobar-Henriques, M.1    Langer, T.2
  • 45
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D.G., Novak, I. and Dikic, I. (2009) A role for ubiquitin in selective autophagy. Mol. Cell, 34, 259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 48
    • 84883492814 scopus 로고    scopus 로고
    • Parkin- and PINK1-dependent mitophagy in neurons: will the real pathway please stand up?
    • Grenier, K., McLelland, G.L. and Fon, E.A. (2013) Parkin- and PINK1-dependent mitophagy in neurons: will the real pathway please stand up?. Front. Neurol., 4, 100.
    • (2013) Front. Neurol. , vol.4 , pp. 100
    • Grenier, K.1    McLelland, G.L.2    Fon, E.A.3
  • 49
    • 80053352130 scopus 로고    scopus 로고
    • Mitochondrial quality control by the ubiquitin-proteasome system
    • Taylor, E.B. and Rutter, J. (2011) Mitochondrial quality control by the ubiquitin-proteasome system. Biochem. Soc. Trans., 39, 1509-1513.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1509-1513
    • Taylor, E.B.1    Rutter, J.2
  • 51
    • 84880788882 scopus 로고    scopus 로고
    • The principal PINK1 and Parkin cellular events triggered in response to dissipation of mitochondrial membrane potential occur in primary neurons
    • Koyano, F., Okatsu, K., Ishigaki, S., Fujioka, Y., Kimura, M., Sobue, G., Tanaka, K. and Matsuda, N. (2013) The principal PINK1 and Parkin cellular events triggered in response to dissipation of mitochondrial membrane potential occur in primary neurons. Genes Cells., 18, 672-681.
    • (2013) Genes Cells. , vol.18 , pp. 672-681
    • Koyano, F.1    Okatsu, K.2    Ishigaki, S.3    Fujioka, Y.4    Kimura, M.5    Sobue, G.6    Tanaka, K.7    Matsuda, N.8
  • 52
    • 84858701257 scopus 로고    scopus 로고
    • Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • Cai, Q., Zakaria, H.M., Simone, A. and Sheng, Z.H. (2012) Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Curr. Biol., 22, 545-552.
    • (2012) Curr. Biol. , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 53
    • 84864873195 scopus 로고    scopus 로고
    • Long time-lapse imaging reveals unique features of PARK2/Parkin-mediated mitophagy in mature cortical neurons
    • Cai, Q., Zakaria, H.M. and Sheng, Z.H. (2012) Long time-lapse imaging reveals unique features of PARK2/Parkin-mediated mitophagy in mature cortical neurons. Autophagy, 8, 976-978.
    • (2012) Autophagy , vol.8 , pp. 976-978
    • Cai, Q.1    Zakaria, H.M.2    Sheng, Z.H.3
  • 56
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii, S.R., Kishi, C., Ishihara, N. and 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
  • 59
    • 0025847597 scopus 로고
    • Axonal transport of two major components of the ubiquitin system: free ubiquitin and ubiquitin carboxyl-terminal hydrolase PGP 9.5
    • Bizzi, A., Schaetzle, B., Patton, A., Gambetti, P. and Autilio-Gambetti, L. (1991) Axonal transport of two major components of the ubiquitin system: free ubiquitin and ubiquitin carboxyl-terminal hydrolase PGP 9.5. Brain Res., 548, 292-299.
    • (1991) Brain Res. , vol.548 , pp. 292-299
    • Bizzi, A.1    Schaetzle, B.2    Patton, A.3    Gambetti, P.4    Autilio-Gambetti, L.5
  • 60
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Liu, Y., Fallon, L., Lashuel, H.A., Liu, Z. and Lansbury, P.T. Jr. (2002) The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell, 111, 209-218.
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury, P.T.5
  • 62
    • 76549084350 scopus 로고    scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase L1 is required for maintaining the structure and function of the neuromuscular junction
    • Chen, F., Sugiura, Y., Myers, K.G., Liu, Y. and Lin, W. (2010) Ubiquitin carboxyl-terminal hydrolase L1 is required for maintaining the structure and function of the neuromuscular junction. Proc. Natl Acad. Sci. USA, 107, 1636-1641.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1636-1641
    • Chen, F.1    Sugiura, Y.2    Myers, K.G.3    Liu, Y.4    Lin, W.5
  • 64
    • 70349755717 scopus 로고    scopus 로고
    • Reversal of long-term dendritic spine alterations in Alzheimer disease models
    • Smith, D.L., Pozueta, J., Gong, B., Arancio, O. and Shelanski, M. (2009) Reversal of long-term dendritic spine alterations in Alzheimer disease models. Proc. Natl Acad. Sci. USA, 106, 16877-16882.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16877-16882
    • Smith, D.L.1    Pozueta, J.2    Gong, B.3    Arancio, O.4    Shelanski, M.5
  • 66
    • 84878766949 scopus 로고    scopus 로고
    • β-Amyloid (Aβ) oligomers impair brain-derived neurotrophic factor retrograde trafficking by down-regulating ubiquitin C-terminal hydrolase, UCH-L1
    • Poon,W.W., Carlos, A.J., Aguilar, B.L., Berchtold, N.C., Kawano, C.K., Zograbyan, V., Yaopruke, T., Shelanski, M. and Cotman, C.W. (2013) β-Amyloid (Aβ) oligomers impair brain-derived neurotrophic factor retrograde trafficking by down-regulating ubiquitin C-terminal hydrolase, UCH-L1. J. Biol. Chem., 288, 16937-16948.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16937-16948
    • Poon, W.W.1    Carlos, A.J.2    Aguilar, B.L.3    Berchtold, N.C.4    Kawano, C.K.5    Zograbyan, V.6    Yaopruke, T.7    Shelanski, M.8    Cotman, C.W.9
  • 67
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitincarboxyl-terminal hydrolase L1 associated with idiopathic Parkinson'sand Alzheimer's disease
    • Choi, J., Levey, A.I., Weintraub, S.T., Rees, H.D., Gearing, M., Chin, L.S. and Li, L. (2004) Oxidative modifications and down-regulation of ubiquitincarboxyl-terminal hydrolase L1 associated with idiopathic Parkinson'sand Alzheimer's disease. J. Biol. Chem., 279, 13256-13264.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 68
    • 0035884954 scopus 로고    scopus 로고
    • Use of cDNA microarray in the search for molecular markers involved in the onset of Alzheimer's disease dementia
    • Pasinetti, G.M. (2001) Use of cDNA microarray in the search for molecular markers involved in the onset of Alzheimer's disease dementia. J. Neurosci. Res., 65, 471-476.
    • (2001) J. Neurosci. Res. , vol.65 , pp. 471-476
    • Pasinetti, G.M.1
  • 74
    • 0036968953 scopus 로고    scopus 로고
    • Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain
    • Rohn, T.T., Rissman, R.A., Davis, M.C., Kim, Y.E., Cotman, C. W. and Head, E. (2002) Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain. Neurobiol. Dis., 11, 341-354.
    • (2002) Neurobiol. Dis. , vol.11 , pp. 341-354
    • Rohn, T.T.1    Rissman, R.A.2    Davis, M.C.3    Kim, Y.E.4    Cotman, C.W.5    Head, E.6
  • 75
    • 79957996565 scopus 로고    scopus 로고
    • Amyloid beta-mediated cell death of cultured hippocampal neurons reveals extensive Tau fragmentation without increased full-length tau phosphorylation
    • Reifert, J., Hartung-Cranston, D. and Feinstein, S.C. (2011) Amyloid beta-mediated cell death of cultured hippocampal neurons reveals extensive Tau fragmentation without increased full-length tau phosphorylation. J. Biol. Chem., 286, 20797-20811.
    • (2011) J. Biol. Chem. , vol.286 , pp. 20797-20811
    • Reifert, J.1    Hartung-Cranston, D.2    Feinstein, S.C.3
  • 76
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration
    • Park, S.Y. and Ferreira, A. (2005) The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J. Neurosci., 25, 5365-5375.
    • (2005) J. Neurosci. , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 81
    • 79960826207 scopus 로고    scopus 로고
    • The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons
    • Yu, W., Sun, Y., Guo, S. and Lu, B. (2011) The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons. Hum. Mol. Genet., 20, 3227-3240.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 3227-3240
    • Yu, W.1    Sun, Y.2    Guo, S.3    Lu, B.4
  • 82
    • 84858397292 scopus 로고    scopus 로고
    • Mitofusin2 mutations disrupt axonal mitochondrial positioning and promote axon degeneration
    • Misko, A.L., Sasaki, Y., Tuck, E., Milbrandt, J. and Baloh, R.H. (2012) Mitofusin2 mutations disrupt axonal mitochondrial positioning and promote axon degeneration. J. Neurosci., 32, 4145-4155.
    • (2012) J. Neurosci. , vol.32 , pp. 4145-4155
    • Misko, A.L.1    Sasaki, Y.2    Tuck, E.3    Milbrandt, J.4    Baloh, R.H.5
  • 84
    • 79959364986 scopus 로고    scopus 로고
    • Dynamics of the degradation of ubiquitinated proteins by proteasomes and autophagy: association with sequestosome 1/p62
    • Myeku, N. and Figueiredo-Pereira, M.E. (2011) Dynamics of the degradation of ubiquitinated proteins by proteasomes and autophagy: association with sequestosome 1/p62. J. Biol. Chem., 286, 22426-22440.
    • (2011) J. Biol. Chem. , vol.286 , pp. 22426-22440
    • Myeku, N.1    Figueiredo-Pereira, M.E.2
  • 86
    • 84861544095 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to depletion of functional mitochondria in chronic MPP(+) toxicity: dual roles for ERK1/2
    • Zhu, J.H., Gusdon, A.M., Cimen, H., Van Houten, B., Koc, E. and Chu, C.T. (2012) Impaired mitochondrial biogenesis contributes to depletion of functional mitochondria in chronic MPP(+) toxicity: dual roles for ERK1/2. Cell Death Dis., 3, e312.
    • (2012) Cell Death Dis. , vol.3 , pp. e312
    • Zhu, J.H.1    Gusdon, A.M.2    Cimen, H.3    Van Houten, B.4    Koc, E.5    Chu, C.T.6
  • 89
    • 77955437274 scopus 로고    scopus 로고
    • How could Parkinmediated ubiquitination of mitofusin promote mitophagy?
    • Ziviani, E. and Whitworth, A.J. (2010) How could Parkinmediated ubiquitination of mitofusin promote mitophagy?. Autophagy, 6, 660-662.
    • (2010) Autophagy , vol.6 , pp. 660-662
    • Ziviani, E.1    Whitworth, A.J.2
  • 91
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex
    • Misko, A., Jiang, S.,Wegorzewska, I., Milbrandt, J. and Baloh, R.H. (2010) Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J. Neurosci., 30, 4232-4240.
    • (2010) J. Neurosci. , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 93
    • 58149397537 scopus 로고    scopus 로고
    • Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: neuroprotection by CAST overexpression
    • Rao, M.V., Mohan, P.S., Peterhoff, C.M., Yang, D.S., Schmidt, S.D., Stavrides, P.H., Campbell, J., Chen, Y., Jiang, Y., Paskevich, P.A. 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
  • 94
    • 79953019314 scopus 로고    scopus 로고
    • The mitochondrial inner membrane GTPase, optic atrophy 1 (Opa1), restores mitochondrial morphology and promotes neuronal survival following excitotoxicity
    • Jahani-Asl, A., Pilon-Larose, K., Xu,W., MacLaurin, J.G., Park, D.S., McBride, H.M. and Slack, R.S. (2011) The mitochondrial inner membrane GTPase, optic atrophy 1 (Opa1), restores mitochondrial morphology and promotes neuronal survival following excitotoxicity. J. Biol. Chem., 286, 4772-4782.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4772-4782
    • Jahani-Asl, A.1    Pilon-Larose, K.2    Xu, W.3    MacLaurin, J.G.4    Park, D.S.5    McBride, H.M.6    Slack, R.S.7
  • 95
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice
    • Takano, J., Tomioka, M., Tsubuki, S., Higuchi, M., Iwata, N., Itohara, S., Maki, M. and Saido, T.C. (2005) Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J. Biol. Chem., 280, 16175-16184.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3    Higuchi, M.4    Iwata, N.5    Itohara, S.6    Maki, M.7    Saido, T.C.8
  • 96
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • Higuchi, M., Tomioka, M., Takano, J., Shirotani, K., Iwata, N., Masumoto, H., Maki, M., Itohara, S. and Saido, T.C. (2005) Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors. J. Biol. Chem., 280, 15229-15237.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3    Shirotani, K.4    Iwata, N.5    Masumoto, H.6    Maki, M.7    Itohara, S.8    Saido, T.C.9
  • 97
  • 98
    • 84890339047 scopus 로고    scopus 로고
    • Hexokinase activity is required for recruitment of parkin to depolarized mitochondria
    • McCoy, M.K., Kaganovich, A., Rudenko, I.N., Ding, J. and Cookson, M.R. (2014) Hexokinase activity is required for recruitment of parkin to depolarized mitochondria. Hum. Mol. Genet., 23, 145-156.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 145-156
    • McCoy, M.K.1    Kaganovich, A.2    Rudenko, I.N.3    Ding, J.4    Cookson, M.R.5
  • 100
    • 84872680354 scopus 로고    scopus 로고
    • The interplay of neuronal mitochondrial dynamics and bioenergetics: implications for Parkinson's disease
    • Van Laar, V.S. and Berman, S.B. (2013) The interplay of neuronal mitochondrial dynamics and bioenergetics: implications for Parkinson's disease. Neurobiol. Dis., 51, 43-55.
    • (2013) Neurobiol. Dis. , vol.51 , pp. 43-55
    • Van Laar, V.S.1    Berman, S.B.2
  • 104
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
    • Zheng, X. and Hunter, T. (2013) Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res., 23, 886-897.
    • (2013) Cell Res. , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2
  • 106
    • 34249845272 scopus 로고    scopus 로고
    • Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1
    • Meray, R.K. and Lansbury, P.T. Jr. (2007) Reversible monoubiquitination regulates the Parkinson disease-associated ubiquitin hydrolase UCH-L1. J. Biol. Chem., 282, 10567-10575.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10567-10575
    • Meray, R.K.1    Lansbury, P.T.2
  • 107
    • 84873843566 scopus 로고    scopus 로고
    • PTEN-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem (iPS) cell-derived neurons
    • Rakovic, A., Shurkewitsch, K., Seibler, P., Grünewald, A., Zanon, A., Hagenah, J., Krainc, D. and Klein, C. (2013) PTEN-induced putative kinase 1 (PINK1)-dependent ubiquitination of endogenous Parkin attenuates mitophagy: study in human primary fibroblasts and induced pluripotent stem (iPS) cell-derived neurons. J. Biol. Chem., 288, 2223-2237.
    • (2013) J. Biol. Chem. , vol.288 , pp. 2223-2237
    • Rakovic, A.1    Shurkewitsch, K.2    Seibler, P.3    Grünewald, A.4    Zanon, A.5    Hagenah, J.6    Krainc, D.7    Klein, C.8
  • 109
    • 50249146177 scopus 로고    scopus 로고
    • Insights into links between familial and sporadic Parkinson's disease: physical relationship between UCH-L1 variants and chaperone-mediated autophagy
    • Kabuta, T. and Wada, K. (2008) Insights into links between familial and sporadic Parkinson's disease: physical relationship between UCH-L1 variants and chaperone-mediated autophagy. Autophagy, 4, 827-829.
    • (2008) Autophagy , vol.4 , pp. 827-829
    • Kabuta, T.1    Wada, K.2
  • 110
    • 53049101345 scopus 로고    scopus 로고
    • Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperonemediated autophagy
    • Kabuta, T., Furuta, A., Aoki, S., Furuta, K. andWada, K. (2008) Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperonemediated autophagy. J. Biol. Chem., 283, 23731-23738.
    • (2008) J. Biol. Chem. , vol.283 , pp. 23731-23738
    • Kabuta, T.1    Furuta, A.2    Aoki, S.3    Furuta, K.4    Wada, K.5
  • 111
  • 113
    • 81255190781 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease
    • Calkins, M.J., Manczak, M., Mao, P., Shirendeb, U. and Reddy, P.H. (2011) Impaired mitochondrial biogenesis, defective axonal transport of mitochondria, abnormal mitochondrial dynamics and synaptic degeneration in a mouse model of Alzheimer's disease. Hum. Mol. Genet., 20, 4515-4529.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4515-4529
    • Calkins, M.J.1    Manczak, M.2    Mao, P.3    Shirendeb, U.4    Reddy, P.H.5
  • 116
    • 38449113394 scopus 로고    scopus 로고
    • Synaptosome proteomics
    • Bai, F. and Witzmann, F. (2007) Synaptosome proteomics. Subcell Biochem., 43, 77-98.
    • (2007) Subcell Biochem. , vol.43 , pp. 77-98
    • Bai, F.1    Witzmann, F.2
  • 117
    • 33847686377 scopus 로고    scopus 로고
    • Proteomic and functional alterations in brain mitochondria from Tg2576 mice occur before amyloid plaque deposition
    • Gillardon, F., Rist, W., Kussmaul, L., Vogel, J., Berg, M., Danzer, K., Kraut, N. and Hengerer, B. (2007) Proteomic and functional alterations in brain mitochondria from Tg2576 mice occur before amyloid plaque deposition. Proteomics, 7, 605-616.
    • (2007) Proteomics , vol.7 , pp. 605-616
    • Gillardon, F.1    Rist, W.2    Kussmaul, L.3    Vogel, J.4    Berg, M.5    Danzer, K.6    Kraut, N.7    Hengerer, B.8
  • 118
    • 84866681445 scopus 로고    scopus 로고
    • Human P301Lmutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive deficits
    • Harris, J.A., Koyama, A., Maeda, S., Ho, K., Devidze, N., Dubal, D.B., Yu, G.Q., Masliah, E. and Mucke, L. (2012) Human P301Lmutant tau expression in mouse entorhinal-hippocampal network causes tau aggregation and presynaptic pathology but no cognitive deficits. PLoS One, 7, e45881.
    • (2012) PLoS One , vol.7 , pp. e45881
    • Harris, J.A.1    Koyama, A.2    Maeda, S.3    Ho, K.4    Devidze, N.5    Dubal, D.B.6    Yu, G.Q.7    Masliah, E.8    Mucke, L.9
  • 120
    • 84879232559 scopus 로고    scopus 로고
    • Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission
    • Mohamed, N.V., Herrou, T., Plouffe, V., Piperno, N. and Leclerc, N. (2013) Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission. Eur. J .Neurosci., 37, 1939-1948.
    • (2013) Eur. J .Neurosci. , vol.37 , pp. 1939-1948
    • Mohamed, N.V.1    Herrou, T.2    Plouffe, V.3    Piperno, N.4    Leclerc, N.5
  • 121
    • 44149124887 scopus 로고    scopus 로고
    • Autophagy in neuroprotection and neurodegeneration: a question of balance
    • Cherra, S.J. III and Chu, C.T. (2008) Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurol., 3, 309-323.
    • (2008) Future Neurol. , vol.3 , pp. 309-323
    • Cherra, S.J.1    Chu, C.T.2
  • 122
    • 84872691988 scopus 로고    scopus 로고
    • Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons
    • Cherra, S.J. III, Steer, E., Gusdon, A.M., Kiselyov, K. and Chu, C.T. (2013) Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons. Am. J. Pathol., 182, 474-484.
    • (2013) Am. J. Pathol. , vol.182 , pp. 474-484
    • Cherra, S.J.1    Steer, E.2    Gusdon, A.M.3    Kiselyov, K.4    Chu, C.T.5
  • 123
    • 85027948203 scopus 로고    scopus 로고
    • Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson's disease
    • Erratum in Nat Cell Biol., 2011;13:734
    • Wong, A.S., Lee, R.H., Cheung, A.Y., Yeung, P.K., Chung, S.K., Cheung, Z.H. and Ip, N.Y. (2011) Cdk5-mediated phosphorylation of endophilin B1 is required for induced autophagy in models of Parkinson's disease. Nat Cell Biol., 13, 568-579. Erratum in Nat Cell Biol., 2011;13:734.
    • (2011) Nat Cell Biol. , vol.13 , pp. 568-579
    • Wong, A.S.1    Lee, R.H.2    Cheung, A.Y.3    Yeung, P.K.4    Chung, S.K.5    Cheung, Z.H.6    Ip, N.Y.7
  • 124
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium- induced cell death
    • Zhu, J.H., Horbinski, C., Guo, F., Watkins, S., Uchiyama, Y. and Chu, C.T. (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
  • 126
    • 60549091933 scopus 로고    scopus 로고
    • Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis
    • Pacheco, C.D., Elrick, M.J. and Lieberman, A.P. (2009) Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis. Hum. Mol. Genet., 18, 956-965.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 956-965
    • Pacheco, C.D.1    Elrick, M.J.2    Lieberman, A.P.3
  • 127
    • 78049383132 scopus 로고    scopus 로고
    • Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo
    • Chinta, S.J., Mallajosyula, J.K., Rane, A. and Andersen, J.K. (2010) Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neurosci. Lett., 486, 235-239.
    • (2010) Neurosci. Lett. , vol.486 , pp. 235-239
    • Chinta, S.J.1    Mallajosyula, J.K.2    Rane, A.3    Andersen, J.K.4
  • 130
    • 84867565502 scopus 로고    scopus 로고
    • Parkin Null Cortical Neuronal/ glial cultures are resistant to amyloid-β1-42 toxicity: a role for autophagy?
    • Solano, R.M., Casarejos, M.J., Gómez, A., Perucho, J., de Yébenes, J.G. and Mena, M.A. (2012) Parkin Null Cortical Neuronal/ glial cultures are resistant to amyloid-β1-42 toxicity: a role for autophagy?. J. Alzheimers Dis., 32, 57-76.
    • (2012) J. Alzheimers Dis. , vol.32 , pp. 57-76
    • Solano, R.M.1    Casarejos, M.J.2    Gómez, A.3    Perucho, J.4    de Yébenes, J.G.5    Mena, M.A.6
  • 131
    • 84896733279 scopus 로고    scopus 로고
    • Mitochondrial dismissal in mammals, from protein degradation to mitophagy
    • Campello, S., Strappazzon, F. and Cecconi, F. (2014) Mitochondrial dismissal in mammals, from protein degradation to mitophagy. Biochim. Biophys. Acta, 1837, 451-460.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 451-460
    • Campello, S.1    Strappazzon, F.2    Cecconi, F.3
  • 134
    • 84868196007 scopus 로고    scopus 로고
    • A double-edged sword with therapeutic potential: an updated role of autophagy in ischemic cerebral injury
    • Wei, K., Wang, P. and Miao, C.Y. (2012) A double-edged sword with therapeutic potential: an updated role of autophagy in ischemic cerebral injury. CNS Neurosci. Therap., 18, 879-886.
    • (2012) CNS Neurosci. Therap. , vol.18 , pp. 879-886
    • Wei, K.1    Wang, P.2    Miao, C.Y.3
  • 136
    • 46249113267 scopus 로고    scopus 로고
    • The S18Y polymorphic variant of UCH-L1 confers an antioxidant function to neuronal cells
    • Kyratzi, E., Pavlaki, M. and Stefanis, L. (2008) The S18Y polymorphic variant of UCH-L1 confers an antioxidant function to neuronal cells. Hum. Mol. Genet., 17, 2160-2171.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2160-2171
    • Kyratzi, E.1    Pavlaki, M.2    Stefanis, L.3
  • 138
    • 33847069643 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment
    • Butterfield, D.A., Gnjec, A., Poon, H.F., Castegna, A., Pierce, W.M., Klein, J.B. and Martins, R.N. (2006) Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment. J. Alzheimers Dis., 10, 391-397.
    • (2006) J. Alzheimers Dis. , vol.10 , pp. 391-397
    • Butterfield, D.A.1    Gnjec, A.2    Poon, H.F.3    Castegna, A.4    Pierce, W.M.5    Klein, J.B.6    Martins, R.N.7
  • 140
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna, A., Aksenov, M., Aksenova, M., Thongboonkerd, V., Klein, J.B., Pierce, W.M., Booze, R., Markesbery, W.R. and Butterfield, D.A. (2002) Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol. Med., 33, 562-571.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 143
    • 33646869931 scopus 로고    scopus 로고
    • Genetic association between Ubiquitin Carboxy-terminal Hydrolase-L1 gene S18Y polymorphism and sporadic Alzheimer's disease in a Chinese Han population
    • Xue, S. and Jia, J. (2006) Genetic association between Ubiquitin Carboxy-terminal Hydrolase-L1 gene S18Y polymorphism and sporadic Alzheimer's disease in a Chinese Han population. Brain Res., 1087, 28-32.
    • (2006) Brain Res. , vol.1087 , pp. 28-32
    • Xue, S.1    Jia, J.2
  • 144
    • 84855695865 scopus 로고    scopus 로고
    • Cross-functional E3 ligases Parkin and Cterminus Hsp70-interacting protein in neurodegenerative disorders
    • Kumar, P., Pradhan, K., Karunya, R., Ambasta, R.K. and Querfurth, H.W. (2012) Cross-functional E3 ligases Parkin and Cterminus Hsp70-interacting protein in neurodegenerative disorders. J. Neurochem., 120, 350-370.
    • (2012) J. Neurochem. , vol.120 , pp. 350-370
    • Kumar, P.1    Pradhan, K.2    Karunya, R.3    Ambasta, R.K.4    Querfurth, H.W.5
  • 147
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung, K.K., Thomas, B., Li, X., Pletnikova, O., Troncoso, J.C., Marsh, L., Dawson, V.L. and Dawson, T.M. (2004) S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science, 304, 1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, V.L.7    Dawson, T.M.8
  • 150
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang, C., Ko, H.S., Thomas, B., Tsang, F., Chew, K.C., Tay, S. P., Ho, M.W., Lim, T.M., Soong, T.W., Pletnikova, O. et al. (2005) Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum. Mol. Genet., 14, 3885-3897.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3885-3897
    • Wang, C.1    Ko, H.S.2    Thomas, B.3    Tsang, F.4    Chew, K.C.5    Tay, S.P.6    Ho, M.W.7    Lim, T.M.8    Soong, T.W.9    Pletnikova, O.10
  • 151
    • 84872480032 scopus 로고    scopus 로고
    • Diminished parkin solubility and co-localization with intraneuronal amyloid-β are associated with autophagic defects in Alzheimer's disease
    • Lonskaya, I., Shekoyan, A.R., Hebron, M.L., Desforges, N., Algarzae, N.K. and Moussa, C.E. (2013) Diminished parkin solubility and co-localization with intraneuronal amyloid-β are associated with autophagic defects in Alzheimer's disease. J. Alzheimers Dis., 33, 231-247.
    • (2013) J. Alzheimers Dis. , vol.33 , pp. 231-247
    • Lonskaya, I.1    Shekoyan, A.R.2    Hebron, M.L.3    Desforges, N.4    Algarzae, N.K.5    Moussa, C.E.6
  • 153
    • 34250344611 scopus 로고    scopus 로고
    • Phosphorylation of Parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation
    • Avraham, E., Rott, R., Liani, E., Szargel, R. and Engelender, S. (2007) Phosphorylation of Parkin by the cyclin-dependent kinase 5 at the linker region modulates its ubiquitin-ligase activity and aggregation. J. Biol. Chem., 282, 12842-12850.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12842-12850
    • Avraham, E.1    Rott, R.2    Liani, E.3    Szargel, R.4    Engelender, S.5
  • 155
    • 0022263028 scopus 로고
    • The role of estrogen on the proliferation of human breast tumor cells (MCF-7)
    • Soto, A.M. and Sonnenschein, C. (1985) The role of estrogen on the proliferation of human breast tumor cells (MCF-7). J. Steroid. Biochem., 23, 87-94.
    • (1985) J. Steroid. Biochem. , vol.23 , pp. 87-94
    • Soto, A.M.1    Sonnenschein, C.2
  • 156
    • 0027944481 scopus 로고
    • Development of a method for measuring cell number: application to CNS primary neuronal culture
    • Volontè, C., Ciotti, M.T. and Battistini, L. (1994) Development of a method for measuring cell number: application to CNS primary neuronal culture. Cytometry, 17, 274-276.
    • (1994) Cytometry , vol.17 , pp. 274-276
    • Volontè, C.1    Ciotti, M.T.2    Battistini, L.3
  • 157
    • 0022686460 scopus 로고
    • An automated colorimetric microassay for neuronotrophic factors
    • Manthorpe, M., Fagnani, R., Skaper, S.D. and Varon, S. (1986) An automated colorimetric microassay for neuronotrophic factors. Brain Res., 390, 191-198.
    • (1986) Brain Res. , vol.390 , pp. 191-198
    • Manthorpe, M.1    Fagnani, R.2    Skaper, S.D.3    Varon, S.4
  • 158
    • 50949120648 scopus 로고    scopus 로고
    • Reactive oxygen species generation is modulated by mitochondrial kinases: correlation with mitochondrial antioxidant peroxidases in rat tissues
    • Santiago, A.P., Chaves, E.A., Oliveira, M.F. and Galina, A. (2008) Reactive oxygen species generation is modulated by mitochondrial kinases: correlation with mitochondrial antioxidant peroxidases in rat tissues. Biochimie, 90, 1566-1577.
    • (2008) Biochimie , vol.90 , pp. 1566-1577
    • Santiago, A.P.1    Chaves, E.A.2    Oliveira, M.F.3    Galina, A.4
  • 159
    • 13444291931 scopus 로고    scopus 로고
    • Extracellular protons differentially potentiate the responses of native AMPA receptor subtypes regulating neurotransmitter release
    • Pittaluga, A., Segantini, D., Feligioni, M. and Raiteri, M. (2005) Extracellular protons differentially potentiate the responses of native AMPA receptor subtypes regulating neurotransmitter release. Br. J. Pharmacol., 144, 293-299.
    • (2005) Br. J. Pharmacol. , vol.144 , pp. 293-299
    • Pittaluga, A.1    Segantini, D.2    Feligioni, M.3    Raiteri, M.4
  • 160
    • 31844452224 scopus 로고    scopus 로고
    • Trafficking of presynaptic AMPAreceptors mediating neurotransmitter release: neuronal selectivity and relationships with sensitivity to cyclothiazide
    • Pittaluga, A., Feligioni, M., Longordo, F., Luccini, E. and Raiteri, M. (2006) Trafficking of presynaptic AMPAreceptors mediating neurotransmitter release: neuronal selectivity and relationships with sensitivity to cyclothiazide. Neuropharmacology, 50, 286-296.
    • (2006) Neuropharmacology , vol.50 , pp. 286-296
    • Pittaluga, A.1    Feligioni, M.2    Longordo, F.3    Luccini, E.4    Raiteri, M.5
  • 161
    • 34447536752 scopus 로고    scopus 로고
    • αCAMKII autophosphorylation levels differ depending on subcellular localization
    • Davies, K.D., Alvestad, R.M., Coultrap, S.J. and Browning, M. D. (2007) αCAMKII autophosphorylation levels differ depending on subcellular localization. Brain Res., 1158, 39-49.
    • (2007) Brain Res. , vol.1158 , pp. 39-49
    • Davies, K.D.1    Alvestad, R.M.2    Coultrap, S.J.3    Browning, M.D.4
  • 162
    • 84863484589 scopus 로고    scopus 로고
    • Calpastatin overexpression limits calpain-mediated proteolysis and behavioral deficits following traumatic brain injury
    • Schoch, K.M., Evans, H.N., Brelsfoard, J.M., Madathil, S.K., Takano, J., Saido, T.C. and Saatman, K.E. (2012) Calpastatin overexpression limits calpain-mediated proteolysis and behavioral deficits following traumatic brain injury. Exp. Neurol., 236, 371-282.
    • (2012) Exp. Neurol. , vol.236 , pp. 282-371
    • Schoch, K.M.1    Evans, H.N.2    Brelsfoard, J.M.3    Madathil, S.K.4    Takano, J.5    Saido, T.C.6    Saatman, K.E.7


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