메뉴 건너뛰기




Volumn , Issue JUN, 2010, Pages

The relationship between parkin and protein aggregation in neurodegenerative diseases

Author keywords

synuclein; A ; Dementia; Parkin; Synucleinopathies; Tau; Tauopathies; Tdp 43

Indexed keywords


EID: 84855644890     PISSN: None     EISSN: 16640640     Source Type: Journal    
DOI: 10.3389/fpsyt.2010.00015     Document Type: Review
Times cited : (18)

References (185)
  • 2
    • 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., and Checler, F. (2000). 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, 79-82.
    • (2000) Neurosci. Lett. , vol.285 , pp. 79-82
    • Ancolio, K.1    Alves da Costa, C.2    Ueda, K.3    Checler, F.4
  • 4
    • 0035377241 scopus 로고    scopus 로고
    • Features of the parkin/ariadnelike ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme Ubch7
    • Ardley, H. C., Tan, N. G., Rose, S. A., Markham, A. F., and Robinson, P. A. (2001). Features of the parkin/ariadnelike ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. J. Biol. Chem. 276, 19640-19647.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19640-19647
    • Ardley, H.C.1    Tan, N.G.2    Rose, S.A.3    Markham, A.F.4    Robinson, P.A.5
  • 9
    • 34547727312 scopus 로고    scopus 로고
    • Development of alphasynuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease
    • Braak, H., Sastre, M., and Del Tredici, K. (2007). Development of alphasynuclein immunoreactive astrocytes in the forebrain parallels stages of intraneuronal pathology in sporadic Parkinson's disease. Acta Neuropathol. 114, 231-241.
    • (2007) Acta Neuropathol , vol.114 , pp. 231-241
    • Braak, H.1    Sastre, M.2    Del Tredici, K.3
  • 11
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti, E., and Baralle, F. E. (2008). Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front. Biosci. 13, 867-878.
    • (2008) Front. Biosci. , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 12
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti, E., Brindisi, A., Giombi, M., Tisminetzky, S., Ayala, Y. M., and Baralle, F. E. (2005). TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J. Biol. Chem. 280, 37572-37584.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5    Baralle, F.E.6
  • 14
    • 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 beta-amyloidogenesis
    • Cataldo, A. M., Barnett, J. L., Pieroni, C., and Nixon, R. A. (1997). Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. 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
  • 15
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations
    • Cataldo, A. M., Peterhoff, C. M., Troncoso, J. C., Gomez-Isla, T., Hyman, B. T., and Nixon, R. A. (2000). Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am. J. Pathol. 157, 277-286.
    • (2000) Am. J. 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
  • 17
    • 73449111577 scopus 로고    scopus 로고
    • Mitochondrial autophagy as a compensatory response to PINK1 deficiency
    • Cherra, S. J. III, Dagda, R. K., Tandon, A., and Chu, C. T. (2009). Mitochondrial autophagy as a compensatory response to PINK1 deficiency. Autophagy 5, 1213-1214.
    • (2009) Autophagy , vol.5 , pp. 1213-1214
    • Cherra III, S.J.1    Dagda, R.K.2    Tandon, A.3    Chu, C.T.4
  • 18
    • 76449094465 scopus 로고    scopus 로고
    • Parkin-mediated ubiquitin signalling in aggresome formation and autophagy
    • Chin, L. S., Olzmann, J. A., and Li, L. (2010). Parkin-mediated ubiquitin signalling in aggresome formation and autophagy. Biochem. Soc. Trans. 38, 144-149.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 144-149
    • Chin, L.S.1    Olzmann, J.A.2    Li, L.3
  • 19
    • 0029879877 scopus 로고    scopus 로고
    • Glial inclusions in CNS degenerative diseases
    • Chin, S. S., and Goldman, J. E. (1996). Glial inclusions in CNS degenerative diseases. J. Neuropathol. Exp. Neurol. 55, 499-508.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 499-508
    • Chin, S.S.1    Goldman, J.E.2
  • 20
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewybody formation in Parkinson disease
    • Chung, K. K., Zhang, Y., Lim, K. L., Tanaka, Y., Huang, H., Gao, J., Ross, C. A., Dawson, V. L., and Dawson, T. M. (2001). Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewybody formation in Parkinson disease. Nat. Med. 7, 1144-1150.
    • (2001) Nat. Med. , vol.7 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 21
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook, D. G., Forman, M. S., Sung, J. C., Leight, S., Kolson, D. L., Iwatsubo, T., Lee, V. M., and Doms, R. W. (1997). Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat. Med. 3, 1021-1023.
    • (1997) Nat. Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6    Lee, V.M.7    Doms, R.W.8
  • 22
    • 76949087985 scopus 로고    scopus 로고
    • Mitochondrial quality control: insights on how Parkinson's disease related genes PINK1, parkin, and Omi/HtrA2 interact to maintain mitochondrial homeostasis
    • Dagda, R. K., and Chu, C. T. (2009). Mitochondrial quality control: insights on how Parkinson's disease related genes PINK1, parkin, and Omi/HtrA2 interact to maintain mitochondrial homeostasis. J. Bioenerg. Biomembr. 41, 473-479.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 473-479
    • Dagda, R.K.1    Chu, C.T.2
  • 23
    • 0035120525 scopus 로고    scopus 로고
    • Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease
    • D'Andrea, M. R., Nagele, R. G., Wang, H. Y., Peterson, P. A., and Lee, D. H. (2001). Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease. Histopathology 38, 120-134.
    • (2001) Histopathology , vol.38 , pp. 120-134
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.Y.3    Peterson, P.A.4    Lee, D.H.5
  • 26
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson, T. M., and Dawson, V. L. (2003). Molecular pathways of neurodegeneration in Parkinson's disease. Science 302, 819-822.
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 27
    • 0032886707 scopus 로고    scopus 로고
    • Tau and synuclein and their role in neuropathology
    • Dickson, D. W. (1999). Tau and synuclein and their role in neuropathology. Brain Pathol. 9, 657-661.
    • (1999) Brain Pathol , vol.9 , pp. 657-661
    • Dickson, D.W.1
  • 28
    • 0029657947 scopus 로고    scopus 로고
    • Cytoskeletal pathology in non-Alzheimer degenerative dementia: new lesions in diffuse Lewy body disease, Pick's disease, and corticobasal degeneration
    • Dickson, D. W., Feany, M. B., Yen, S. H., Mattiace, L. A., and Davies, P. (1996). Cytoskeletal pathology in non-Alzheimer degenerative dementia: new lesions in diffuse Lewy body disease, Pick's disease, and corticobasal degeneration. J. Neural Transm. Suppl. 47, 31-46.
    • (1996) J. Neural Transm. Suppl. , vol.47 , pp. 31-46
    • Dickson, D.W.1    Feany, M.B.2    Yen, S.H.3    Mattiace, L.A.4    Davies, P.5
  • 31
    • 0036772311 scopus 로고    scopus 로고
    • Intracellular A-beta amyloid, a sign for worse things to come?
    • Echeverria, V., and Cuello, A. C. (2002). Intracellular A-beta amyloid, a sign for worse things to come? Mol. Neurobiol. 26, 299-316.
    • (2002) Mol. Neurobiol , vol.26 , pp. 299-316
    • Echeverria, V.1    Cuello, A.C.2
  • 32
    • 0037134505 scopus 로고    scopus 로고
    • Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)
    • Edbauer, D., Willem, M., Lammich, S., Steiner, H., and Haass, C. (2002). Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). J. Biol. Chem. 277, 13389-13393.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 34
    • 0029062956 scopus 로고
    • Widespread cytoskeletal pathology characterizes corticobasal degeneration
    • Feany, M. B., and Dickson, D. W. (1995). Widespread cytoskeletal pathology characterizes corticobasal degeneration. Am. J. Pathol. 146, 1388-1396.
    • (1995) Am. J. Pathol. , vol.146 , pp. 1388-1396
    • Feany, M.B.1    Dickson, D.W.2
  • 37
    • 33644824239 scopus 로고    scopus 로고
    • Interface between tauopathies and synucleinopathies: a tale of two proteins
    • Galpern, W. R., and Lang, A. E. (2006). Interface between tauopathies and synucleinopathies: a tale of two proteins. Ann. Neurol. 59, 449-458.
    • (2006) Ann. Neurol. , vol.59 , pp. 449-458
    • Galpern, W.R.1    Lang, A.E.2
  • 42
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., and Crowther, R. A. (1989). Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 44
    • 15544380902 scopus 로고    scopus 로고
    • Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis
    • Greene, J. C., Whitworth, A. J., Andrews, L. A., Parker, T. J., and Pallanck, L. J. (2005). Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis. Hum. Mol. Genet. 14, 799-811.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 799-811
    • Greene, J.C.1    Whitworth, A.J.2    Andrews, L.A.3    Parker, T.J.4    Pallanck, L.J.5
  • 47
    • 33751250197 scopus 로고    scopus 로고
    • Genetics of familial and sporadic amyotrophic lateral sclerosis
    • Gros-Louis, F., Gaspar, C., and Rouleau, G. A. (2006). Genetics of familial and sporadic amyotrophic lateral sclerosis. Biochim. Biophys. Acta 1762, 956-972.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 956-972
    • Gros-Louis, F.1    Gaspar, C.2    Rouleau, G.A.3
  • 50
    • 0034745017 scopus 로고    scopus 로고
    • Intraneuronal abeta-amyloid precedes development of amyloid plaques in Down syndrome
    • Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E., and Troncoso, J. C. (2001). Intraneuronal abeta-amyloid precedes development of amyloid plaques in Down syndrome. Arch. Pathol. Lab. Med. 125, 489-492.
    • (2001) Arch. Pathol. Lab. Med. , vol.125 , pp. 489-492
    • Gyure, K.A.1    Durham, R.2    Stewart, W.F.3    Smialek, J.E.4    Troncoso, J.C.5
  • 52
    • 0033919992 scopus 로고    scopus 로고
    • Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using alpha-synuclei n immunohistochemistry
    • Hamilton, R. L. (2000). Lewy bodies in Alzheimer's disease: a neuropathological review of 145 cases using alpha-synuclei nimmunohistochemistry. Brain Pathol. 10, 378-384.
    • (2000) Brain Pathol , vol.10 , pp. 378-384
    • Hamilton, R.L.1
  • 53
    • 0029097783 scopus 로고
    • Distribution of tangles and threads in the cerebral cortex in progressive supranuclear palsy
    • Hanihara, T., Amano, N., Takahashi, T., Nagatomo, H., and Yagashita, S. (1995). Distribution of tangles and threads in the cerebral cortex in progressive supranuclear palsy. Neuropathol. Appl. Neurobiol. 21, 319-326.
    • (1995) Neuropathol. Appl. Neurobiol. , vol.21 , pp. 319-326
    • Hanihara, T.1    Amano, N.2    Takahashi, T.3    Nagatomo, H.4    Yagashita, S.5
  • 54
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 55
    • 0028120382 scopus 로고
    • Senile dementia of Lewy body type and Alzheimer type are biochemically distinct in terms of paired helical filaments and hyperphosphorylated tau protein
    • Harrington, C. R., Perry, R. H., Perry, E. K., Hurt, J., McKeith, I. G., Roth, M., and Wischik, C. M. (1994). Senile dementia of Lewy body type and Alzheimer type are biochemically distinct in terms of paired helical filaments and hyperphosphorylated tau protein. Dementia 5, 215-228.
    • (1994) Dementia , vol.5 , pp. 215-228
    • Harrington, C.R.1    Perry, R.H.2    Perry, E.K.3    Hurt, J.4    McKeith, I.G.5    Roth, M.6    Wischik, C.M.7
  • 58
    • 0027199893 scopus 로고
    • Alzheimer's lesions labelled by anti-ubiquitin antibodies: comparison with other staining techniques A study of 15 cases with graded intellectual status in ageing and Alzheimer's disease
    • He, Y., Duyckaerts, C., Delaere, P., Piette, F., and Hauw, J. J. (1993). Alzheimer's lesions labelled by anti-ubiquitin antibodies: comparison with other staining techniques. A study of 15 cases with graded intellectual status in ageing and Alzheimer's disease. Neuropathol. Appl. Neurobiol. 19, 364-371.
    • (1993) Neuropathol. Appl. Neurobiol. , vol.19 , pp. 364-371
    • He, Y.1    Duyckaerts, C.2    Delaere, P.3    Piette, F.4    Hauw, J.J.5
  • 60
    • 0036685608 scopus 로고    scopus 로고
    • Transgenic mouse model of tauopathies with glial pathology and nervous system degeneration
    • Higuchi, M., Ishihara, T., Zhang, B., Hong, M., Andreadis, A., Trojanowski, J., and Lee, V. M. (2002). Transgenic mouse model of tauopathies with glial pathology and nervous system degeneration. Neuron 35, 433-446.
    • (2002) Neuron , vol.35 , pp. 433-446
    • Higuchi, M.1    Ishihara, T.2    Zhang, B.3    Hong, M.4    Andreadis, A.5    Trojanowski, J.6    Lee, V.M.7
  • 61
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubulebinding domains and variable N-terminal domains
    • Himmler, A., Drechsel, D., Kirschner, M. W., and Martin, D. W. Jr. (1989). Tau consists of a set of proteins with repeated C-terminal microtubulebinding domains and variable N-terminal domains. Mol. Cell. Biol. 9, 1381-1388.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 62
    • 0026721235 scopus 로고
    • Distribution of cortical neurofibrillary tangles in progressive supranuclear palsy: a quantitative analysis of six cases
    • Hof, P. R., Delacourte, A., and Bouras, C. (1992). Distribution of cortical neurofibrillary tangles in progressive supranuclear palsy: a quantitative analysis of six cases. Acta Neuropathol. 84, 45-51.
    • (1992) Acta Neuropathol , vol.84 , pp. 45-51
    • Hof, P.R.1    Delacourte, A.2    Bouras, C.3
  • 64
    • 0033767459 scopus 로고    scopus 로고
    • Parkin is associated with actin filaments in neuronal and nonneural cells
    • Huynh, D. P., Scoles, D. R., Ho, T. H., Del Bigio, M. R., and Pulst, S. M. (2000). Parkin is associated with actin filaments in neuronal and nonneural cells. Ann. Neurol. 48, 737-744.
    • (2000) Ann. Neurol. , vol.48 , pp. 737-744
    • Huynh, D.P.1    Scoles, D.R.2    Ho, T.H.3    Del Bigio, M.R.4    Pulst, S.M.5
  • 65
    • 27844554819 scopus 로고    scopus 로고
    • Effect of overexpression of wild-type or mutant parkin on the cellular response induced by toxic insults
    • Hyun, D. H., Lee, M., Halliwell, B., and Jenner, P. (2005). Effect of overexpression of wild-type or mutant parkin on the cellular response induced by toxic insults. J. Neurosci. Res. 82, 232-244.
    • (2005) J. Neurosci. Res. , vol.82 , pp. 232-244
    • Hyun, D.H.1    Lee, M.2    Halliwell, B.3    Jenner, P.4
  • 66
    • 0037047311 scopus 로고    scopus 로고
    • Effect of wild-type or mutant Parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome
    • Hyun, D. H., Lee, M., Hattori, N., Kubo, S., Mizuno, Y., Halliwell, B., and Jenner, P. (2002). Effect of wild-type or mutant Parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome. J. Biol. Chem. 277, 28572-28577.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28572-28577
    • Hyun, D.H.1    Lee, M.2    Hattori, N.3    Kubo, S.4    Mizuno, Y.5    Halliwell, B.6    Jenner, P.7
  • 67
  • 68
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., and Takahashi, R. (2001). An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105, 891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 69
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai, Y., Soda, M., and Takahashi, R. (2000). Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275, 35661-35664.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 71
    • 43649103517 scopus 로고    scopus 로고
    • Astrocytic tau pathology positively correlates with neurofibrillary tangle density in progressive supranuclear palsy
    • Ito, K., Arai, K., Yoshiyama, Y., Kashiwado, K., Sakakibara, Y., and Hattori, T. (2008). Astrocytic tau pathology positively correlates with neurofibrillary tangle density in progressive supranuclear palsy. Acta Neuropathol. 115, 623-628.
    • (2008) Acta Neuropathol , vol.115 , pp. 623-628
    • Ito, K.1    Arai, K.2    Yoshiyama, Y.3    Kashiwado, K.4    Sakakibara, Y.5    Hattori, T.6
  • 72
    • 0027978991 scopus 로고
    • Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics
    • Iwatsubo, T., Hasegawa, M., and Ihara, Y. (1994). Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics. Acta Neuropathol. 88, 129-136.
    • (1994) Acta Neuropathol , vol.88 , pp. 129-136
    • Iwatsubo, T.1    Hasegawa, M.2    Ihara, Y.3
  • 73
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes, R., Spillantini, M. G., and Goedert, M. (1994). Identification of two distinct synucleins from human brain. FEBS Lett. 345, 27-32.
    • (1994) FEBS Lett , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 74
    • 7944238570 scopus 로고    scopus 로고
    • Lewy body-related alpha-synucleinopathy in the aged human brain
    • Jellinger, K. A. (2004). Lewy body-related alpha-synucleinopathy in the aged human brain. J. Neural Transm. 111, 1219-1235.
    • (2004) J. Neural Transm. , vol.111 , pp. 1219-1235
    • Jellinger, K.A.1
  • 75
    • 76449083770 scopus 로고    scopus 로고
    • The molecular mechanism of mitochondria autophagy in yeast
    • Kanki, T., and Klionsky, D. J. (2010). The molecular mechanism of mitochondria autophagy in yeast. Mol. Microbiol. 75, 795-800.
    • (2010) Mol. Microbiol. , vol.75 , pp. 795-800
    • Kanki, T.1    Klionsky, D.J.2
  • 76
    • 77950371695 scopus 로고    scopus 로고
    • PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy
    • Kawajiri, S., Saiki, S., Sato, S., Sato, F., Hatano, T., Eguchi, H., and Hattori, N. (2010). PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy. FEBS Lett. 584, 1073-1079.
    • (2010) FEBS Lett , vol.584 , pp. 1073-1079
    • Kawajiri, S.1    Saiki, S.2    Sato, S.3    Sato, F.4    Hatano, T.5    Eguchi, H.6    Hattori, N.7
  • 78
    • 33646408797 scopus 로고    scopus 로고
    • Parkin is protective for substantia nigra dopamine neurons in a tau gene transfer neurodegeneration model
    • Klein, R. L., Dayton, R. D., Henderson, K. M., and Petrucelli, L. (2006). Parkin is protective for substantia nigra dopamine neurons in a tau gene transfer neurodegeneration model. Neurosci. Lett. 401, 130-135.
    • (2006) Neurosci. Lett. , vol.401 , pp. 130-135
    • Klein, R.L.1    Dayton, R.D.2    Henderson, K.M.3    Petrucelli, L.4
  • 79
    • 24044494918 scopus 로고    scopus 로고
    • Tau gene transfer, but not alpha-synuclein, induces both progressive dopamine neuron degeneration and rotational behavior in the rat
    • Klein, R. L., Dayton, R. D., Lin, W. L., and Dickson, D. W. (2005). Tau gene transfer, but not alpha-synuclein, induces both progressive dopamine neuron degeneration and rotational behavior in the rat. Neurobiol. Dis. 20, 64-73.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 64-73
    • Klein, R.L.1    Dayton, R.D.2    Lin, W.L.3    Dickson, D.W.4
  • 82
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo, E. H., and Squazzo, S. L. (1994). Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269, 17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 83
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., and Grundke-Iqbal, I. (1993). Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem.268, 24374-24384.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 86
    • 0028981717 scopus 로고
    • The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla, F. M., Tinkle, B. T., Bieberich, C. J., Haudenschild, C. C., and Jay, G. (1995). The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat. Genet. 9, 21-30.
    • (1995) Nat. Genet , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 87
    • 0141428795 scopus 로고    scopus 로고
    • Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders
    • Layfield, R., Cavey, J. R., and Lowe, J. (2003). Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders. Ageing Res. Rev. 2, 343-356.
    • (2003) Ageing Res. Rev. , vol.2 , pp. 343-356
    • Layfield, R.1    Cavey, J.R.2    Lowe, J.3
  • 88
    • 0035109909 scopus 로고    scopus 로고
    • Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult
    • Lee, M., Hyun, D., Halliwell, B., and Jenner, P. (2001a). Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult. J. Neurochem. 76, 998-1009.
    • (2001) J. Neurochem. , vol.76 , pp. 998-1009
    • Lee, M.1    Hyun, D.2    Halliwell, B.3    Jenner, P.4
  • 91
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., and Selkoe, D. J. (2003). Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 1087-1093.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 93
    • 34748872706 scopus 로고    scopus 로고
    • The role of intracellular amyloid beta in Alzheimer's disease
    • Li, M., Chen, L., Lee, D. H., Yu, L. C., and Zhang, Y. (2007). The role of intracellular amyloid beta in Alzheimer's disease. Prog. Neurobiol. 83, 131-139.
    • (2007) Prog. Neurobiol. , vol.83 , pp. 131-139
    • Li, M.1    Chen, L.2    Lee, D.H.3    Yu, L.C.4    Zhang, Y.5
  • 94
    • 27144472378 scopus 로고    scopus 로고
    • Alpha-Synuclein aggregation in pathological aging and Alzheimer's disease: the impact of beta-amyloid plaque level
    • Lippa, S. M., Lippa, C. F., and Mori, H. (2005). Alpha-Synuclein aggregation in pathological aging and Alzheimer's disease: the impact of beta-amyloid plaque level. Am. J. Alzheimers Dis. Other Demen. 20, 315-318.
    • (2005) Am. J. Alzheimers Dis. Other Demen. , vol.20 , pp. 315-318
    • Lippa, S.M.1    Lippa, C.F.2    Mori, H.3
  • 95
    • 10644281090 scopus 로고    scopus 로고
    • Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alphasynuclein rat model of Parkinson's disease
    • Lo Bianco, C., Schneider, B. L., Bauer, M., Sajadi, A., Brice, A., Iwatsubo, T., and Aebischer, P. (2004). Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alphasynuclein rat model of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 101, 17510-17515.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17510-17515
    • Lo Bianco, C.1    Schneider, B.L.2    Bauer, M.3    Sajadi, A.4    Brice, A.5    Iwatsubo, T.6    Aebischer, P.7
  • 96
    • 0037044240 scopus 로고    scopus 로고
    • The overlap of amyotrophic lateral sclerosis and frontotemporal dementia
    • Lomen-Hoerth, C., Anderson, T., and Miller, B. (2002). The overlap of amyotrophic lateral sclerosis and frontotemporal dementia. Neurology 59, 1077-1079.
    • (2002) Neurology , vol.59 , pp. 1077-1079
    • Lomen-Hoerth, C.1    Anderson, T.2    Miller, B.3
  • 98
    • 0037383052 scopus 로고    scopus 로고
    • Relationship between betaamyloid degradation and the 26S proteasome in neural cells
    • Lopez Salon, M., Pasquini, L., Besio Moreno, M., Pasquini, J. M., and Soto, E. (2003). Relationship between betaamyloid degradation and the 26S proteasome in neural cells. Exp. Neurol. 180, 131-143.
    • (2003) Exp. Neurol. , vol.180 , pp. 131-143
    • Lopez Salon, M.1    Pasquini, L.2    Besio Moreno, M.3    Pasquini, J.M.4    Soto, E.5
  • 101
    • 34548741834 scopus 로고    scopus 로고
    • rAAV-mediated nigral human parkin over-expression partially ameliorates motor deficits via enhanced dopamine neurotransmission in a rat model of Parkinson's disease
    • Manfredsson, F. P., Burger, C., Sullivan, L. F., Muzyczka, N., Lewin, A. S., and Mandel, R. J. (2007). rAAV-mediated nigral human parkin over-expression partially ameliorates motor deficits via enhanced dopamine neurotransmission in a rat model of Parkinson's disease. Exp. Neurol. 207, 289-301.
    • (2007) Exp. Neurol. , vol.207 , pp. 289-301
    • Manfredsson, F.P.1    Burger, C.2    Sullivan, L.F.3    Muzyczka, N.4    Lewin, A.S.5    Mandel, R.J.6
  • 103
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught, K. S., and Jenner, P. (2001). Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297, 191-194.
    • (2001) Neurosci. Lett. , vol.297 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 105
    • 33751267701 scopus 로고    scopus 로고
    • Parkin: a multifaceted ubiquitin ligase
    • Moore, D. J. (2006). Parkin: a multifaceted ubiquitin ligase. Biochem. Soc. Trans. 34, 749-753.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 749-753
    • Moore, D.J.1
  • 107
    • 0033151716 scopus 로고    scopus 로고
    • A novel transactivation domain in parkin
    • Morett, E., and Bork, P. (1999). A novel transactivation domain in parkin. Trends Biochem. Sci. 24, 229-231.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 229-231
    • Morett, E.1    Bork, P.2
  • 111
    • 62649103875 scopus 로고    scopus 로고
    • Parkin attenuates wild-type tau modification in the presence of beta-amyloid and alpha-synuclein
    • Moussa, C. E. (2009). Parkin attenuates wild-type tau modification in the presence of beta-amyloid and alpha-synuclein. J. Mol. Neurosci. 37, 25-36.
    • (2009) J. Mol. Neurosci. , vol.37 , pp. 25-36
    • Moussa, C.E.1
  • 112
    • 2442534084 scopus 로고    scopus 로고
    • Differential cytotoxicity of human wild type and mutant alpha-synuclein in human neuroblastoma SH-SY5Y cells in the presence of dopamine
    • Moussa, C. E., Wersinger, C., Tomita, Y., and Sidhu, A. (2004). Differential cytotoxicity of human wild type and mutant alpha-synuclein in human neuroblastoma SH-SY5Y cells in the presence of dopamine. Biochemistry 43, 5539-5550.
    • (2004) Biochemistry , vol.43 , pp. 5539-5550
    • Moussa, C.E.1    Wersinger, C.2    Tomita, Y.3    Sidhu, A.4
  • 113
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju, P., Lewis, J., Easson, C., Yen, S., Hackett, J., Hutton, M., and Yen, S. H. (1999). Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett. 447, 195-199.
    • (1999) FEBS Lett , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 115
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • doi:10.1371/journal. pbio.1000298
    • Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D. F., Gautier, C. A., Shen, J., Cookson, M. R., and Youle, R. J. (2010). PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 8, e1000298. doi:10.1371/journal. pbio.1000298.
    • (2010) PLoS Biol , vol.8
    • Narendra, D.P.1    Jin, S.M.2    Tanaka, A.3    Suen, D.F.4    Gautier, C.A.5    Shen, J.6    Cookson, M.R.7    Youle, R.J.8
  • 116
    • 0034528007 scopus 로고    scopus 로고
    • Classification and description of frontotemporal dementias
    • Neary, D., Snowden, J. S., and Mann, D. M. (2000). Classification and description of frontotemporal dementias. Ann. N. Y. Acad. Sci. 920, 46-51.
    • (2000) Ann. N. Y. Acad. Sci. , vol.920 , pp. 46-51
    • Neary, D.1    Snowden, J.S.2    Mann, D.M.3
  • 118
    • 4944267025 scopus 로고    scopus 로고
    • Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer's neurofibrillary tangles
    • Nemes, Z., Devreese, B., Steinert, P. M., Van Beeumen, J., and Fesus, L. (2004). Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer's neurofibrillary tangles. FASEB J. 18, 1135-1137.
    • (2004) FASEB J , vol.18 , pp. 1135-1137
    • Nemes, Z.1    Devreese, B.2    Steinert, P.M.3    Van Beeumen, J.4    Fesus, L.5
  • 119
    • 35348853257 scopus 로고    scopus 로고
    • TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis
    • Neumann, M., Kwong, L. K., Sampathu, D. M., Trojanowski, J. Q., and Lee, V. M. (2007a). TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis. Arch. Neurol. 64, 1388-1394.
    • (2007) Arch. Neurol. , vol.64 , pp. 1388-1394
    • Neumann, M.1    Kwong, L.K.2    Sampathu, D.M.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 122
    • 0026700385 scopus 로고
    • Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy
    • Nishimura, M., Namba, Y., Ikeda, K., and Oda, M. (1992). Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy. Neurosci. Lett. 143, 35-38.
    • (1992) Neurosci. Lett. , vol.143 , pp. 35-38
    • Nishimura, M.1    Namba, Y.2    Ikeda, K.3    Oda, M.4
  • 123
    • 0029071320 scopus 로고
    • Immunocytochemical characterization of glial fibrillary tangles in Alzheimer's disease brain
    • Nishimura, M., Tomimoto, H., Suenaga, T., Namba, Y., Ikeda, K., Akiguchi, I., and Kimura, J. (1995). Immunocytochemical characterization of glial fibrillary tangles in Alzheimer's disease brain. Am. J. Pathol. 146, 1052-1058.
    • (1995) Am. J. Pathol. , vol.146 , pp. 1052-1058
    • Nishimura, M.1    Tomimoto, H.2    Suenaga, T.3    Namba, Y.4    Ikeda, K.5    Akiguchi, I.6    Kimura, J.7
  • 124
    • 33746921646 scopus 로고    scopus 로고
    • Alzheimer disease: cellular and molecular aspects
    • discussion 450-441
    • Octave, J. N. (2005). Alzheimer disease: cellular and molecular aspects. Bull. Mem. Acad. R. Med. Belg. 160, 445-449; discussion 450-441.
    • (2005) Bull. Mem. Acad. R. Med. Belg. , vol.160 , pp. 445-449
    • Octave, J.N.1
  • 125
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo, S., Caccamo, A., Kitazawa, M., Tseng, B. P., and LaFerla, F. M. (2003). Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol. Aging 24, 1063-1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 127
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli, P., and Brown, R. H. (2006). Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 7, 710-723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 128
    • 8144227320 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration with ubiquitin-only-immunoreactive neuronal changes: broadening the clinical picture to include progressive supranuclear palsy
    • Paviour, D. C., Lees, A. J., Josephs, K. A., Ozawa, T., Ganguly, M., Strand, C., Godbolt, A., Howard, R. S., Revesz, T., and Holton, J. L. (2004). Frontotemporal lobar degeneration with ubiquitin-only-immunoreactive neuronal changes: broadening the clinical picture to include progressive supranuclear palsy. Brain 127, 2441-2451.
    • (2004) Brain , vol.127 , pp. 2441-2451
    • Paviour, D.C.1    Lees, A.J.2    Josephs, K.A.3    Ozawa, T.4    Ganguly, M.5    Strand, C.6    Godbolt, A.7    Howard, R.S.8    Revesz, T.9    Holton, J.L.10
  • 131
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • Pesah, Y., Pham, T., Burgess, H., Middlebrooks, B., Verstreken, P., Zhou, Y., Harding, M., Bellen, H., and Mardon, G. (2004). Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131, 2183-2194.
    • (2004) Development , vol.131 , pp. 2183-2194
    • Pesah, Y.1    Pham, T.2    Burgess, H.3    Middlebrooks, B.4    Verstreken, P.5    Zhou, Y.6    Harding, M.7    Bellen, H.8    Mardon, G.9
  • 132
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli, L., O'Farrell, C., Lockhart, P. J., Baptista, M., Kehoe, K., Vink, L., Choi, P., Wolozin, B., Farrer, M., Hardy, J., and Cookson, M. R. (2002). Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 36, 1007-1019.
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6    Choi, P.7    Wolozin, B.8    Farrer, M.9    Hardy, J.10    Cookson, M.R.11
  • 135
    • 10044281817 scopus 로고    scopus 로고
    • Lewy bodies in the amygdala: increase of alpha-synuclein aggregates in neurodegenerative diseases with taubased inclusions
    • Popescu, A., Lippa, C. F., Lee, V. M., and Trojanowski, J. Q. (2004). Lewy bodies in the amygdala: increase of alpha-synuclein aggregates in neurodegenerative diseases with taubased inclusions. Arch. Neurol. 61, 1915-1919.
    • (2004) Arch. Neurol. , vol.61 , pp. 1915-1919
    • Popescu, A.1    Lippa, C.F.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 137
    • 0037062609 scopus 로고    scopus 로고
    • The prevalence of frontotemporal dementia
    • Ratnavalli, E., Brayne, C., Dawson, K., and Hodges, J. R. (2002). The prevalence of frontotemporal dementia. Neurology 58, 1615-1621.
    • (2002) Neurology , vol.58 , pp. 1615-1621
    • Ratnavalli, E.1    Brayne, C.2    Dawson, K.3    Hodges, J.R.4
  • 138
    • 77951226607 scopus 로고    scopus 로고
    • [beta]-Amyloid1-42 gene transfer model exhibits intraneuronal amyloid, gliosis, tau phosphorylation, and neuronal loss
    • Rebeck, G. W., Hoe, H. S., and Moussa, C. E. (2010). [beta]-Amyloid1-42 gene transfer model exhibits intraneuronal amyloid, gliosis, tau phosphorylation, and neuronal loss. J. Biol. Chem. 285, 7440-7446.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7440-7446
    • Rebeck, G.W.1    Hoe, H.S.2    Moussa, C.E.3
  • 139
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren, Y., Zhao, J., and Feng, J. (2003). Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J. Neurosci. 23, 3316-3324.
    • (2003) J. Neurosci. , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 141
    • 40749134969 scopus 로고    scopus 로고
    • Parkin polymorphisms in progressive supranuclear palsy
    • Ros, R., Ampuero, I., and Garcia de Yebenes, J. (2008). Parkin polymorphisms in progressive supranuclear palsy. J. Neurol. Sci. 268, 176-178.
    • (2008) J. Neurol. Sci. , vol.268 , pp. 176-178
    • Ros, R.1    Ampuero, I.2    Garcia de Yebenes, J.3
  • 142
    • 0027164824 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D. R. (1993). Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 364, 362.
    • (1993) Nature , vol.364 , pp. 362
    • Rosen, D.R.1
  • 143
    • 73949083524 scopus 로고    scopus 로고
    • Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function
    • Rosen, K. M., Moussa, C. E., Lee, H. K., Kumar, P., Kitada, T., Qin, G., Fu, Q., and Querfurth, H. W. (2010). Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function. J. Neurosci. Res. 88, 167-178.
    • (2010) J. Neurosci. Res. , vol.88 , pp. 167-178
    • Rosen, K.M.1    Moussa, C.E.2    Lee, H.K.3    Kumar, P.4    Kitada, T.5    Qin, G.6    Fu, Q.7    Querfurth, H.W.8
  • 145
    • 0036812559 scopus 로고    scopus 로고
    • Progressive supranuclear palsy and tau hyperphosphorylation in a patient with a C212Y parkin mutation
    • Sanchez, M. P., Gonzalo, I., Avila, J., and De Yebenes, J. G. (2002). Progressive supranuclear palsy and tau hyperphosphorylation in a patient with a C212Y parkin mutation. J. Alzheimers Dis. 4, 399-404.
    • (2002) J. Alzheimers Dis. , vol.4 , pp. 399-404
    • Sanchez, M.P.1    Gonzalo, I.2    Avila, J.3    De Yebenes, J.G.4
  • 146
    • 1042292018 scopus 로고    scopus 로고
    • Endoplasmic reticulum-localized amyloid betapeptide is degraded in the cytosol by two distinct degradation pathways
    • Schmitz, A., Schneider, A., Kummer, M. P., and Herzog, V. (2004). Endoplasmic reticulum-localized amyloid betapeptide is degraded in the cytosol by two distinct degradation pathways. Traffic 5, 89-101.
    • (2004) Traffic , vol.5 , pp. 89-101
    • Schmitz, A.1    Schneider, A.2    Kummer, M.P.3    Herzog, V.4
  • 147
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell, L. C., Berriman, J., Jakes, R., Goedert, M., and Crowther, R. A. (2000). Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. U.S.A. 97, 4897-4902.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 150
    • 0031781642 scopus 로고    scopus 로고
    • Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture
    • Skovronsky, D. M., Doms, R. W., and Lee, V. M. (1998). Detection of a novel intraneuronal pool of insoluble amyloid beta protein that accumulates with time in culture. J. Cell Biol. 141, 1031-1039.
    • (1998) J. Cell Biol. , vol.141 , pp. 1031-1039
    • Skovronsky, D.M.1    Doms, R.W.2    Lee, V.M.3
  • 153
    • 0035097503 scopus 로고    scopus 로고
    • Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alphasynuclein mutation
    • Spira, P. J., Sharpe, D. M., Halliday, G., Cavanagh, J., and Nicholson, G. A. (2001). Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr alphasynuclein mutation. Ann. Neurol. 49, 313-319.
    • (2001) Ann. Neurol. , vol.49 , pp. 313-319
    • Spira, P.J.1    Sharpe, D.M.2    Halliday, G.3    Cavanagh, J.4    Nicholson, G.A.5
  • 155
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • Staropoli, J. F., McDermott, C., Martinat, C., Schulman, B., Demireva, E., and Abeliovich, A. (2003). Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37, 735-749.
    • (2003) Neuron , vol.37 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 156
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis, L., Larsen, K. E., Rideout, H. J., Sulzer, D., and Greene, L. A. (2001). Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J. Neurosci. 21, 9549-9560.
    • (2001) J. Neurosci. , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 157
    • 0036550597 scopus 로고    scopus 로고
    • Significance of intracellular Abeta42 accumulation in Alzheimer's disease
    • Tabira, T., Chui, D. H., and Kuroda, S. (2002). Significance of intracellular Abeta42 accumulation in Alzheimer's disease. Front. Biosci. 7, a44-a49.
    • (2002) Front. Biosci. , vol.7
    • Tabira, T.1    Chui, D.H.2    Kuroda, S.3
  • 158
    • 33749002522 scopus 로고    scopus 로고
    • Recent advances in the genetics of amyotrophic lateral sclerosis and frontotemporal dementia: common pathways in neurodegenerative disease
    • Talbot, K., and Ansorge, O. (2006). Recent advances in the genetics of amyotrophic lateral sclerosis and frontotemporal dementia: common pathways in neurodegenerative disease. Hum. Mol. Genet. 15, R182-R187.
    • (2006) Hum. Mol. Genet. , vol.15
    • Talbot, K.1    Ansorge, O.2
  • 159
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation
    • Tan, C. F., Eguchi, H., Tagawa, A., Onodera, O., Iwasaki, T., Tsujino, A., Nishizawa, M., Kakita, A., and Takahashi, H. (2007). TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol. 113, 535-542.
    • (2007) Acta Neuropathol , vol.113 , pp. 535-542
    • Tan, C.F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 160
    • 77950499364 scopus 로고    scopus 로고
    • Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network
    • Tanaka, A. (2010). Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network. FEBS Lett. 584, 1386-1392.
    • (2010) FEBS Lett , vol.584 , pp. 1386-1392
    • Tanaka, A.1
  • 161
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondriadependent apoptosis
    • Tanaka, Y., Engelender, S., Igarashi, S., Rao, R. K., Wanner, T., Tanzi, R. E., Sawa, A., V, L. D., Dawson, T. M., and Ross, C. A. (2001). Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondriadependent apoptosis. Hum. Mol. Genet. 10, 919-926.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5    Tanzi, R.E.6    Sawa, A.V.L.D.7    Dawson, T.M.8    Ross, C.A.9
  • 162
    • 0035976835 scopus 로고    scopus 로고
    • alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris, G. K., Layfield, R., and Spillantini, M. G. (2001). alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509, 22-26.
    • (2001) FEBS Lett , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 163
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai, Y. C., Fishman, P. S., Thakor, N. V., and Oyler, G. A. (2003). Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 278, 22044-22055.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 164
    • 0029052277 scopus 로고
    • Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits
    • Tu, P. H., Elder, G., Lazzarini, R. A., Nelson, D., Trojanowski, J. Q., and Lee, V. M. (1995). Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits. J. Cell Biol. 129, 1629-1640.
    • (1995) J. Cell Biol. , vol.129 , pp. 1629-1640
    • Tu, P.H.1    Elder, G.2    Lazzarini, R.A.3    Nelson, D.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 167
    • 0344256486 scopus 로고    scopus 로고
    • Structural diversity and functional implications of the eukaryotic TDP gene family
    • Wang, H. Y., Wang, I. F., Bose, J., and Shen, C. K. (2004). Structural diversity and functional implications of the eukaryotic TDP gene family. Genomics 83, 130-139.
    • (2004) Genomics , vol.83 , pp. 130-139
    • Wang, H.Y.1    Wang, I.F.2    Bose, J.3    Shen, C.K.4
  • 168
    • 20344369560 scopus 로고    scopus 로고
    • Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
    • Whitworth, A. J., Theodore, D. A., Greene, J. C., Benes, H., Wes, P. D., and Pallanck, L. J. (2005). Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 102, 8024-8029.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8024-8029
    • Whitworth, A.J.1    Theodore, D.A.2    Greene, J.C.3    Benes, H.4    Wes, P.D.5    Pallanck, L.J.6
  • 169
    • 75949104449 scopus 로고    scopus 로고
    • Mitochondria get a Parkin' ticket
    • Wild, P., and 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
  • 171
    • 0032800818 scopus 로고    scopus 로고
    • Intracellular APP processing and A beta production in Alzheimer disease
    • Wilson, C. A., Doms, R. W., and Lee, V. M. (1999). Intracellular APP processing and A beta production in Alzheimer disease. J. Neuropathol. Exp. Neurol. 58, 787-794.
    • (1999) J. Neuropathol. Exp. Neurol , vol.58 , pp. 787-794
    • Wilson, C.A.1    Doms, R.W.2    Lee, V.M.3
  • 172
    • 71849084134 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease
    • Winklhofer, K. F., and Haass, C. (2010). Mitochondrial dysfunction in Parkinson's disease. Biochim. Biophys. Acta 1802, 29-44.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 29-44
    • Winklhofer, K.F.1    Haass, C.2
  • 173
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton, M. J., Igaz, L. M., Wong, M. M., Kwong, L. K., Trojanowski, J. Q., and Lee, V. M. (2008). Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283, 13302-13309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 174
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide--the first step of a fatal cascade
    • Wirths, O., Multhaup, G., and Bayer, T. A. (2004). A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide--the first step of a fatal cascade. J. Neurochem. 91, 513-520.
    • (2004) J. Neurochem. , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 175
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 doubletransgenic mice
    • Wirths, O., Multhaup, G., Czech, C., Blanchard, V., Moussaoui, S., Tremp, G., Pradier, L., Beyreuther, K., and Bayer, T. A. (2001). Intraneuronal Abeta accumulation precedes plaque formation in beta-amyloid precursor protein and presenilin-1 doubletransgenic mice. Neurosci. Lett. 306, 116-120.
    • (2001) Neurosci. Lett , vol.306 , pp. 116-120
    • Wirths, O.1    Multhaup, G.2    Czech, C.3    Blanchard, V.4    Moussaoui, S.5    Tremp, G.6    Pradier, L.7    Beyreuther, K.8    Bayer, T.A.9
  • 178
    • 0028004473 scopus 로고
    • Astrocytic straight tubules in the brain of a patient with Pick's disease
    • Yamazaki, M., Nakano, I., Imazu, O., Kaieda, R., and Terashi, A. (1994). Astrocytic straight tubules in the brain of a patient with Pick's disease. Acta Neuropathol. 88, 587-591.
    • (1994) Acta Neuropathol , vol.88 , pp. 587-591
    • Yamazaki, M.1    Nakano, I.2    Imazu, O.3    Kaieda, R.4    Terashi, A.5
  • 179
    • 15244354724 scopus 로고    scopus 로고
    • Tau and alpha-synuclein inclusions in a case of familial frontotemporal dementia and progressive aphasia
    • Yancopoulou, D., Xuereb, J. H., Crowther, R. A., Hodges, J. R., and Spillantini, M. G. (2005). Tau and alpha-synuclein inclusions in a case of familial frontotemporal dementia and progressive aphasia. J. Neuropathol. Exp. Neurol. 64, 245-253.
    • (2005) J. Neuropathol. Exp. Neurol. , vol.64 , pp. 245-253
    • Yancopoulou, D.1    Xuereb, J.H.2    Crowther, R.A.3    Hodges, J.R.4    Spillantini, M.G.5
  • 180
    • 0028945660 scopus 로고
    • Evidence that A beta 42 is the real culprit in Alzheimer's disease
    • Younkin, S. G. (1995). Evidence that A beta 42 is the real culprit in Alzheimer's disease. Ann. Neurol. 37, 287-288.
    • (1995) Ann. Neurol. , vol.37 , pp. 287-288
    • Younkin, S.G.1
  • 182
    • 77953695068 scopus 로고    scopus 로고
    • Reticulocyte mitophagy: monitoring mitochondrial clearance in a mammalian model
    • Zhang, J., and Ney, P. A. (2010). Reticulocyte mitophagy: monitoring mitochondrial clearance in a mammalian model. Autophagy 6, 405-408.
    • (2010) Autophagy , vol.6 , pp. 405-408
    • Zhang, J.1    Ney, P.A.2
  • 183
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein
    • Zhang, Y., Gao, J., Chung, K. K., Huang, H., Dawson, V. L., and Dawson, T. M. (2000). Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. U.S.A. 97, 13354-13359.
    • (2000) CDCrel-1. Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 185
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
    • Ziviani, E., Tao, R. N., and Whitworth, A. J. (2010). Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107, 5018-5023.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.