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Volumn 18, Issue 2, 2003, Pages 509-517

Ubiquitinated inclusions and neuronal cell death

Author keywords

Apoptosis; Lewy body; Neurodegenerative; Parkinson's disease; Proteasome

Indexed keywords

ALPHA SYNUCLEIN; CASPASE; CELL CYCLE PROTEIN; DACTINOMYCIN; EPOXOMICIN; FIBRILLAR COLLAGEN; LACTACYSTIN; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN KINASE; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

EID: 0037378117     PISSN: 02133911     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (30)

References (96)
  • 1
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • Amerik A.Y., Swaminathan S., Krantz B.A., Wilkinson K.D. and Hochstrasser M. (1997) In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16, 4826-4838.
    • (1997) EMBO J. , vol.16 , pp. 4826-4838
    • Amerik, A.Y.1    Swaminathan, S.2    Krantz, B.A.3    Wilkinson, K.D.4    Hochstrasser, M.5
  • 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
  • 3
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck P.K., Chan H.Y., Trojanowski J.Q., Lee V.M. and Bonini N.N. (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295, 865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.N.5
  • 4
    • 0028859433 scopus 로고
    • Characterization of a dominant negative mutant of the cell-cycle ubiquitin-conjugating enzyme Cdc34
    • Banerjee A., Deshaies R.J. and Chau V. (1995) Characterization of a dominant negative mutant of the cell-cycle ubiquitin-conjugating enzyme Cdc34. J. Biol. Chem. 270, 26209-26215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26209-26215
    • Banerjee, A.1    Deshaies, R.J.2    Chau, V.3
  • 5
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M. and Kopito R.R. (2001). Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 7
    • 0033324249 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis in learning and memory
    • Chain D.G., Schwartz J.H. and Hegde A.N. (1999). Ubiquitin-mediated proteolysis in learning and memory. Mol. Neurobiol. 20, 125-142.
    • (1999) Mol. Neurobiol. , vol.20 , pp. 125-142
    • Chain, D.G.1    Schwartz, J.H.2    Hegde, A.N.3
  • 9
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body 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. (2001a). Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body 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
  • 10
    • 2942618660 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders
    • Chung K.K., Dawson V.L. and Dawson T.M. (2001b). The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders. TINS 24, S7-S14.
    • (2001) TINS , vol.24
    • Chung, K.K.1    Dawson, V.L.2    Dawson, T.M.3
  • 11
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. (1998). The ubiquitin-proteasome pathway: On protein death and cell life. EMBO J. 17, 7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 12
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke P.G. (1990). Developmental cell death: Morphological diversity and multiple mechanisms. Anat. Embryol. (Berl) 181, 195-213.
    • (1990) Anat. Embryol. (Berl) , vol.181 , pp. 195-213
    • Clarke, P.G.1
  • 13
    • 0033215063 scopus 로고    scopus 로고
    • Synucleins in synaptic plasticity and neurodegenerative disorders
    • Clayton D.F. and George J.M. (1999) Synucleins in synaptic plasticity and neurodegenerative disorders. J. Neurosci. Res. 58, 120-129.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 120-129
    • Clayton, D.F.1    George, J.M.2
  • 14
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway K.A., Harper J.D. and Lansbury P.T. (1998). Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4, 1318-1320.
    • (1998) Nat. Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 15
    • 0034048193 scopus 로고    scopus 로고
    • Regional brain atrophy in progressive supranuclear palsy and Lewy body disease
    • Cordato N.J., Halliday G.M., Harding A.J., Hely M.A. and Morris J.G. (2000). Regional brain atrophy in progressive supranuclear palsy and Lewy body disease. Ann. Neurol. 47, 718-728.
    • (2000) Ann. Neurol. , vol.47 , pp. 718-728
    • Cordato, N.J.1    Halliday, G.M.2    Harding, A.J.3    Hely, M.A.4    Morris, J.G.5
  • 16
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings C.J., Mancini M.A., Antalffy B., DeFranco D.B., Orr H.T. and Zoghbi H.Y. (1998). Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148-154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    Defranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 17
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler H. (1997). Activation of the cell death program by inhibition of proteasome function. Proc. Natl. Acad. Sci. USA 94, 855-860.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 855-860
    • Drexler, H.1
  • 20
    • 0002846537 scopus 로고
    • Parkinsonism
    • Rowland L.P. (ed). Williams & Wilkins. Philadelphia.
    • Fahn S. (1995). Parkinsonism. In: Merritt's Textbook of Neurology. 9th ed. Rowland L.P. (ed). Williams & Wilkins. Philadelphia. pp 713-730.
    • (1995) Merritt's Textbook of Neurology. 9th ed , pp. 713-730
    • Fahn, S.1
  • 21
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany M.B. and Bender W.W. (2000). A Drosophila model of Parkinson's disease. Nature 404, 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 22
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany G. and Schreiber S.L. (1998). Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273, 8545-8548.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8545-8548
    • Fenteany, G.1    Schreiber, S.L.2
  • 23
    • 0028136875 scopus 로고
    • A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S Proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell
    • Figueiredo-Pereira M., Berg K. and Wilk S. (1994). A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S Proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell. J. Neurochem. 63, 1578-1581.
    • (1994) J. Neurochem. , vol.63 , pp. 1578-1581
    • Figueiredo-Pereira, M.1    Berg, K.2    Wilk, S.3
  • 26
    • 0033788434 scopus 로고    scopus 로고
    • Rat alpha-synuclein interacts with tat binding protein 1, a component of the 26S proteasomal complex
    • Ghee M., Fournier A. and Mallet J. (2000). Rat alpha-synuclein interacts with tat binding protein 1, a component of the 26S proteasomal complex. J. Neurochem. 75, 2221-2224.
    • (2000) J. Neurochem. , vol.75 , pp. 2221-2224
    • Ghee, M.1    Fournier, A.2    Mallet, J.3
  • 27
    • 0003316846 scopus 로고
    • The neuropathology of Parkinsonian disorders
    • Jankovic J. and Tolosa E. (eds). Williams & Wilkins
    • Gibb W.R.G. (1993). The neuropathology of Parkinsonian disorders. In: Parkinson's Disease and Movement Disorders. 2nd ed. Jankovic J. and Tolosa E. (eds). Williams & Wilkins. pp 254-270.
    • (1993) Parkinson's Disease and Movement Disorders. 2nd ed , pp. 254-270
    • Gibb, W.R.G.1
  • 28
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg M.S. and Lansbury Jr P.T. (2000). Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat. Cell. Biol. 2, E115-E119.
    • (2000) Nat. Cell. Biol. , vol.2
    • Goldberg, M.S.1    Lansbury P.T., Jr.2
  • 29
    • 0020517951 scopus 로고
    • Lewy bodies of Parkinson's disease contain neurofilament antigens
    • Goldman J.E., Yen S.H., Chiu F.C. and Peress N.S. (1983). Lewy bodies of Parkinson's disease contain neurofilament antigens. Science 221, 1082-1084.
    • (1983) Science , vol.221 , pp. 1082-1084
    • Goldman, J.E.1    Yen, S.H.2    Chiu, F.C.3    Peress, N.S.4
  • 32
    • 0033919992 scopus 로고    scopus 로고
    • Lewy bodies in Alzheimer's disease: A neuropathological review of 145 cases using alpha-synuclein immunohistochemistry
    • Hamilton R.L. (2000). Lewy bodies in Alzheimer's disease: A neuropathological review of 145 cases using alpha-synuclein immunohistochemistry. Brain Pathol. 10, 378-384.
    • (2000) Brain Pathol. , vol.10 , pp. 378-384
    • Hamilton, R.L.1
  • 33
    • 0031283220 scopus 로고    scopus 로고
    • The Lewy body variant of Alzheimer disease
    • Hansen L.A. (1997). The Lewy body variant of Alzheimer disease. J. Neural Transm. Suppl. 51, 83-93.
    • (1997) J. Neural Transm. Suppl. , vol.51 , pp. 83-93
    • Hansen, L.A.1
  • 34
    • 0032551656 scopus 로고    scopus 로고
    • Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease
    • Hashimoto M., Shu L.J., Sisk A., Xia Y., Takeda A., Sundsmo M. and Masliah E. (1998). Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease. Brain Res. 799, 301-306.
    • (1998) Brain Res. , vol.799 , pp. 301-306
    • Hashimoto, M.1    Shu, L.J.2    Sisk, A.3    Xia, Y.4    Takeda, A.5    Sundsmo, M.6    Masliah, E.7
  • 35
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. (2001). Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2, 195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 37
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • Ii K., Ito H., Tanaka K. and Hirano A. (1997). Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. 56, 125-131.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 125-131
    • Ii, K.1    Ito, H.2    Tanaka, K.3    Hirano, A.4
  • 38
    • 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. 276, 35661-35664.
    • (2000) J. Biol. Chem. , vol.276 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 39
    • 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
  • 40
    • 0029866793 scopus 로고    scopus 로고
    • Purification and characterization of Lewy bodies from the brains of patients with diffuse Lewy body disease
    • Iwatsubo T., Yamaguchi H., Fujimuro M., Yokosawa H., Ihara Y., Trojanowski J.Q. and Lee V.M. (1996) Purification and characterization of Lewy bodies from the brains of patients with diffuse Lewy body disease. Am. J. Pathol. 148, 1517-1529.
    • (1996) Am. J. Pathol. , vol.148 , pp. 1517-1529
    • Iwatsubo, T.1    Yamaguchi, H.2    Fujimuro, M.3    Yokosawa, H.4    Ihara, Y.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 41
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana N.R., Zemskov E.A., Wang G.H. and Nukina N. (2001) Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet. 10, 1049-1059.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.H.3    Nukina, N.4
  • 42
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J.N., Hanni K.B. and Markesbery W.R. (2000a). Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75, 436-439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 43
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging: Implications for oxidative stress
    • Keller J.N., Hanni K.B. and Markesbery W.R. (2000b). Possible involvement of proteasome inhibition in aging: Implications for oxidative stress. Mech. Ageing Dev. 113, 61-70.
    • (2000) Mech. Ageing Dev. , vol.113 , pp. 61-70
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 44
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • Keller J.N., Huang F.F. and Markesbery W.R. (2000c). Decreased levels of proteasome activity and proteasome expression in aging spinal cord. Neuroscience 98, 149-156.
    • (2000) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 46
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement I.A., Skinner P.J., Kaytor M.D., Yi H., Hersch S.M., Clark H.B., Zoghbi H.Y. and Orr H.T. (1998) Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95, 41-53.
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 48
    • 0036247208 scopus 로고    scopus 로고
    • Parkinson's disease: One biochemical pathway to fit all genes?
    • Kruger R., Eberhardt O., Riess O. and Schulz J.B. (2002). Parkinson's disease: One biochemical pathway to fit all genes? Trends Mol. Med. 8, 236-240.
    • (2002) Trends Mol. Med. , vol.8 , pp. 236-240
    • Kruger, R.1    Eberhardt, O.2    Riess, O.3    Schulz, J.B.4
  • 50
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases
    • Larsen C.N., Krantz B.A. and Wilkinson K.D. (1998). Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases. Biochemistry 37, 3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 51
    • 0036066121 scopus 로고    scopus 로고
    • Autophagy in neurons: A review
    • Larsen K.E. and Sulzer D. (2002). Autophagy in neurons: A review. Histol. Histopathol. 17, 897-908.
    • (2002) Histol. Histopathol , vol.17 , pp. 897-908
    • Larsen, K.E.1    Sulzer, D.2
  • 52
    • 0035037689 scopus 로고    scopus 로고
    • Does an inhibition of the ubiquitin/26S proteasome pathway of protein degradation underlie the pathogenesis of non-familial Alzheimer's disease?
    • Layfield R. (2001) Does an inhibition of the ubiquitin/26S proteasome pathway of protein degradation underlie the pathogenesis of non-familial Alzheimer's disease? Med. Hypotheses 56, 395-399.
    • (2001) Med. Hypotheses , vol.56 , pp. 395-399
    • Layfield, R.1
  • 53
    • 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. (2001). 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
  • 55
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten K., De Vrij F.M., Verhoef L.G., Fischer D.F., Van Leeuwen F.W., Hol E.M., Masucci M.G. and Dantuma N.P. (2002). Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol. 157, 417-427.
    • (2002) J. Cell Biol. , vol.157 , pp. 417-427
    • Lindsten, K.1    De Vrij, F.M.2    Verhoef, L.G.3    Fischer, D.F.4    Van Leeuwen, F.W.5    Hol, E.M.6    Masucci, M.G.7    Dantuma, N.P.8
  • 57
    • 0030962262 scopus 로고    scopus 로고
    • p53-dependent induction of apoptosis by proteasome inhibitors
    • Lopes U., Ernhardt P., Yao R. and Cooper G. (1997). p53-dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem. 272, 12893-12896.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12893-12896
    • Lopes, U.1    Ernhardt, P.2    Yao, R.3    Cooper, G.4
  • 58
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristics of human neurodegenerative diseases
    • Lowe J., McDermott H., Landon M., Mayer R.J. and Wilkinson K.D. (1990). Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristics of human neurodegenerative diseases. J. Pathol. 161, 153-160.
    • (1990) J. Pathol. , vol.161 , pp. 153-160
    • Lowe, J.1    McDermott, H.2    Landon, M.3    Mayer, R.J.4    Wilkinson, K.D.5
  • 60
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah E., Rockenstein E., Veinbergs I., Mallory M., Hashimoto M., Takeda A., Sagara Y., Sisk A. and Mucke L. (2000). Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 287, 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 61
    • 0033923545 scopus 로고    scopus 로고
    • Alpha-synuclein-immunoreactive cortical Lewy bodies are associated with cognitive impairment in Parkinson's disease
    • Mattila P.M., Rinne J.O., Helenius H., Dickson D.W. and Roytta M. (2000) Alpha-synuclein-immunoreactive cortical Lewy bodies are associated with cognitive impairment in Parkinson's disease. Acta Neuropathol. (Berl) 100, 285-290.
    • (2000) Acta Neuropathol. (Berl) , vol.100 , pp. 285-290
    • Mattila, P.M.1    Rinne, J.O.2    Helenius, H.3    Dickson, D.W.4    Roytta, M.5
  • 62
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught K. 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.1    Jenner, P.2
  • 64
    • 0037025111 scopus 로고    scopus 로고
    • Selective loss of 20S proteasome-subunits in the substantia nigra pars compacta in Parkinson's disease
    • McNaught K.S., Belizaire R., Jenner P. and Olanow C.W. and Isacson O. (2002a). Selective loss of 20S proteasome-subunits in the substantia nigra pars compacta in Parkinson's disease. Neurosci. Lett. 326, 155-158.
    • (2002) Neurosci. Lett. , vol.326 , pp. 155-158
    • McNaught, K.S.1    Belizaire, R.2    Jenner, P.3    Olanow, C.W.4    Isacson, O.5
  • 65
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • McNaught K.S., Mytilineou C., Jnobaptiste R., Yabut J., Shashidharan P., Jenner P. and Olanow C.W. (2002b). Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. J. Neurochem. 81, 301-306.
    • (2002) J. Neurochem. , vol.81 , pp. 301-306
    • McNaught, K.S.1    Mytilineou, C.2    Jnobaptiste, R.3    Yabut, J.4    Shashidharan, P.5    Jenner, P.6    Olanow, C.W.7
  • 66
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N. and Crews C.M. (1999). Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96, 10403-10897.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10897
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 67
    • 0034726119 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington's disease patients and transgenic mouse models
    • Mezey E., Reddy P.H., Dehejia A., Young T.A., Polymeropoulos M.H., Brownstein M.J. and Tagle D.A. (2000). Alpha-synuclein immunoreactivity of huntingtin polyglutamine aggregates in striatum and cortex of Huntington's disease patients and transgenic mouse models. Neurosci. Lett. 28, 289, 29-32.
    • (2000) Neurosci. Lett. , vol.28 , Issue.289 , pp. 29-32
    • Mezey, E.1    Reddy, P.H.2    Dehejia, A.3    Young, T.A.4    Polymeropoulos, M.H.5    Brownstein, M.J.6    Tagle, D.A.7
  • 68
    • 0032513291 scopus 로고    scopus 로고
    • Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2
    • Monney L., Otter I., Olivier R., Ozer H.L., Haas A.L., Omura S. and Borner C. (1998). Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2. J. Biol. Chem. 273, 6121-6131.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6121-6131
    • Monney, L.1    Otter, I.2    Olivier, R.3    Ozer, H.L.4    Haas, A.L.5    Omura, S.6    Borner, C.7
  • 69
    • 0031822077 scopus 로고    scopus 로고
    • A review of Lewy body disease, an emerging concept of cortical dementia
    • Papka M., Rubio A. and Schiffer R.B. (1998). A review of Lewy body disease, an emerging concept of cortical dementia. J. Neuropsychiatry Clin. Neurosci. 10, 267-279.
    • (1998) J. Neuropsychiatry Clin. Neurosci. , vol.10 , pp. 267-279
    • Papka, M.1    Rubio, A.2    Schiffer, R.B.3
  • 70
    • 0030694346 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors and dominant negative cyclin-dependent kinase 4 and 6 promote survival of NGF-deprived sympathetic neurons
    • Park D.S., Levine B., Ferrari G. and Greene L.A. (1997). Cyclin-dependent kinase inhibitors and dominant negative cyclin-dependent kinase 4 and 6 promote survival of NGF-deprived sympathetic neurons. J. Neurosci. 17, 8975-8983.
    • (1997) J. Neurosci. , vol.17 , pp. 8975-8983
    • Park, D.S.1    Levine, B.2    Ferrari, G.3    Greene, L.A.4
  • 71
    • 0342393043 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells
    • Pasquini L.A., Moreno M.B., Adamo A.M., Pasquini J.M. and Soto E. (2000). Lactacystin, a specific inhibitor of the proteasome, induces apoptosis and activates caspase-3 in cultured cerebellar granule cells. J. Neurosci. Res. 59, 601-611.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 601-611
    • Pasquini, L.A.1    Moreno, M.B.2    Adamo, A.M.3    Pasquini, J.M.4    Soto, E.5
  • 72
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart C.M. (2000). Ubiquitin in chains. Trends Biochem. Sci. 25, 544-548.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 73
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. (2001). Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 74
    • 0021929906 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides
    • Pickart C.M. and Rose I.A. (1985). Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J. Biol. Chem. 260, 7903-7910
    • (1985) J. Biol. Chem. , vol.260 , pp. 7903-7910
    • Pickart, C.M.1    Rose, I.A.2
  • 75
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26 S proteasome by polyubiquitin chains synthesized to have defined lengths
    • Piotrowski J., Beal R., Hoffman L., Wilkinson K.D., Cohen R.E. and Pickart C.M. (1997). Inhibition of the 26 S proteasome by polyubiquitin chains synthesized to have defined lengths. J. Biol. Chem. 272, 23712-23716.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23712-23716
    • Piotrowski, J.1    Beal, R.2    Hoffman, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 77
    • 0000991680 scopus 로고    scopus 로고
    • Proteasome inhibitors induce cytochrome c-caspase-3-like protease-mediated apoptosis in cultured cortical neurons
    • Qiu J.H., Asai A., Chi S., Saito N., Hamada H. and Kirino T. (2000). Proteasome inhibitors induce cytochrome c-caspase-3-like protease-mediated apoptosis in cultured cortical neurons. J. Neurosci. 20, 259-265.
    • (2000) J. Neurosci. , vol.20 , pp. 259-265
    • Qiu, J.H.1    Asai, A.2    Chi, S.3    Saito, N.4    Hamada, H.5    Kirino, T.6
  • 78
    • 0036432029 scopus 로고    scopus 로고
    • Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination
    • Rideout H.J. and Stefanis L. (2002) Proteasomal inhibition-induced inclusion formation and death in cortical neurons require transcription and ubiquitination. Mol. Cell. Neurosci. 21, 223-238.
    • (2002) Mol. Cell. Neurosci. , vol.21 , pp. 223-238
    • Rideout, H.J.1    Stefanis, L.2
  • 79
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/a-synuclein-immunoreactive inclusions in PC12 cells
    • Rideout H.J., Larsen K.L., Sulzer D. and Stefanis L (2001). Proteasomal inhibition leads to formation of ubiquitin/a-synuclein-immunoreactive inclusions in PC12 cells. J. Neurochem. 78, 899-908.
    • (2001) J. Neurochem. , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.L.2    Sulzer, D.3    Stefanis, L.4
  • 80
    • 0037442820 scopus 로고    scopus 로고
    • Cyclin dependent kinase activity is required for apoptotic death but not inclusion formation in cortical neurons following proteasomal inhibition
    • (in press)
    • Rideout H.J., Wang Q., Park D.S. and Stefanis L. (2003). Cyclin dependent kinase activity is required for apoptotic death but not inclusion formation in cortical neurons following proteasomal inhibition. J. Neurosci. (in press).
    • (2003) J. Neurosci.
    • Rideout, H.J.1    Wang, Q.2    Park, D.S.3    Stefanis, L.4
  • 82
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F., Finbeiner S., Devy D. and Greenberg M. (1998). Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finbeiner, S.2    Devy, D.3    Greenberg, M.4
  • 86
    • 0032475877 scopus 로고    scopus 로고
    • Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial?
    • Sisodia S.S. (1998). Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial? Cell 95, 1-4.
    • (1998) Cell , vol.95 , pp. 1-4
    • Sisodia, S.S.1
  • 89
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini M.G., Crowther R.A., Jakes R., Hasegawa M. and Goedert M. (1998). Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. USA 95, 6469-6473.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 90
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant, but not wild type, α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen K.L., Rideout H.J., Sulzer D.S. and Greene L.A. (2001a). Expression of A53T mutant, but not wild type, α-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.L.2    Rideout, H.J.3    Sulzer, D.S.4    Greene, L.A.5
  • 91
    • 0035109875 scopus 로고    scopus 로고
    • Synuclein-1 is selectively upregulated in response to NGF treatment in PC12 cells
    • Stefanis L., Kholodilov N., Rideout H.J., Burke R.E. an Greene L.A. (2001b). Synuclein-1 is selectively upregulated in response to NGF treatment in PC12 cells. J. Neurochem. 76, 1165-1176.
    • (2001) J. Neurochem. , vol.76 , pp. 1165-1176
    • Stefanis, L.1    Kholodilov, N.2    Rideout, H.J.3    Burke, R.E.4    Greene, L.A.5
  • 93
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower J.S., Hoffman L., Rechsteiner M. and Pickart C.M. (2000.) Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94-102.
    • (2000) EMBO J , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 94
    • 0031762949 scopus 로고    scopus 로고
    • Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia
    • Trojanowski J.Q., Goedert M., Iwatsubo T. and Lee V.M. (1998). Fatal attractions: Abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia. Cell Death Differ. 5, 832-837.
    • (1998) Cell Death Differ. , vol.5 , pp. 832-837
    • Trojanowski, J.Q.1    Goedert, M.2    Iwatsubo, T.3    Lee, V.M.4
  • 96
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • 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. USA 97, 13354-13359.
    • (2000) Proc. Natl. Acad. Sci. USA , 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


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