메뉴 건너뛰기




Volumn 16, Issue 11, 2002, Pages 2136-2148

Aggresome-related biogenesis of Lewy bodies

Author keywords

synuclein; tubulin; Centrosome; Parkinson's disease; Proteasome

Indexed keywords

CELL PROTEIN; GAMMA TUBULIN; HEAT SHOCK PROTEIN 70; PERICENTRIN; PROTEASOME; PROTEIN ANTIBODY; PROTEIN PA28; PROTEIN PA700; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 0036456584     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1460-9568.2002.02301.x     Document Type: Article
Times cited : (242)

References (63)
  • 1
    • 0030805622 scopus 로고    scopus 로고
    • A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease
    • Alam, Z.I., Daniel, S.E., Lees, A.J., Marsden, D.C., Jenner, P. & Halliwell, B. (1997) A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J. Neurochem., 69, 1326-1329.
    • (1997) J. Neurochem. , vol.69 , pp. 1326-1329
    • Alam, Z.I.1    Daniel, S.E.2    Lees, A.J.3    Marsden, D.C.4    Jenner, P.5    Halliwell, B.6
  • 2
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a drosophila model of Parkinson's disease
    • Auluck, P.K., Chan, E., Trojanowski, J.Q., Lee, V. & Bonini, N.M. (2002) Chaperone suppression of alpha-synuclein toxicity in a drosophila model of Parkinson's disease. Science, 295, 865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, E.2    Trojanowski, J.Q.3    Lee, V.4    Bonini, N.M.5
  • 3
    • 0032930953 scopus 로고    scopus 로고
    • Microtubules and neuronal polarity: Lessons from mitosis
    • Baas, P.W. (1999) Microtubules and neuronal polarity: Lessons from mitosis. Neuron, 22, 23-31.
    • (1999) Neuron , vol.22 , pp. 23-31
    • Baas, P.W.1
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F., Sampat, R.M. & 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
  • 5
    • 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. & Dawson, T.M. (2001) Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease. Nature Med., 7, 1144-1150.
    • (2001) Nature 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
  • 6
    • 0028218025 scopus 로고
    • Pericentrin, a highly conserved centrosome protein involved in microtubule organization
    • Doxsey, S.J., Stein, P., Evans, L., Calarco, P.D. & Kirschner, M. (1994) Pericentrin, a highly conserved centrosome protein involved in microtubule organization. Cell, 76, 639-650.
    • (1994) Cell , vol.76 , pp. 639-650
    • Doxsey, S.J.1    Stein, P.2    Evans, L.3    Calarco, P.D.4    Kirschner, M.5
  • 7
    • 0032915723 scopus 로고    scopus 로고
    • Numerous and widespread alpha-synuclein-negative Lewy bodies in an asymptomatic patient
    • van Duinen, S.G., Lammers, G.J., Maat-Schieman, M.L. & Roos, R.A. (1999) Numerous and widespread alpha-synuclein-negative Lewy bodies in an asymptomatic patient. Acta Neuropathol. (Berl.), 97, 533-539.
    • (1999) Acta Neuropathol. (Berl.) , vol.97 , pp. 533-539
    • Van Duinen, S.G.1    Lammers, G.J.2    Maat-Schieman, M.L.3    Roos, R.A.4
  • 8
    • 0035939105 scopus 로고    scopus 로고
    • The expression of mRNAs for the proteasome complex is developmentally regulated in the rat mesencephalon
    • El-Khodor, B.F., Kholodilov, N.G., Yarygina, O. & Burke, R.E. (2001) The expression of mRNAs for the proteasome complex is developmentally regulated in the rat mesencephalon. Brain Res. Dev. Brain Res., 129, 47-56.
    • (2001) Brain Res. Dev. Brain Res. , vol.129 , pp. 47-56
    • El-Khodor, B.F.1    Kholodilov, N.G.2    Yarygina, O.3    Burke, R.E.4
  • 9
    • 0034614416 scopus 로고    scopus 로고
    • Activity and regulation of the centrosome-associated proteasome
    • Fabunmi, R.P., Wigley, W.C., Thomas, P.J. & DeMartino, G.N. (2000) Activity and regulation of the centrosome-associated proteasome. J. Biol. Chem., 275, 409-413.
    • (2000) J. Biol. Chem. , vol.275 , pp. 409-413
    • Fabunmi, R.P.1    Wigley, W.C.2    Thomas, P.J.3    DeMartino, G.N.4
  • 10
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany, G. & 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
  • 11
    • 0030606288 scopus 로고    scopus 로고
    • Pathological lesions of Alzheimer's disease and dementia with Lewy bodies brains exhibit immunoreactivity to an ATPase that is a regulatory subunit of the 26S proteasome
    • Fergusson, J., Landon, M., Lowe, J., Dawson, S.P., Layfield, R., Hanger, D.P. & Mayer, R.J. (1996) Pathological lesions of Alzheimer's disease and dementia with Lewy bodies brains exhibit immunoreactivity to an ATPase that is a regulatory subunit of the 26S proteasome. Neurosci Lett., 219, 167-170.
    • (1996) Neurosci Lett. , vol.219 , pp. 167-170
    • Fergusson, J.1    Landon, M.2    Lowe, J.3    Dawson, S.P.4    Layfield, R.5    Hanger, D.P.6    Mayer, R.J.7
  • 12
    • 0031962268 scopus 로고    scopus 로고
    • Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay
    • Floor, E. & Wetzel, M.G. (1998) Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay. J. Neurochem., 70, 268-275.
    • (1998) J. Neurochem. , vol.70 , pp. 268-275
    • Floor, E.1    Wetzel, M.G.2
  • 13
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno, L.S. (1996) Neuropathology of Parkinson's disease. J. Neuropathol. Exp. Neurol., 55, 259-272.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 14
    • 0035680611 scopus 로고    scopus 로고
    • Aggresome formation in liver cells in response to different toxic mechanisms: Role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin
    • French, B.A., van Leeuwen, F., Riley, N.E., Yuan, Q.X., Bardag-Gorce, F., Gaal, K., Lue, Y.H., Marceau, N. & French, S.W. (2001) Aggresome formation in liver cells in response to different toxic mechanisms: Role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin. Exp. Mol. Pathol., 71, 241-246.
    • (2001) Exp. Mol. Pathol. , vol.71 , pp. 241-246
    • French, B.A.1    Van Leeuwen, F.2    Riley, N.E.3    Yuan, Q.X.4    Bardag-Gorce, F.5    Gaal, K.6    Lue, Y.H.7    Marceau, N.8    French, S.W.9
  • 15
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • Fujimuro, M., Sawada, H. & Yokosawa, H. (1994) Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett., 349, 173-180.
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 16
    • 0035050618 scopus 로고    scopus 로고
    • Caretaker or undertaker? The role of the proteasome in aging
    • Gaczynska, M., Osmulski, P.A. & Ward, W.F. (2001) Caretaker or undertaker? The role of the proteasome in aging. Mech. Ageing Dev., 122, 235-254.
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 235-254
    • Gaczynska, M.1    Osmulski, P.A.2    Ward, W.F.3
  • 18
    • 0023898945 scopus 로고
    • The relevance of the Lewy body to the pathogenesis of idiopathic Parkinson's disease
    • Gibb, W.R. & Lees, A.J. (1988) The relevance of the Lewy body to the pathogenesis of idiopathic Parkinson's disease. J. Neurol. Neurosurg. Psychiatry, 51, 745-752.
    • (1988) J. Neurol. Neurosurg. Psychiatry , vol.51 , pp. 745-752
    • Gibb, W.R.1    Lees, A.J.2
  • 19
    • 0343527226 scopus 로고    scopus 로고
    • alpha-Synuclein immunoreactivity in dementia with Lewy bodies: Morphological staging and comparison with ubiquitin immunostaining
    • Gomez-Tortosa, E., Newell, K., Irizarry, M.C., Sanders, J.L. & Hyman, B.T. (2000) alpha-Synuclein immunoreactivity in dementia with Lewy bodies: Morphological staging and comparison with ubiquitin immunostaining. Acta Neuropathol. (Berl.), 99, 352-357.
    • (2000) Acta Neuropathol. (Berl.) , vol.99 , pp. 352-357
    • Gomez-Tortosa, E.1    Newell, K.2    Irizarry, M.C.3    Sanders, J.L.4    Hyman, B.T.5
  • 21
    • 0030059868 scopus 로고    scopus 로고
    • L-DOPA up-regulates glutathione and protects mesencephalic cultures against oxidative stress
    • Han, S.K., Mytilineou, C. & Cohen, G. (1996) L-DOPA up-regulates glutathione and protects mesencephalic cultures against oxidative stress. J. Neurochem., 66, 501-510.
    • (1996) J. Neurochem. , vol.66 , pp. 501-510
    • Han, S.K.1    Mytilineou, C.2    Cohen, G.3
  • 22
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. & Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: From nascent chain to folded protein. Science, 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 23
    • 0036500862 scopus 로고    scopus 로고
    • Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: Relevance to Huntington's disease
    • Hoffner, G., Kahlem, P. & Djian, P. (2002) Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: Relevance to Huntington's disease. J. Cell Sci., 115, 941-948.
    • (2002) J. Cell Sci. , vol.115 , pp. 941-948
    • Hoffner, G.1    Kahlem, P.2    Djian, P.3
  • 24
    • 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. & 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
  • 25
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • Jenner, P. & Olanow, C.W. (1998) Understanding cell death in Parkinson's disease. Ann. Neurol., 44, S72-S84.
    • (1998) Ann. Neurol. , vol.44
    • Jenner, P.1    Olanow, C.W.2
  • 26
    • 0032824809 scopus 로고    scopus 로고
    • Axonal transport of synucleins is mediated by all rate components
    • Jensen, P.H., Li, J.Y., Dahlstrom, A. & Dotti, C.G. (1999) Axonal transport of synucleins is mediated by all rate components. Eur. J. Neurosci., 11, 3369-3376.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 3369-3376
    • Jensen, P.H.1    Li, J.Y.2    Dahlstrom, A.3    Dotti, C.G.4
  • 27
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L. & Kopito, R.R. (1998) Aggresomes: A cellular response to misfolded proteins. J. Cell Biol., 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 28
    • 0033621398 scopus 로고    scopus 로고
    • Aberrant protein deposition and neurological disease
    • Kaytor, M.D. & Warren, S.T. (1999) Aberrant protein deposition and neurological disease. J. Biol. Chem., 274, 37507-37510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37507-37510
    • Kaytor, M.D.1    Warren, S.T.2
  • 29
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R.R. (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol., 10, 524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 30
    • 0030814627 scopus 로고    scopus 로고
    • Synaptically coupled central nervous system neurons lack centrosomal gamma-tubulin
    • Leask, A., Obrietan, K. & Stearns, T. (1997) Synaptically coupled central nervous system neurons lack centrosomal gamma-tubulin. Neurosci. Lett., 229, 17-20.
    • (1997) Neurosci. Lett. , vol.229 , pp. 17-20
    • Leask, A.1    Obrietan, K.2    Stearns, T.3
  • 32
    • 0034309848 scopus 로고    scopus 로고
    • Nuclear magnetic relaxation dispersion profiles of substantia nigra pars compacta in Parkinson's disease patients are consistent with protein aggregation
    • Lopiano, L., Fasano, M., Giraudo, S., Digilio, G., Koenig, S.H., Torre, E., Bergamasco, B. & Aime, S. (2000) Nuclear magnetic relaxation dispersion profiles of substantia nigra pars compacta in Parkinson's disease patients are consistent with protein aggregation. Neurochem. Int., 37, 331-336.
    • (2000) Neurochem. Int. , vol.37 , pp. 331-336
    • Lopiano, L.1    Fasano, M.2    Giraudo, S.3    Digilio, G.4    Koenig, S.H.5    Torre, E.6    Bergamasco, B.7    Aime, S.8
  • 33
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
    • Lowe, J., McDermott, H., Landon, M., Mayer, R.J. & Wilkinson, K.D. (1990) Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic 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
  • 34
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma, J. & Lindquist, S. (2001) Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl Acad. Sci. USA, 98, 14955-14960.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 35
    • 0028297514 scopus 로고
    • Multicatalytic proteinase is associated with characteristic oval structures in cortical Lewy bodies: An immunocytochemical study with light and electron microscopy
    • Masaki, T., Ishiura, S., Sugita, H. & Kwak, S. (1994) Multicatalytic proteinase is associated with characteristic oval structures in cortical Lewy bodies: An immunocytochemical study with light and electron microscopy. J. Neurol. Sci., 122, 127-134.
    • (1994) J. Neurol. Sci. , vol.122 , pp. 127-134
    • Masaki, T.1    Ishiura, S.2    Sugita, H.3    Kwak, S.4
  • 36
    • 0037025111 scopus 로고    scopus 로고
    • Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease
    • McNaught, K.S., Belezaire, R., Jenner, P., Olanow, C.W. & Isacson, O. (2002a) Selective loss of 20S proteasome alpha-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    Belezaire, R.2    Jenner, P.3    Olanow, C.W.4    Isacson, O.5
  • 38
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught, K.S. & 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
  • 42
    • 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
  • 48
    • 0036132046 scopus 로고    scopus 로고
    • Occurrence of glutamate receptor subunit 1-containing aggresome-like structures during normal development of rat spinal cord interneurons
    • Serrando, M., Casanovas, A. & Esquerda, J.E. (2002) Occurrence of glutamate receptor subunit 1-containing aggresome-like structures during normal development of rat spinal cord interneurons. J. Comp. Neurol., 442, 23-34.
    • (2002) J. Comp. Neurol. , vol.442 , pp. 23-34
    • Serrando, M.1    Casanovas, A.2    Esquerda, J.E.3
  • 49
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M.Y. & Goldberg, A.L. (2001) Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron, 29, 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 53
    • 0037177250 scopus 로고    scopus 로고
    • Jr (2002) Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • Shtilerman, M.D., Ding, T.T. & Lansbury, P.T. Jr (2002) Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry, 41, 3855-3860.
    • Biochemistry , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury, P.T.3
  • 54
    • 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. & 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
  • 55
    • 0025849047 scopus 로고
    • Gamma-tubulin is a highly conserved component of the centrosome
    • Stearns, T., Evans, L. & Kirschner, M. (1991) Gamma-tubulin is a highly conserved component of the centrosome. Cell, 65, 825-836.
    • (1991) Cell , vol.65 , pp. 825-836
    • Stearns, T.1    Evans, L.2    Kirschner, M.3
  • 56
    • 0035976835 scopus 로고    scopus 로고
    • alpha-Synuclein metabolism and aggregation is linged to ubiqutin-independent degradation by the proteasome
    • 25504
    • Tofaris, G.K., Layfield, R. & Spillantini, M.G. (2001) alpha-Synuclein metabolism and aggregation is linged to ubiqutin-independent degradation by the proteasome. FEBS Lett., 25504, 1-5.
    • (2001) FEBS Lett. , pp. 1-5
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 57
    • 0035824651 scopus 로고    scopus 로고
    • Sensitivity of mammalian cells expressing mutant ubiquitin to protein damaging agents
    • Tsirigotis, M., Zhang, M., Chiu, R.K., Wouters, B.G. & Gray, D.A. (2001) Sensitivity of mammalian cells expressing mutant ubiquitin to protein damaging agents. J. Biol. Chem, 276, 46073-46078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46073-46078
    • Tsirigotis, M.1    Zhang, M.2    Chiu, R.K.3    Wouters, B.G.4    Gray, D.A.5
  • 58
    • 0037181497 scopus 로고    scopus 로고
    • Accelerated alpha-synuclein fibrillation in crowded milieu
    • Uversky, V.N.E.M.C., Bower, K.S., Li, J. & Fink, A.L. (2002) Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett., 515, 99-103.
    • (2002) FEBS Lett. , vol.515 , pp. 99-103
    • Uversky, V.N.E.M.C.1    Bower, K.S.2    Li, J.3    Fink, A.L.4
  • 59
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P. & Baumeister, W. (1999) The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu. Rev. Biochem., 68, 1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 60
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lueder, G., Lehrach, H. & Wanker, E.E. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell, 12, 1393-1407.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 63
    • 0031662791 scopus 로고    scopus 로고
    • The Golgi apparatus and the centrosome are localized to the sites of newly emerging axons in cerebellar granule neurons in vitro
    • Zmuda, J.F. & Rivas, R.J. (1998) The Golgi apparatus and the centrosome are localized to the sites of newly emerging axons in cerebellar granule neurons in vitro. Cell Motil. Cytoskeleton, 41, 18-38.
    • (1998) Cell Motil. Cytoskeleton , vol.41 , pp. 18-38
    • Zmuda, J.F.1    Rivas, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.