메뉴 건너뛰기




Volumn 20, Issue 1, 2004, Pages 14-28

Decrease of Hsp25 protein expression precedes degeneration of motoneurons in ALS-SOD1 mice

Author keywords

ALS; Heat shock protein; Molecular chaperone; Motoneuron; Neurodegenerative diseases

Indexed keywords

CELLULOSE ACETATE; HEAT SHOCK PROTEIN 25; MESSENGER RNA; SUPEROXIDE DISMUTASE;

EID: 3142692478     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1460-9568.2004.03430.x     Document Type: Article
Times cited : (78)

References (55)
  • 1
    • 0037827756 scopus 로고    scopus 로고
    • The neuroprotective effects of heat shock protein 27 overexpression in transgenic animals against kainate-induced seizures and hippocampal cell death
    • Akbar, M.T., Lundberg, A.M., Liu, K., Vidyadaran, S., Wells, K.E., Dolatshad, H., Wynn, S., Wells, D.J., Latchman, D.S. & de Belleroche, J. (2003) The neuroprotective effects of heat shock protein 27 overexpression in transgenic animals against kainate-induced seizures and hippocampal cell death. J. Biol. Chem., 278, 19956-19965.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19956-19965
    • Akbar, M.T.1    Lundberg, A.M.2    Liu, K.3    Vidyadaran, S.4    Wells, K.E.5    Dolatshad, H.6    Wynn, S.7    Wells, D.J.8    Latchman, D.S.9    De Belleroche, J.10
  • 6
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening, W., Roy, J., Giasson, B., Figlewicz, D.A., Mushynski, W.E. & Durham, H.D. (1999) Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J. Neurochem., 72, 693-699.
    • (1999) J. Neurochem. , vol.72 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 10
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham, H.D., Roy, J., Dong, L. & Figlewicz, D.A. (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol., 56, 523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 11
    • 0037077277 scopus 로고    scopus 로고
    • S-thiolation of HSP27 regulates its multimeric aggregate size independently of phosphorylation
    • Eaton, P., Fuller, W. & Shattock, M.J. (2002) S-thiolation of HSP27 regulates its multimeric aggregate size independently of phosphorylation. J. Biol. Chem., 277, 21189-21196.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21189-21196
    • Eaton, P.1    Fuller, W.2    Shattock, M.J.3
  • 12
    • 0033591453 scopus 로고    scopus 로고
    • The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species
    • Ehrnsperger, M., Lilie, H., Gaestel, M. & Buchner, J. (1999) The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species. J. Biol. Chem., 274, 14867-14874.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14867-14874
    • Ehrnsperger, M.1    Lilie, H.2    Gaestel, M.3    Buchner, J.4
  • 14
    • 0041344579 scopus 로고    scopus 로고
    • Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria
    • Field, L.S., Furukawa, Y., O'Halloran, T.V. & Culotta, V.C. (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J. Biol. Chem., 278, 28052-28059.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28052-28059
    • Field, L.S.1    Furukawa, Y.2    O'Halloran, T.V.3    Culotta, V.C.4
  • 15
    • 0035437866 scopus 로고    scopus 로고
    • Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis
    • Guegan, C., Vila, M., Rosoklija, G., Hays, A.P. & Przedborski, S. (2001) Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis. J. Neurosci., 21, 6569-6576.
    • (2001) J. Neurosci. , vol.21 , pp. 6569-6576
    • Guegan, C.1    Vila, M.2    Rosoklija, G.3    Hays, A.P.4    Przedborski, S.5
  • 17
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes
    • Ito, H., Kamei, K., Iwamoto, I., Inaguma, Y., Garcia-Mata, R., Sztul, E. & Kato, K. (2002) Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes. J. Biochem. (Tokyo), 131, 593-603.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Garcia-Mata, R.5    Sztul, E.6    Kato, K.7
  • 18
    • 0027742866 scopus 로고
    • Alpha B-crystallin and 27-kD heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers
    • Iwaki, T., Iwaki, A., Tateishi, J., Sakaki, Y. & Goldman, J.E. (1993) Alpha B-crystallin and 27-kD heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. Am. J. Pathol., 143, 487-495.
    • (1993) Am. J. Pathol. , vol.143 , pp. 487-495
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Sakaki, Y.4    Goldman, J.E.5
  • 19
    • 3142675385 scopus 로고    scopus 로고
    • Mutant SOD1 protein accumulates in vacuolated mitochondria, in cytosolic filamentous aggregates, and in periaxonal glia in ALS-SOD1 mouse spinal cord
    • Jaarsma, D. & Haasdijk, E.D. (2001) Mutant SOD1 protein accumulates in vacuolated mitochondria, in cytosolic filamentous aggregates, and in periaxonal glia in ALS-SOD1 mouse spinal cord. Soc. Neurosci. Abstr., 31, 984.982.
    • (2001) Soc. Neurosci. Abstr. , vol.31 , pp. 984982
    • Jaarsma, D.1    Haasdijk, E.D.2
  • 20
    • 0034520591 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial degeneration, axonal degeneration and premature motoneuron death, and accelerates the development of motoneuron disease in mice expressing fALS-mutant SOD1
    • Jaarsma, D., Haasdijk, E., Grashorn, J.A.C., Van Duijn, W., Verspaget, H., London, J. & Holstege, J.C. (2000) Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial degeneration, axonal degeneration and premature motoneuron death, and accelerates the development of motoneuron disease in mice expressing fALS-mutant SOD1. Neurobiol. Dis., 7, 623-643.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 623-643
    • Jaarsma, D.1    Haasdijk, E.2    Grashorn, J.A.C.3    Van Duijn, W.4    Verspaget, H.5    London, J.6    Holstege, J.C.7
  • 21
    • 0034821922 scopus 로고    scopus 로고
    • CuZn superoxide dismutase (SOD1) accumulate in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis (ALS)-linked SOD1 mutations
    • Jaarsma, D., Rognoni, F., Van Duijn, W., Verspaget, H., Haasdijk, E.D. & Holstege, J.C. (2001) CuZn superoxide dismutase (SOD1) accumulate in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis (ALS)-linked SOD1 mutations. Acta Neuropathol., 102, 293-305.
    • (2001) Acta Neuropathol. , vol.102 , pp. 293-305
    • Jaarsma, D.1    Rognoni, F.2    Van Duijn, W.3    Verspaget, H.4    Haasdijk, E.D.5    Holstege, J.C.6
  • 23
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston, J.A., Dalton, M.J., Gurney, M.E. & Kopito, R.R. (2000) Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl Acad. Sci. USA, 97, 12571-12576.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 25
    • 0036716317 scopus 로고    scopus 로고
    • Innervation-dependent phosphorylation and accumulation of alphaB-crystallin and Hsp27 as insoluble complexes in disused muscle
    • Kato, K., Ito, H., Kamei, K., Iwamoto, I. & Inaguma, Y. (2002) Innervation-dependent phosphorylation and accumulation of alphaB-crystallin and Hsp27 as insoluble complexes in disused muscle. FASEB J., 16, 1432-1434.
    • (2002) FASEB J. , vol.16 , pp. 1432-1434
    • Kato, K.1    Ito, H.2    Kamei, K.3    Iwamoto, I.4    Inaguma, Y.5
  • 26
    • 0033026002 scopus 로고    scopus 로고
    • Responses of heat shock proteins hsp27, alphaB-crystallin, and hsp70 in rat brain after kainic acid-induced seizure activity
    • Kato, K., Katoh-Semba, R., Takeuchi, I.K., Ito, H. & Kamei, K. (1999) Responses of heat shock proteins hsp27, alphaB-crystallin, and hsp70 in rat brain after kainic acid-induced seizure activity. J. Neurochem., 73, 229-236.
    • (1999) J. Neurochem. , vol.73 , pp. 229-236
    • Kato, K.1    Katoh-Semba, R.2    Takeuchi, I.K.3    Ito, H.4    Kamei, K.5
  • 27
    • 0028956899 scopus 로고
    • Immunohistochemical localization of the low molecular weight stress protein HSP27 following focal cerebral ischemia in the rat
    • Kato, H., Kogure, K., Liu, X.H., Araki, T., Kato, K. & Itoyama, Y. (1995) Immunohistochemical localization of the low molecular weight stress protein HSP27 following focal cerebral ischemia in the rat. Brain. Res., 679, 1-7.
    • (1995) Brain. Res. , vol.679 , pp. 1-7
    • Kato, H.1    Kogure, K.2    Liu, X.H.3    Araki, T.4    Kato, K.5    Itoyama, Y.6
  • 28
    • 0031238776 scopus 로고    scopus 로고
    • A differential and time dependent decrease in AMPA-type glutamate receptor subunits in spinal motoneurons after sciatic nerve injury
    • Kennis, J.H.H. & Holstege, J.C. (1997) A differential and time dependent decrease in AMPA-type glutamate receptor subunits in spinal motoneurons after sciatic nerve injury. Exp. Neurol., 147, 18-27.
    • (1997) Exp. Neurol. , vol.147 , pp. 18-27
    • Kennis, J.H.H.1    Holstege, J.C.2
  • 29
    • 0038707391 scopus 로고    scopus 로고
    • Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: Evaluation of oxidative hypotheses
    • Liochev, S.I. & Fridovich, I. (2003) Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: evaluation of oxidative hypotheses. Free Radic. Biol. Med., 34, 1383-1389.
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1383-1389
    • Liochev, S.I.1    Fridovich, I.2
  • 30
    • 0030603146 scopus 로고    scopus 로고
    • Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells
    • Loktionova, S.A., Ilyinskaya, O.P., Gabai, V.L. & Kabakov, A.E. (1996) Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells. FEBS Lett., 392, 100-104.
    • (1996) FEBS Lett. , vol.392 , pp. 100-104
    • Loktionova, S.A.1    Ilyinskaya, O.P.2    Gabai, V.L.3    Kabakov, A.E.4
  • 31
    • 0032604157 scopus 로고    scopus 로고
    • Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis
    • Lyons, T.J., Gralla, E.B. & Valentine, J.S. (1999) Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis. Met. Ions Biol. Syst., 36, 125-177.
    • (1999) Met. Ions Biol. Syst. , vol.36 , pp. 125-177
    • Lyons, T.J.1    Gralla, E.B.2    Valentine, J.S.3
  • 32
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
    • Mehlen, P., Schulze-Osthoff, K. & Arrigo, A.P. (1996) Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J. Biol. Chem., 271, 16510-16514.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 34
    • 0032506695 scopus 로고    scopus 로고
    • Role of heat shock protein Hsp25 in the response of the orofacial nuclei motor system to physiological stress
    • Murashov, A.K., Talebian, S. & Wolgemuth, D.J. (1998) Role of heat shock protein Hsp25 in the response of the orofacial nuclei motor system to physiological stress. Mol. Brain Res., 63, 14-24.
    • (1998) Mol. Brain Res. , vol.63 , pp. 14-24
    • Murashov, A.K.1    Talebian, S.2    Wolgemuth, D.J.3
  • 35
    • 0038452604 scopus 로고    scopus 로고
    • Expression of the activating transcription factor 3 prevents c-Jun N-terminal kinase-induced neuronal death by promoting heat shock protein 27 expression and Akt activation
    • Nakagomi, S., Suzuki, Y., Namikawa, K., Kiryu-Seo, S. & Kiyama, H. (2003) Expression of the activating transcription factor 3 prevents c-Jun N-terminal kinase-induced neuronal death by promoting heat shock protein 27 expression and Akt activation. J. Neurosci., 23, 5187-5196.
    • (2003) J. Neurosci. , vol.23 , pp. 5187-5196
    • Nakagomi, S.1    Suzuki, Y.2    Namikawa, K.3    Kiryu-Seo, S.4    Kiyama, H.5
  • 36
    • 0037173038 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: A proposed mechanism
    • Okado-Matsumoto, A. & Fridovich, I. (2002) Amyotrophic lateral sclerosis: a proposed mechanism. Proc. Natl Acad. Sci. USA, 99, 9010-9014.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9010-9014
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 37
    • 0030561264 scopus 로고    scopus 로고
    • Expression of the 27 000 mol. wt heat shock protein following kainic acid-induced status epilepticus in the rat
    • Plumier, J.C., Armstrong, J.N., Landry, J., Babity, J.M., Robertson, H.A. & Currie, R.W. (1996) Expression of the 27 000 mol. wt heat shock protein following kainic acid-induced status epilepticus in the rat. Neuroscience, 75, 849-856.
    • (1996) Neuroscience , vol.75 , pp. 849-856
    • Plumier, J.C.1    Armstrong, J.N.2    Landry, J.3    Babity, J.M.4    Robertson, H.A.5    Currie, R.W.6
  • 38
    • 0030760798 scopus 로고    scopus 로고
    • Constitutive expression of the 27-kDa heat shock protein (Hsp27) in sensory and motor neurons of the rat nervous system
    • Plumier, J.C., Hopkins, D.A., Robertson, H.A. & Currie, R.W. (1997) Constitutive expression of the 27-kDa heat shock protein (Hsp27) in sensory and motor neurons of the rat nervous system. J. Comp. Neurol., 384, 409-428.
    • (1997) J. Comp. Neurol. , vol.384 , pp. 409-428
    • Plumier, J.C.1    Hopkins, D.A.2    Robertson, H.A.3    Currie, R.W.4
  • 39
    • 0039171658 scopus 로고    scopus 로고
    • Analysis of the role of Hsp2S phosphorylation reveals the importance of the oligomerization state of this small heat shock protein in its protective function against TNFalpha- and hydrogen peroxide-induced cell death
    • Preville, X., Schultz, H., Knauf, U., Gaestel, M. & Arrigo, A.P. (1998) Analysis of the role of Hsp2S phosphorylation reveals the importance of the oligomerization state of this small heat shock protein in its protective function against TNFalpha- and hydrogen peroxide-induced cell death. J. Cell. Biochem., 69, 436-452.
    • (1998) J. Cell. Biochem. , vol.69 , pp. 436-452
    • Preville, X.1    Schultz, H.2    Knauf, U.3    Gaestel, M.4    Arrigo, A.P.5
  • 40
    • 0028297910 scopus 로고
    • Expression of small heat-shock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia
    • Renkawek, K., Bosnian, G.J. & de Jong, W.W. (1994) Expression of small heat-shock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia. Acta Neuropathol., 87, 511-519.
    • (1994) Acta Neuropathol. , vol.87 , pp. 511-519
    • Renkawek, K.1    Bosnian, G.J.2    De Jong, W.W.3
  • 41
  • 42
    • 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
  • 43
    • 0035918258 scopus 로고    scopus 로고
    • Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder, G.A., Lacourse, M.C., Minotti, S. & Durham, H.D. (2001) Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem., 276, 12791-12796.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4
  • 44
    • 0034662807 scopus 로고    scopus 로고
    • Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1 (G93A) mutation of familial amyotrophic lateral sclerosis
    • Stieber, A., Gonatas, J.O. & Gonatas, N.K. (2000) Aggregates of mutant protein appear progressively in dendrites, in periaxonal processes of oligodendrocytes, and in neuronal and astrocytic perikarya of mice expressing the SOD1 (G93A) mutation of familial amyotrophic lateral sclerosis. J. Neurol. Sci., 177, 114-123.
    • (2000) J. Neurol. Sci. , vol.177 , pp. 114-123
    • Stieber, A.1    Gonatas, J.O.2    Gonatas, N.K.3
  • 45
    • 0037072549 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 improve neurite outgrowth and suppress intracytoplasmic aggregate formation in cultured neuronal cells expressing mutant SOD1
    • Takeuchi, H., Kobayashi, Y., Yoshihara, T., Niwa, J., Doyu, M., Ohtsuka, K. & Sobue, G. (2002) Hsp70 and Hsp40 improve neurite outgrowth and suppress intracytoplasmic aggregate formation in cultured neuronal cells expressing mutant SOD1. Brain. Res., 949, 11.
    • (2002) Brain. Res. , vol.949 , pp. 11
    • Takeuchi, H.1    Kobayashi, Y.2    Yoshihara, T.3    Niwa, J.4    Doyu, M.5    Ohtsuka, K.6    Sobue, G.7
  • 46
    • 0033231022 scopus 로고    scopus 로고
    • Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P
    • Tamanini, F., Van Unen, L., Bakker, C., Sacchi, N., Galjaard, H., Oostra, B.A. & Hoogeveen, A.T. (1999) Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P. Biochem. J., 343, 517-523.
    • (1999) Biochem. J. , vol.343 , pp. 517-523
    • Tamanini, F.1    Van Unen, L.2    Bakker, C.3    Sacchi, N.4    Galjaard, H.5    Oostra, B.A.6    Hoogeveen, A.T.7
  • 47
    • 0037458564 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction
    • Tiwari, A. & Hayward, L.J. (2003) Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction. J. Biol. Chem., 278, 5984-5992.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5984-5992
    • Tiwari, A.1    Hayward, L.J.2
  • 48
    • 0036892683 scopus 로고    scopus 로고
    • Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis
    • Urushitani, M., Kurisu, J., Tsukita, K. & Takahashi, R. (2002) Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis. J. Neurochem., 83, 1030-1042.
    • (2002) J. Neurochem. , vol.83 , pp. 1030-1042
    • Urushitani, M.1    Kurisu, J.2    Tsukita, K.3    Takahashi, R.4
  • 49
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • Valentine, J.S. & Hart, P.J. (2003) Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc. Natl Acad. Sci. USA, 100, 3617-3622.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 52
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones - Cellular machines for protein folding
    • Walter, S. & Buchner, J. (2002) Molecular chaperones - cellular machines for protein folding. Angew. Chem., 41, 1098-1113.
    • (2002) Angew. Chem. , vol.41 , pp. 1098-1113
    • Walter, S.1    Buchner, J.2
  • 53
    • 0036199623 scopus 로고    scopus 로고
    • High molecular weight complexes of mutant superoxide dismutase 1: Age-dependent and tissue-specific accumulation
    • Wang, J., Xu, G. & Borchelt, D.R. (2002) High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. Neurobiol. Dis., 9, 139-148.
    • (2002) Neurobiol. Dis. , vol.9 , pp. 139-148
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 54
    • 0037494974 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3
    • Wen, F.C., Li, Y.H., Tsai, H.F., Lin, C.H., Li, C., Liu, C.S., Lii, C.K., Nukina, N. & Hsieh, M. (2003) Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. FEBS Lett., 546, 307-314.
    • (2003) FEBS Lett. , vol.546 , pp. 307-314
    • Wen, F.C.1    Li, Y.H.2    Tsai, H.F.3    Lin, C.H.4    Li, C.5    Liu, C.S.6    Lii, C.K.7    Nukina, N.8    Hsieh, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.