메뉴 건너뛰기




Volumn 7, Issue C, 2001, Pages 131-162

Molecular chaperones and age-related degenerative disorders

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0005125363     PISSN: 15663124     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1566-3124(01)07018-3     Document Type: Review
Times cited : (13)

References (198)
  • 1
    • 0032769206 scopus 로고    scopus 로고
    • Hyperthermia: How to recognize and prevent heat-related illnesses
    • Ballester J.M., and Harchelroad F.P. Hyperthermia: How to recognize and prevent heat-related illnesses. Geriatrics 54 (1999) 20-24
    • (1999) Geriatrics , vol.54 , pp. 20-24
    • Ballester, J.M.1    Harchelroad, F.P.2
  • 2
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connel P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., and Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cellul. Biol. 19 (1999) 4535-4545
    • (1999) Mol. Cellul. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connel, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.-Y.6    Patterson, C.7
  • 4
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt D.R., Taraboulos A., and Prusiner S.B. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267 (1992) 16188-16199
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 5
    • 0032925851 scopus 로고    scopus 로고
    • Food restriction reduces brain damage and improves behavioral outcome following excitotoxic and metabolic insults
    • Bruce-Keller A.J., Umberger G., McFall R., and Mattson M.P. Food restriction reduces brain damage and improves behavioral outcome following excitotoxic and metabolic insults. Ann. Neurol. 45 (1999) 8-15
    • (1999) Ann. Neurol. , vol.45 , pp. 8-15
    • Bruce-Keller, A.J.1    Umberger, G.2    McFall, R.3    Mattson, M.P.4
  • 6
    • 0030802669 scopus 로고    scopus 로고
    • The sequence of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus-Thermus group and cyanobacteria
    • Bustard K., and Gupta R.S. The sequence of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus-Thermus group and cyanobacteria. J. Mol. Evol. 45 (1997) 193-205
    • (1997) J. Mol. Evol. , vol.45 , pp. 193-205
    • Bustard, K.1    Gupta, R.S.2
  • 7
    • 0028898217 scopus 로고
    • Hormone-dependent transactivation by the human androgen receptor is regulated by a dnaJ protein
    • Caplan A.J., Langley E., Wilson E.M., and Vidal J. Hormone-dependent transactivation by the human androgen receptor is regulated by a dnaJ protein. J. Biol. Chem. 270 (1995) 5251-5257
    • (1995) J. Biol. Chem. , vol.270 , pp. 5251-5257
    • Caplan, A.J.1    Langley, E.2    Wilson, E.M.3    Vidal, J.4
  • 8
    • 0026696593 scopus 로고
    • Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons
    • Cheetham M.E., Brion J.-P., and Anderton B.H. Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons. Biochem. J. 284 (1992) 469-476
    • (1992) Biochem. J. , vol.284 , pp. 469-476
    • Cheetham, M.E.1    Brion, J.-P.2    Anderton, B.H.3
  • 9
    • 0027216523 scopus 로고
    • Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein
    • Chellaiah A., Davis A., and Mohanakumar T. Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein. Biochim. Biophys. Acta 1174 (1993) 111-113
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 111-113
    • Chellaiah, A.1    Davis, A.2    Mohanakumar, T.3
  • 10
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery
    • Chen S., and Smith D.F. Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J. Biol. Chem. 273 (1998) 35194-35200
    • (1998) J. Biol. Chem. , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 12
    • 15844408798 scopus 로고    scopus 로고
    • APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein
    • Chow N., Korenberg J.R., Chen X.-N., and Neve R.L. APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J. Biol. Chem. 271 (1996) 11339-11346
    • (1996) J. Biol. Chem. , vol.271 , pp. 11339-11346
    • Chow, N.1    Korenberg, J.R.2    Chen, X.-N.3    Neve, R.L.4
  • 13
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: On protein death and cell life. EMBO J. 17 (1998) 7151-7160
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 14
    • 0030872849 scopus 로고    scopus 로고
    • A novel subfamily of Hsp70s in the endoplasmic reticulum
    • Craven R.A., Tyson J.R., and Stirling C.J. A novel subfamily of Hsp70s in the endoplasmic reticulum. Trends Cell Biol. 7 (1997) 277-282
    • (1997) Trends Cell Biol. , vol.7 , pp. 277-282
    • Craven, R.A.1    Tyson, J.R.2    Stirling, C.J.3
  • 15
    • 0033529933 scopus 로고    scopus 로고
    • The alpha-2 macroglobulin gene is not associated with Alzheimer's disease in a case-control sample
    • Crawford F., Town T., Freeman M., Schinka J., Gold M., Duara R., and Mullan M. The alpha-2 macroglobulin gene is not associated with Alzheimer's disease in a case-control sample. Neurosci. Lett. 270 (1999) 133-136
    • (1999) Neurosci. Lett. , vol.270 , pp. 133-136
    • Crawford, F.1    Town, T.2    Freeman, M.3    Schinka, J.4    Gold, M.5    Duara, R.6    Mullan, M.7
  • 16
    • 0029813255 scopus 로고    scopus 로고
    • The presenilin genes: A new gene family involved in Alzheimer disease pathology
    • Cruts M., Hendriks L., and van Broechoven C. The presenilin genes: A new gene family involved in Alzheimer disease pathology. Hum. Mol. Genet. 5 (1996) 1449-1455
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1449-1455
    • Cruts, M.1    Hendriks, L.2    van Broechoven, C.3
  • 17
    • 0031873752 scopus 로고    scopus 로고
    • The 90 kDa molecular chaperone family: Structure, function and clinical applications
    • Csermely P., Schnaider T., Sôti C., Prohászka Z., and Nardai G. The 90 kDa molecular chaperone family: Structure, function and clinical applications. Pharmacol. & Ther. 79 (1998) 129-168
    • (1998) Pharmacol. & Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Sôti, C.3    Prohászka, Z.4    Nardai, G.5
  • 18
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA 1
    • Cummings C.J., Mancini M.A., Antalfy B., DeFranco D.b., Orr H.T., and Zoghbi H. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA 1. Nature Genet. 19 (1998) 148-154
    • (1998) Nature Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalfy, B.3    DeFranco, D.b.4    Orr, H.T.5    Zoghbi, H.6
  • 19
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr D.M., Langer T., and Douglas M.G. DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19 (1994) 176-181
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 21
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman S.K., Raymond G.J., Caughey B., and Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. USA 94 (1997) 13938-13943
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13938-13943
    • DebBurman, S.K.1    Raymond, G.J.2    Caughey, B.3    Lindquist, S.4
  • 22
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin-small heat shock protein superfamily
    • De Jong W.W., Caspers G.J., and Leunissen J.A. Genealogy of the alpha-crystallin-small heat shock protein superfamily. Int. J. Biol. Macromol. 22 (1998) 151-162
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • De Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 23
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., and Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997) 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 24
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel L., Löwe J., Stock D., Stetter K.O., Huber R., and Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93 (1998) 125-138
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Löwe, J.2    Stock, D.3    Stetter, K.O.4    Huber, R.5    Steinbacher, S.6
  • 25
    • 0033562167 scopus 로고    scopus 로고
    • Evidence for a novel set of small heat-shock proteins that associates with the mitochondria of murine PC12 cells and protects NADH:ubiquinone oxidoreductase from heat and oxidative stress
    • Downs C.A., Jones L.R., and Heckathorn S.A. Evidence for a novel set of small heat-shock proteins that associates with the mitochondria of murine PC12 cells and protects NADH:ubiquinone oxidoreductase from heat and oxidative stress. Arch. Biochem. Biophys. 365 (1999) 344-350
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 344-350
    • Downs, C.A.1    Jones, L.R.2    Heckathorn, S.A.3
  • 26
    • 0033566286 scopus 로고    scopus 로고
    • Dietary restriction and 2-deoxyglucose administration improve behavioral outcome and reduce degeneration of dopaminergic neurons in models of Parkinson's disease
    • Duan W., and Mattson M.P. Dietary restriction and 2-deoxyglucose administration improve behavioral outcome and reduce degeneration of dopaminergic neurons in models of Parkinson's disease. J. Neurosci. Res. 57 (1999) 195-206
    • (1999) J. Neurosci. Res. , vol.57 , pp. 195-206
    • Duan, W.1    Mattson, M.P.2
  • 28
    • 0009486302 scopus 로고    scopus 로고
    • Protéins de stress et vieillissement
    • Favatier F., and Polla B. Protéins de stress et vieillissement. L'Année Gérontologique 10 (1996) 217-224
    • (1996) L'Année Gérontologique , vol.10 , pp. 217-224
    • Favatier, F.1    Polla, B.2
  • 29
    • 0030049067 scopus 로고    scopus 로고
    • Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration
    • Feany M.B., Mattiace L.A., and Dickson D.W. Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration. J. Neuropathol. Exp. Neurol. 55 (1996) 53-67
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 53-67
    • Feany, M.B.1    Mattiace, L.A.2    Dickson, D.W.3
  • 30
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari D.M., and Söling H.-D. The protein disulphide-isomerase family: Unravelling a string of folds. Biochem. J. 339 (1999) 1-10
    • (1999) Biochem. J. , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Söling, H.-D.2
  • 31
    • 0032502955 scopus 로고    scopus 로고
    • The mode of action of peptidyl prolyl cis/trans isomerases in vivo: Binding vs. catalysis
    • Fisher G., Tradler T., and Zarnt T. The mode of action of peptidyl prolyl cis/trans isomerases in vivo: Binding vs. catalysis. FEBS Lett. 426 (1998) 17-20
    • (1998) FEBS Lett. , vol.426 , pp. 17-20
    • Fisher, G.1    Tradler, T.2    Zarnt, T.3
  • 32
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman J., and Höhfeld J. Chaperones get in touch: The Hip-Hop connection. Trends Biochem. Sci. 22 (1997) 87-92
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 33
    • 0032491412 scopus 로고    scopus 로고
    • The chaperone cofactor Hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities
    • Gebauer M., Melki R., and Gehring U. The chaperone cofactor Hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities. J. Biol. Chem. 273 (1998) 29475-29480
    • (1998) J. Biol. Chem. , vol.273 , pp. 29475-29480
    • Gebauer, M.1    Melki, R.2    Gehring, U.3
  • 34
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional γ- and α-tubulin
    • Geissler S., Siegers K., and Schiebel E. A novel protein complex promoting formation of functional γ- and α-tubulin. EMBO J. 17 (1998) 952-966
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 35
    • 0033033062 scopus 로고    scopus 로고
    • Chromosome missegregation and trisomy 21 mosaicism in Alzheimer's disease
    • Geller L.N., and Potter H. Chromosome missegregation and trisomy 21 mosaicism in Alzheimer's disease. Neurobiol. Dis. 6 (1999) 167-179
    • (1999) Neurobiol. Dis. , vol.6 , pp. 167-179
    • Geller, L.N.1    Potter, H.2
  • 36
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., and Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 (1998) 73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 37
    • 0028169905 scopus 로고
    • Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury
    • Goodman Y., and Mattson M.P. Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid β-peptide-induced oxidative injury. Exp. Neurol. 128 (1994) 1-12
    • (1994) Exp. Neurol. , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.P.2
  • 38
    • 0028019049 scopus 로고
    • Ubiquitin-mediated degradative pathway degrades the extracellular but not the intracellular form of amyloid β-protein precursor
    • Gregori L., Bhasin R., and Goldgaber D. Ubiquitin-mediated degradative pathway degrades the extracellular but not the intracellular form of amyloid β-protein precursor. Biochem. Biophys. Res. Commun. 203 (1994) 1731-1738
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1731-1738
    • Gregori, L.1    Bhasin, R.2    Goldgaber, D.3
  • 39
    • 0032956536 scopus 로고    scopus 로고
    • Discontinuous occurrence of the hsp70(dnaK) gene among archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein
    • Gribaldo S., Lumia V., Creti R., Conway de Macario E., Sanangelantoni, and Cammarano P. Discontinuous occurrence of the hsp70(dnaK) gene among archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein. J. Bacteriol. 181 (1999) 434-443
    • (1999) J. Bacteriol. , vol.181 , pp. 434-443
    • Gribaldo, S.1    Lumia, V.2    Creti, R.3    Conway de Macario, E.4    Sanangelantoni5    Cammarano, P.6
  • 40
    • 0022516004 scopus 로고
    • Characterization of messenger RNA from the cerebral cortex of control and Alzheimer-afflicted brain
    • Guillemette J.G., Wong L., Crapper, McLachlan C., and Lewis P.N. Characterization of messenger RNA from the cerebral cortex of control and Alzheimer-afflicted brain. J. Neurochem. 47 (1986) 987-997
    • (1986) J. Neurochem. , vol.47 , pp. 987-997
    • Guillemette, J.G.1    Wong, L.2    Crapper3    McLachlan, C.4    Lewis, P.N.5
  • 41
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta R.S. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol. Microbiol. 15 (1995) 1-11
    • (1995) Mol. Microbiol. , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 42
    • 0028785298 scopus 로고
    • Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species
    • Gupta R.S. Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species. Mol. Biol. Evol. 12 (1995) 1063-1073
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 1063-1073
    • Gupta, R.S.1
  • 43
    • 0031794743 scopus 로고    scopus 로고
    • Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes
    • Gupta R.S. Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes. Microbiol. Mol. Biol. Rev. 62 (1998) 1435-1491
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1435-1491
    • Gupta, R.S.1
  • 44
    • 0028344493 scopus 로고
    • Cloning of Giardia lamblia heat shock protein HSP70 homologs: Implications regarding origin of eukaryotic cells and endoplasmic reticulum
    • Gupta R.S., Aitken K., Falah M., and Singh B. Cloning of Giardia lamblia heat shock protein HSP70 homologs: Implications regarding origin of eukaryotic cells and endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 91 (1994) 2895-2899
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2895-2899
    • Gupta, R.S.1    Aitken, K.2    Falah, M.3    Singh, B.4
  • 45
    • 0028674882 scopus 로고
    • Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus
    • Gupta R.S., and Singh B. Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus. Curr. Biol. 4 (1994) 1104-1114
    • (1994) Curr. Biol. , vol.4 , pp. 1104-1114
    • Gupta, R.S.1    Singh, B.2
  • 46
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwel B., and Gutteridge J.M. Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol. 86 (1990) 1-85
    • (1990) Methods Enzymol. , vol.86 , pp. 1-85
    • Halliwel, B.1    Gutteridge, J.M.2
  • 48
    • 0032817946 scopus 로고    scopus 로고
    • The internal globus pallidus is affected in progressive supranuclear palsy and Parkinson's disease
    • Hardman C.D., and Halliday G.M. The internal globus pallidus is affected in progressive supranuclear palsy and Parkinson's disease. Exper. Neurol. 158 (1999) 135-142
    • (1999) Exper. Neurol. , vol.158 , pp. 135-142
    • Hardman, C.D.1    Halliday, G.M.2
  • 50
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris D.A. Cellular biology of prion diseases. Clin. Microbiol. Rev. 12 (1999) 429-444
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 51
    • 0033582587 scopus 로고    scopus 로고
    • Thermodynamics of model prions and its implications for the problem of prion protein folding
    • Harrison P.M., Chan H.S., Prusiner S.B., and Cohen F.E. Thermodynamics of model prions and its implications for the problem of prion protein folding. J. Mol. Biol. 286 (1999) 593-606
    • (1999) J. Mol. Biol. , vol.286 , pp. 593-606
    • Harrison, P.M.1    Chan, H.S.2    Prusiner, S.B.3    Cohen, F.E.4
  • 52
    • 0028958602 scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U., and Martin J. Molecular chaperones in cellular protein folding. Curr. Op. Struct. Biol. 5 (1995) 92-102
    • (1995) Curr. Op. Struct. Biol. , vol.5 , pp. 92-102
    • Hartl, F.U.1    Martin, J.2
  • 53
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes S.A., and Dice J.F. Roles of molecular chaperones in protein degradation. Cell Biol. 132 (1996) 255-258
    • (1996) Cell Biol. , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 54
    • 0033597914 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces expression of the stress response genes hop and H411
    • Heine H., Delude R.L., Monks B.G., Espevik T., and Golenbock D.T. Bacterial lipopolysaccharide induces expression of the stress response genes hop and H411. J. Biol. Chem. 274 (1999) 21049-21055
    • (1999) J. Biol. Chem. , vol.274 , pp. 21049-21055
    • Heine, H.1    Delude, R.L.2    Monks, B.G.3    Espevik, T.4    Golenbock, D.T.5
  • 55
    • 0032035278 scopus 로고    scopus 로고
    • Proteolysis and chaperones: The destruction/reconstruction dilemma
    • Herman C., and D'Ari R. Proteolysis and chaperones: The destruction/reconstruction dilemma. Curr. Op. Microbiol. 1 (1998) 204-209
    • (1998) Curr. Op. Microbiol. , vol.1 , pp. 204-209
    • Herman, C.1    D'Ari, R.2
  • 56
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld J., Minami Y., and F.U. Hartl F.U. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83 (1995) 589-598
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    F.U. Hartl, F.U.3
  • 57
    • 0031665081 scopus 로고    scopus 로고
    • HSP47, a collagen-specific molecular chaperone, delays the secretion of type III procollagen transfected in human embryonic kidney cell line 293
    • A possible role for HSP47 in collagen modification
    • Hosokawa N., Hohenadl C., Satoh M., Kühn K., and Nagata K. HSP47, a collagen-specific molecular chaperone, delays the secretion of type III procollagen transfected in human embryonic kidney cell line 293. A possible role for HSP47 in collagen modification. J. Biochem. 124 (1998) 654-662
    • (1998) J. Biochem. , vol.124 , pp. 654-662
    • Hosokawa, N.1    Hohenadl, C.2    Satoh, M.3    Kühn, K.4    Nagata, K.5
  • 58
    • 0033564204 scopus 로고    scopus 로고
    • Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state
    • Hourichi M., and Caughey B. Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state. EMBO J. 18 (1999) 3193-3203
    • (1999) EMBO J. , vol.18 , pp. 3193-3203
    • Hourichi, M.1    Caughey, B.2
  • 59
    • 0033575213 scopus 로고    scopus 로고
    • The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator
    • Hsiao P.-W., Lin D.-L., Nakao R., and Chang C. The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator. J. Biol. Chem. 274 (1999) 20229-20234
    • (1999) J. Biol. Chem. , vol.274 , pp. 20229-20234
    • Hsiao, P.-W.1    Lin, D.-L.2    Nakao, R.3    Chang, C.4
  • 60
    • 0029656091 scopus 로고    scopus 로고
    • Structures of prion proteins and conformational models for prion diseases
    • Huang Z., Prusiner S.B., and Cohen F.E. Structures of prion proteins and conformational models for prion diseases. Curr. Top. Microbiol. Immunol. 207 (1996) 49-67
    • (1996) Curr. Top. Microbiol. Immunol. , vol.207 , pp. 49-67
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 62
    • 0024521440 scopus 로고
    • αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T., Kime-Iwaki A., Liem R.K.H., and Goldman J.E. αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57 (1989) 71-78
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kime-Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 63
    • 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., and Goldman. 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 (1993) 487-495
    • (1993) Am. J. Pathol. , vol.143 , pp. 487-495
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Sakaki, Y.4    Goldman5
  • 65
    • 0032873941 scopus 로고    scopus 로고
    • Localisation of presenilin 2 in human and rodent pancreatic islet β-cells
    • Met239Val presenilin 2 variant is not associated with diabetes in man
    • Jaikaran E.T.A.S., Marcon G., Levesque L., St George-Hyslop P., Fraser P.E., and Clark A. Localisation of presenilin 2 in human and rodent pancreatic islet β-cells. Met239Val presenilin 2 variant is not associated with diabetes in man. J. Cell Sci. 112 (1999) 2137-2144
    • (1999) J. Cell Sci. , vol.112 , pp. 2137-2144
    • Jaikaran, E.T.A.S.1    Marcon, G.2    Levesque, L.3    St George-Hyslop, P.4    Fraser, P.E.5    Clark, A.6
  • 66
    • 0032854754 scopus 로고    scopus 로고
    • Cerebellar allografts survive and transiently alleviate ataxia in transgenic model of spinocerebellar ataxia type-1
    • Kaemmerer W.F., and Low W.C. Cerebellar allografts survive and transiently alleviate ataxia in transgenic model of spinocerebellar ataxia type-1. Exp. Neurol. 158 (1999) 301-311
    • (1999) Exp. Neurol. , vol.158 , pp. 301-311
    • Kaemmerer, W.F.1    Low, W.C.2
  • 67
    • 0026775476 scopus 로고
    • Ultrastructural and immunohistochemical studies on ballooned cortical neurons in Creutzfeldt-Jakob disease: Expression of alpha-B-crystallin, ubiquitin and stress-response protein 27
    • Kato S., Hirano A., Umahara T., Llena J.F., Herz F., and Ohama E. Ultrastructural and immunohistochemical studies on ballooned cortical neurons in Creutzfeldt-Jakob disease: Expression of alpha-B-crystallin, ubiquitin and stress-response protein 27. Acta Neuropathol. Berl. 84 (1992) 443-448
    • (1992) Acta Neuropathol. Berl. , vol.84 , pp. 443-448
    • Kato, S.1    Hirano, A.2    Umahara, T.3    Llena, J.F.4    Herz, F.5    Ohama, E.6
  • 68
    • 0028288494 scopus 로고
    • Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain
    • Kenward N., Hope J., Landon M., and Mayer R.J. Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain. J. Neurochem. 62 (1994) 1870-1877
    • (1994) J. Neurochem. , vol.62 , pp. 1870-1877
    • Kenward, N.1    Hope, J.2    Landon, M.3    Mayer, R.J.4
  • 69
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim K.K., Kim R., and Kim S.-H. Crystal structure of a small heat-shock protein. Nature 394 (1998) 595-599
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.-H.3
  • 70
    • 13144276278 scopus 로고    scopus 로고
    • Small heat shock protein of Methanococcus jannaschii, a hyperthermophile
    • Kim R., Kim K.K., Yokota H., and Kim S.-H. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. Proc. Natl. Acad. Sci. USA 95 (1998) 9129-9133
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9129-9133
    • Kim, R.1    Kim, K.K.2    Yokota, H.3    Kim, S.-H.4
  • 71
    • 0032560551 scopus 로고    scopus 로고
    • The thermosome: Archetype of group II chaperonins
    • Klumpp M., and Baumeister W. The thermosome: Archetype of group II chaperonins. FEBS Lett. 430 (1998) 73-77
    • (1998) FEBS Lett. , vol.430 , pp. 73-77
    • Klumpp, M.1    Baumeister, W.2
  • 72
    • 0033608219 scopus 로고    scopus 로고
    • Proteasome inhibitors induced the association of Alzheimer's amyloid precursor protein with Hsc73
    • Kouchi Z., Sorimachi H., Suzuki K., and Ishiura S. Proteasome inhibitors induced the association of Alzheimer's amyloid precursor protein with Hsc73. Biochem. Biophys. Res. Commun. 254 (1999) 804-810
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 804-810
    • Kouchi, Z.1    Sorimachi, H.2    Suzuki, K.3    Ishiura, S.4
  • 73
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y., Segal M., Normington K., Gething M.-J., and Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332 (1988) 462-464
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 74
    • 0032840954 scopus 로고    scopus 로고
    • β-amyloid immunoreactivity in astrocytes in Alzheimer's disease brain biopsies: An electron microscope study
    • Kurt M.A., Davies D.C., and Kidd M. β-amyloid immunoreactivity in astrocytes in Alzheimer's disease brain biopsies: An electron microscope study. Exper. Neurol. 158 (1999) 221-228
    • (1999) Exper. Neurol. , vol.158 , pp. 221-228
    • Kurt, M.A.1    Davies, D.C.2    Kidd, M.3
  • 75
    • 0032775680 scopus 로고    scopus 로고
    • ATM: The product of the gene mutated in ataxia-telangiectasia
    • Lavin M.F. ATM: The product of the gene mutated in ataxia-telangiectasia. Intl. J. Biochem. Cell Biol. 31 (1999) 735-740
    • (1999) Intl. J. Biochem. Cell Biol. , vol.31 , pp. 735-740
    • Lavin, M.F.1
  • 76
    • 0033168080 scopus 로고    scopus 로고
    • 2-Deoxy-D-Glucose protects hippocampal neurons against excitotoxic and oxidative injury: Evidence for the involvment of stress proteins
    • Lee J., Bruce-Keller A.J., Kruman Y., Chan S.L., and Mattson M.P. 2-Deoxy-D-Glucose protects hippocampal neurons against excitotoxic and oxidative injury: Evidence for the involvment of stress proteins. J. Neurosci. Res. 57 (1999) 48-61
    • (1999) J. Neurosci. Res. , vol.57 , pp. 48-61
    • Lee, J.1    Bruce-Keller, A.J.2    Kruman, Y.3    Chan, S.L.4    Mattson, M.P.5
  • 78
    • 0032811511 scopus 로고    scopus 로고
    • Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice
    • Li H., Li S.-H., Cheng A.L., Mangiarini L., Bates G.P., and Li X.-J. Ultrastructural localization and progressive formation of neuropil aggregates in Huntington's disease transgenic mice. Hum. Mol. Genet. 8 (1999) 1227-1236
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1227-1236
    • Li, H.1    Li, S.-H.2    Cheng, A.L.3    Mangiarini, L.4    Bates, G.P.5    Li, X.-J.6
  • 80
    • 0032582489 scopus 로고    scopus 로고
    • Extended life-span and stress resistance in the Drosophila mutant methuselah
    • Lin Y.-J., Seroude L., and Benzer S. Extended life-span and stress resistance in the Drosophila mutant methuselah. Science 282 (1998) 943-946
    • (1998) Science , vol.282 , pp. 943-946
    • Lin, Y.-J.1    Seroude, L.2    Benzer, S.3
  • 82
    • 0032516849 scopus 로고    scopus 로고
    • Multiple molecular chaperones interact with apolipoprotein B during its maturation
    • Linnik K.M., and Herscovitz H. Multiple molecular chaperones interact with apolipoprotein B during its maturation. J. Biol. Chem. 273 (1998) 21368-21373
    • (1998) J. Biol. Chem. , vol.273 , pp. 21368-21373
    • Linnik, K.M.1    Herscovitz, H.2
  • 83
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M., Kramer P., LaMorticella D.M., Murphey W., Lovrien E.W., and Weleber R.G. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum. Mol. Genet. 7 (1998) 471-474
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 85
    • 0023917701 scopus 로고
    • Alz-50, ubiquitin and tau immunoreactivity of neurofibrillary tangles, Pick bodies and Lewy bodies
    • Love S., Saitoh T., Quijada S., Cole G.M., and Terry R.D. Alz-50, ubiquitin and tau immunoreactivity of neurofibrillary tangles, Pick bodies and Lewy bodies. J. Neuropathol. Exp. Neurol. 47 (1988) 393-405
    • (1988) J. Neuropathol. Exp. Neurol. , vol.47 , pp. 393-405
    • Love, S.1    Saitoh, T.2    Quijada, S.3    Cole, G.M.4    Terry, R.D.5
  • 86
    • 0023927981 scopus 로고
    • Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebella astrocytomas, cytoplasmic bodies in muscle, and Mallory bodies in alcoholic liver disease
    • Lowe J., Blanchard A., Morrell K., Lennox G., Reynolds L., Bilette M., Landon M., and Mayer R.J. Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebella astrocytomas, cytoplasmic bodies in muscle, and Mallory bodies in alcoholic liver disease. J. Pathol. 155 (1988) 9-15
    • (1988) J. Pathol. , vol.155 , pp. 9-15
    • Lowe, J.1    Blanchard, A.2    Morrell, K.3    Lennox, G.4    Reynolds, L.5    Bilette, M.6    Landon, M.7    Mayer, R.J.8
  • 88
    • 0026452020 scopus 로고
    • Immunoreactivity to ubiquitin-protein conjugates is present early in the disease process in the brains of scrapie-infected mice
    • Lowe J., Fergusson J., Kenward N., Landon M., Brown J., Hope J., and Mayer R.J. Immunoreactivity to ubiquitin-protein conjugates is present early in the disease process in the brains of scrapie-infected mice. J. Pathol. 168 (1992) 169-177
    • (1992) J. Pathol. , vol.168 , pp. 169-177
    • Lowe, J.1    Fergusson, J.2    Kenward, N.3    Landon, M.4    Brown, J.5    Hope, J.6    Mayer, R.J.7
  • 89
    • 0027407247 scopus 로고
    • Ubiquitin in neurodegenerative diseases
    • Lowe J., Mayer R.J., and Landon M. Ubiquitin in neurodegenerative diseases. Brain Pathol. 3 (1993) 55-65
    • (1993) Brain Pathol. , vol.3 , pp. 55-65
    • Lowe, J.1    Mayer, R.J.2    Landon, M.3
  • 90
    • 0029188297 scopus 로고
    • Heat-shock proteins and molecular chaperones: Implications for pathogenesis, diagnostics, and therapeutics
    • Macario A.J.L. Heat-shock proteins and molecular chaperones: Implications for pathogenesis, diagnostics, and therapeutics. Intl. J. Clin. Lab. Res. 25 (1995) 59-70
    • (1995) Intl. J. Clin. Lab. Res. , vol.25 , pp. 59-70
    • Macario, A.J.L.1
  • 91
    • 0344500848 scopus 로고    scopus 로고
    • The archaeal molecular chaperone machine: Peculiarities and paradoxes
    • Macario A.J.L., and Conway de Macario E. The archaeal molecular chaperone machine: Peculiarities and paradoxes. Genetics 152 (1999) 1277-1283
    • (1999) Genetics , vol.152 , pp. 1277-1283
    • Macario, A.J.L.1    Conway de Macario, E.2
  • 92
    • 0008517596 scopus 로고    scopus 로고
    • Heat shock response. Overview
    • Fink G. (Ed), Academic Press, San Diego, CA in press
    • Macario A.J.L., and Conway de Macario E. Heat shock response. Overview. In: Fink G. (Ed). The Encyclopedia of Stress (2000), Academic Press, San Diego, CA in press
    • (2000) The Encyclopedia of Stress
    • Macario, A.J.L.1    Conway de Macario, E.2
  • 93
    • 0033043766 scopus 로고    scopus 로고
    • Heat acclimation increases the basal HSP72 level and alters its production dynamics during heat stress
    • (5 Pt 2)
    • Maloyan A., Palmon A., and Horowitz M. Heat acclimation increases the basal HSP72 level and alters its production dynamics during heat stress. Am. J. Physiol. 276 (1999) R1506-R1515 (5 Pt 2)
    • (1999) Am. J. Physiol. , vol.276
    • Maloyan, A.1    Palmon, A.2    Horowitz, M.3
  • 95
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark R.J., Pang Z., Geddes J.W., Uchida K., and Mattson M.P. Amyloid β-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation. J. Neurosci. 17 (1997) 1046-1054
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 96
    • 0030779677 scopus 로고    scopus 로고
    • Cellular action of β-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M.P. Cellular action of β-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77 (1997) 1081-1132
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 97
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: The busy life of Hsp90
    • Mayer M.P., and Bukau B. Molecular chaperones: The busy life of Hsp90. Curr. Biol. 9 (1999) R322-R325
    • (1999) Curr. Biol. , vol.9
    • Mayer, M.P.1    Bukau, B.2
  • 98
    • 0032518022 scopus 로고    scopus 로고
    • Protective and damaging effects of stress mediators
    • McEwen B.S. Protective and damaging effects of stress mediators. New Eng. J. Med. 338 (1998) 171-179
    • (1998) New Eng. J. Med. , vol.338 , pp. 171-179
    • McEwen, B.S.1
  • 99
    • 0032912252 scopus 로고    scopus 로고
    • Stress and hippocampal plasticity
    • McEwen B.S. Stress and hippocampal plasticity. Annu. Rev. Neurosci. 22 (1999) 105-122
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 105-122
    • McEwen, B.S.1
  • 100
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham G.C., Lu Z., King S., Sorscher E., Tousson A., and Cyr D.M. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J. 18 (1999) 1492-1505
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 101
    • 0033575256 scopus 로고    scopus 로고
    • Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex
    • Misselwitz B., Staeck O., Matlack K.E.S., and Rapoport T.A. Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J. Biol. Chem. 274 (1999) 20110-20115
    • (1999) J. Biol. Chem. , vol.274 , pp. 20110-20115
    • Misselwitz, B.1    Staeck, O.2    Matlack, K.E.S.3    Rapoport, T.A.4
  • 102
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H., Kondo J., and Ihara Y. Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science 235 (1987) 1641-1644
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 103
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto R.I. Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes & Dev. 12 (1998) 3788-3796
    • (1998) Genes & Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 104
    • 0032587169 scopus 로고    scopus 로고
    • αB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski P.J., Valdez M.M., and Clark J.L. αB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest. Ophtalmol. Vis. Sci. 40 (1999) 951-958
    • (1999) Invest. Ophtalmol. Vis. Sci. , vol.40 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2    Clark, J.L.3
  • 105
    • 0344389028 scopus 로고    scopus 로고
    • Multiple small heat shock proteins in rhizobia
    • Munchbach M., Nocker A., and Narberhaus F. Multiple small heat shock proteins in rhizobia. J. Bacteriol. 181 (1998) 83-90
    • (1998) J. Bacteriol. , vol.181 , pp. 83-90
    • Munchbach, M.1    Nocker, A.2    Narberhaus, F.3
  • 106
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro S., and Pelham H.R.B. An Hsp70-like protein in the ER: Identity with 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46 (1986) 291-300
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 107
    • 0030569286 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA encoding rat mitochondrial GrpE, a stress-inducible nucleotide-exchange factor of ubiquitous appearance in mammalian organs
    • Naylor D.J., Hoogenraad N.J., and Hoj P.B. Isolation and characterization of cDNA encoding rat mitochondrial GrpE, a stress-inducible nucleotide-exchange factor of ubiquitous appearance in mammalian organs. FEBS Lett. 396 (1996) 181-188
    • (1996) FEBS Lett. , vol.396 , pp. 181-188
    • Naylor, D.J.1    Hoogenraad, N.J.2    Hoj, P.B.3
  • 108
    • 0032516866 scopus 로고    scopus 로고
    • Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-like proteins, the co-chaperones of specific Hsp70 members
    • Naylor D.J., Stines A.P., Hoogenraad N.J., and Hoj P.B. Evidence for the existence of distinct mammalian cytosolic, microsomal, and two mitochondrial GrpE-like proteins, the co-chaperones of specific Hsp70 members. J. Biol. Chem. 273 (1998) 21169-21177
    • (1998) J. Biol. Chem. , vol.273 , pp. 21169-21177
    • Naylor, D.J.1    Stines, A.P.2    Hoogenraad, N.J.3    Hoj, P.B.4
  • 109
    • 0032005026 scopus 로고    scopus 로고
    • Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
    • Netzer W.J., and Hartl F.U. Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci. 23 (1998) 68-73
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 68-73
    • Netzer, W.J.1    Hartl, F.U.2
  • 110
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam G.P., Wegrzyn R.D., Lindquist S.L., and Chernoff Y.O. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19 (1999) 1325-1333
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 111
    • 0030949349 scopus 로고    scopus 로고
    • The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion
    • Nishikawa S., and Endo T. The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion. J. Biol. Chem. 272 (1997) 12889-12892
    • (1997) J. Biol. Chem. , vol.272 , pp. 12889-12892
    • Nishikawa, S.1    Endo, T.2
  • 114
    • 0027254681 scopus 로고
    • Human cDNA encoding DnaJ protein homologue
    • Oh S., Iwahori A., and Kato S. Human cDNA encoding DnaJ protein homologue. Biochim. Biophys. Acta 1174 (1993) 114-116
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 114-116
    • Oh, S.1    Iwahori, A.2    Kato, S.3
  • 116
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell D.A., Kowal A.S., Singer M.A., and Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372 (1994) 475-478
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 117
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino M.M., Liu J.-J., Glover J.R., and Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273 (1996) 622-626
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.-J.2    Glover, J.R.3    Lindquist, S.4
  • 120
    • 0033022771 scopus 로고    scopus 로고
    • Involvement of oxidative stress on the impairment of energy metabolism induced by Aβ peptides on PC12 cells: Protection by antioxidants
    • Pereira C., Santos M.S., and Oliveira C. Involvement of oxidative stress on the impairment of energy metabolism induced by Aβ peptides on PC12 cells: Protection by antioxidants. Neurobiol. Dis. 6 (1999) 209-219
    • (1999) Neurobiol. Dis. , vol.6 , pp. 209-219
    • Pereira, C.1    Santos, M.S.2    Oliveira, C.3
  • 123
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains
    • Perry G., Friedman R., Shaw G., and Chau V. Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains. Proc. Natl. Acad. Sci. USA 84 (1987) 3033-3036
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 124
    • 0030910776 scopus 로고    scopus 로고
    • Mitochondrial biogenesis: The Tom and Tim machine
    • Pfanner N., and Meijer M. Mitochondrial biogenesis: The Tom and Tim machine. Curr. Biol. 7 (1997) R100-R103
    • (1997) Curr. Biol. , vol.7
    • Pfanner, N.1    Meijer, M.2
  • 126
    • 0032995727 scopus 로고    scopus 로고
    • Receptor-mediated transport of human amyloid β-protein 1-40 and 1-42 at the blood-brain barrier
    • Poduslo J.F., Curran G.L., Sanyal B., and Selkoe D.J. Receptor-mediated transport of human amyloid β-protein 1-40 and 1-42 at the blood-brain barrier. Neurobiol. Dis. 6 (1999) 190-199
    • (1999) Neurobiol. Dis. , vol.6 , pp. 190-199
    • Poduslo, J.F.1    Curran, G.L.2    Sanyal, B.3    Selkoe, D.J.4
  • 127
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 129
    • 0029134871 scopus 로고
    • Spinocerebellar ataxia type I and Machado-Joseph disease: Incidence of CAG expansions among adult-onset ataxia patients from 311 families with dominant, recessive, or sporadic ataxia
    • Ranum L.P.W., Lundgren J.K., Schut L.J., Ahrens M.J., Perlman S., Aita J., Bird T.D., Gomez C., and Orr H.T. Spinocerebellar ataxia type I and Machado-Joseph disease: Incidence of CAG expansions among adult-onset ataxia patients from 311 families with dominant, recessive, or sporadic ataxia. Am. J. Hum. Gen. 57 (1995) 603-608
    • (1995) Am. J. Hum. Gen. , vol.57 , pp. 603-608
    • Ranum, L.P.W.1    Lundgren, J.K.2    Schut, L.J.3    Ahrens, M.J.4    Perlman, S.5    Aita, J.6    Bird, T.D.7    Gomez, C.8    Orr, H.T.9
  • 130
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow J., von Ahsen O., Bömer U., and Pfanner N. Molecular chaperones: Towards a characterization of the heat-shock protein 70 family. Trends Cell Biol. 7 (1997) 129-133
    • (1997) Trends Cell Biol. , vol.7 , pp. 129-133
    • Rassow, J.1    von Ahsen, O.2    Bömer, U.3    Pfanner, N.4
  • 132
    • 0033574162 scopus 로고    scopus 로고
    • The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
    • Rommelaere H., De Neve M., Melki R., Vandekerckhove J., and Ampe C. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. Biochemistry 38 (1999) 3246-3257
    • (1999) Biochemistry , vol.38 , pp. 3246-3257
    • Rommelaere, H.1    De Neve, M.2    Melki, R.3    Vandekerckhove, J.4    Ampe, C.5
  • 133
    • 0028871765 scopus 로고
    • Spinocerebellar ataxias and ataxins
    • Rosenberg R.N. Spinocerebellar ataxias and ataxins. New Eng. J. Med. 333 (1995) 1351-1353
    • (1995) New Eng. J. Med. , vol.333 , pp. 1351-1353
    • Rosenberg, R.N.1
  • 137
    • 0030755261 scopus 로고    scopus 로고
    • The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter
    • Ryan M.T., Herd S.M., Sberna G., Samuel M.M., Hoogenraad N.J., and Hoj P.B. The genes encoding mammalian chaperonin 60 and chaperonin 10 are linked head-to-head and share a bidirectional promoter. Gene 196 (1997) 9-17
    • (1997) Gene , vol.196 , pp. 9-17
    • Ryan, M.T.1    Herd, S.M.2    Sberna, G.3    Samuel, M.M.4    Hoogenraad, N.J.5    Hoj, P.B.6
  • 138
    • 0030927540 scopus 로고    scopus 로고
    • The role of molecular chaperones in mitochondrial protein import and folding
    • Ryan M.T., Naylor D.J., Hoj P.B., Clark M.S., and Hoogenraad N.J. The role of molecular chaperones in mitochondrial protein import and folding. Intl. Rev. Cytol. 174 (1997) 127-193
    • (1997) Intl. Rev. Cytol. , vol.174 , pp. 127-193
    • Ryan, M.T.1    Naylor, D.J.2    Hoj, P.B.3    Clark, M.S.4    Hoogenraad, N.J.5
  • 139
    • 0033542142 scopus 로고    scopus 로고
    • Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone
    • Saborio G.P., Soto C., Kascsak R.J., Levy E., Kascsak R., Harris D.A., and Frangione B. Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 258 (1999) 470-475
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 470-475
    • Saborio, G.P.1    Soto, C.2    Kascsak, R.J.3    Levy, E.4    Kascsak, R.5    Harris, D.A.6    Frangione, B.7
  • 140
    • 0031008564 scopus 로고    scopus 로고
    • The Hsp70 homologue Lhslp is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates
    • Saris N., Holkeri H., Craven R.A., Stirling C.J., and Makarow M. The Hsp70 homologue Lhslp is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. J. Cell Biol. 137 (1997) 813-821
    • (1997) J. Cell Biol. , vol.137 , pp. 813-821
    • Saris, N.1    Holkeri, H.2    Craven, R.A.3    Stirling, C.J.4    Makarow, M.5
  • 143
    • 0031441886 scopus 로고    scopus 로고
    • Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP
    • Schirmer E.C., and Lindquist S. Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP. Proc. Natl. Acad. Sci. USA 94 (1997) 13932-13937
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13932-13937
    • Schirmer, E.C.1    Lindquist, S.2
  • 144
    • 0030908014 scopus 로고    scopus 로고
    • Corticobasal degeneration: Neuropathologic and clinical heterogeneity
    • Schneider J.A., Watts R.L., Gearing M., Brewer R.P., and Mirra S.S. Corticobasal degeneration: Neuropathologic and clinical heterogeneity. Neurol. 48 (1997) 959-969
    • (1997) Neurol. , vol.48 , pp. 959-969
    • Schneider, J.A.1    Watts, R.L.2    Gearing, M.3    Brewer, R.P.4    Mirra, S.S.5
  • 145
    • 0033169079 scopus 로고    scopus 로고
    • Presenilins in their infancy
    • Schweisguth F. Presenilins in their infancy. Chem. Biol. 6 (1999) R187-R190
    • (1999) Chem. Biol. , vol.6
    • Schweisguth, F.1
  • 146
    • 0033119401 scopus 로고    scopus 로고
    • Non-conventional infectious elements in filamentous fungi
    • Silar P., and Daboussi M.-J. Non-conventional infectious elements in filamentous fungi. Trends Genet. 15 (1999) 141-145
    • (1999) Trends Genet. , vol.15 , pp. 141-145
    • Silar, P.1    Daboussi, M.-J.2
  • 148
    • 0032814135 scopus 로고    scopus 로고
    • Alzheimer's disease and the amyloid β protein: What is the role of amyloid?
    • Small D.H., and McLean C.A. Alzheimer's disease and the amyloid β protein: What is the role of amyloid?. J. Neurochem. 73 (1999) 443-449
    • (1999) J. Neurochem. , vol.73 , pp. 443-449
    • Small, D.H.1    McLean, C.A.2
  • 150
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien D.L., Cummings C.J., Adams H.P., Mancini M.G., Patel K., DeMartino G.N., Marcelli M., Weigel N.L., and Mancini M.A. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum. Mol. Gen. 8 (1999) 731-741
    • (1999) Hum. Mol. Gen. , vol.8 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    DeMartino, G.N.6    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 153
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F.E., DeArmond S.J., and Prusiner S.B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83 (1995) 79-90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 154
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosome
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosome. Cell 72 (1993) 971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 156
    • 0033134869 scopus 로고    scopus 로고
    • Aggregates in neurodegenerative disease: Crowds and power?
    • Tran P.B., and Miller R.J. Aggregates in neurodegenerative disease: Crowds and power?. Trends Neurol. Sci. 22 (1999) 194-197
    • (1999) Trends Neurol. Sci. , vol.22 , pp. 194-197
    • Tran, P.B.1    Miller, R.J.2
  • 157
    • 0031733824 scopus 로고    scopus 로고
    • Lectins as chaperones in glycoprotein folding
    • Trombetta E.S., and Helenius A. Lectins as chaperones in glycoprotein folding. Curr. Op. Struct. Biol. 8 (1998) 587-592
    • (1998) Curr. Op. Struct. Biol. , vol.8 , pp. 587-592
    • Trombetta, E.S.1    Helenius, A.2
  • 159
    • 0032869168 scopus 로고    scopus 로고
    • An update on the role of free radicals and antioxidant defense in human disease
    • Vendemiale G., Grattagliano I., and Altomare E. An update on the role of free radicals and antioxidant defense in human disease. Intl. J. Clin. Lab. Res. 29 (1999) 49-55
    • (1999) Intl. J. Clin. Lab. Res. , vol.29 , pp. 49-55
    • Vendemiale, G.1    Grattagliano, I.2    Altomare, E.3
  • 161
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner I., Arlt H., van Dyck L., Langer T., and Neupert W. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13 (1994) 5135-5145
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    van Dyck, L.3    Langer, T.4    Neupert, W.5
  • 162
    • 0032837741 scopus 로고    scopus 로고
    • The levels of soluble versus insoluble Aβ distinguish Alzheimer's disease from normal and pathologic aging
    • Wang J., Dickson D.W., Trojanowsi J.Q., and Lee V.M.-Y. The levels of soluble versus insoluble Aβ distinguish Alzheimer's disease from normal and pathologic aging. Exp. Neurol. 158 (1999) 328-337
    • (1999) Exp. Neurol. , vol.158 , pp. 328-337
    • Wang, J.1    Dickson, D.W.2    Trojanowsi, J.Q.3    Lee, V.M.-Y.4
  • 164
    • 0031551576 scopus 로고    scopus 로고
    • Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae
    • Westermann B., and Neupert W. Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae. J. Mol. Biol. 272 (1997) 477-483
    • (1997) J. Mol. Biol. , vol.272 , pp. 477-483
    • Westermann, B.1    Neupert, W.2
  • 167
    • 0001010955 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic cytosolic chaperonin-containing TCP-1
    • Bukau B. (Ed), Harwood Academic Publishers, Australia
    • Willison K.R. Composition and function of the eukaryotic cytosolic chaperonin-containing TCP-1. In: Bukau B. (Ed). Molecular Chaperones and Folding Catalysts (1999), Harwood Academic Publishers, Australia 555-571
    • (1999) Molecular Chaperones and Folding Catalysts , pp. 555-571
    • Willison, K.R.1
  • 168
    • 0032488048 scopus 로고    scopus 로고
    • A manifesto for microbial genomics
    • Woese C.R. A manifesto for microbial genomics. Curr. Biol. 8 (1998) R781-R783
    • (1998) Curr. Biol. , vol.8
    • Woese, C.R.1
  • 169
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese C.R., Kandler O., and Wheelis M.L. Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. USA 87 (1990) 4576-4579
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 170
    • 0031725057 scopus 로고    scopus 로고
    • Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT
    • Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., and Reed S.I. Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT. Mol. Cellul. Biol. 18 (1998) 7584-7589
    • (1998) Mol. Cellul. Biol. , vol.18 , pp. 7584-7589
    • Won, K.-A.1    Schumacher, R.J.2    Farr, G.W.3    Horwich, A.L.4    Reed, S.I.5
  • 172
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease
    • Xia W., Zhang J., Perez R., Koo E.H., and Selkoe D.J. Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease. Proc. Natl. Acad. Sci. USA 94 (1997) 8208-8213
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Perez, R.3    Koo, E.H.4    Selkoe, D.J.5
  • 173
    • 0031447219 scopus 로고    scopus 로고
    • Overexpression of unliganded steroid receptors activates endogenous heat shock factor
    • Xiao N., and DeFranco D.B. Overexpression of unliganded steroid receptors activates endogenous heat shock factor. Mol. Endocrinol. 11 (1997) 1365-1374
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1365-1374
    • Xiao, N.1    DeFranco, D.B.2
  • 174
    • 0033034101 scopus 로고    scopus 로고
    • Ubiqutin system: Selectivity and timing of protein destruction
    • (1999)
    • Yamao F. Ubiqutin system: Selectivity and timing of protein destruction. J. Biochem. 125 (1999) 223-229 (1999)
    • (1999) J. Biochem. , vol.125 , pp. 223-229
    • Yamao, F.1
  • 175
    • 0033575336 scopus 로고    scopus 로고
    • Intracellular accumulation of insoluble, newly synthesized Aβn-42 in amyloid precursor protein-transfected cells that have been treated with Aβ1-42
    • Yang A.J., Chandswangbhuvana D., Shu T., Henschen A., and Glabe C.G. Intracellular accumulation of insoluble, newly synthesized Aβn-42 in amyloid precursor protein-transfected cells that have been treated with Aβ1-42. J. Biol. Chem. 274 (1999) 20650-20656
    • (1999) J. Biol. Chem. , vol.274 , pp. 20650-20656
    • Yang, A.J.1    Chandswangbhuvana, D.2    Shu, T.3    Henschen, A.4    Glabe, C.G.5
  • 176
    • 0033519893 scopus 로고    scopus 로고
    • Complement regulators C1 inhibitor and CD59 do not significantly inhibit complement activation in Alzheimer disease
    • Yasojima K., McGeer E.G., and McGeer P.L. Complement regulators C1 inhibitor and CD59 do not significantly inhibit complement activation in Alzheimer disease. Brain Res. 833 (1999) 297-301
    • (1999) Brain Res. , vol.833 , pp. 297-301
    • Yasojima, K.1    McGeer, E.G.2    McGeer, P.L.3
  • 177
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis
    • Yu Z., Luo H., Fu W., and Mattson M.P. The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis. Exp. Neurol. 155 (1999) 302-314
    • (1999) Exp. Neurol. , vol.155 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 178
    • 0033567058 scopus 로고    scopus 로고
    • Protein folding in a specialized compartment: The endoplasmic reticulum
    • Zapun A., Jakob C.A., Thomas D.Y., and Bergeron J.J.M. Protein folding in a specialized compartment: The endoplasmic reticulum. Structure 7 (1999) R173-R182
    • (1999) Structure , vol.7
    • Zapun, A.1    Jakob, C.A.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 179
    • 0034714463 scopus 로고    scopus 로고
    • Localization of flotillins in human brain and their accumulation with the progression of Alzheimer's disease pathology
    • Kokubo H., Lemere C.A., and Yamaguchi H. Localization of flotillins in human brain and their accumulation with the progression of Alzheimer's disease pathology. Neurosc. Lett. 290 (2000) 93-96
    • (2000) Neurosc. Lett. , vol.290 , pp. 93-96
    • Kokubo, H.1    Lemere, C.A.2    Yamaguchi, H.3
  • 181
    • 0034662915 scopus 로고    scopus 로고
    • Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease
    • Carmichael J., Chatellier J., Woolfson A., Milstein C., Fehrst A.R., and Rubinsztein D.C. Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease. Proc. Natl. Acad. Sci. USA 97 (2000) 9701-9705
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9701-9705
    • Carmichael, J.1    Chatellier, J.2    Woolfson, A.3    Milstein, C.4    Fehrst, A.R.5    Rubinsztein, D.C.6
  • 182
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana N.R., Tanaka M., Wang G., and Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 9 (2000) 2009-2018
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 185
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharamocyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • Moriyama H., Edskes H.K., and Wickner R.B. [URE3] prion propagation in Saccharamocyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cellul. Biol. 20 (2000) 8916-8922
    • (2000) Mol. Cellul. Biol. , vol.20 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 186
    • 0034623960 scopus 로고    scopus 로고
    • The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome
    • Jin T., Gu Y., Zanuso G., Sy M., Kumar A., Cohen M., Gambetti P., and Singh N. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J. Biol. Chem. 275 (2000) 38699-38704
    • (2000) J. Biol. Chem. , vol.275 , pp. 38699-38704
    • Jin, T.1    Gu, Y.2    Zanuso, G.3    Sy, M.4    Kumar, A.5    Cohen, M.6    Gambetti, P.7    Singh, N.8
  • 187
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of aging
    • Finkel T., and Holbrook N.J. Oxidants, oxidative stress and the biology of aging. Nature 408 (2000) 239-247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 189
    • 0034088054 scopus 로고    scopus 로고
    • Beneficial effects of dietary restriction on cerebral cortical synaptic terminals: Preservation of glucose and glutamate transport and mitochondrial function after exposure to amyloid beta-peptide, iron, and 3-nitropropionic acid
    • Guo Z.H., Ersoz A., Butterfield D.A., and Mattson M.P. Beneficial effects of dietary restriction on cerebral cortical synaptic terminals: Preservation of glucose and glutamate transport and mitochondrial function after exposure to amyloid beta-peptide, iron, and 3-nitropropionic acid. J. Neurochem. 75 (2000) 314-320
    • (2000) J. Neurochem. , vol.75 , pp. 314-320
    • Guo, Z.H.1    Ersoz, A.2    Butterfield, D.A.3    Mattson, M.P.4
  • 190
    • 0034116190 scopus 로고    scopus 로고
    • ALS-linked Cu/ZnSOD mutation impairs cerebral synaptic glucose and glutamate transport and exacerbates ischemic brain injury
    • Guo Z.H., Kindy M.S., Kruman I., and Mattson M.P. ALS-linked Cu/ZnSOD mutation impairs cerebral synaptic glucose and glutamate transport and exacerbates ischemic brain injury. J. Cer. Blood Flow Metab. 20 (2000) 463-468
    • (2000) J. Cer. Blood Flow Metab. , vol.20 , pp. 463-468
    • Guo, Z.H.1    Kindy, M.S.2    Kruman, I.3    Mattson, M.P.4
  • 191
    • 0002639306 scopus 로고    scopus 로고
    • Neurotrophic factors protect cortical synaptic terminals against amyloid- and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function
    • Guo Z.H., and Mattson M.P. Neurotrophic factors protect cortical synaptic terminals against amyloid- and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function. Cer. Cortex 10 (2000) 50-57
    • (2000) Cer. Cortex , vol.10 , pp. 50-57
    • Guo, Z.H.1    Mattson, M.P.2
  • 192
    • 0033766916 scopus 로고    scopus 로고
    • In vivo 2-deoxyglucose administration preserves glucose and glutamate transport and mitochondrial function in cortical synaptic terminals after exposure to amyloid beta-peptide and iron: Evidence for a stress response
    • Guo Z.H., and Mattson M.P. In vivo 2-deoxyglucose administration preserves glucose and glutamate transport and mitochondrial function in cortical synaptic terminals after exposure to amyloid beta-peptide and iron: Evidence for a stress response. Exp. Neurol. 166 (2000) 173-179
    • (2000) Exp. Neurol. , vol.166 , pp. 173-179
    • Guo, Z.H.1    Mattson, M.P.2
  • 193
    • 0034077078 scopus 로고    scopus 로고
    • 4-Hydroxynonenal induces oxidative stress and death of cultured spinal cord neurons
    • Malecki A., Garrido R., Mattson M.P., Hennig B., and Toborek M. 4-Hydroxynonenal induces oxidative stress and death of cultured spinal cord neurons. J. Neurochem. 74 (2000) 2278-2287
    • (2000) J. Neurochem. , vol.74 , pp. 2278-2287
    • Malecki, A.1    Garrido, R.2    Mattson, M.P.3    Hennig, B.4    Toborek, M.5
  • 194
    • 0033400774 scopus 로고    scopus 로고
    • Aberrant stress response associated with severe hypoglycemia in a transgenic mouse model of Alzheimer's disease
    • Pedersen W.A., Culmsee C., Ziegler D., Herman J.P., and Mattson M.P. Aberrant stress response associated with severe hypoglycemia in a transgenic mouse model of Alzheimer's disease. J. Mol. Neurosc. 13 (1999) 159-165
    • (1999) J. Mol. Neurosc. , vol.13 , pp. 159-165
    • Pedersen, W.A.1    Culmsee, C.2    Ziegler, D.3    Herman, J.P.4    Mattson, M.P.5
  • 197
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach A., Carmichael J., Swartz J., Furlong R.A., Narain Y., Rankin J., and Rubinsztein D.C. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl. Acad. Sci. USA 97 (2000) 2898-2903
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5    Rankin, J.6    Rubinsztein, D.C.7
  • 198
    • 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.K., Huang H., Dawson V.L., and Dawson T.M. 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 (2000) 13354-13359
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.