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Volumn 18, Issue 6, 1998, Pages 721-729

Abnormalities in stress proteins in prion diseases

Author keywords

Heat shock proteins; Molecular chaperones; Prion diseases; PrP(C); PrP(Sc)

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; PRION PROTEIN;

EID: 0032428513     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020282205041     Document Type: Review
Times cited : (22)

References (37)
  • 1
    • 0027509361 scopus 로고
    • The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion
    • Brown, C. R., Martin, R. L., Hansen, W. J., Beckmann, R. P., and Welch, W. J. (1993). The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J. Cell Biol. 120:1101-1112.
    • (1993) J. Cell Biol. , vol.120 , pp. 1101-1112
    • Brown, C.R.1    Martin, R.L.2    Hansen, W.J.3    Beckmann, R.P.4    Welch, W.J.5
  • 3
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases:importance of seeding
    • Come, J. H., Fraser, P. E., and Lansbury, P. T., Jr. (1993). A kinetic model for amyloid formation in the prion diseases:importance of seeding. Proc. Natl. Acad. Sci. USA 90:5959-5963.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury Jr., P.T.3
  • 4
    • 0028484034 scopus 로고
    • Prion-like factors in yeast
    • Cox, B. (1994). Prion-like factors in yeast. Curr. Biol. 8:744-748.
    • (1994) Curr. Biol. , vol.8 , pp. 744-748
    • Cox, B.1
  • 5
    • 0028922696 scopus 로고
    • Etiology and pathogenesis of prion diseases
    • DeArmond, S. J., and Prusiner, S. B. (1995). Etiology and pathogenesis of prion diseases. Am. J. Pathol. 146:785-811.
    • (1995) Am. J. Pathol. , vol.146 , pp. 785-811
    • DeArmond, S.J.1    Prusiner, S.B.2
  • 8
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C., and Welch, W. J. (1993). Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9:601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 9
    • 0027159497 scopus 로고
    • Synthetic peptides corresponding to different mutated regions of the amyloid gene in familial Creutzfeldt-Jakob disease show enhanced in vitro formation of morphologically different amyloid fibrils
    • Goldfarb, L. G., Brown, P., Haltia, M., Ghiso, J., Frangione, B., and Gajdusek, D. C. (1993). Synthetic peptides corresponding to different mutated regions of the amyloid gene in familial Creutzfeldt-Jakob disease show enhanced in vitro formation of morphologically different amyloid fibrils. Proc. Natl. Acad. Sci. USA 90:4451-4454.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4451-4454
    • Goldfarb, L.G.1    Brown, P.2    Haltia, M.3    Ghiso, J.4    Frangione, B.5    Gajdusek, D.C.6
  • 10
    • 0023473545 scopus 로고
    • Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern
    • Gorevic, P. D., Castano, E. M., Sarma, R., and Frangione, B. (1987). Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic X-ray diffraction pattern. Biochem. Biophys. Res. Commun. 147:854-862.
    • (1987) Biochem. Biophys. Res. Commun. , vol.147 , pp. 854-862
    • Gorevic, P.D.1    Castano, E.M.2    Sarma, R.3    Frangione, B.4
  • 12
    • 0025823394 scopus 로고
    • A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity
    • Harris, D. A., Falls, D. L., Johnson, F. A., and Fischbach, G. D. (1991). A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity. Proc. Natl. Acad. Sci. USA 88:7664-7668.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7664-7668
    • Harris, D.A.1    Falls, D.L.2    Johnson, F.A.3    Fischbach, G.D.4
  • 13
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P., and Hartl, F. U. (1993). Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62:349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 15
    • 0025681138 scopus 로고
    • Spontaneous neurodegeneration in transgenic mice with mutant prion protein
    • Hsiao, K. K., Scott, M., Foster, D., Groth, D. F., DeArmond, S. J., and Prusiner, S. B. (1990). Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 250:1587-1590.
    • (1990) Science , vol.250 , pp. 1587-1590
    • Hsiao, K.K.1    Scott, M.2    Foster, D.3    Groth, D.F.4    DeArmond, S.J.5    Prusiner, S.B.6
  • 16
    • 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. (1994). Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain. J. Neurochem. 62:1870-1877.
    • (1994) J. Neurochem. , vol.62 , pp. 1870-1877
    • Kenward, N.1    Hope, J.2    Landon, M.3    Mayer, R.J.4
  • 18
    • 0027220589 scopus 로고
    • Protein traffic on the heat shock promoter: Parking, stalling, and trucking along
    • Lis, J., and Wu, C. (1993). Protein traffic on the heat shock promoter: Parking, stalling, and trucking along. Cell 74:1-4.
    • (1993) Cell , vol.74 , pp. 1-4
    • Lis, J.1    Wu, C.2
  • 21
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 23
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C. J., Burdick, D., Walencewicz, A. J., Glabe, C. G., and Cotman, C. W. (1993). Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. J. Neurosci. 13:1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 24
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 25
  • 27
    • 0003382064 scopus 로고
    • Nucleic acids and scrapie prions
    • Prusiner, S. B., Collinge, J., Powell, J., and Anderton, B. (eds.), Ellis Horwood, London
    • Riesner, D., Kellings, K., Meyer, N., Mirenda, C., and Prusiner, S. B. (1992). Nucleic acids and scrapie prions. In Prusiner, S. B., Collinge, J., Powell, J., and Anderton, B. (eds.), Prion Diseases of Humans and Animals, Ellis Horwood, London, pp. 341-358.
    • (1992) Prion Diseases of Humans and Animals , pp. 341-358
    • Riesner, D.1    Kellings, K.2    Meyer, N.3    Mirenda, C.4    Prusiner, S.B.5
  • 28
    • 0027229676 scopus 로고
    • Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes
    • Scott, M., Groth, D., Foster, D., Torchia, M., Yang, S.-L., DeArmond, S. J., and Prusiner, S. B. (1993). Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 73:979-988.
    • (1993) Cell , vol.73 , pp. 979-988
    • Scott, M.1    Groth, D.2    Foster, D.3    Torchia, M.4    Yang, S.-L.5    DeArmond, S.J.6    Prusiner, S.B.7
  • 29
    • 0027534612 scopus 로고
    • Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993). Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32:1991-2002.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 30
    • 0025373111 scopus 로고
    • Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells
    • Taraboulos, A., Serban, D., and Prusiner, S. B. (1990). Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J. Cell Biol. 110:2117-2132.
    • (1990) J. Cell Biol. , vol.110 , pp. 2117-2132
    • Taraboulos, A.1    Serban, D.2    Prusiner, S.B.3
  • 32
    • 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. (1995). Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:1-12.
    • (1995) Cell , vol.83 , pp. 1-12
    • 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
  • 33
    • 0027925653 scopus 로고
    • Heat shock proteins functioning as molecular chaperones: Their roles in normal and stressed cells
    • Welch, W. J. (1993). Heat shock proteins functioning as molecular chaperones: Their roles in normal and stressed cells. Phil. Trans. Roy Soc. Lond. 339:327-333.
    • (1993) Phil. Trans. Roy Soc. Lond. , vol.339 , pp. 327-333
    • Welch, W.J.1
  • 34
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch, W. J., and Feramisco, J. R. (1984). Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J. Biol. Chem. 259:4501-4513.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 35
    • 0022642301 scopus 로고
    • Conservation of the cellular gene encoding the scrapie prion protein
    • Westaway, D., and Prusiner, S. B. (1986). Conservation of the cellular gene encoding the scrapie prion protein. Nucleic Acids Res. 14:2035-2044.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 2035-2044
    • Westaway, D.1    Prusiner, S.B.2
  • 36
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • Westaway, D., DeArmond, S. J., Cayetano-Canlas, J., Groth, D., Foster, D., Yang, S.-L., Torchia, M., Carlson, G. A., and Prusiner, S. B. (1994). Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76:117-129.
    • (1994) Cell , vol.76 , pp. 117-129
    • Westaway, D.1    DeArmond, S.J.2    Cayetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.-L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9
  • 37
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner, R. B. (1994). [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae. Science 264:566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.