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Volumn 293, Issue 2, 1999, Pages 313-320

Protein misfolding and prion diseases

Author keywords

Alzheimer's disease; Creutzfeldt Jakob disease; Prion; Protein folding

Indexed keywords

PRION PROTEIN;

EID: 0032742943     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2990     Document Type: Article
Times cited : (139)

References (62)
  • 5
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen F. E., Prusiner S. B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67:1998;793-819.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 12
    • 0024434503 scopus 로고
    • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
    • Endo T., Groth D., Prusiner S. B., Kobata A. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry. 28:1989;8380-8388.
    • (1989) Biochemistry , vol.28 , pp. 8380-8388
    • Endo, T.1    Groth, D.2    Prusiner, S.B.3    Kobata, A.4
  • 15
    • 0031587047 scopus 로고    scopus 로고
    • Cannibalism and Kuru
    • Goodfield J. Cannibalism and Kuru. Nature. 387:1997;841.
    • (1997) Nature , vol.387 , pp. 841
    • Goodfield, J.1
  • 19
    • 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., Prusiner S. B. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science. 250:1990;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
  • 22
    • 0030342679 scopus 로고    scopus 로고
    • Scrapie prions: A three-dimensional model of an infectious fragment
    • Huang Z., Prusiner S. B., Cohen F. E. Scrapie prions: a three-dimensional model of an infectious fragment. Fold. Design. 1:1996;13-19.
    • (1996) Fold. Design , vol.1 , pp. 13-19
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 25
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J. T., Lansbury P. T. Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell. 73:1993;1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 28
    • 0032477873 scopus 로고    scopus 로고
    • The environmental dependency of protein folding best explains prion and amyloid diseases
    • Kelly J. W. The environmental dependency of protein folding best explains prion and amyloid diseases. Proc. Natl Acad. Sci. USA. 95:1998;930-932.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 930-932
    • Kelly, J.W.1
  • 30
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30 M, and L55P amyloid fibril formation
    • Lashuel H. A., Lai Z., Kelly J. W. Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30 M, and L55P amyloid fibril formation. Biochemistry. 37:1998;17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 31
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann S., Glockshuber R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry. 38:1999;3258-3267.
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 32
    • 0030728226 scopus 로고    scopus 로고
    • Mad cows meet psi-chotic yeast: The expansion of the prion hypothesis
    • Lindquist S. Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell. 89:1997;495-498.
    • (1997) Cell , vol.89 , pp. 495-498
    • Lindquist, S.1
  • 33
    • 0030045089 scopus 로고    scopus 로고
    • Structural and genetic analysis of the folding and function of T4 lysozyme
    • Matthews B. W. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J. 10:1996;35-41.
    • (1996) FASEB J. , vol.10 , pp. 35-41
    • Matthews, B.W.1
  • 34
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley M. P., Bolton D. C., Prusiner S. B. A protease-resistant protein is a structural component of the scrapie prion. Cell. 35:1983;57-62.
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 36
    • 0031556954 scopus 로고    scopus 로고
    • The structural link between polymerization and sickle cell disease
    • Mirchev R., Ferrone F. A. The structural link between polymerization and sickle cell disease. J. Mol. Biol. 265:1997;475-479.
    • (1997) J. Mol. Biol. , vol.265 , pp. 475-479
    • Mirchev, R.1    Ferrone, F.A.2
  • 43
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner S. B. Prion diseases and the BSE crisis. Science. 278:1997;245-251.
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 45
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner S. B., Groth D. F., Bolton D. C., Kent S. B., Hood L. E. Purification and structural studies of a major scrapie prion protein. Cell. 38:1984;127-134.
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 50
    • 0030952101 scopus 로고    scopus 로고
    • Expression of the calcitonin gene family in medullary thyroid carcinoma
    • Schifter S. Expression of the calcitonin gene family in medullary thyroid carcinoma. Peptides. 18:1997;307-317.
    • (1997) Peptides , vol.18 , pp. 307-317
    • Schifter, S.1
  • 52
    • 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., Prusiner S. B. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell. 73:1993;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
  • 54
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl N., Baldwin M. A., Burlingame A. L., Prusiner S. B. Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry. 29:1990;8879-8884.
    • (1990) Biochemistry , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 57
    • 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., 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
  • 60
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles J. H., Cohen F. E., Prusiner S. B., Goodin D. B., Wright P. E., Dyson J. H. Copper binding to the prion protein: Structural implications of four identical cooperative binding sites. Proc. Natl Acad. Sci. USA. 96:1999;2042-2047.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2042-2047
    • Viles, J.H.1    Cohen, F.E.2    Prusiner, S.B.3    Goodin, D.B.4    Wright, P.E.5    Dyson, J.H.6
  • 61
    • 0030443751 scopus 로고    scopus 로고
    • Prions and RNA viruses of Saccharomyces cerevisiae
    • Wickner R. B. Prions and RNA viruses of Saccharomyces cerevisiae. Annu. Rev. Genet. 30:1996;109-139.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 109-139
    • Wickner, R.B.1
  • 62
    • 0025120245 scopus 로고
    • Non-hydrophobic extracy to plasmic determinant of stop transfer in the prion protein
    • Yost C. S., Lopez C. D., Prusiner S. B., Myers R. M., Lingappa V. R. Non-hydrophobic extracy to plasmic determinant of stop transfer in the prion protein. Nature. 343:1990;669-672.
    • (1990) Nature , vol.343 , pp. 669-672
    • Yost, C.S.1    Lopez, C.D.2    Prusiner, S.B.3    Myers, R.M.4    Lingappa, V.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.