메뉴 건너뛰기




Volumn 84, Issue 22, 2010, Pages 12030-12038

Distinct stability states of disease-associated human prion protein identified by conformation-dependent immunoassay

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

EID: 78049519681     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01057-10     Document Type: Article
Times cited : (28)

References (54)
  • 2
    • 0037813125 scopus 로고    scopus 로고
    • Improved conformation-dependent immunoassay: Suitability for human prion detection with enhanced sensitivity
    • Bellon, A., W. Seyfert-Brandt, W. Lang, H. Baron, A. Gröner, and M. Vey. 2003. Improved conformation-dependent immunoassay: suitability for human prion detection with enhanced sensitivity. J. Gen. Virol. 84:1921-1925.
    • (2003) J. Gen. Virol. , vol.84 , pp. 1921-1925
    • Bellon, A.1    Seyfert-Brandt, W.2    Lang, W.3    Baron, H.4    Gröner, A.5    Vey, M.6
  • 4
    • 0032570091 scopus 로고
    • 1755 and all that: A historical primer of transmissible spongiform encephalopathy
    • Brown, P., and R. Bradley. 1989. 1755 and all that: a historical primer of transmissible spongiform encephalopathy. Br. Med. J. 317:1688-1692.
    • (1989) Br. Med. J. , vol.317 , pp. 1688-1692
    • Brown, P.1    Bradley, R.2
  • 6
    • 0141515178 scopus 로고    scopus 로고
    • TSE strain variation
    • Bruce, M. E. 2003. TSE strain variation. Br. Med. Bull. 66:99-108.
    • (2003) Br. Med. Bull. , vol.66 , pp. 99-108
    • Bruce, M.E.1
  • 7
    • 70349937836 scopus 로고    scopus 로고
    • Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: Its effect on the phenotype and prion-type characteristics
    • Cali, I., R. Castellani, A. Alshekhlee, Y. Cohen, J. Blevins, J. Yuan, J. P. Langeveld, P. Parchi, J. G. Safar, W. Q. Zou, and P. Gambetti. 2009. Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics. Brain 132:2643-2658.
    • (2009) Brain , vol.132 , pp. 2643-2658
    • Cali, I.1    Castellani, R.2    Alshekhlee, A.3    Cohen, Y.4    Blevins, J.5    Yuan, J.6    Langeveld, J.P.7    Parchi, P.8    Safar, J.G.9    Zou, W.Q.10    Gambetti, P.11
  • 8
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey, B., and G. Baron. 2006. Prions and their partners in crime. Nature 443:803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.2
  • 10
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • Collinge, J., K. C. L. Sidle, J. Meads, J. Ironside, and A. F. Hill. 1996. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383:685-690.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 11
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge, J., and A. R. Clarke. 2007. A general model of prion strains and their pathogenicity. Science 318:930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 15
    • 0030342679 scopus 로고
    • Scrapie prions: A three-dimensional model of an infectious fragment
    • Huang, Z., S. B. Prusiner, and F. E. Cohen. 1995. Scrapie prions: a three-dimensional model of an infectious fragment. Fold. Des. 1:13-19.
    • (1995) Fold. Des. , vol.1 , pp. 13-19
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 17
    • 68149100194 scopus 로고    scopus 로고
    • Prion diseases
    • S. Love, D. N. Lious, and D. Ellison (ed.), 8th ed., Hodder Arnold, London, United Kingdom
    • Ironside, J. W., B. Ghetti, M. W. Head, P. Piccardo, and R. G. Will. 2008. Prion diseases, p. 1197-1273. In S. Love, D. N. Lious, and D. Ellison (ed.), Greenfield's neuropathology, 8th ed., vol. 2. Hodder Arnold, London, United Kingdom.
    • (2008) Greenfield's Neuropathology , vol.2 , pp. 1197-1273
    • Ironside, J.W.1    Ghetti, B.2    Head, M.W.3    Piccardo, P.4    Will, R.G.5
  • 19
    • 0029819057 scopus 로고    scopus 로고
    • Partial unfolding and refolding of scrapie-associated prion protein: Evidence for a critical 16-kDa C-terminal domain
    • Kocisko, D. A., P. T. Landsbury, and B. Caughey. 1996. Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain. Biochemistry 35:13434-13442.
    • (1996) Biochemistry , vol.35 , pp. 13434-13442
    • Kocisko, D.A.1    Landsbury, P.T.2    Caughey, B.3
  • 22
    • 26444434251 scopus 로고    scopus 로고
    • Selective precipitation of prions by polyoxometalate complexes
    • Lee, I. S., J. R. Long, S. B. Prusiner, and J. G. Safar. 2005. Selective precipitation of prions by polyoxometalate complexes. J. Am. Chem. Soc. 127:13802-13803.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13802-13803
    • Lee, I.S.1    Long, J.R.2    Prusiner, S.B.3    Safar, J.G.4
  • 26
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structures of the prion protein yields two distinct self-propagating states
    • Makarava, N., and I. V. Baskakov. 2008. The same primary structures of the prion protein yields two distinct self-propagating states. J. Biol. Chem. 283:15988-15996.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 29
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley, M. P., R. K. Meyer, L. Kenaga, F. Rahbar, R. Cotter, A. Serban, and S. B. Prusiner. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65:1340-1351.
    • (1991) J. Virol. , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3    Rahbar, F.4    Cotter, R.5    Serban, A.6    Prusiner, S.B.7
  • 31
    • 0028240984 scopus 로고
    • Properties of the scrapie prion protein: Quantitative analysis of protease resistance
    • DOI 10.1021/bi00185a033
    • Oesch, B., M. Jensen, P. Nilsson, and J. Fogh. 1994. Properties of the scrapie prion protein: quantitative analysis of protease resistance. Biochemistry 33:5926-5931. (Pubitemid 24184598)
    • (1994) Biochemistry , vol.33 , Issue.19 , pp. 5926-5931
    • Oesch, B.1    Jensen, M.2    Nilsson, P.3    Fogh, J.4
  • 42
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein
    • Safar, J., P. P. Roller, D. C. Gajdusek, and C. J. Gibbs. 1993. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268:20276-20284.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs, C.J.4
  • 46
    • 0036900691 scopus 로고    scopus 로고
    • TSE agent strain and PrP: Structure and function
    • Somerville, R. A. 2002. TSE agent strain and PrP: structure and function. Trends Biochem. Sci. 27:606-612.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 606-612
    • Somerville, R.A.1
  • 47
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. 1968. Protein denaturation. Adv. Protein Chem. 23:121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 48
    • 33846490771 scopus 로고    scopus 로고
    • Proteinase K-sensitive disease-associated ovine prion protein revealed by conformation-dependent immunoassay
    • Thackray, A. M., L. Hopkins, and R. Bujdoso. 2007. Proteinase K-sensitive disease-associated ovine prion protein revealed by conformation-dependent immunoassay. Biochem. J. 401:475-483.
    • (2007) Biochem. J. , vol.401 , pp. 475-483
    • Thackray, A.M.1    Hopkins, L.2    Bujdoso, R.3
  • 51
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang, F., X. Wang, C. G. Yuan, and J. Ma. 2010. Generating a prion with bacterially expressed recombinant prion protein. Science 327:1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.