메뉴 건너뛰기




Volumn 322, Issue 4, 2002, Pages 799-814

Amyloidogenic unfolding intermediates differentiate sheep prion protein variants

Author keywords

Amyloidogenic intermediate; PrP genetic polymorphism; Scrapie susceptibility; Sheep prion protein; Unfolding pathway

Indexed keywords

AMYLOID PROTEIN; PRION PROTEIN; THIOFLAVINE;

EID: 0036387276     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00856-2     Document Type: Article
Times cited : (110)

References (37)
  • 1
    • 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
  • 2
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C., McKinley, M. P. & Prusiner, S. B. (1982). Identification of a protein that purifies with the scrapie prion. Science, 218, 1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 3
    • 0026094450 scopus 로고
    • Electrospray mass spectrometry of the glycosyl-inositol phospholipid of the scrapie prion protein
    • Stahl, N., Baldwin, M. A. & Prusiner, S. B. (1991). Electrospray mass spectrometry of the glycosyl-inositol phospholipid of the scrapie prion protein. Cell Biol. Int. Rep. 15, 853-862.
    • (1991) Cell Biol. Int. Rep. , vol.15 , pp. 853-862
    • Stahl, N.1    Baldwin, M.A.2    Prusiner, S.B.3
  • 5
    • 0029802278 scopus 로고    scopus 로고
    • Novel polymorphisms in the caprine PrP gene: A codon 142 mutation associated with scrapie incubation period
    • Goldmann, W., Martin, T., Foster, J., Hughes, S., Smith, G., Hughes, K. et al. (1996). Novel polymorphisms in the caprine PrP gene: a codon 142 mutation associated with scrapie incubation period. J. Gen. Virol. 77, 2885-2891.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2885-2891
    • Goldmann, W.1    Martin, T.2    Foster, J.3    Hughes, S.4    Smith, G.5    Hughes, K.6
  • 6
    • 0028928171 scopus 로고
    • Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie
    • Belt, P. B., Muileman, I. H., Schreuder, B. E., Bos-de Ruijter, J., Gielkens, A. L. & Smits, M. A. (1995). Identification of five allelic variants of the sheep PrP gene and their association with natural scrapie. J. Gen. Virol. 76, 509-517.
    • (1995) J. Gen. Virol. , vol.76 , pp. 509-517
    • Belt, P.B.1    Muileman, I.H.2    Schreuder, B.E.3    Bos-de Ruijter, J.4    Gielkens, A.L.5    Smits, M.A.6
  • 7
    • 0032925271 scopus 로고    scopus 로고
    • Prion protein gene polymorphisms in sheep with natural scrapie and healthy controls in Norway
    • Tranulis, M. A., Osland, A., Bratberg, B. & Ulvund, M. J. (1999). Prion protein gene polymorphisms in sheep with natural scrapie and healthy controls in Norway. J. Gen. Virol. 80, 1073-1077.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1073-1077
    • Tranulis, M.A.1    Osland, A.2    Bratberg, B.3    Ulvund, M.J.4
  • 8
    • 0032913328 scopus 로고    scopus 로고
    • Genetic susceptibility and transmission factors in scrapie: Detailed analysis of an epidemic in a closed flock of Romanov
    • Elsen, J. M., Amigues, Y., Schelcher, F., Ducrocq, V., Andreoletti, O., Eychenne, F. et al. (1999). Genetic susceptibility and transmission factors in scrapie: detailed analysis of an epidemic in a closed flock of Romanov. Arch. Virol. 144, 431-445.
    • (1999) Arch. Virol. , vol.144 , pp. 431-445
    • Elsen, J.M.1    Amigues, Y.2    Schelcher, F.3    Ducrocq, V.4    Andreoletti, O.5    Eychenne, F.6
  • 9
    • 0028349264 scopus 로고
    • PrP genotype and agent effects in scrapie: Change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie
    • Goldmann, W., Hunter, N., Smith, G., Foster, J. & Hope, J. (1994). PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75, 989-995.
    • (1994) J. Gen. Virol. , vol.75 , pp. 989-995
    • Goldmann, W.1    Hunter, N.2    Smith, G.3    Foster, J.4    Hope, J.5
  • 10
    • 0032892688 scopus 로고    scopus 로고
    • Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie CH1641
    • Hope, J., Wood, S. C., Birkett, C. R., Chong, A., Bruce, M. E., Cairns, D. et al. (1999). Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie CH1641. J. Gen. Virol. 80, 1-4.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1-4
    • Hope, J.1    Wood, S.C.2    Birkett, C.R.3    Chong, A.4    Bruce, M.E.5    Cairns, D.6
  • 11
    • 0034784764 scopus 로고    scopus 로고
    • Distribution of the prion protein in sheep terminally affected with BSE following experimental oral transmission
    • Foster, J. D., Parnham, D. W., Hunter, N. & Bruce, M. (2001). Distribution of the prion protein in sheep terminally affected with BSE following experimental oral transmission. J. Gen. Virol. 82, 2319-2326.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2319-2326
    • Foster, J.D.1    Parnham, D.W.2    Hunter, N.3    Bruce, M.4
  • 12
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki, W., Petersen, R. B., Gambetti, P. & Surewicz, W. K. (1998). Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 273, 31048-31052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 13
    • 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. (1999). Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry, 38, 3258-3267.
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 15
    • 0034127890 scopus 로고    scopus 로고
    • High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility
    • Rezaei, H., Marc, D., Choiset, Y., Takahashi, M., Hui Bon Hoa, G., Haertle, T. et al. (2000). High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur. J. Biochem. 267, 2833-2839.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2833-2839
    • Rezaei, H.1    Marc, D.2    Choiset, Y.3    Takahashi, M.4    Hui Bon Hoa, G.5    Haertle, T.6
  • 16
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W. (1998). The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 17
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly, J. W. (2000). Mechanisms of amyloidogenesis. Nature Struct. Biol. 7, 824-826.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 18
    • 0030572627 scopus 로고    scopus 로고
    • Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein
    • Hornemann, S. & Glockshuber, R. (1996). Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein. J. Mol. Biol. 261, 614-619.
    • (1996) J. Mol. Biol. , vol.261 , pp. 614-619
    • Hornemann, S.1    Glockshuber, R.2
  • 19
    • 0032568592 scopus 로고    scopus 로고
    • A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
    • Hornemann, S. & Glockshuber, R. (1998). A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc. Natl Acad. Sci. USA, 95, 6010-6014.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6010-6014
    • Hornemann, S.1    Glockshuber, R.2
  • 20
    • 0031789527 scopus 로고    scopus 로고
    • Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation
    • Post, K., Pitschke, M., Schafer, O., Wille, H., Appel, T. R., Kirsch, D. et al. (1998). Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation. Biol. Chem. 379, 1307-1317.
    • (1998) Biol. Chem. , vol.379 , pp. 1307-1317
    • Post, K.1    Pitschke, M.2    Schafer, O.3    Wille, H.4    Appel, T.R.5    Kirsch, D.6
  • 22
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPr90-231
    • Swietnicki, W., Morillas, M., Chen, S. G., Gambetti, P. & Surewicz, W. K. (2000). Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry, 39, 424-431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 23
    • 0035849540 scopus 로고    scopus 로고
    • On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein
    • Morillas, M., Vanik, D. L. & Surewicz, W. K. (2001). On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein. Biochemistry, 40, 6982-6987.
    • (2001) Biochemistry , vol.40 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 24
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • Baskakov, I. V., Legname, G., Prusiner, S. B. & Cohen, F. E. (2001). Folding of prion protein to its native alpha-helical conformation is under kinetic control. J. Biol. Chem. 276, 19687-19690.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 25
    • 0035951859 scopus 로고    scopus 로고
    • The role of disulfide bridge in the folding and stability of the recombinant human prion protein
    • Maiti, N. R. & Surewicz, W. K. (2001). The role of disulfide bridge in the folding and stability of the recombinant human prion protein. J. Biol. Chem. 276, 2427-2431.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2427-2431
    • Maiti, N.R.1    Surewicz, W.K.2
  • 26
    • 0034943638 scopus 로고    scopus 로고
    • Folding dynamics and energetics of recombinant prion proteins
    • Glockshuber, R. (2001). Folding dynamics and energetics of recombinant prion proteins. Advan. Protein Chem. 57, 83-105.
    • (2001) Advan. Protein Chem. , vol.57 , pp. 83-105
    • Glockshuber, R.1
  • 27
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. (1979). Stability of proteins: small globular proteins. Advan. Protein Chem. 33, 167-241.
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 28
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deleage, G. & Geourjon, C. (1993). An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput. Appl. Biosci. 9, 197-199.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 197-199
    • Deleage, G.1    Geourjon, C.2
  • 29
    • 0034537674 scopus 로고    scopus 로고
    • A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP
    • Meyer, R. K., Lustig, A., Oesch, B., Fatzer, R., Zurbriggen, A. & Vandevelde, M. (2000). A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP. J. Biol. Chem. 275, 38081-38087.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38081-38087
    • Meyer, R.K.1    Lustig, A.2    Oesch, B.3    Fatzer, R.4    Zurbriggen, A.5    Vandevelde, M.6
  • 30
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • Sanchez-Ruiz, J. M., Lopez-Lacomba, J. L., Cortijo, M. & Mateo, P. L. (1988). Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry, 27, 1648-1652.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 31
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N. & Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 33
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz, J. M. (1992). Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61, 921-935.
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 34
    • 0035853093 scopus 로고    scopus 로고
    • Mapping the early steps in the pH-induced conformational conversion of the prion protein
    • Alonso, D. O., DeArmond, S. J., Cohen, F. E. & Daggett, V. (2001). Mapping the early steps in the pH-induced conformational conversion of the prion protein. Proc. Natl Acad. Sci. USA, 98, 2985-2989.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2985-2989
    • Alonso, D.O.1    DeArmond, S.J.2    Cohen, F.E.3    Daggett, V.4
  • 35
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko, K., Zulianello, L., Scott, M., Cooper, C. M., Wallace, A. C., James, T. L. et al. (1997). Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl Acad. Sci. USA, 94, 10069-10074.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3    Cooper, C.M.4    Wallace, A.C.5    James, T.L.6
  • 36
    • 0035798377 scopus 로고    scopus 로고
    • Chaperonin-mediated de novo generation of prion protein aggregates
    • Stockel, J. & Hartl, F. U. (2001). Chaperonin-mediated de novo generation of prion protein aggregates. J. Mol. Biol. 313, 861-872.
    • (2001) J. Mol. Biol. , vol.313 , pp. 861-872
    • Stockel, J.1    Hartl, F.U.2
  • 37
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado, M., Merkel, J. S. & Regan, L. (2000). A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl Acad. Sci. USA, 97, 8979-8984.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.