메뉴 건너뛰기




Volumn 79, Issue 19, 2005, Pages 12355-12364

An aggregation-specific enzyme-linked immunosorbent assay: Detection of conformational differences between recombinant PrP protein dimers and PrP Sc aggregates

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY PRP; PRION PROTEIN; PROTEINASE K; UNCLASSIFIED DRUG;

EID: 25144445814     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.19.12355-12364.2005     Document Type: Article
Times cited : (43)

References (41)
  • 2
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C., M. P. McKinley, and S. B. Prusiner. 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
  • 4
    • 0036672005 scopus 로고    scopus 로고
    • Factors affecting interactions between prion protein isoforms
    • Caughey, B., and G. S. Baron. 2002. Factors affecting interactions between prion protein isoforms. Biochem. Soc. Trans. 30:565-569.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 565-569
    • Caughey, B.1    Baron, G.S.2
  • 5
    • 0029583794 scopus 로고
    • Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state
    • Caughey, B., D. A. Kocisko, G. J. Raymond, and P. T. Lansbury, Jr. 1995. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2:807-817.
    • (1995) Chem. Biol. , vol.2 , pp. 807-817
    • Caughey, B.1    Kocisko, D.A.2    Raymond, G.J.3    Lansbury Jr., P.T.4
  • 6
    • 0032742943 scopus 로고    scopus 로고
    • Protein misfolding and prion diseases
    • Cohen, F. E. 1999. Protein misfolding and prion diseases. J. Mol. Biol. 293:313-320.
    • (1999) J. Mol. Biol. , vol.293 , pp. 313-320
    • Cohen, F.E.1
  • 7
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen, F. E., and S. B. Prusiner. 1998. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67:793-819.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 8
    • 9144258359 scopus 로고    scopus 로고
    • Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue
    • Curin, S. V., M. Bresjanac, M. Popovic, H. K. Pretnar, V. Galvani, R. Rupreht, M. Cernilec, T. Vranac, I. Hafner, and R. Jerala. 2004. Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue. J. Biol. Chem. 279:3794-3798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3794-3798
    • Curin, S.V.1    Bresjanac, M.2    Popovic, M.3    Pretnar, H.K.4    Galvani, V.5    Rupreht, R.6    Cernilec, M.7    Vranac, T.8    Hafner, I.9    Jerala, R.10
  • 9
    • 0035979274 scopus 로고    scopus 로고
    • Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody
    • Enari, M., E. Flechsig, and C. Weissmann. 2001. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc. Natl. Acad. Sci. USA 98:9295-9299.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9295-9299
    • Enari, M.1    Flechsig, E.2    Weissmann, C.3
  • 10
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith, J. S. 1967. Self-replication and scrapie. Nature 215:1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 12
    • 0035805643 scopus 로고    scopus 로고
    • Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain
    • Horiuchi, M., G. S. Baron, L. W. Xiong, and B. Caughey. 2001. Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain. J. Biol. Chem. 276:15489-15497.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15489-15497
    • Horiuchi, M.1    Baron, G.S.2    Xiong, L.W.3    Caughey, B.4
  • 13
    • 0029656091 scopus 로고    scopus 로고
    • Structures of prion proteins and conformational models for prion diseases
    • Huang, Z., S. B. Prusiner, and F. E. Cohen. 1996. Structures of prion proteins and conformational models for prion diseases. Curr. Top. Microbiol. Immunol. 207:49-67.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.207 , pp. 49-67
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 15
    • 0034682866 scopus 로고    scopus 로고
    • Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N-terminus
    • Li, R., T. Liu, B.-S. Wong, T. Pan, M. Morillas, W. Swietnicki, K. O'Rourke, P. Gambetti, W. K. Surewicz, and M.-S. Sy. 2000. Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N-terminus. J. Mol. Biol. 301:567-574.
    • (2000) J. Mol. Biol. , vol.301 , pp. 567-574
    • Li, R.1    Liu, T.2    Wong, B.-S.3    Pan, T.4    Morillas, M.5    Swietnicki, W.6    O'Rourke, K.7    Gambetti, P.8    Surewicz, W.K.9    Sy, M.-S.10
  • 16
    • 0035818448 scopus 로고    scopus 로고
    • SC-like structural properties
    • SC-like structural properties. Biochemistry 40:13390-13396.
    • (2001) Biochemistry , vol.40 , pp. 13390-13396
    • Lu, B.Y.1    Chang, J.Y.2
  • 17
    • 0022494814 scopus 로고
    • Molecular characteristics of prion rods purified from scrapie-infected hamster brains
    • McKinley, M. P., M. B. Braunfeld, C. G. Bellinger, and S. B. Prusiner. 1986. Molecular characteristics of prion rods purified from scrapie-infected hamster brains. J. Infect. Dis. 154:110-120.
    • (1986) J. Infect. Dis. , vol.154 , pp. 110-120
    • McKinley, M.P.1    Braunfeld, M.B.2    Bellinger, C.G.3    Prusiner, S.B.4
  • 18
    • 0034537674 scopus 로고    scopus 로고
    • A monomer-dimer equilibrium of a cellular prion protein (PrPC) not observed with recombinant PrP
    • Meyer, R. K., A. Lustig, B. Oesch, R. Fatzer, A. Zurbriggen, and M. Vandevelde. 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
  • 21
    • 4444356433 scopus 로고    scopus 로고
    • Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion
    • Pan, T., R. Li, S. C. Kang, B. S. Wong, T. Wisniewski, and M. S. Sy. 2004. Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion. J. Neurochem. 90:1205-1217.
    • (2004) J. Neurochem. , vol.90 , pp. 1205-1217
    • Pan, T.1    Li, R.2    Kang, S.C.3    Wong, B.S.4    Wisniewski, T.5    Sy, M.S.6
  • 22
    • 11144247721 scopus 로고    scopus 로고
    • Biochemical fingerprints of prion infection: Accumulations of aberrant full-length and N-terminally truncated PrP species are common features in mouse prion disease
    • Pan, T., P. Wong, B. Chang, C. Li, R. Li, S. C. Kang, T. Wisniewski, and M. S. Sy. 2005. Biochemical fingerprints of prion infection: accumulations of aberrant full-length and N-terminally truncated PrP species are common features in mouse prion disease. J. Virol. 79:934-943.
    • (2005) J. Virol. , vol.79 , pp. 934-943
    • Pan, T.1    Wong, P.2    Chang, B.3    Li, C.4    Li, R.5    Kang, S.C.6    Wisniewski, T.7    Sy, M.S.8
  • 25
    • 0028874320 scopus 로고
    • A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP
    • Priola, S. A., B. Caughey, K. Wehrly, and B. Chesebro. 1995. A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. J. Biol. Chem. 270:3299-3305.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3299-3305
    • Priola, S.A.1    Caughey, B.2    Wehrly, K.3    Chesebro, B.4
  • 26
    • 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
  • 29
    • 0034705438 scopus 로고    scopus 로고
    • Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation
    • Qin, K., D. S. Yang, Y. Yang, M. A. Chishti, L. J. Meng, H. A. Kretzschmar, C. M. Yip, P. E. Fraser, and D. Westaway. 2000. Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation. J. Biol. Chem. 275:19121.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19121
    • Qin, K.1    Yang, D.S.2    Yang, Y.3    Chishti, M.A.4    Meng, L.J.5    Kretzschmar, H.A.6    Yip, C.M.7    Fraser, P.E.8    Westaway, D.9
  • 30
    • 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, Jr. 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 Jr., C.J.4
  • 33
    • 0038576230 scopus 로고    scopus 로고
    • The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein
    • Speare, J. O., T. S. Rush III, M. E. Bloom, and B. Caughey. 2003. The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein. J. Biol. Chem. 278:12522-12529.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12522-12529
    • Speare, J.O.1    Rush III, T.S.2    Bloom, M.E.3    Caughey, B.4
  • 34
    • 0030781922 scopus 로고    scopus 로고
    • H-dependent stability and conformation of the recombinant human prion protein PrP(90-231)
    • Swietnicki, W., R. Petersen, P. Gambetti, and W. K. Surewicz. 1997. pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J. Biol. Chem. 272:27517-27520.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27517-27520
    • Swietnicki, W.1    Petersen, R.2    Gambetti, P.3    Surewicz, W.K.4
  • 35
    • 0036215455 scopus 로고    scopus 로고
    • The role of dimerization in prion replication
    • Tompa, P., G. E. Tusnady, P. Friedrich, and I. Simon. 2002. The role of dimerization in prion replication. Biophys. J. 82:1711-1718.
    • (2002) Biophys. J. , vol.82 , pp. 1711-1718
    • Tompa, P.1    Tusnady, G.E.2    Friedrich, P.3    Simon, I.4
  • 37
  • 38
    • 0037665405 scopus 로고    scopus 로고
    • Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation
    • Winklhofer, K. F., J. Heske, U. Heller, A. Reintjes, W. Muranyi, I. Moarefi, and J. Tatzelt. 2003. Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation. J. Biol. Chem. 278:14961-14970.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14961-14970
    • Winklhofer, K.F.1    Heske, J.2    Heller, U.3    Reintjes, A.4    Muranyi, W.5    Moarefi, I.6    Tatzelt, J.7
  • 40
    • 0344099404 scopus 로고    scopus 로고
    • On-column purification and refolding of recombinant bovine prion protein: Using its octarepeat sequences as a natural affinity tag
    • Yin, S. M., Y. Zheng, and P. Tien. 2003. On-column purification and refolding of recombinant bovine prion protein: using its octarepeat sequences as a natural affinity tag. Protein Expr. Purif. 32:104-109.
    • (2003) Protein Expr. Purif. , vol.32 , pp. 104-109
    • Yin, S.M.1    Zheng, Y.2    Tien, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.