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Volumn 47, Issue 23, 2008, Pages 6267-6278

Expansion of the octarepeat domain alters the misfolding pathway but not the folding pathway of the prion protein

Author keywords

[No Author keywords available]

Indexed keywords

FOLDING PATHWAY; MISFOLDING; PRION PROTEIN (PRP);

EID: 44949123779     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800253c     Document Type: Article
Times cited : (21)

References (55)
  • 5
    • 0028235176 scopus 로고
    • Human spongiform encephalopathy: The National Institutes of Health series of 300 cases of experimentally transmitted disease
    • Brown, P., Gibbs, C. J., Jr., Rodgers-Johnson, P., Asher, D. M., Sulima, M. P., Bacote, A., Goldfarb, L. G., and Gajdusek, D. C. (1994) Human spongiform encephalopathy: The National Institutes of Health series of 300 cases of experimentally transmitted disease. Ann. Neurol. 35, 513-529.
    • (1994) Ann. Neurol , vol.35 , pp. 513-529
    • Brown, P.1    Gibbs Jr., C.J.2    Rodgers-Johnson, P.3    Asher, D.M.4    Sulima, M.P.5    Bacote, A.6    Goldfarb, L.G.7    Gajdusek, D.C.8
  • 8
    • 27544439092 scopus 로고    scopus 로고
    • Transgenic mice expressing bovine PrP with a four extra repeat octapeptide insert mutation show a spontaneous, non-transmissible, neurodegenerative disease and an expedited course of BSE infection
    • Castilla, J., Gutierrez-Adan, A., Brun, A., Pintado, B., Salguero, F. J., Parra, B., Segundo, F. D., Ramirez, M. A., Rabano, A., Cano, M. J., and Torres, J. M. (2005) Transgenic mice expressing bovine PrP with a four extra repeat octapeptide insert mutation show a spontaneous, non-transmissible, neurodegenerative disease and an expedited course of BSE infection. FEBS Lett. 579, 6237-6246.
    • (2005) FEBS Lett , vol.579 , pp. 6237-6246
    • Castilla, J.1    Gutierrez-Adan, A.2    Brun, A.3    Pintado, B.4    Salguero, F.J.5    Parra, B.6    Segundo, F.D.7    Ramirez, M.A.8    Rabano, A.9    Cano, M.J.10    Torres, J.M.11
  • 9
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa, R., Piccardo, P., Ghetti, B., and Harris, D. A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351.
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 11
    • 34249995984 scopus 로고    scopus 로고
    • Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice
    • Li, A., Piccardo, P., Barmada, S. J., Ghetti, B., and Harris, D. A. (2007) Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. EMBO J. 26, 2777-2785.
    • (2007) EMBO J , vol.26 , pp. 2777-2785
    • Li, A.1    Piccardo, P.2    Barmada, S.J.3    Ghetti, B.4    Harris, D.A.5
  • 12
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wuthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413, 282-288.
    • (1997) FEBS Lett , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 13
    • 0242662244 scopus 로고    scopus 로고
    • The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site
    • Zahn, R. (2003) The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site. J. Mol. Biol. 334, 477-488.
    • (2003) J. Mol. Biol , vol.334 , pp. 477-488
    • Zahn, R.1
  • 14
    • 0033863775 scopus 로고    scopus 로고
    • NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: A loop conformation with histidine and tryptophan in close proximity
    • Yoshida, H., Matsushima, N., Kumaki, Y., Nakata, M., and Hikichi, K. (2000) NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: A loop conformation with histidine and tryptophan in close proximity. J. Biochem. 128, 271-281.
    • (2000) J. Biochem , vol.128 , pp. 271-281
    • Yoshida, H.1    Matsushima, N.2    Kumaki, Y.3    Nakata, M.4    Hikichi, K.5
  • 15
    • 4644372554 scopus 로고    scopus 로고
    • Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction
    • Blanch, E. W., Gill, A. C., Rhie, A. G., Hope, J., Hecht, L., Nielsen, K., and Barron, L. D. (2004) Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction. J. Mol. Biol. 343, 467-476.
    • (2004) J. Mol. Biol , vol.343 , pp. 467-476
    • Blanch, E.W.1    Gill, A.C.2    Rhie, A.G.3    Hope, J.4    Hecht, L.5    Nielsen, K.6    Barron, L.D.7
  • 16
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio, B., and Tamburro, A. M. (2002) Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions. Chirality 14, 782-792.
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 18
    • 33746376976 scopus 로고    scopus 로고
    • Evidence for polyproline II helical structure in short polyglutamine tracts
    • Chellgren, B. W., Miller, A. F., and Creamer, T. P. (2006) Evidence for polyproline II helical structure in short polyglutamine tracts. J. Mol. Biol. 361, 362-371.
    • (2006) J. Mol. Biol , vol.361 , pp. 362-371
    • Chellgren, B.W.1    Miller, A.F.2    Creamer, T.P.3
  • 19
    • 17644422781 scopus 로고    scopus 로고
    • Urea promotes polyproline II helix formation: Implications for protein denatured states
    • Whittington, S. J., Chellgren, B. W., Hermann, V. M., and Creamer, T. P. (2005) Urea promotes polyproline II helix formation: Implications for protein denatured states. Biochemistry 44, 6269-6275.
    • (2005) Biochemistry , vol.44 , pp. 6269-6275
    • Whittington, S.J.1    Chellgren, B.W.2    Hermann, V.M.3    Creamer, T.P.4
  • 20
    • 1942519322 scopus 로고    scopus 로고
    • Conformation of prion protein repeat peptides probed by FRET measurements and molecular dynamics simulations
    • Gustiananda, M., Liggins, J. R., Cummins, P. L., and Gready, J. E. (2004) Conformation of prion protein repeat peptides probed by FRET measurements and molecular dynamics simulations. Biophys. J. 86, 2467-2483.
    • (2004) Biophys. J , vol.86 , pp. 2467-2483
    • Gustiananda, M.1    Liggins, J.R.2    Cummins, P.L.3    Gready, J.E.4
  • 21
  • 22
    • 33645639813 scopus 로고    scopus 로고
    • The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions
    • Leliveld, S. R., Dame, R. T., Wuite, G. J., Stitz, L., and Korth, C. (2006) The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions. J. Biol. Chem. 281, 3268-3275.
    • (2006) J. Biol. Chem , vol.281 , pp. 3268-3275
    • Leliveld, S.R.1    Dame, R.T.2    Wuite, G.J.3    Stitz, L.4    Korth, C.5
  • 23
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • Millhauser, G. L. (2007) Copper and the prion protein: Methods, structures, function, and disease. Annu. Rev. Phys. Chem. 58, 299-320.
    • (2007) Annu. Rev. Phys. Chem. 58 , pp. 299-320
    • Millhauser, G.L.1
  • 24
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey, B., and Baron, G. S. (2006) Prions and their partners in crime. Nature 443, 803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 25
    • 34147112306 scopus 로고    scopus 로고
    • Copper and zinc promote interactions between membrane-anchored peptides of the metal binding domain of the prion protein
    • Kenward, A. G., Bartolotti, L. J., and Burns, C. S. (2007) Copper and zinc promote interactions between membrane-anchored peptides of the metal binding domain of the prion protein. Biochemistry 46, 4261-4271.
    • (2007) Biochemistry , vol.46 , pp. 4261-4271
    • Kenward, A.G.1    Bartolotti, L.J.2    Burns, C.S.3
  • 26
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley, A., Whitmore, L., and Wallace, B. A. (2002) DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18, 211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 27
    • 44949120143 scopus 로고    scopus 로고
    • Keller, R, 2004 The Computer Aided Resonance Assignment Tutorial version 1.8.4, CANTINA Verlag, Goldau, Switzerland
    • Keller, R. (2004) The Computer Aided Resonance Assignment Tutorial version 1.8.4, CANTINA Verlag, Goldau, Switzerland.
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 29
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer, M., Rulicke, T., Raeber, A., Sailer, A., Moser, M., Oesch, B., Brandner, S., Aguzzi, A., and Weissmann, C. (1996) Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15, 1255-1264.
    • (1996) EMBO J , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5    Oesch, B.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 31
    • 0028716614 scopus 로고
    • Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators
    • Grishina, I. B., and Woody, R. W. (1994) Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators. Faraday Discuss., 245-262.
    • (1994) Faraday Discuss , pp. 245-262
    • Grishina, I.B.1    Woody, R.W.2
  • 32
    • 0028578686 scopus 로고
    • Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G
    • Kuszewski, J., Clore, G. M., and Gronenborn, A. M. (1994) Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G. Protein Sci. 3, 1945-1952.
    • (1994) Protein Sci , vol.3 , pp. 1945-1952
    • Kuszewski, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 33
    • 0030042552 scopus 로고    scopus 로고
    • Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy
    • Gronenborn, A. M., and Clore, G. M. (1996) Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy. Protein Sci. 5, 174-177.
    • (1996) Protein Sci , vol.5 , pp. 174-177
    • Gronenborn, A.M.1    Clore, G.M.2
  • 34
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • Kelly, S. M., and Price, N. C. (2000) The use of circular dichroism in the investigation of protein structure and function. Curr. Protein Pept. Sci. 1, 349-384.
    • (2000) Curr. Protein Pept. Sci , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 35
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 36
    • 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., and 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
  • 39
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • Calzolai, L., and Zahn, R. (2003) Influence of pH on NMR structure and stability of the human prion protein globular domain. J. Biol. Chem. 278, 35592-35596.
    • (2003) J. Biol. Chem , vol.278 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 40
    • 37249001722 scopus 로고    scopus 로고
    • High titers of transmissible spongiform encephalopathy infectivity associated with extremely low levels of PrPSc in vivo
    • Barron, R. M., Campbell, S. L., King, D., Bellon, A., Chapman, K. E., Williamson, R. A., and Manson, J. C. (2007) High titers of transmissible spongiform encephalopathy infectivity associated with extremely low levels of PrPSc in vivo. J. Biol. Chem. 282, 35878-35886.
    • (2007) J. Biol. Chem , vol.282 , pp. 35878-35886
    • Barron, R.M.1    Campbell, S.L.2    King, D.3    Bellon, A.4    Chapman, K.E.5    Williamson, R.A.6    Manson, J.C.7
  • 43
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B., and Lansbury, P. T. (2003) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298.
    • (2003) Annu. Rev. Neurosci. 26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 45
    • 33644540192 scopus 로고    scopus 로고
    • Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation
    • Moore, R. A., Herzog, C., Errett, J., Kocisko, D. A., Arnold, K. M., Hayes, S. F., and Priola, S. A. (2006) Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation. Protein Sci. 15, 609-619.
    • (2006) Protein Sci , vol.15 , pp. 609-619
    • Moore, R.A.1    Herzog, C.2    Errett, J.3    Kocisko, D.A.4    Arnold, K.M.5    Hayes, S.F.6    Priola, S.A.7
  • 47
    • 39749094951 scopus 로고    scopus 로고
    • Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion
    • Biasini, E., Medrano, A. Z., Thellung, S., Chiesa, R., and Harris, D. A. (2007) Multiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion. J Neurochem 104, 1293-1308.
    • (2007) J Neurochem , vol.104 , pp. 1293-1308
    • Biasini, E.1    Medrano, A.Z.2    Thellung, S.3    Chiesa, R.4    Harris, D.A.5
  • 49
    • 33748176879 scopus 로고    scopus 로고
    • Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy
    • Kachel, N., Kremer, W., Zahn, R., and Kalbitzer, H. R. (2006) Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy. BMC Struct. Biol. 6, 16.
    • (2006) BMC Struct. Biol , vol.6 , pp. 16
    • Kachel, N.1    Kremer, W.2    Zahn, R.3    Kalbitzer, H.R.4
  • 50
    • 38349185509 scopus 로고    scopus 로고
    • Molecular model of an α-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations
    • Kaimann, T., Metzger, S., Kuhlmann, K., Brandt, B., Birkmann, E., Holtje, H. D., and Riesner, D. (2007) Molecular model of an α-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations. J. Mol. Biol. 376, 582-596.
    • (2007) J. Mol. Biol , vol.376 , pp. 582-596
    • Kaimann, T.1    Metzger, S.2    Kuhlmann, K.3    Brandt, B.4    Birkmann, E.5    Holtje, H.D.6    Riesner, D.7
  • 52
    • 0000522537 scopus 로고    scopus 로고
    • Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat
    • Chen, Y. W., Stott, K., and Perutz, M. F. (1999) Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat. Proc. Natl. Acad. Sci. U.S.A. 96, 1257-1261.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 1257-1261
    • Chen, Y.W.1    Stott, K.2    Perutz, M.F.3
  • 53
    • 34548510580 scopus 로고    scopus 로고
    • The length dependence of the polyQ-mediated protein aggregation
    • Barton, S., Jacak, R., Khare, S. D., Ding, F., and Dokholyan, N. V. (2007) The length dependence of the polyQ-mediated protein aggregation. J. Biol. Chem. 282, 25487-25492.
    • (2007) J. Biol. Chem , vol.282 , pp. 25487-25492
    • Barton, S.1    Jacak, R.2    Khare, S.D.3    Ding, F.4    Dokholyan, N.V.5
  • 54
  • 55
    • 34548221936 scopus 로고    scopus 로고
    • Structural and hydration properties of the partially unfolded states of the prion protein
    • De Simone, A., Zagari, A., and Derreumaux, P. (2007) Structural and hydration properties of the partially unfolded states of the prion protein. Biophys. J. 93, 1284-1292.
    • (2007) Biophys. J , vol.93 , pp. 1284-1292
    • De Simone, A.1    Zagari, A.2    Derreumaux, P.3


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