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Volumn 362, Issue 4, 2006, Pages 810-820

Osmolyte Trimethylamine N-Oxide Converts Recombinant α-Helical Prion Protein to its Soluble β-Structured Form at High Temperature

Author keywords

amyloid; osmolyte; prion; prion protein; soluble prion protein oligomers

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLAMIDE; OLIGOMER; PRION PROTEIN; PROTEINASE K; RECOMBINANT PROTEIN; THIOFLAVINE; TRIMETHYLAMINE OXIDE; TRYPTOPHAN;

EID: 33748327055     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.060     Document Type: Article
Times cited : (31)

References (58)
  • 2
    • 0031905248 scopus 로고    scopus 로고
    • Effects of copper on survival of prion protein knockout neurons and glia
    • Brown D.R., Schmidt B., and Kretzschmar H.A. Effects of copper on survival of prion protein knockout neurons and glia. J. Neurochem. 70 (1998) 1686-1693
    • (1998) J. Neurochem. , vol.70 , pp. 1686-1693
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 4
    • 0036371353 scopus 로고    scopus 로고
    • PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1
    • Derrington E., Gabus C., Leblanc C., Chnaidermann J., Grave L., Dormont D., et al. PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. C. R. Biol. 325 (2002) 17-23
    • (2002) C. R. Biol. , vol.325 , pp. 17-23
    • Derrington, E.1    Gabus, C.2    Leblanc, C.3    Chnaidermann, J.4    Grave, L.5    Dormont, D.6
  • 5
    • 0032472239 scopus 로고    scopus 로고
    • BSE and prions: uncertainties about the agent
    • Chesebro B. BSE and prions: uncertainties about the agent. Science 279 (1998) 42-43
    • (1998) Science , vol.279 , pp. 42-43
    • Chesebro, B.1
  • 6
    • 0029035284 scopus 로고
    • Viral particles are required for infection in neurodegenerative Creutzfeldt-Jakob disease
    • Manuelidis L., Sklaviadis T., Akoitz A., and Fritch W. Viral particles are required for infection in neurodegenerative Creutzfeldt-Jakob disease. Proc. Natl Acad. Sci. USA 23 (1995) 5124-5128
    • (1995) Proc. Natl Acad. Sci. USA , vol.23 , pp. 5124-5128
    • Manuelidis, L.1    Sklaviadis, T.2    Akoitz, A.3    Fritch, W.4
  • 9
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J., Saá P., Hetz C., and Soto C. In vitro generation of infectious scrapie prions. Cell 121 (2005) 195-206
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saá, P.2    Hetz, C.3    Soto, C.4
  • 11
    • 26844542536 scopus 로고    scopus 로고
    • Assembly of natural and recombinant prion protein into fibrils
    • Leffers K.-W., Willie H., Stohr J., Junger E., and Riesner D. Assembly of natural and recombinant prion protein into fibrils. Biol. Chem. 386 (2005) 569-580
    • (2005) Biol. Chem. , vol.386 , pp. 569-580
    • Leffers, K.-W.1    Willie, H.2    Stohr, J.3    Junger, E.4    Riesner, D.5
  • 12
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • Deleault N.R., Geoghegan J.C., Nishina K., Kascsak R., Williamson R.A., and Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J. Biol. Chem. 280 (2005) 26873-26879
    • (2005) J. Biol. Chem. , vol.280 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 13
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro Y., Machado F., Juliano L., Juliano M.A., Brentani R.R., and Foguel D. DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276 (2001) 49400-49409
    • (2001) J. Biol. Chem. , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3    Juliano, M.A.4    Brentani, R.R.5    Foguel, D.6
  • 14
    • 0032880060 scopus 로고    scopus 로고
    • Polymerization of murine recombinant prion protein in nucleic acid solution
    • Nandi P.K., and Leclerc E. Polymerization of murine recombinant prion protein in nucleic acid solution. Arch. Virol. 144 (1999) 1751-1763
    • (1999) Arch. Virol. , vol.144 , pp. 1751-1763
    • Nandi, P.K.1    Leclerc, E.2
  • 15
    • 0041735109 scopus 로고    scopus 로고
    • Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro
    • Adler V., Zeiler B., Kryukov V., Kascsak R., Rubenstein R., and Grossman A. Small, highly structured RNAs participate in the conversion of human recombinant PrP(Sen) to PrP(Res) in vitro. J. Mol. Biol. 332 (2003) 47-57
    • (2003) J. Mol. Biol. , vol.332 , pp. 47-57
    • Adler, V.1    Zeiler, B.2    Kryukov, V.3    Kascsak, R.4    Rubenstein, R.5    Grossman, A.6
  • 16
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault N.R., Lucassen R.W., and Supattapone S. RNA molecules stimulate prion protein conversion. Nature 425 (2003) 717-720
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 17
    • 1242294476 scopus 로고    scopus 로고
    • Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4′-dianilino-1,1′-binaphthyl-5,5′-sulfonate (bis-ANS)
    • Cordeiro Y., Lima L.M., Gomes M.P., Foguel D., and Silva J.L. Modulation of prion protein oligomerization, aggregation, and beta-sheet conversion by 4,4′-dianilino-1,1′-binaphthyl-5,5′-sulfonate (bis-ANS). J. Biol. Chem. 279 (2004) 5346-5352
    • (2004) J. Biol. Chem. , vol.279 , pp. 5346-5352
    • Cordeiro, Y.1    Lima, L.M.2    Gomes, M.P.3    Foguel, D.4    Silva, J.L.5
  • 18
  • 19
    • 7944239531 scopus 로고    scopus 로고
    • The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites
    • Leffers K.W., Schell J., Jansen K., Lucassen R., Kaimann T., Haertle T., et al. The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites. J. Mol. Biol. 344 (2004) 839-853
    • (2004) J. Mol. Biol. , vol.344 , pp. 839-853
    • Leffers, K.W.1    Schell, J.2    Jansen, K.3    Lucassen, R.4    Kaimann, T.5    Haertle, T.6
  • 20
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova O.V., Breydo L., Parfenov A.S., Salnikov V.V., and Baskakov I.V. In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J. Mol. Biol. 346 (2005) 645-659
    • (2005) J. Mol. Biol. , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 21
    • 14744284214 scopus 로고    scopus 로고
    • Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities
    • Rezaei H., Eghiaian F., Perez J., Doublet B., Choiset Y., Nagel-Steger L., et al. Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities. J. Mol. Biol. 347 (2005) 665-679
    • (2005) J. Mol. Biol. , vol.347 , pp. 665-679
    • Rezaei, H.1    Eghiaian, F.2    Perez, J.3    Doublet, B.4    Choiset, Y.5    Nagel-Steger, L.6
  • 22
    • 33644958800 scopus 로고    scopus 로고
    • Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions
    • Luhrs T., Zahn R., and Wuthrich K. Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions. J. Mol. Biol. 357 (2006) 833-841
    • (2006) J. Mol. Biol. , vol.357 , pp. 833-841
    • Luhrs, T.1    Zahn, R.2    Wuthrich, K.3
  • 23
    • 23644449548 scopus 로고    scopus 로고
    • Influence of the N-terminal domain on the aggregation properties of the prion protein
    • Frankenfield K.N., Powers E.T., and Kelly J.W. Influence of the N-terminal domain on the aggregation properties of the prion protein. Protein Sci. 14 (2005) 2154-2166
    • (2005) Protein Sci. , vol.14 , pp. 2154-2166
    • Frankenfield, K.N.1    Powers, E.T.2    Kelly, J.W.3
  • 24
    • 0036713563 scopus 로고    scopus 로고
    • Unusual property of prion protein unfolding in neutral salt solution
    • Nandi P.K., Leclerc E., and Marc D. Unusual property of prion protein unfolding in neutral salt solution. Biochemistry 41 (2002) 11017-11024
    • (2002) Biochemistry , vol.41 , pp. 11017-11024
    • Nandi, P.K.1    Leclerc, E.2    Marc, D.3
  • 25
    • 0032483027 scopus 로고    scopus 로고
    • Osmolyte-driven contraction of a random coil protein
    • Qu Y., Bolen C.L., and Bolen D.W. Osmolyte-driven contraction of a random coil protein. Proc. Natl. Acad. Sci. USA 95 (1998) 9268-9273
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9268-9273
    • Qu, Y.1    Bolen, C.L.2    Bolen, D.W.3
  • 26
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: natural selection of a thermodynamic force in protein folding
    • Bolen D.W., and Baskakov I.V. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310 (2001) 955-960
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-960
    • Bolen, D.W.1    Baskakov, I.V.2
  • 27
    • 0034758487 scopus 로고    scopus 로고
    • The role of conformational flexibility in prion propagation and maintenance for Sup35p
    • Scheibel T., and Lindquist S.L. The role of conformational flexibility in prion propagation and maintenance for Sup35p. Nature Struct. Biol. 8 (2001) 958-965
    • (2001) Nature Struct. Biol. , vol.8 , pp. 958-965
    • Scheibel, T.1    Lindquist, S.L.2
  • 28
    • 0032884397 scopus 로고    scopus 로고
    • Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and trimethylamine-N-oxide
    • Gursky O. Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and trimethylamine-N-oxide. Protein Sci. 8 (1999) 2055-2064
    • (1999) Protein Sci. , vol.8 , pp. 2055-2064
    • Gursky, O.1
  • 29
    • 0036076894 scopus 로고    scopus 로고
    • Osmolyte effects on helix formation in peptides and the stability of coiled-coils
    • Celinski S.A., and Scholtz J.M. Osmolyte effects on helix formation in peptides and the stability of coiled-coils. Protein Sci. 11 (2002) 2048-2051
    • (2002) Protein Sci. , vol.11 , pp. 2048-2051
    • Celinski, S.A.1    Scholtz, J.M.2
  • 30
    • 0029832863 scopus 로고    scopus 로고
    • hemical chaperones interfere with the formation of scrapie prion protein
    • Tatzelt J., Prusiner S.B., and Welch W.J. hemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15 (1996) 6363-6373
    • (1996) EMBO J. , vol.15 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 31
    • 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., Rush III T.S., Bloom M.E., and Caughey B. The role of helix 1 aspartates and salt bridges in the stability and conversion of prion protein. J. Biol. Chem. 278 (2003) 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
  • 32
    • 0033614844 scopus 로고    scopus 로고
    • Water-soluble beta-sheet models which self-assemble into fibrilar structures
    • Janek K., Behlke J., Zipper Z., Fabian H., Georgalis Y., Beyermann M., et al. Water-soluble beta-sheet models which self-assemble into fibrilar structures. Biochemistry 38 (1999) 8246-8252
    • (1999) Biochemistry , vol.38 , pp. 8246-8252
    • Janek, K.1    Behlke, J.2    Zipper, Z.3    Fabian, H.4    Georgalis, Y.5    Beyermann, M.6
  • 33
    • 1642488929 scopus 로고    scopus 로고
    • Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
    • Niraula T.N., Konno T., Li H., Yamada H., Akasaka K., and Tatchibana H. Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Proc. Natl Acad. Sci. USA 101 (2004) 4089-4093
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4089-4093
    • Niraula, T.N.1    Konno, T.2    Li, H.3    Yamada, H.4    Akasaka, K.5    Tatchibana, H.6
  • 34
    • 0032537229 scopus 로고    scopus 로고
    • Determination of the frequency and distribution of vascular and parenchymal amyloid with polyclonal and N-terminal-specific PrP antibodies in scrapie-affected sheep and mice
    • Jeffrey M., Goodsir C.M., Holliman A., Higgins R.J., Bruce M.E., McBride P.A., et al. Determination of the frequency and distribution of vascular and parenchymal amyloid with polyclonal and N-terminal-specific PrP antibodies in scrapie-affected sheep and mice. Vet. Rec. 16 (1998) 534-537
    • (1998) Vet. Rec. , vol.16 , pp. 534-537
    • Jeffrey, M.1    Goodsir, C.M.2    Holliman, A.3    Higgins, R.J.4    Bruce, M.E.5    McBride, P.A.6
  • 35
    • 0022802258 scopus 로고
    • The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP)
    • Hope J., Morton L.J., Farquhar C.F., Multhaup J., and Kimberlin R.H. The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO J. 5 (1986) 2591-2597
    • (1986) EMBO J. , vol.5 , pp. 2591-2597
    • Hope, J.1    Morton, L.J.2    Farquhar, C.F.3    Multhaup, J.4    Kimberlin, R.H.5
  • 36
    • 0035798377 scopus 로고    scopus 로고
    • Chaperonin-mediated de novo generation of prion protein aggregates
    • Stöckel J., and Hartl U. Chaperonin-mediated de novo generation of prion protein aggregates. J. Mol. Biol. 313 (2005) 861-872
    • (2005) J. Mol. Biol. , vol.313 , pp. 861-872
    • Stöckel, J.1    Hartl, U.2
  • 37
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas M., Swietnicki W., Gambetti P., Surewicz W.K., and Haertle T. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274 (1999) 36859-36865
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4    Haertle, T.5
  • 38
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 40
    • 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., and Surewicz W.K. On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein. Biochemistry 40 (2001) 6982-6987
    • (2001) Biochemistry , vol.40 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 41
    • 0036970469 scopus 로고    scopus 로고
    • DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid
    • Nandi P.K., Lelerc E., Nicole J.-C., and Takahashi M. DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. J. Mol. Biol. 322 (2002) 153-161
    • (2002) J. Mol. Biol. , vol.322 , pp. 153-161
    • Nandi, P.K.1    Lelerc, E.2    Nicole, J.-C.3    Takahashi, M.4
  • 42
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein
    • Safar J., Roller P.P., Gajdusek D.C., and Gibbs Jr. C.J. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268 (1993) 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
  • 43
    • 5444232817 scopus 로고    scopus 로고
    • Preventing misfolding of the prion protein by trimethylamine N-oxide
    • Bennion B.J., DeMarco M.L., and Daggett V. Preventing misfolding of the prion protein by trimethylamine N-oxide. Biochemistry 43 (2004) 12955-12963
    • (2004) Biochemistry , vol.43 , pp. 12955-12963
    • Bennion, B.J.1    DeMarco, M.L.2    Daggett, V.3
  • 44
    • 15744404427 scopus 로고    scopus 로고
    • Counteracting osmolyte trimethylamine N-oxide destabilizes proteins at pH below its pKa. Measurements of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide
    • Singh R.K., Haque I., and Ahmad F. Counteracting osmolyte trimethylamine N-oxide destabilizes proteins at pH below its pKa. Measurements of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide. J. Biol. Chem. 280 (2005) 11035-11042
    • (2005) J. Biol. Chem. , vol.280 , pp. 11035-11042
    • Singh, R.K.1    Haque, I.2    Ahmad, F.3
  • 45
    • 0030896451 scopus 로고    scopus 로고
    • Correcting temperature-sensitive protein folding defects
    • Brown C.R., Hong-Brown L.Q., and Welch W.J. Correcting temperature-sensitive protein folding defects. J. Clin. Invest. 99 (1997) 1432-1444
    • (1997) J. Clin. Invest. , vol.99 , pp. 1432-1444
    • Brown, C.R.1    Hong-Brown, L.Q.2    Welch, W.J.3
  • 46
    • 0035955689 scopus 로고    scopus 로고
    • Natural Osmolyte Trimethylamine N-oxide corrects assembly defects of mutant branched-chain α-ketoacid decarboxylase in maple syrup urine disease
    • Song J.-L., and Chuang D.T. Natural Osmolyte Trimethylamine N-oxide corrects assembly defects of mutant branched-chain α-ketoacid decarboxylase in maple syrup urine disease. J. Biol. Chem. 276 (2001) 40241-40246
    • (2001) J. Biol. Chem. , vol.276 , pp. 40241-40246
    • Song, J.-L.1    Chuang, D.T.2
  • 47
    • 0034969249 scopus 로고    scopus 로고
    • Prevention of Ppolymerization of M and Z-antitrypsin (a-AT) with trimethylamine N-oxide. Implications for the treatment of-AT deficiency
    • Devlin G.L., Parfrey H., Tew D.J., Lomas D.A., and Bottomley S.P. Prevention of Ppolymerization of M and Z-antitrypsin (a-AT) with trimethylamine N-oxide. Implications for the treatment of-AT deficiency. Am. J. Respir. Cell Mol. Biol. 24 (2001) 727-732
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.24 , pp. 727-732
    • Devlin, G.L.1    Parfrey, H.2    Tew, D.J.3    Lomas, D.A.4    Bottomley, S.P.5
  • 48
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-beta aggregation pathway with chemical chaperones
    • Yang D.-S., Yip C.M., Huang J., Chakarabartty A., and Fraser P.E. Manipulating the amyloid-beta aggregation pathway with chemical chaperones. J. Biol. Chem. 274 (1999) 32970-32974
    • (1999) J. Biol. Chem. , vol.274 , pp. 32970-32974
    • Yang, D.-S.1    Yip, C.M.2    Huang, J.3    Chakarabartty, A.4    Fraser, P.E.5
  • 49
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky V.N., Li J., and Fink A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 276 (2001) 10737-10744
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 50
    • 0035976814 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide-induced folding of alpha-synuclein
    • Uversky V.N., Li J., and Fink A.L. Trimethylamine-N-oxide-induced folding of alpha-synuclein. FEBS Letters 509 (2001) 31-35
    • (2001) FEBS Letters , vol.509 , pp. 31-35
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 51
    • 0842304735 scopus 로고    scopus 로고
    • Additive transfer free energies of the peptide backbone unit that are independent of model compounds and the choice of concentration scale
    • Auton M., and Bolen D.W. Additive transfer free energies of the peptide backbone unit that are independent of model compounds and the choice of concentration scale. Biochemistry 43 (2004) 1329-1342
    • (2004) Biochemistry , vol.43 , pp. 1329-1342
    • Auton, M.1    Bolen, D.W.2
  • 52
    • 23244459863 scopus 로고    scopus 로고
    • Osmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: origin of osmolyte compatibility
    • Athawale M.V., Dordick J.S., and Garde S. Osmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: origin of osmolyte compatibility. Biophys. J. 89 (2005) 858-866
    • (2005) Biophys. J. , vol.89 , pp. 858-866
    • Athawale, M.V.1    Dordick, J.S.2    Garde, S.3
  • 53
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich M., and Dobson C.M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21 (2002) 5682-5690
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 54
    • 0032101278 scopus 로고    scopus 로고
    • Theory of kinetic partitioning in protein folding with possible applications to prions
    • Abkevich V.I., Gutin A.M., and Shakhnovich E.I. Theory of kinetic partitioning in protein folding with possible applications to prions. Proteins: Struct. Funct. Genet. 31 (1998) 335-344
    • (1998) Proteins: Struct. Funct. Genet. , vol.31 , pp. 335-344
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 55
    • 0032742943 scopus 로고    scopus 로고
    • Protein misfolding and prion diseases
    • Cohen F.E. Protein misfolding and prion diseases. J. Mol. Biol. 293 (1999) 313-320
    • (1999) J. Mol. Biol. , vol.293 , pp. 313-320
    • Cohen, F.E.1
  • 56
    • 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. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26 (2003) 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 57
    • 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., Hoa G.H.B., Haertle T., et al. 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 (2000) 2833-2839
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2833-2839
    • Rezaei, H.1    Marc, D.2    Choiset, Y.3    Takahashi, M.4    Hoa, G.H.B.5    Haertle, T.6
  • 58
    • 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. 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


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