메뉴 건너뛰기




Volumn 21, Issue 1, 2012, Pages 38-49

Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process

Author keywords

Amyloid fibrils; Calorimetry method; KI oxidation method; Prion protein; Ultrasonic power

Indexed keywords

AMYLOID; POTASSIUM IODIDE; PRION PROTEIN;

EID: 84455204797     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.755     Document Type: Article
Times cited : (25)

References (42)
  • 1
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • DOI 10.1038/383685a0
    • Collinge J, Sidle KC, Meads J, Ironside J, Hill AF (1996) Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383:685-690. (Pubitemid 26360638)
    • (1996) Nature , vol.383 , Issue.6602 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 6
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian Prion Biology: One Century of Evolving Concepts
    • DOI 10.1016/S0092-8674(03)01031-6
    • Aguzzi A, Polymenidou M (2004) Mammalian prion biology: one century of evolving concepts. Cell 116: 313-327. (Pubitemid 38167320)
    • (2004) Cell , vol.116 , Issue.2 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 7
    • 9444267651 scopus 로고    scopus 로고
    • The state of the prion
    • Weissmann C (2004) The state of the prion. Nat Rev Microbiol 2:861-871.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 861-871
    • Weissmann, C.1
  • 9
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan CG, Ma J (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
  • 11
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • DOI 10.1038/35081095
    • Saborio GP, Permanne B, Soto C (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411:810-813. (Pubitemid 32588105)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 13
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc
    • Bocharova OV, Breydo L, Parfenov AS, Salnikov VV, Baskakov IV (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc. J Mol Biol 346:645-659.
    • (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
  • 14
    • 57649136747 scopus 로고    scopus 로고
    • Critical region for amyloid fibril formation of mouse prion protein: Unusual amyloidgenic properties of the helix 2 peptide
    • Yamaguchi K, Matsumoto T, Kuwata K (2008) Critical region for amyloid fibril formation of mouse prion protein: unusual amyloidgenic properties of the helix 2 peptide. Biochemistry 47:13242-13251.
    • (2008) Biochemistry , vol.47 , pp. 13242-13251
    • Yamaguchi, K.1    Matsumoto, T.2    Kuwata, K.3
  • 15
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • DOI 10.1016/j.cell.2005.02.011
    • Castilla J, Saá P, Hetz C, Soto C (2005) In vitro generation of infectious scrapie prions. Cell 121:195-206. (Pubitemid 40546388)
    • (2005) Cell , vol.121 , Issue.2 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 16
    • 24744446203 scopus 로고    scopus 로고
    • Detection of prions in blood
    • DOI 10.1038/nm1286
    • Castilla J, Saá P, Soto C (2005) Detection of prions in blood. Nat Med 11:982-985. (Pubitemid 41294444)
    • (2005) Nature Medicine , vol.11 , Issue.9 , pp. 982-985
    • Castilla, J.1    Saa, P.2    Soto, C.3
  • 18
    • 34547638271 scopus 로고    scopus 로고
    • Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein
    • DOI 10.1038/nmeth1066, PII NMETH1066
    • Atarashi R, Moore RA, Sim VL, Hughson AG, Dorward DW, Onwubiko HA, Priola SA, Caughey B (2007) Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat Methods 4:645-650. (Pubitemid 47202476)
    • (2007) Nature Methods , vol.4 , Issue.8 , pp. 645-650
    • Atarashi, R.1    Moore, R.A.2    Sim, V.L.3    Hughson, A.G.4    Dorward, D.W.5    Onwubiko, H.A.6    Priola, S.A.7    Caughey, B.8
  • 19
    • 65349089704 scopus 로고    scopus 로고
    • Hyperefficient PrPSc amplification of mouseadapted BSE and scrapie strain by protein misfolding cyclic amplification technique
    • Fujihara A, Atarashi R, Fuse T, Ubagai K, Nakagaki T, Yamaguchi N, Ishibashi D, Katamine S, Nishida N (2009) Hyperefficient PrPSc amplification of mouseadapted BSE and scrapie strain by protein misfolding cyclic amplification technique. FEBS J 276:2841-2848.
    • (2009) FEBS J , vol.276 , pp. 2841-2848
    • Fujihara, A.1    Atarashi, R.2    Fuse, T.3    Ubagai, K.4    Nakagaki, T.5    Yamaguchi, N.6    Ishibashi, D.7    Katamine, S.8    Nishida, N.9
  • 21
    • 38149142280 scopus 로고    scopus 로고
    • Seed-dependent accelerated fibrillation of α-synuclein induced by periodic ultrasonication treatment
    • Kim HJ, Chatani E, Goto Y, Paik SR (2007) Seed-dependent accelerated fibrillation of α-synuclein induced by periodic ultrasonication treatment. J Microbiol Biotechnol 17:2027-2032.
    • (2007) J Microbiol Biotechnol , vol.17 , pp. 2027-2032
    • Kim, H.J.1    Chatani, E.2    Goto, Y.3    Paik, S.R.4
  • 24
    • 67651087325 scopus 로고    scopus 로고
    • Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils
    • Chatani E, Lee Y, Yagi H, Yoshimura Y, Naiki H, Goto Y (2009) Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils. Proc Natl Acad Sci USA 106:11119-11124.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11119-11124
    • Chatani, E.1    Lee, Y.2    Yagi, H.3    Yoshimura, Y.4    Naiki, H.5    Goto, Y.6
  • 26
    • 0037405940 scopus 로고    scopus 로고
    • A standard method to calibrate sonochemical efficiency of an individual reaction system
    • DOI 10.1016/S1350-4177(03)00084-1
    • Koda S, Kimura T, Kondo T, Mitome H (2003) A standard method to calibrate sonochemical efficiency of an individual reaction system. Ultrason Sonochem 10: 149-156. (Pubitemid 36506684)
    • (2003) Ultrasonics Sonochemistry , vol.10 , Issue.3 , pp. 149-156
    • Koda, S.1    Kimura, T.2    Kondo, T.3    Mitome, H.4
  • 27
    • 35848959712 scopus 로고    scopus 로고
    • Effects of ultrasonic frequency and liquid height on sonochemical efficiency of large-scale sonochemical reactors
    • DOI 10.1016/j.ultsonch.2007.03.012, PII S1350417707000661
    • Asakura Y, Nishida T, Matsuoka T, Koda S (2008) Effects of ultrasonic frequency and liquid height on sonochemical efficiency of large-scale sonochemical reactors. Ultrason Sonochem 15:244-250. (Pubitemid 350061185)
    • (2008) Ultrasonics Sonochemistry , vol.15 , Issue.3 , pp. 244-250
    • Asakura, Y.1    Nishida, T.2    Matsuoka, T.3    Koda, S.4
  • 28
    • 0030285966 scopus 로고    scopus 로고
    • Quantification of ultrasonic intensity based on the decomposition reaction of porphyrin
    • Nomura H, Koda S, Yasuda K, Kojima Y (1996) Quantification of ultrasonic intensity based on the decomposition reaction of porphyrin. Ultrason Sonochem 3: S153-S156.
    • (1996) Ultrason Sonochem , vol.3
    • Nomura, H.1    Koda, S.2    Yasuda, K.3    Kojima, Y.4
  • 29
    • 0030196858 scopus 로고    scopus 로고
    • Copolymerization of sodium styrene sulphonate and vinylpyrrolidone under ultrasonic irradiation
    • Koda S, Amano T, Nomura H (1996) Copolymerization of sodium styrene sulphonate and vinylpyrrolidone under ultrasonic irradiation. Ultrason Sonochem 3: S91-S95.
    • (1996) Ultrason Sonochem , vol.3
    • Koda, S.1    Amano, T.2    Nomura, H.3
  • 30
    • 78149417674 scopus 로고    scopus 로고
    • Fluorescence quantum yield of thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils
    • Sulatskaya AI, Maskevich AA, Kuznetsova IM, Uversky VN, Turoverov KK (2010) Fluorescence quantum yield of thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils. PLoS ONE 5: e15385.
    • (2010) PLoS ONE , vol.5
    • Sulatskaya, A.I.1    Maskevich, A.A.2    Kuznetsova, I.M.3    Uversky, V.N.4    Turoverov, K.K.5
  • 31
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB (1983) A protease- resistant protein is a structural component of the scrapie prion. Cell 35:57-62. (Pubitemid 14240218)
    • (1983) Cell , vol.35 , Issue.1 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 33
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • DOI 10.1016/j.bbapap.2003.12.008, PII S1570963904000020
    • Uversky VN, Fink AL (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698:131-153. (Pubitemid 38591469)
    • (2004) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1698 , Issue.2 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 34
    • 0030781922 scopus 로고    scopus 로고
    • pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231)
    • DOI 10.1074/jbc.272.44.27517
    • Swietnicki W, Petersen R, Gambetti P, Surewicz WK (1997) pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J Biol Chem 272:27517-27520. (Pubitemid 27473537)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.44 , pp. 27517-27520
    • Swietnicki, W.1    Petersen, R.2    Gambetti, P.3    Surewicz, W.K.4
  • 36
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue WX, Homans SW, Radford SE (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 105:8926-8931.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8926-8931
    • Xue, W.X.1    Homans, S.W.2    Radford, S.E.3
  • 37
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structure of the prion protein yields two distinct selfpropagating states
    • Makarava N, Baskakov IV (2008) The same primary structure of the prion protein yields two distinct selfpropagating states. J Biol Chem 283:15988-15996.
    • (2008) J Biol Chem , vol.283 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 42
    • 0028673096 scopus 로고
    • Analysis of multidimensional spectroscopic data to monitor unfolding of proteins
    • Ramsay GD, Eftink MR (1994) Analysis of multidimensional spectroscopic data to monitor unfolding of proteins. Methods Enzymol 240:615-645.
    • (1994) Methods Enzymol , vol.240 , pp. 615-645
    • Ramsay, G.D.1    Eftink, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.