메뉴 건너뛰기




Volumn 109, Issue 14, 2012, Pages 5283-5288

Direct observation of multiple misfolding pathways in a single prion protein molecule

Author keywords

Optical tweezers; Protein folding

Indexed keywords

PRION PROTEIN;

EID: 84859465192     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1107736109     Document Type: Article
Times cited : (123)

References (55)
  • 1
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M (2009) Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16:574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 2
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11:777-788.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 56249130752 scopus 로고    scopus 로고
    • Alpha-Synuclein misfolding: Single molecule AFM force spectroscopy study
    • Yu J, Malkova S, Lyubchenko YL (2008) Alpha-Synuclein misfolding: Single molecule AFM force spectroscopy study. J Mol Biol 384:992-1001.
    • (2008) J Mol Biol , vol.384 , pp. 992-1001
    • Yu, J.1    Malkova, S.2    Lyubchenko, Y.L.3
  • 8
    • 79959830883 scopus 로고    scopus 로고
    • Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins
    • Borgia MB, et al. (2011) Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins. Nature 474:662-665.
    • (2011) Nature , vol.474 , pp. 662-665
    • Borgia, M.B.1
  • 9
    • 35948935175 scopus 로고    scopus 로고
    • Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy
    • DOI 10.1007/s10895-007-0187-z
    • Hillger F, Nettels D, Dorsch S, Schuler B (2007) Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy. J Fluoresc 17:759-765. (Pubitemid 350075694)
    • (2007) Journal of Fluorescence , vol.17 , Issue.6 , pp. 759-765
    • Hillger, F.1    Nettels, D.2    Dorsch, S.3    Schuler, B.4
  • 10
    • 77950659588 scopus 로고    scopus 로고
    • Early aggregation steps in alpha-synuclein as measured by FCS and FRET: Evidence for a contagious conformational change
    • Nath S, Meuvis J, Hendrix J, Carl SA, Engelborghs Y (2010) Early aggregation steps in alpha-synuclein as measured by FCS and FRET: Evidence for a contagious conformational change. Biophys J 98:1302-1311.
    • (2010) Biophys J , vol.98 , pp. 1302-1311
    • Nath, S.1    Meuvis, J.2    Hendrix, J.3    Carl, S.A.4    Engelborghs, Y.5
  • 11
    • 55749087363 scopus 로고    scopus 로고
    • Direct characterization of amyloidogenic oligomers by singlemolecule fluorescence
    • Orte A, et al. (2008) Direct characterization of amyloidogenic oligomers by singlemolecule fluorescence. Proc Natl Acad Sci USA 105:14424-14429.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14424-14429
    • Orte, A.1
  • 12
  • 13
    • 67650747654 scopus 로고    scopus 로고
    • Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions
    • Caughey B, Baron GS, Chesebro B, Jeffrey M (2009) Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 78:177-204.
    • (2009) Annu Rev Biochem , vol.78 , pp. 177-204
    • Caughey, B.1    Baron, G.S.2    Chesebro, B.3    Jeffrey, M.4
  • 14
    • 65249161100 scopus 로고    scopus 로고
    • Prion diseases and their biochemical mechanisms
    • Cobb NJ, Surewicz WK (2009) Prion diseases and their biochemical mechanisms. Biochemistry 48:2574-2585.
    • (2009) Biochemistry , vol.48 , pp. 2574-2585
    • Cobb, N.J.1    Surewicz, W.K.2
  • 15
    • 0030967895 scopus 로고    scopus 로고
    • Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
    • James TL, et al. (1997) Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci USA 94:10086-10091.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10086-10091
    • James, T.L.1
  • 18
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan KM, et al. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90:10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1
  • 19
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure
    • Cobb NJ, Sonnichsen FD, McHaourab H, Surewicz WK (2007) Molecular architecture of human prion protein amyloid: A parallel, in-register beta-structure. Proc Natl Acad Sci USA 104:18946-18951.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sonnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 24
    • 0032979289 scopus 로고    scopus 로고
    • Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates
    • DOI 10.1038/9323
    • Wildegger G, Liemann S, Glockshuber R (1999) Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat Struct Biol 6:550-553. (Pubitemid 29252834)
    • (1999) Nature Structural Biology , vol.6 , Issue.6 , pp. 550-553
    • Wildegger, G.1    Liemann, S.2    Glockshuber, R.3
  • 25
    • 33748342540 scopus 로고    scopus 로고
    • Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments
    • DOI 10.1021/ja063880b
    • Apetri AC, Maki K, Roder H, Surewicz WK (2006) Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J Am Chem Soc 128:11673-11678. (Pubitemid 44338858)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.35 , pp. 11673-11678
    • Apetri, A.C.1    Maki, K.2    Roder, H.3    Surewicz, W.K.4
  • 26
    • 65249125818 scopus 로고    scopus 로고
    • Folding kinetics of the human prion protein probed by temperature jump
    • Hart T, et al. (2009) Folding kinetics of the human prion protein probed by temperature jump. Proc Natl Acad Sci USA 106:5651-5656.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5651-5656
    • Hart, T.1
  • 27
    • 40349108841 scopus 로고    scopus 로고
    • The elusive intermediate on the folding pathway of the prion protein
    • DOI 10.1111/j.1742-4658.2008.06293.x
    • Jenkins DC, Sylvester ID, Pinheiro TJ (2008) The elusive intermediate on the folding pathway of the prion protein. FEBS J 275:1323-1335. (Pubitemid 351342226)
    • (2008) FEBS Journal , vol.275 , Issue.6 , pp. 1323-1335
    • Jenkins, D.C.1    Sylvester, I.D.2    Pinheiro, T.J.T.3
  • 28
    • 0037108168 scopus 로고    scopus 로고
    • Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc?
    • Kuwata K, et al. (2002) Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc? Biochemistry 41:12277-12283.
    • (2002) Biochemistry , vol.41 , pp. 12277-12283
    • Kuwata, K.1
  • 30
    • 78649824640 scopus 로고    scopus 로고
    • Optical trapping with high forces reveals unexpected behaviors of prion fibrils
    • Dong J, Castro CE, Boyce MC, Lang MJ, Lindquist S (2010) Optical trapping with high forces reveals unexpected behaviors of prion fibrils. Nat Struct Mol Biol 17:1422-1430.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1422-1430
    • Dong, J.1    Castro, C.E.2    Boyce, M.C.3    Lang, M.J.4    Lindquist, S.5
  • 31
    • 55549146133 scopus 로고    scopus 로고
    • Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy
    • Ganchev DN, Cobb NJ, Surewicz K, Surewicz WK (2008) Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy. Biophys J 95:2909-2915.
    • (2008) Biophys J , vol.95 , pp. 2909-2915
    • Ganchev, D.N.1    Cobb, N.J.2    Surewicz, K.3    Surewicz, W.K.4
  • 32
    • 76549238253 scopus 로고
    • The pleated sheet, a new layer configuration of polypeptide chains
    • Pauling L, Corey RB (1951) The pleated sheet, a new layer configuration of polypeptide chains. Proc Natl Acad Sci USA 37:251-256.
    • (1951) Proc Natl Acad Sci USA , vol.37 , pp. 251-256
    • Pauling, L.1    Corey, R.B.2
  • 34
    • 25444512161 scopus 로고    scopus 로고
    • Biochemistry: Direct observation of the three-state folding of a single protein molecule
    • DOI 10.1126/science.1116702
    • Cecconi C, Shank EA, Bustamante C, Marqusee S (2005) Direct observation of the three-state folding of a single protein molecule. Science 309:2057-2060. (Pubitemid 41362324)
    • (2005) Science , vol.309 , Issue.5743 , pp. 2057-2060
    • Cecconi, G.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 35
    • 76649093956 scopus 로고    scopus 로고
    • Full distance-resolved folding energy landscape of one single protein molecule
    • Gebhardt JC, Bornschlogl T, Rief M (2010) Full distance-resolved folding energy landscape of one single protein molecule. Proc Natl Acad Sci USA 107:2013-2018.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2013-2018
    • Gebhardt, J.C.1    Bornschlogl, T.2    Rief, M.3
  • 37
    • 80053216036 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy of the add adenine riboswitch relates folding to regulatory mechanism
    • Neupane K, Yu H, Foster DAN, Wang F, Woodside MT (2011) Single-molecule force spectroscopy of the add adenine riboswitch relates folding to regulatory mechanism. Nucleic Acids Res 39:7677-7687.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7677-7687
    • Neupane, K.1    Yu, H.2    Foster, D.A.N.3    Wang, F.4    Woodside, M.T.5
  • 39
    • 0035951859 scopus 로고    scopus 로고
    • The role of disulfide bridge in the folding and stability of the recombinant human prion protein
    • Maiti NR, Surewicz WK (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
  • 40
    • 34548221936 scopus 로고    scopus 로고
    • Structural and hydration properties of the partially unfolded states of the prion protein
    • DOI 10.1529/biophysj.107.108613
    • De Simone A, Zagari A, Derreumaux P (2007) Structural and hydration properties of the partially unfolded states of the prion protein. Biophys J 93:1284-1292. (Pubitemid 47330908)
    • (2007) Biophysical Journal , vol.93 , Issue.4 , pp. 1284-1292
    • De Simone, A.1    Zagari, A.2    Derreumaux, P.3
  • 44
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • DOI 10.1126/science.1073725
    • Ma J,Wollmann R, Lindquist S (2002) Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-1785. (Pubitemid 35404120)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 45
    • 79951623972 scopus 로고    scopus 로고
    • Detailed biophysical characterization of the acid-induced PrP(c) to PrP(beta) conversion process
    • Bjorndahl TC, et al. (2011) Detailed biophysical characterization of the acid-induced PrP(c) to PrP(beta) conversion process. Biochemistry 50:1162-1173.
    • (2011) Biochemistry , vol.50 , pp. 1162-1173
    • Bjorndahl, T.C.1
  • 46
    • 77954239509 scopus 로고    scopus 로고
    • The oligomerization properties of prion protein are restricted to the H2H3 domain
    • Chakroun N, et al. (2010) The oligomerization properties of prion protein are restricted to the H2H3 domain. FASEB J 24:3222-3231.
    • (2010) FASEB J , vol.24 , pp. 3222-3231
    • Chakroun, N.1
  • 47
    • 34250330794 scopus 로고    scopus 로고
    • Oligomerization of the human prion protein proceeds via a molten globule intermediate
    • DOI 10.1074/jbc.M608926200
    • Gerber R, Tahiri-Alaoui A, Hore PJ, James W (2007) Oligomerization of the human prion protein proceeds via a molten globule intermediate. J Biol Chem 282:6300-6307. (Pubitemid 47100833)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6300-6307
    • Gerber, R.1    Tahiri-Alaoui, A.2    Hore, P.J.3    James, W.4
  • 48
    • 70349195971 scopus 로고    scopus 로고
    • The consequences of pathogenic mutations to the human prion protein
    • van der Kamp MW, Daggett V (2009) The consequences of pathogenic mutations to the human prion protein. Protein Eng Des Sel 22:461-468.
    • (2009) Protein Eng des Sel , vol.22 , pp. 461-468
    • Van Der Kamp, M.W.1    Daggett, V.2
  • 49
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia cell and purified by high-affinity column refolding
    • DOI 10.1016/S0014-5793(97)01330-6, PII S0014579397013306
    • Zahn R, von Schroetter C, Wuthrich K (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett 417:400-404. (Pubitemid 27511631)
    • (1997) FEBS Letters , vol.417 , Issue.3 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wuthrich, K.3
  • 50
    • 0037965529 scopus 로고    scopus 로고
    • Prion protein selectively binds copper(II) ions
    • DOI 10.1021/bi972827k
    • Stockel J, Safar J, Wallace AC, Cohen FE, Prusiner SB (1998) Prion protein selectively binds copper(II) ions. Biochemistry 37:7185-7193. (Pubitemid 28235199)
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7185-7193
    • Stockel, J.1    Safar, J.2    Wallace, A.C.3    Cohen, F.E.4    Prusiner, S.B.5
  • 51
    • 45849099139 scopus 로고    scopus 로고
    • Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers
    • Cecconi C, Shank EA, Dahlquist FW, Marqusee S, Bustamante C (2008) Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers. Eur Biophys J 37:729-738.
    • (2008) Eur Biophys J , vol.37 , pp. 729-738
    • Cecconi, C.1    Shank, E.A.2    Dahlquist, F.W.3    Marqusee, S.4    Bustamante, C.5
  • 52
    • 38849204944 scopus 로고    scopus 로고
    • Direct observation of hierarchical folding in single riboswitch aptamers
    • DOI 10.1126/science.1151298
    • Greenleaf WJ, Frieda KL, Foster DA,Woodside MT, Block SM (2008) Direct observation of hierarchical folding in single riboswitch aptamers. Science 319:630-633. (Pubitemid 351197067)
    • (2008) Science , vol.319 , Issue.5863 , pp. 630-633
    • Greenleaf, W.J.1    Frieda, K.L.2    Foster, D.A.N.3    Woodside, M.T.4    Block, S.M.5
  • 55
    • 77953231020 scopus 로고    scopus 로고
    • The folding cooperativity of a protein is controlled by its chain topology
    • Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C (2010) The folding cooperativity of a protein is controlled by its chain topology. Nature 465:637-640.
    • (2010) Nature , vol.465 , pp. 637-640
    • Shank, E.A.1    Cecconi, C.2    Dill, J.W.3    Marqusee, S.4    Bustamante, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.