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Volumn 4, Issue 4, 2010, Pages 265-274

Nanoimaging for prion related diseases

Author keywords

Atomic force microscopy; Force spectroscopy; Nanomedicine; Prion; Protein misfolding

Indexed keywords

PRION PROTEIN;

EID: 78650206856     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.4.4.13125     Document Type: Review
Times cited : (18)

References (101)
  • 1
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • DOI 10.1126/science.1138718
    • Collinge J, Clarke AR. A general model of prion strains and their pathogenicity. Science 2007; 318:930-6. (Pubitemid 350098981)
    • (2007) Science , vol.318 , Issue.5852 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 2
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of beta-sheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance
    • Baxa U, Wickner RB, Steven AC, Anderson DE, Marekov LN, Yau WM, et al. Characterization of beta-sheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance. Biochemistry 2007; 46:13149-62.
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.E.4    Marekov, L.N.5    Yau, W.M.6
  • 3
    • 23244449092 scopus 로고    scopus 로고
    • Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
    • Chan JC, Oyler NA, Yau WM, Tycko R. Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 2005; 44:10669-80.
    • (2005) Biochemistry , vol.44 , pp. 10669-10680
    • Chan, J.C.1    Oyler, N.A.2    Yau, W.M.3    Tycko, R.4
  • 4
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure
    • Shewmaker F, Wickner RB, Tycko R. Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc Natl Acad Sci USA 2006; 103:19754-9.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 5
    • 40649098246 scopus 로고    scopus 로고
    • Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure
    • Wickner RB, Dyda F, Tycko R. Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure. Proc Natl Acad Sci USA 2008; 105:2403.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 2403
    • Wickner, R.B.1    Dyda, F.2    Tycko, R.3
  • 7
    • 0035997080 scopus 로고    scopus 로고
    • Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: Evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance
    • Balbach JJ, Petkova AT, Oyler NA, Antzutkin ON, Gordon DJ, Meredith SC, et al. Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys J 2002; 83:1205-16.
    • (2002) Biophys J , vol.83 , pp. 1205-1216
    • Balbach, J.J.1    Petkova, A.T.2    Oyler, N.A.3    Antzutkin, O.N.4    Gordon, D.J.5    Meredith, S.C.6
  • 8
    • 0344255649 scopus 로고    scopus 로고
    • Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide
    • Petkova AT, Buntkowsky G, Dyda F, Leapman RD, Yau WM, Tycko R. Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J Mol Biol 2004; 335:247-60.
    • (2004) J Mol Biol , vol.335 , pp. 247-260
    • Petkova, A.T.1    Buntkowsky, G.2    Dyda, F.3    Leapman, R.D.4    Yau, W.M.5    Tycko, R.6
  • 10
    • 27844499292 scopus 로고    scopus 로고
    • Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment
    • Madine J, Doig AJ, Kitmitto A, Middleton DA. Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment. Biochem Soc Trans 2005; 33:1113-5.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1113-1115
    • Madine, J.1    Doig, A.J.2    Kitmitto, A.3    Middleton, D.A.4
  • 11
    • 0034723150 scopus 로고    scopus 로고
    • Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties
    • Tenidis K, Waldner M, Bernhagen J, Fischle W, Bergmann M, Weber M, et al. Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. J Mol Biol 2000; 295:1055-71.
    • (2000) J Mol Biol , vol.295 , pp. 1055-1071
    • Tenidis, K.1    Waldner, M.2    Bernhagen, J.3    Fischle, W.4    Bergmann, M.5    Weber, M.6
  • 12
    • 0034647438 scopus 로고    scopus 로고
    • Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain
    • Krebs MR, Wilkins DK, Chung EW, Pitkeathly MC, Chamberlain AK, Zurdo J, et al. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J Mol Biol 2000; 300:541-9.
    • (2000) J Mol Biol , vol.300 , pp. 541-549
    • Krebs, M.R.1    Wilkins, D.K.2    Chung, E.W.3    Pitkeathly, M.C.4    Chamberlain, A.K.5    Zurdo, J.6
  • 14
    • 0345827608 scopus 로고    scopus 로고
    • Sequence determinants of amyloid fibril formation
    • Lopez de la Paz M, Serrano L. Sequence determinants of amyloid fibril formation. Proc Natl Acad Sci USA 2004; 101:87-92.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 87-92
    • Lopez De La Paz, M.1    Serrano, L.2
  • 15
    • 28044457195 scopus 로고    scopus 로고
    • The amyloid stretch hypothesis: Recruiting proteins toward the dark side
    • Esteras-Chopo A, Serrano L, Lopez de la Paz M. The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc Natl Acad Sci USA 2005; 102:16672-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16672-16677
    • Esteras-Chopo, A.1    Serrano, L.2    Lopez De La Paz, M.3
  • 16
    • 11844249426 scopus 로고    scopus 로고
    • Hot regions in protein - Protein interactions: The organization and contribution of structurally conserved hot spot residues
    • Keskin O, Ma B, Nussinov R. Hot regions in protein - protein interactions: the organization and contribution of structurally conserved hot spot residues. J Mol Biol 2005; 345:1281-94.
    • (2005) J Mol Biol , vol.345 , pp. 1281-1294
    • Keskin, O.1    Ma, B.2    Nussinov, R.3
  • 18
    • 34249903623 scopus 로고    scopus 로고
    • Prion recognition elements govern nucleation, strain specificity and species barriers
    • Tessier PM, Lindquist S. Prion recognition elements govern nucleation, strain specificity and species barriers. Nature 2007; 447:556-61.
    • (2007) Nature , vol.447 , pp. 556-561
    • Tessier, P.M.1    Lindquist, S.2
  • 20
    • 76749102953 scopus 로고    scopus 로고
    • Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1
    • Kadnar ML, Articov G, Derkatch IL. Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1. PLoS Genet 2010; 6:1000824.
    • (2010) PLoS Genet , vol.6 , pp. 1000824
    • Kadnar, M.L.1    Articov, G.2    Derkatch, I.L.3
  • 21
    • 77249124926 scopus 로고    scopus 로고
    • Differences in prion strain conformations result from non-native interactions in a nucleus
    • Ohhashi Y, Ito K, Toyama BH, Weissman JS, Tanaka M. Differences in prion strain conformations result from non-native interactions in a nucleus. Nat Chem Biol 2010; 6:225-30.
    • (2010) Nat Chem Biol , vol.6 , pp. 225-230
    • Ohhashi, Y.1    Ito, K.2    Toyama, B.H.3    Weissman, J.S.4    Tanaka, M.5
  • 22
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins SR, Douglass A, Vale RD, Weissman JS. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol 2004; 2:321.
    • (2004) PLoS Biol , vol.2 , pp. 321
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 23
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • Ban T, Hamada D, Hasegawa K, Naiki H, Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem 2003; 278:16462-5.
    • (2003) J Biol Chem , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 24
    • 33749508090 scopus 로고    scopus 로고
    • Direct Observation of Amyloid Growth Monitored by Total Internal Reflection Fluorescence Microscopy
    • DOI 10.1016/S0076-6879(06)13005-0, PII S0076687906130050, Amyloid, Prions, and Other Protein Aggregates, Part C
    • Ban T, Goto Y. Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy. Methods Enzymol 2006; 413:91-102. (Pubitemid 44528686)
    • (2006) Methods in Enzymology , vol.413 , pp. 91-102
    • Ban, T.1    Goto, Y.2
  • 26
    • 2942592408 scopus 로고    scopus 로고
    • Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy
    • Hoyer W, Cherny D, Subramaniam V, Jovin TM. Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy. J Mol Biol 2004; 340:127-39.
    • (2004) J Mol Biol , vol.340 , pp. 127-139
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 27
    • 0033616587 scopus 로고    scopus 로고
    • In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation
    • Kowalewski T, Holtzman DM. In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation. Proc Natl Acad Sci USA 1999; 96:3688-93.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3688-3693
    • Kowalewski, T.1    Holtzman, D.M.2
  • 28
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • Goldsbury C, Kistler J, Aebi U, Arvinte T, Cooper GJ. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J Mol Biol 1999; 285:33-9.
    • (1999) J Mol Biol , vol.285 , pp. 33-39
    • Goldsbury, C.1    Kistler, J.2    Aebi, U.3    Arvinte, T.4    Cooper, G.J.5
  • 29
    • 22844448175 scopus 로고    scopus 로고
    • Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates
    • Goldsbury C, Green J. Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates. Methods Mol Biol 2005; 299:103-28.
    • (2005) Methods Mol Biol , vol.299 , pp. 103-128
    • Goldsbury, C.1    Green, J.2
  • 31
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace AH, Weissman JS. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat Struct Biol 2002; 9:389-96.
    • (2002) Nat Struct Biol , vol.9 , pp. 389-396
    • DePace, A.H.1    Weissman, J.S.2
  • 33
    • 34249993165 scopus 로고    scopus 로고
    • The prion strain phenomenon: Molecular basis and unprecedented features
    • Morales R, Abid K, Soto C. The prion strain phenomenon: molecular basis and unprecedented features. Biochim Biophys Acta 2007; 1772:681-91.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 681-691
    • Morales, R.1    Abid, K.2    Soto, C.3
  • 34
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005; 307:262-5.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 35
    • 17044435107 scopus 로고    scopus 로고
    • Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins
    • Tanaka M, Chien P, Yonekura K, Weissman JS. Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins. Cell 2005; 121:49-62.
    • (2005) Cell , vol.121 , pp. 49-62
    • Tanaka, M.1    Chien, P.2    Yonekura, K.3    Weissman, J.S.4
  • 36
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids
    • DOI 10.1016/j.cell.2005.01.034
    • Jones EM, Surewicz WK. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 2005; 121:63-72. (Pubitemid 40501168)
    • (2005) Cell , vol.121 , Issue.1 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2
  • 38
    • 34247504580 scopus 로고    scopus 로고
    • Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p
    • van der Wel PC, Lewandowski JR, Griffin RG. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J Am Chem Soc 2007; 129:5117-30.
    • (2007) J Am Chem Soc , vol.129 , pp. 5117-5130
    • Van Der Wel, P.C.1    Lewandowski, J.R.2    Griffin, R.G.3
  • 39
    • 33744954409 scopus 로고    scopus 로고
    • Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay
    • Novitskaya V, Makarava N, Bellon A, Bocharova OV, Bronstein IB, Williamson RA, et al. Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J Biol Chem 2006; 281:15536-45.
    • (2006) J Biol Chem , vol.281 , pp. 15536-15545
    • Novitskaya, V.1    Makarava, N.2    Bellon, A.3    Bocharova, O.V.4    Bronstein, I.B.5    Williamson, R.A.6
  • 40
    • 26444514550 scopus 로고    scopus 로고
    • Intersheet rearrangement of polypeptides during nucleation of {beta}-sheet aggregates
    • Petty SA, Decatur SM. Intersheet rearrangement of polypeptides during nucleation of {beta}-sheet aggregates. Proc Natl Acad Sci USA 2005; 102:14272-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14272-14277
    • Petty, S.A.1    Decatur, S.M.2
  • 41
    • 66149084447 scopus 로고    scopus 로고
    • Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution
    • Shim SH, Gupta R, Ling YL, Strasfeld DB, Raleigh DP, Zanni MT. Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. P Natl Acad Sci USA 2009; 106:6614-9.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 6614-6619
    • Shim, S.H.1    Gupta, R.2    Ling, Y.L.3    Strasfeld, D.B.4    Raleigh, D.P.5    Zanni, M.T.6
  • 42
    • 34250172716 scopus 로고    scopus 로고
    • Probing a fibrillation nucleus directly by deep ultraviolet Raman spectroscopy
    • Shashilov V, Xu M, Ermolenkov VV, Fredriksen L, Lednev IK. Probing a fibrillation nucleus directly by deep ultraviolet Raman spectroscopy. J Am Chem Soc 2007; 129:6972-3.
    • (2007) J Am Chem Soc , vol.129 , pp. 6972-6973
    • Shashilov, V.1    Xu, M.2    Ermolenkov, V.V.3    Fredriksen, L.4    Lednev, I.K.5
  • 43
    • 38349002568 scopus 로고    scopus 로고
    • 2D correlation deep UV resonance raman spectroscopy of early events of lysozyme fibrillation: Kinetic mechanism and potential interpretation pitfalls
    • Shashilov VA, Lednev IK. 2D correlation deep UV resonance raman spectroscopy of early events of lysozyme fibrillation: kinetic mechanism and potential interpretation pitfalls. J Am Chem Soc 2008; 130:309-17.
    • (2008) J Am Chem Soc , vol.130 , pp. 309-317
    • Shashilov, V.A.1    Lednev, I.K.2
  • 44
    • 78650208709 scopus 로고    scopus 로고
    • Different Individual Amyloid Fibrils Exhibit Different Beta Sheet Secondary Structures via Near-field Infrared Spectroscopy
    • Paulite M, Fakhraai Z, Gunari N, Tanur A, GW. Different Individual Amyloid Fibrils Exhibit Different Beta Sheet Secondary Structures via Near-field Infrared Spectroscopy. Biophys J 2009; 96:87.
    • (2009) Biophys J , vol.96 , pp. 87
    • Paulite, M.1    Fakhraai, Z.2    Gunari, N.3    Tanur, A.4    G, W.5
  • 45
  • 46
    • 0000274050 scopus 로고    scopus 로고
    • Nanoscale chemical analysis by tip-enhanced Raman spectroscopy
    • Stockle RM, Suh YD, Deckert V, Zenobi R. Nanoscale chemical analysis by tip-enhanced Raman spectroscopy. Chem Phys Lett 2000; 318:131-6.
    • (2000) Chem Phys Lett , vol.318 , pp. 131-136
    • Stockle, R.M.1    Suh, Y.D.2    Deckert, V.3    Zenobi, R.4
  • 48
    • 0345817128 scopus 로고    scopus 로고
    • Surface enhanced Raman spectroscopy: Towards single molecule spectroscopy
    • Pettinger B, Picardi G, Schuster G, Ertl G. Surface enhanced Raman spectroscopy: towards single molecule spectroscopy. Electrochem 2000; 68:942-9.
    • (2000) Electrochem , vol.68 , pp. 942-949
    • Pettinger, B.1    Picardi, G.2    Schuster, G.3    Ertl, G.4
  • 49
    • 43049122464 scopus 로고    scopus 로고
    • Tip-enhanced Raman scattering
    • Bailo E, Deckert V. Tip-enhanced Raman scattering. Chem Soc Rev 2008; 37:921-30.
    • (2008) Chem Soc Rev , vol.37 , pp. 921-930
    • Bailo, E.1    Deckert, V.2
  • 50
    • 34347388834 scopus 로고    scopus 로고
    • Reply to Comment on "Scanning-probe Raman spectroscopy with single-molecule sensitivity"
    • Neacsu CC, Dreyer J, Behr N, Raschke MB. Reply to Comment on "Scanning-probe Raman spectroscopy with single-molecule sensitivity". Phys Rev B 2007; 75:236402.
    • (2007) Phys Rev B , vol.75 , pp. 236402
    • Neacsu, C.C.1    Dreyer, J.2    Behr, N.3    Raschke, M.B.4
  • 51
    • 41049086536 scopus 로고    scopus 로고
    • Tip-enhanced Raman spectroscopy of single RNA strands: Towards a novel direct-sequencing method
    • Bailo E, Deckert V. Tip-enhanced Raman spectroscopy of single RNA strands: towards a novel direct-sequencing method. Angew Chem Int Ed Engl 2008; 47:1658-61.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 1658-1661
    • Bailo, E.1    Deckert, V.2
  • 52
    • 62749155773 scopus 로고    scopus 로고
    • Ultraflat transparent gold nanoplates - Ideal substrates for tip-enhanced Raman scattering experiments
    • Deckert-Gaudig T, Deckert V. Ultraflat transparent gold nanoplates - ideal substrates for tip-enhanced Raman scattering experiments. Small 2009; 5:432-6.
    • (2009) Small , vol.5 , pp. 432-436
    • Deckert-Gaudig, T.1    Deckert, V.2
  • 53
    • 77951567654 scopus 로고    scopus 로고
    • Aromatic amino acid monolayers sandwiched between gold and silver: A combined tip-enhanced raman and theoretical approach
    • Deckert-Gaudig T, Rauls E, Deckert V. Aromatic amino acid monolayers sandwiched between gold and silver: a combined tip-enhanced raman and theoretical approach. J Phys Chem C 2010; 114:7412-20.
    • (2010) J Phys Chem C , vol.114 , pp. 7412-7420
    • Deckert-Gaudig, T.1    Rauls, E.2    Deckert, V.3
  • 54
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet 2005; 6:435-50.
    • (2005) Nat Rev Genet , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 55
    • 33646126278 scopus 로고    scopus 로고
    • New insights into prion structure and toxicity
    • Harris DA, True HL. New insights into prion structure and toxicity. Neuron 2006; 50:353-7.
    • (2006) Neuron , vol.50 , pp. 353-357
    • Harris, D.A.1    True, H.L.2
  • 56
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146-58.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 57
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M, Collins SR, Toyama BH, Weissman JS. The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585-9.
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 58
    • 31444452768 scopus 로고    scopus 로고
    • The battle of the fold: Chaperones take on prions
    • True HL. The battle of the fold: chaperones take on prions. Trends Genet 2006; 22:110-7.
    • (2006) Trends Genet , vol.22 , pp. 110-117
    • True, H.L.1
  • 61
    • 39049119728 scopus 로고    scopus 로고
    • Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size
    • Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, Baskakov IV. Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J Mol Biol 2008; 376:1155-67.
    • (2008) J Mol Biol , vol.376 , pp. 1155-1167
    • Sun, Y.1    Makarava, N.2    Lee, C.I.3    Laksanalamai, P.4    Robb, F.T.5    Baskakov, I.V.6
  • 63
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998; 95:6448-53.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 65
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • Scherzinger E, Lurz R, Turmaine M, Mangiarini L, Hollenbach B, Hasenbank R, et al. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo. Cell 1997; 90:549-58.
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3    Mangiarini, L.4    Hollenbach, B.5    Hasenbank, R.6
  • 66
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Abeta oligomers: The solution to an Alzheimer's disease conundrum?
    • Klein WL, Krafft GA, Finch CE. Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 2001; 24:219-24.
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 67
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 2007; 8:101-12.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 68
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg MS, Lansbury PT Jr. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nat Cell Biol 2000; 2:115-9.
    • (2000) Nat Cell Biol , vol.2 , pp. 115-119
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 70
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000; 289:1317-21.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6
  • 71
    • 70450224432 scopus 로고    scopus 로고
    • Role of small oligomers on the amyloidogenic aggregation free-energy landscape
    • He X, Giurleo JT, Talaga DS. Role of small oligomers on the amyloidogenic aggregation free-energy landscape. J Mol Biol 2009; 395:134-54.
    • (2009) J Mol Biol , vol.395 , pp. 134-154
    • He, X.1    Giurleo, J.T.2    Talaga, D.S.3
  • 72
    • 33644843938 scopus 로고    scopus 로고
    • Species barriers in prion diseases - Brief review
    • Moore RA, Vorberg I, Priola SA. Species barriers in prion diseases - brief review. Arch Virol 2005; 187-202.
    • (2005) Arch Virol , pp. 187-202
    • Moore, R.A.1    Vorberg, I.2    Priola, S.A.3
  • 73
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • Vanik DL, Surewicz KA, Surewicz WK. Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol Cell 2004; 14:139-45.
    • (2004) Mol Cell , vol.14 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3
  • 74
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid and human disease. Annu Rev Biochem 2006; 75:333-66.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 75
    • 77953522394 scopus 로고    scopus 로고
    • Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission
    • Chen B, Bruce KL, Newnam GP, Gyoneva S, Romanyuk AV, Chernoff YO. Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol Microbiol 2010; 76:1483-99.
    • (2010) Mol Microbiol , vol.76 , pp. 1483-1499
    • Chen, B.1    Bruce, K.L.2    Newnam, G.P.3    Gyoneva, S.4    Romanyuk, A.V.5    Chernoff, Y.O.6
  • 76
    • 33847307713 scopus 로고    scopus 로고
    • Prion species barrier between the closely related yeast proteins is detected despite coaggregation
    • Chen B, Newnam GP, Chernoff YO. Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc Natl Acad Sci USA 2007; 104:2791-6.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2791-2796
    • Chen, B.1    Newnam, G.P.2    Chernoff, Y.O.3
  • 77
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson CM. Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 2004; 15:3-16.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 78
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci 1999; 24:329-32.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 79
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova AT, Ishii Y, Balbach JJ, Antzutkin ON, Leapman RD, Delaglio F, et al. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 2002; 99:16742-7.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5    Delaglio, F.6
  • 80
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA 1994; 91:5355-8.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 81
    • 29044443820 scopus 로고    scopus 로고
    • Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease
    • Watson D, Castano E, Kokjohn TA, Kuo YM, Lyubchenko Y, Pinsky D, et al. Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease. Neurol Res 2005; 27:869-81.
    • (2005) Neurol Res , vol.27 , pp. 869-881
    • Watson, D.1    Castano, E.2    Kokjohn, T.A.3    Kuo, Y.M.4    Lyubchenko, Y.5    Pinsky, D.6
  • 82
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen S, Ferrone FA, Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc Natl Acad Sci USA 2002; 99:11884-9.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 85
    • 30344457011 scopus 로고    scopus 로고
    • Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation
    • DOI 10.1016/j.jmb.2005.11.034, PII S0022283605014221
    • Bader R, Bamford R, Zurdo J, Luisi BF, Dobson CM. Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation. J Mol Biol 2006; 356:189-208. (Pubitemid 43069737)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.1 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 86
    • 33745727173 scopus 로고    scopus 로고
    • Interpreting the aggregation kinetics of amyloid peptides
    • Pellarin R, Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J Mol Biol 2006; 360:882-92.
    • (2006) J Mol Biol , vol.360 , pp. 882-892
    • Pellarin, R.1    Caflisch, A.2
  • 88
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci USA 2007; 104:2649-54.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 90
    • 66749136907 scopus 로고    scopus 로고
    • Dynamic properties of pH-dependent structural organization of the amyloidogenic beta-protein (1-40)
    • Rubinstein A, Lyubchenko YL, Sherman S. Dynamic properties of pH-dependent structural organization of the amyloidogenic beta-protein (1-40). Prion 2009; 3:31-43.
    • (2009) Prion , vol.3 , pp. 31-43
    • Rubinstein, A.1    Lyubchenko, Y.L.2    Sherman, S.3
  • 91
    • 67650082769 scopus 로고    scopus 로고
    • Single-molecule mechanical unfolding of amyloidogenic beta(2)-microglobulin: The forcespectroscopy approach
    • Sorce B, Sabella S, Sandal M, Samori B, Santino A, Cingolani R, et al. Single-molecule mechanical unfolding of amyloidogenic beta(2)-microglobulin: The forcespectroscopy approach. Chemphyschem 2009; 10:1471-7
    • (2009) Chemphyschem , vol.10 , pp. 1471-1477
    • Sorce, B.1    Sabella, S.2    Sandal, M.3    Samori, B.4    Santino, A.5    Cingolani, R.6
  • 92
    • 38949139507 scopus 로고    scopus 로고
    • Conformational equilibria in monomeric alpha-synuclein at the single-molecule level
    • Sandal M, Valle F, Tessari I, Mammi S, Bergantino E, Musiani F, et al. Conformational equilibria in monomeric alpha-synuclein at the single-molecule level. PLoS Biol 2008; 6:6.
    • (2008) PLoS Biol , vol.6 , pp. 6
    • Sandal, M.1    Valle, F.2    Tessari, I.3    Mammi, S.4    Bergantino, E.5    Musiani, F.6
  • 93
    • 59649095836 scopus 로고    scopus 로고
    • Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers
    • Brucale M, Sandal M, Di Maio S, Rampioni A, Tessari I, Tosatto L, et al. Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers. Chembiochem 2009; 10:176-83.
    • (2009) Chembiochem , vol.10 , pp. 176-183
    • Brucale, M.1    Sandal, M.2    Di Maio, S.3    Rampioni, A.4    Tessari, I.5    Tosatto, L.6
  • 96
    • 60549100886 scopus 로고    scopus 로고
    • Early stages for Parkinson's development: Alpha-synuclein misfolding and aggregation
    • Yu J, Lyubchenko YL. Early stages for Parkinson's development: alpha-synuclein misfolding and aggregation. J Neuroimmune Pharm 2009; 4:10-6.
    • (2009) J Neuroimmune Pharm , vol.4 , pp. 10-16
    • Yu, J.1    Lyubchenko, Y.L.2
  • 97
    • 56249130752 scopus 로고    scopus 로고
    • alpha-Synuclein misfolding: Single molecule AFM force spectroscopy study
    • Yu J, Malkova S, Lyubchenko YL. alpha-Synuclein misfolding: single molecule AFM force spectroscopy study. J Mol Biol 2008; 384:992-1001.
    • (2008) J Mol Biol , vol.384 , pp. 992-1001
    • Yu, J.1    Malkova, S.2    Lyubchenko, Y.L.3
  • 98
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques
    • Perutz MF, Pope BJ, Owen D, Wanker EE, Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc Natl Acad Sci USA 2002; 99:5596-600.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 99
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid
    • Balbirnie M, Grothe R, Eisenberg DS. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc Natl Acad Sci USA 2001; 98:2375-80.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 101
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel R, Nassoy P, Leung A, Ritchie K, Evans E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 1999; 397:50-3.
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5


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