메뉴 건너뛰기




Volumn 305, Issue , 2011, Pages 135-168

Prion Protein and its conformational conversion: A structural perspective

Author keywords

Prion diseases; Prion protein folding; Prion strains; Prion structural biology; Prions

Indexed keywords

COPPER; RECOMBINANT PROTEIN;

EID: 80054774250     PISSN: 03401022     EISSN: None     Source Type: Book Series    
DOI: 10.1007/128_2011_165     Document Type: Article
Times cited : (71)

References (186)
  • 2
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • DOI 10.1146/annurev.biochem.72.121801.161837
    • Chien P, Weissman JS, DePace AH (2004) Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 73:617-656 (Pubitemid 39050382)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 4
    • 12144271772 scopus 로고    scopus 로고
    • NMR structure of the bovine prion protein isolated from healthy calf brains
    • DOI 10.1038/sj.embor.7400297
    • Hornemann S, Schorn C, Wuthrich K (2004) NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep 5:1159-1164 (Pubitemid 40103610)
    • (2004) EMBO Reports , vol.5 , Issue.12 , pp. 1159-1164
    • Hornemann, S.1    Schorn, C.2    Wuthrich, K.3
  • 5
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • DOI 10.1016/S0014-5793(97)00920-4, PII S0014579397009204
    • Riek R, Hornemann S, Wider G et al (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 413:282-288 (Pubitemid 27353285)
    • (1997) FEBS Letters , vol.413 , Issue.2 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 6
    • 0031456947 scopus 로고    scopus 로고
    • Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
    • Donne DG, Viles JH, Groth D et al (1997) Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci USA 94: 13452-13457
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13452-13457
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3
  • 8
    • 0242662244 scopus 로고    scopus 로고
    • The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site
    • DOI 10.1016/j.jmb.2003.09.048
    • Zahn R (2003) The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site. J Mol Biol 334:477-488 (Pubitemid 37386348)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.3 , pp. 477-488
    • Zahn, R.1
  • 9
    • 73249135395 scopus 로고    scopus 로고
    • Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan
    • Taubner LM, Bienkiewicz EA, Copié V et al (2010) Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. J Mol Biol 395:475-490
    • (2010) J Mol Biol , vol.395 , pp. 475-490
    • Taubner, L.M.1    Bienkiewicz, E.A.2    Copié, V.3
  • 10
    • 0034649237 scopus 로고    scopus 로고
    • Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy
    • Aronoff-Spencer E, Burns CS, Avdievich NI et al (2000) Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry 39:13760-13771
    • (2000) Biochemistry , vol.39 , pp. 13760-13771
    • Aronoff-Spencer, E.1    Burns, C.S.2    Avdievich, N.I.3
  • 12
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • DOI 10.1038/nature05294, PII NATURE05294
    • Caughey B, Baron GS (2006) Prions and their partners in crime. Nature 443:803-810 (Pubitemid 44622685)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 14
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner SB, Groth DF, Bolton DC et al (1984) Purification and structural studies of a major scrapie prion protein. Cell 38:127-134 (Pubitemid 15216542)
    • (1984) Cell , vol.38 , Issue.1 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3
  • 15
    • 0038208322 scopus 로고    scopus 로고
    • Intra-and interspecies interactions between prion proteins and effects of mutations and polymorphisms
    • DOI 10.1515/BC.2003.088
    • Hundt C, Gauczynski S, Leucht C et al (2003) Intra-and interspecies interactions between prion proteins and effects of mutations and polymorphisms. Biol Chem 384:791-803 (Pubitemid 36747940)
    • (2003) Biological Chemistry , vol.384 , Issue.5 , pp. 791-803
    • Hundt, C.1    Gauczynski, S.2    Leucht, C.3    Riley, M.L.4    Weiss, S.5
  • 16
    • 34247501644 scopus 로고    scopus 로고
    • Mapping of possible prion protein self-interaction domains using peptide arrays
    • Rigter A, Langeveld JPM, Timmers-Parohi D et al (2007) Mapping of possible prion protein self-interaction domains using peptide arrays. BMC Biochem 8:6
    • (2007) BMC Biochem , vol.8 , pp. 6
    • Rigter, A.1    Jpm, L.2    Timmers-Parohi, D.3
  • 18
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • DOI 10.1016/S0896-6273(00)80653-4
    • Chiesa R, Piccardo P, Ghetti B et al (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21:1339-1351 (Pubitemid 29022536)
    • (1998) Neuron , vol.21 , Issue.6 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 21
    • 0034721767 scopus 로고    scopus 로고
    • Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases
    • Zhang Y, Swietnicki W, Zagorski MG et al (2000) Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem 275:33650-33654
    • (2000) J Biol Chem , vol.275 , pp. 33650-33654
    • Zhang, Y.1    Swietnicki, W.2    Zagorski, M.G.3
  • 22
    • 77955367206 scopus 로고    scopus 로고
    • NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features
    • Ilc G, Giachin G, Jaremko Met al (2010) NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. PLoS ONE 5:e11715
    • (2010) PLoS ONE , vol.5
    • Ilc, G.1    Giachin, G.2    Jaremko, M.3
  • 23
    • 75649120399 scopus 로고    scopus 로고
    • Conformational diversity in prion protein variants influences intermolecular beta-sheet formation
    • Lee S, Antony L, Hartmann R et al (2010) Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. EMBO J 29:251-262
    • (2010) EMBO J , vol.29 , pp. 251-262
    • Lee, S.1    Antony, L.2    Hartmann, R.3
  • 25
    • 62449203220 scopus 로고    scopus 로고
    • Crystal structure of human prion protein bound to a therapeutic antibody
    • Antonyuk SV, Trevitt CR, Strange RW et al (2009) Crystal structure of human prion protein bound to a therapeutic antibody. Proc Natl Acad Sci USA 106:2554-2558
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2554-2558
    • Antonyuk, S.V.1    Trevitt, C.R.2    Strange, R.W.3
  • 27
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • DOI 10.1074/jbc.M303005200
    • Calzolai L, Zahn R (2003) Influence of pH on NMR structure and stability of the human prion protein globular domain. J Biol Chem 278:35592-35596 (Pubitemid 37102332)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 28
    • 0034931126 scopus 로고    scopus 로고
    • Three-dimensional structures of prion proteins
    • DOI 10.1016/S0065-3233(01)57018-7
    • Wuthrich K, Riek R (2001) Three-dimensional structures of prion proteins. Adv Protein Chem 57:55-82 (Pubitemid 32622680)
    • (2001) Advances in Protein Chemistry , vol.57 , pp. 55-82
    • Wuthrich, K.1    Riek, R.2
  • 29
    • 63049099537 scopus 로고    scopus 로고
    • Prion protein library of recombinant constructs for structural biology
    • Hornemann S, Christen B, von Schroetter C et al (2009) Prion protein library of recombinant constructs for structural biology. FEBS J 276:2359-2367
    • (2009) FEBS J , vol.276 , pp. 2359-2367
    • Hornemann, S.1    Christen, B.2    Von Schroetter, C.3
  • 36
    • 58549102983 scopus 로고    scopus 로고
    • De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis
    • Sigurdson CJ, Nilsson KPR, Hornemann S et al (2009) De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis. Proc Natl Acad Sci USA 106:304-309
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 304-309
    • Sigurdson, C.J.1    Kpr, N.2    Hornemann, S.3
  • 37
    • 77954972690 scopus 로고    scopus 로고
    • A molecular switch controls interspecies prion disease transmission in mice
    • Sigurdson CJ, Nilsson KPR, Hornemann S et al (2010) A molecular switch controls interspecies prion disease transmission in mice. J Clin Invest 120:2590-2599
    • (2010) J Clin Invest , vol.120 , pp. 2590-2599
    • Sigurdson, C.J.1    Nilsson, K.P.R.2    Hornemann, S.3
  • 38
    • 33645147707 scopus 로고    scopus 로고
    • Prion disease genetics
    • Mead S (2006) Prion disease genetics. Eur J Hum Genet 14:273-281
    • (2006) Eur J Hum Genet , vol.14 , pp. 273-281
    • Mead, S.1
  • 39
    • 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
  • 40
    • 77957669973 scopus 로고    scopus 로고
    • The H187Rmutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form
    • Hosszu LLP, TattumMH, Jones S et al (2010) The H187Rmutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form. Biochemistry 49:8729-8738
    • (2010) Biochemistry , vol.49 , pp. 8729-8738
    • Hosszu, L.L.P.1    Tattum, M.H.2    Jones, S.3
  • 44
    • 0038304770 scopus 로고    scopus 로고
    • Distribution of codon 129 genotype in human growth hormone-treated CJD patients in France and the UK
    • DOI 10.1016/S0140-6736(03)13867-6
    • Brandel J, Preece M, Brown P et al (2003) Distribution of codon 129 genotype in human growth hormone-treated CJD patients in France and the UK. Lancet 362:128-130 (Pubitemid 36831026)
    • (2003) Lancet , vol.362 , Issue.9378 , pp. 128-130
    • Brandel, J.-P.1    Preece, M.2    Brown, P.3    Croes, E.4    Laplanche, J.-L.5    Agid, Y.6    Will, R.7    Alperovitch, A.8
  • 46
    • 0036145653 scopus 로고    scopus 로고
    • Structures of the two 3D domain-swapped RNase A trimers
    • DOI 10.1110/ps.36602
    • Liu Y, Gotte G, Libonati M et al (2002) Structures of the two 3D domain-swapped RNase A trimers. Protein Sci 11:371-380 (Pubitemid 34075800)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 371-380
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 47
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • DOI 10.1110/ps.0201402
    • Liu Y, Eisenberg D (2002) 3D domain swapping: as domains continue to swap. Protein Sci 11:1285-1299 (Pubitemid 34547201)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 48
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease a with three-dimensional domain-swapped and native-like structure
    • DOI 10.1038/nature03916
    • Sambashivan S, Liu Y, Sawaya MR et al (2005) Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature 437:266-269 (Pubitemid 41294490)
    • (2005) Nature , vol.437 , Issue.7056 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 49
    • 59149098864 scopus 로고    scopus 로고
    • Copper and the structural biology of the prion protein
    • Viles JH, Klewpatinond M, Nadal RC (2008) Copper and the structural biology of the prion protein. Biochem Soc Trans 36:1288-1292
    • (2008) Biochem Soc Trans , vol.36 , pp. 1288-1292
    • Viles, J.H.1    Klewpatinond, M.2    Nadal, R.C.3
  • 50
    • 40449128239 scopus 로고    scopus 로고
    • The chemistry of copper binding to PrP: Is there sufficient evidence to elucidate a role for copper in protein function?
    • DOI 10.1042/BJ20071477
    • Davies P, Brown DR (2008) The chemistry of copper binding to PrP: is there sufficient evidence to elucidate a role for copper in protein function? Biochem J 410:237-244 (Pubitemid 351346181)
    • (2008) Biochemical Journal , vol.410 , Issue.2 , pp. 237-244
    • Davies, P.1    Brown, D.R.2
  • 52
    • 0035907363 scopus 로고    scopus 로고
    • Prion protein binds copper within the physiological concentration range
    • Kramer ML, Kratzin HD, Schmidt B et al (2001) Prion protein binds copper within the physiological concentration range. J Biol Chem 276:16711-16719
    • (2001) J Biol Chem , vol.276 , pp. 16711-16719
    • Kramer, M.L.1    Kratzin, H.D.2    Schmidt, B.3
  • 53
    • 0037470178 scopus 로고    scopus 로고
    • Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity. Insights from circular dichroism
    • DOI 10.1074/jbc.M209280200
    • Garnett AP, Viles JH (2003) Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism. J Biol Chem 278: 6795-6802 (Pubitemid 36800668)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6795-6802
    • Garnett, A.P.1    Viles, J.H.2
  • 54
    • 33751108289 scopus 로고    scopus 로고
    • The affinity of copper binding to the prion protein octarepeat domain: Evidence for negative cooperativity
    • DOI 10.1021/bi060948r
    • Walter ED, Chattopadhyay M, Millhauser GL (2006) The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity. Biochemistry 45: 13083-13092 (Pubitemid 44763431)
    • (2006) Biochemistry , vol.45 , Issue.43 , pp. 13083-13092
    • Walter, E.D.1    Chattopadhyay, M.2    Millhauser, G.L.3
  • 57
    • 3542999252 scopus 로고    scopus 로고
    • 111 induces β-sheet formation in the unstructured amyloiodogenic region of the prion protein
    • DOI 10.1074/jbc.M403467200
    • Jones CE, Abdelraheim SR, Brown DR et al (2004) Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein. J Biol Chem 279:32018-32027 (Pubitemid 39014646)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32018-32027
    • Jones, C.E.1    Abdelraheim, S.R.2    Brown, D.E.3    Viles, J.H.4
  • 58
    • 38349169574 scopus 로고    scopus 로고
    • Deconvoluting the Cu2+ binding modes of full-length prion protein
    • Klewpatinond M, Davies P, Bowen S et al (2008) Deconvoluting the Cu2+ binding modes of full-length prion protein. J Biol Chem 283:1870-1881
    • (2008) J Biol Chem , vol.283 , pp. 1870-1881
    • Klewpatinond, M.1    Davies, P.2    Bowen, S.3
  • 59
    • 0034950034 scopus 로고    scopus 로고
    • 2+ to the C-terminal domain of the murine prion protein
    • Cereghetti GM, Schweiger A, Glockshuber R et al (2001) Electron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion protein. Biophys J 81:516-525 (Pubitemid 32605989)
    • (2001) Biophysical Journal , vol.81 , Issue.1 , pp. 516-525
    • Cereghetti, G.M.1    Schweiger, A.2    Glockshuber, R.3    Van Doorslaer, S.4
  • 60
    • 70349506756 scopus 로고    scopus 로고
    • Copper binding extrinsic to the octarepeat region in the prion protein
    • Walter ED, Stevens DJ, Spevacek AR et al (2009) Copper binding extrinsic to the octarepeat region in the prion protein. Curr Protein Pept Sci 10:529-535
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 529-535
    • Walter, E.D.1    Stevens, D.J.2    Spevacek, A.R.3
  • 61
    • 0345714734 scopus 로고    scopus 로고
    • C may inhibit prion disease propagation
    • DOI 10.1016/j.brainres.2003.09.014
    • Hijazi N, Shaked Y, Rosenmann H et al (2003) Copper binding to PrPC may inhibit prion disease propagation. Brain Res 993:192-200 (Pubitemid 37464597)
    • (2003) Brain Research , vol.993 , Issue.1-2 , pp. 192-200
    • Hijazi, N.1    Shaked, Y.2    Rosenmann, H.3    Ben-Hur, T.4    Gabizon, R.5
  • 63
    • 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
  • 64
    • 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
  • 66
    • 2342432162 scopus 로고    scopus 로고
    • The Effect of Disease-associated Mutations on the Folding Pathway of Human Prion Protein
    • DOI 10.1074/jbc.M313581200
    • Apetri AC, Surewicz K, Surewicz WK (2004) The effect of disease-associated mutations on the folding pathway of human prion protein. J Biol Chem 279:18008-18014 (Pubitemid 38560570)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 18008-18014
    • Apetri, A.C.1    Surewicz, K.2    Surewicz, W.K.3
  • 67
    • 0037160126 scopus 로고    scopus 로고
    • Kinetic intermediate in the folding of human prion protein
    • DOI 10.1074/jbc.C200507200
    • Apetri AC, Surewicz WK (2002) Kinetic intermediate in the folding of human prion protein. J Biol Chem 277:44589-44592 (Pubitemid 36159046)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44589-44592
    • Apetri, A.C.1    Surewicz, W.K.2
  • 68
    • 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 et al (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
  • 69
    • 0025876226 scopus 로고
    • N-Terminal truncation of the scrapieassociated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B, Raymond GJ, Ernst D et al (1991) N-Terminal truncation of the scrapieassociated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 65:6597-6603
    • (1991) J Virol , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3
  • 70
    • 65249125818 scopus 로고    scopus 로고
    • Folding kinetics of the human prion protein probed by temperature jump
    • Hart T, Hosszu LLP, Trevitt CR 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    Hosszu, L.L.P.2    Trevitt, C.R.3
  • 71
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki W, Petersen RB, Gambetti P et al (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 273:31048-31052
    • (1998) J Biol Chem , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3
  • 72
    • 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, 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
  • 73
    • 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 et al (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
  • 75
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • DOI 10.1021/bi991967m
    • Swietnicki W, Morillas M, Chen SG et al (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39:424-431 (Pubitemid 30056478)
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 76
    • 0035849540 scopus 로고    scopus 로고
    • On the mechanism of α-helix to β-sheet transition in the recombinant prion protein
    • DOI 10.1021/bi010232q
    • Morillas M, Vanik DL, Surewicz WK (2001) On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein. Biochemistry 40:6982-6987 (Pubitemid 32538246)
    • (2001) Biochemistry , vol.40 , Issue.23 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 77
    • 70349454224 scopus 로고    scopus 로고
    • Differential stability of the bovine prion protein upon urea unfolding
    • Julien O, Chatterjee S, Thiessen A et al (2009) Differential stability of the bovine prion protein upon urea unfolding. Protein Sci 18:2172-2182
    • (2009) Protein Sci , vol.18 , pp. 2172-2182
    • Julien, O.1    Chatterjee, S.2    Thiessen, A.3
  • 78
    • 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 TJT (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
  • 79
    • 0037108168 scopus 로고    scopus 로고
    • Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc?
    • Kuwata K, Li H, Yamada H 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    Li, H.2    Yamada, H.3
  • 81
    • 0346118882 scopus 로고    scopus 로고
    • Folding Intermediates of the Prion Protein Stabilized by Hydrostatic Pressure and Low Temperature
    • DOI 10.1074/jbc.M307354200
    • Martins SM, Chapeaurouge A, Ferreira ST (2003) Folding intermediates of the prion protein stabilized by hydrostatic pressure and low temperature. J Biol Chem 278:50449-50455 (Pubitemid 37548890)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50449-50455
    • Martins, S.M.1    Chapeaurouge, A.2    Ferreira, S.T.3
  • 82
    • 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 et al (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
  • 83
    • 4744351381 scopus 로고    scopus 로고
    • Slow Conformational Dynamics in the Hamster Prion Protein
    • DOI 10.1021/bi036123o
    • Kuwata K, Kamatari YO, Akasaka K et al (2004) Slow conformational dynamics in the hamster prion protein. Biochemistry 43:4439-4446 (Pubitemid 38500572)
    • (2004) Biochemistry , vol.43 , Issue.15 , pp. 4439-4446
    • Kuwata, K.1    Kamatari, Y.O.2    Akasaka, K.3    James, T.L.4
  • 84
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB (1991) Molecular biology of prion diseases. Science 252:1515-1522 (Pubitemid 21917065)
    • (1991) Science , vol.252 , Issue.5012 , pp. 1515-1522
    • Prusiner, S.B.1
  • 86
    • 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
  • 87
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26: 267-298 (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 89
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • Jarrett JT, Lansbury PT (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73:1055-1058 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 90
    • 0036479465 scopus 로고    scopus 로고
    • The utility of prions
    • DOI 10.1016/S1534-5807(02)00118-1, PII S1534580702001181
    • Osherovich LZ, Weissman JS (2002) The utility of prions. Dev Cell 2:143-151 (Pubitemid 38351579)
    • (2002) Developmental Cell , vol.2 , Issue.2 , pp. 143-151
    • Osherovich, L.Z.1    Weissman, J.S.2
  • 91
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • DOI 10.1146/annurev.micro.56.013002.100603
    • Uptain SM, Lindquist S (2002) Prions as protein-based genetic elements. Annu Rev Microbiol 56:703-741 (Pubitemid 35217472)
    • (2002) Annual Review of Microbiology , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 92
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • DOI 10.1038/nature04922, PII NATURE04922
    • Tanaka M, Collins SR, Toyama BH et al (2006) The physical basis of how prion conformations determine strain phenotypes. Nature 442:585-589 (Pubitemid 44167919)
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 93
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling Activities
    • DOI 10.1016/j.molcel.2006.05.042, PII S1097276506003868
    • Shorter J, Lindquist S (2006) Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol Cell 23:425-438 (Pubitemid 44128844)
    • (2006) Molecular Cell , vol.23 , Issue.3 , pp. 425-438
    • Shorter, J.1    Lindquist, S.2
  • 94
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TPJ, Waudby CA, Devlin GL et al (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326:1533-1537
    • (2009) Science , vol.326 , pp. 1533-1537
    • Tpj, K.1    Waudby, C.A.2    Devlin, G.L.3
  • 95
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley MP, Prusiner SB (1982) Identification of a protein that purifies with the scrapie prion. Science 218:1309-1311
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 96
    • 0141577720 scopus 로고    scopus 로고
    • Identification of Novel Proteinase K-resistant C-terminal Fragments of PrP in Creutzfeldt-Jakob Disease
    • DOI 10.1074/jbc.M308550200
    • Zou W, Capellari S, Parchi P et al (2003) Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J Biol Chem 278:40429-40436 (Pubitemid 37280852)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 40429-40436
    • Zou, W.-Q.1    Capellari, S.2    Parchi, P.3    Sy, M.-S.4    Gambetti, P.5    Chen, S.G.6
  • 97
    • 1842644947 scopus 로고    scopus 로고
    • Inherited prion diseases
    • Prusiner SB (ed) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Kong Q, Surewicz WK, Petersen RB et al (2004) Inherited prion diseases. In: Prusiner SB (ed) Prion biology and diseases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2004) Prion Biology and Diseases
    • Kong, Q.1    Surewicz, W.K.2    Petersen, R.B.3
  • 101
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapieassociated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey BW, Dong A, Bhat KS et al (1991) Secondary structure analysis of the scrapieassociated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30:7672-7680
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3
  • 103
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J 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    Baldwin, M.2    Nguyen, J.3
  • 104
    • 0027363495 scopus 로고
    • Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity
    • Safar J, Roller PP, Gajdusek DC et al (1993) Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci 2:2206-2216 (Pubitemid 23354723)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2206-2216
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 105
    • 79953785159 scopus 로고    scopus 로고
    • Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
    • Smirnovas V, Baron GS, Offerdahl DK et al (2011) Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol 18: 504-506
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 504-506
    • Smirnovas, V.1    Baron, G.S.2    Offerdahl, D.K.3
  • 107
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • DOI 10.1038/nature02391
    • King C, Diaz-Avalos R (2004) Protein-only transmission of three yeast prion strains. Nature 428:319-323 (Pubitemid 38418802)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 319-323
    • King, C.-Y.1    Diaz-Avalos, R.2
  • 108
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • DOI 10.1038/nature02392
    • Tanaka M, Chien P, Naber N et al (2004) Conformational variations in an infectious protein determine prion strain differences. Nature 428:323-328 (Pubitemid 38418803)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 109
    • 77449089995 scopus 로고    scopus 로고
    • Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP
    • Jansen C, Parchi P, Capellari S et al (2010) Prion protein amyloidosis with divergent phenotype associated with two novel nonsense mutations in PRNP. Acta Neuropathol 119:189-197
    • (2010) Acta Neuropathol , vol.119 , pp. 189-197
    • Jansen, C.1    Parchi, P.2    Capellari, S.3
  • 112
    • 77950379326 scopus 로고    scopus 로고
    • Fatal transmissible amyloid encephalopathy: A new type of prion disease associated with lack of prion protein membrane anchoring
    • Chesebro B, Race B, Meade-White K et al (2010) Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring. PLoS Pathog 6:e1000800
    • (2010) PLoS Pathog , vol.6
    • Chesebro, B.1    Race, B.2    Meade-White, K.3
  • 113
    • 70349858126 scopus 로고    scopus 로고
    • Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils
    • Sim VL, Caughey B (2009) Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils. Neurobiol Aging 30:2031-2042
    • (2009) Neurobiol Aging , vol.30 , pp. 2031-2042
    • Sim, V.L.1    Caughey, B.2
  • 114
    • 67650747654 scopus 로고    scopus 로고
    • Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions
    • Caughey B, Baron GS, Chesebro B et al (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
  • 115
    • 0021019026 scopus 로고
    • Scrapie prions aggregate to form amyloid-like birefringent rods
    • Prusiner SB, McKinley MP, Bowman KA et al (1983) Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358 (Pubitemid 14202913)
    • (1983) Cell , vol.35 , Issue.2 , pp. 349-358
    • Prusiner, S.B.1    McKinley, M.P.2    Bowman, K.A.3
  • 116
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley MP, Meyer RK, Kenaga L et al (1991) Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 65:1340-1351
    • (1991) J Virol , vol.65 , pp. 1340-1351
    • McKinley, M.P.1    Meyer, R.K.2    Kenaga, L.3
  • 120
    • 0035847005 scopus 로고    scopus 로고
    • 2+ at 1.96 A resolution
    • DOI 10.1006/jmbi.2000.4296
    • Kostrewa D, D'Arcy A, Takacs B et al (2001) Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N- acetylglucosamine and Mg(2+) at 1.96 A resolution. J Mol Biol 305:279-289 (Pubitemid 32099461)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.2 , pp. 279-289
    • Kostrewa, D.1    D'Arcy, A.2    Takacs, B.3    Kamber, M.4
  • 122
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: A parallel, in-register b-structure
    • Cobb NJ, Sonnichsen FD, Mchaourab H et al (2007) Molecular architecture of human prion protein amyloid: a parallel, in-register b-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
  • 123
    • 69949187643 scopus 로고    scopus 로고
    • Molecular mechanisms for protein-encoded inheritance
    • Wiltzius JJW, Landau M, Nelson R et al (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol 16:973-978
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 973-978
    • Wiltzius, J.J.W.1    Landau, M.2    Nelson, R.3
  • 124
    • 70350134002 scopus 로고    scopus 로고
    • Natural and synthetic prion structure from X-ray fiber diffraction
    • Wille H, Bian W, McDonald Met al (2009) Natural and synthetic prion structure from X-ray fiber diffraction. Proc Natl Acad Sci USA 106:16990-16995
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16990-16995
    • Wille, H.1    Bian, W.2    McDonald, M.3
  • 125
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • DOI 10.1126/science.1151839
    • Wasmer C, Lange A, Van Melckebeke H et al (2008) Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319:1523-1526 (Pubitemid 351398180)
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 126
    • 69949163540 scopus 로고    scopus 로고
    • The functional curli amyloid is not based on in-register parallel beta-sheet structure
    • Shewmaker F, McGlinchey RP, Thurber KR et al (2009) The functional curli amyloid is not based on in-register parallel beta-sheet structure. J Biol Chem 284:25065-25076
    • (2009) J Biol Chem , vol.284 , pp. 25065-25076
    • Shewmaker, F.1    McGlinchey, R.P.2    Thurber, K.R.3
  • 127
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • Baskakov IV, Legname G, Prusiner SB et al (2001) Folding of prion protein to its native alpha-helical conformation is under kinetic control. J Biol Chem 276:19687-19690
    • (2001) J Biol Chem , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3
  • 128
    • 0042320356 scopus 로고    scopus 로고
    • Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process
    • DOI 10.1038/nsb961
    • Lee S, Eisenberg D (2003) Seeded conversion of recombinant prion protein to a disulfidebonded oligomer by a reduction-oxidation process. Nat Struct Biol 10:725-730 (Pubitemid 37052411)
    • (2003) Nature Structural Biology , vol.10 , Issue.9 , pp. 725-730
    • Lee, S.1    Eisenberg, D.2
  • 129
    • 3843131903 scopus 로고    scopus 로고
    • Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant. Implications for disease susceptibility to Creutzfeldt-Jakob disease
    • DOI 10.1074/jbc.M401754200
    • Tahiri-Alaoui A, Gill AC, Disterer P et al (2004) Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: implications for disease susceptibility to Creutzfeldt-Jakob disease. J Biol Chem 279:31390-31397 (Pubitemid 39037806)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.30 , pp. 31390-31397
    • Tahiri-Alaoui, A.1    Gill, A.C.2    Disterer, P.3    James, W.4
  • 130
    • 33846485595 scopus 로고    scopus 로고
    • NMR characterization of the pH 4 β-intermediate of the prion protein: The N-terminal half of the protein remains unstructured and retains a high degree of flexibility
    • DOI 10.1042/BJ20060668
    • O'Sullivan DBD, Jones CE, Abdelraheim SR et al (2007) NMR characterization of the pH 4 beta-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility. Biochem J 401:533-540 (Pubitemid 46166434)
    • (2007) Biochemical Journal , vol.401 , Issue.2 , pp. 533-540
    • O'Sullivan, D.B.D.1    Jones, C.E.2    Abdelraheim, S.R.3    Thompsett, A.R.4    Brazier, M.W.5    Toms, H.6    Brown, D.R.7    Viles, J.H.8
  • 131
    • 69249102969 scopus 로고    scopus 로고
    • Conformational properties of b-PrP
    • Hosszu LLP, Trevitt CR, Jones S et al (2009) Conformational properties of b-PrP. J Biol Chem 284:21981-21990
    • (2009) J Biol Chem , vol.284 , pp. 21981-21990
    • Hosszu, L.L.P.1    Trevitt, C.R.2    Jones, S.3
  • 133
    • 1342331870 scopus 로고    scopus 로고
    • The peculiar nature of unfolding of the human prion protein
    • DOI 10.1110/ps.03457204
    • Baskakov IV, Legname G, Gryczynski Z et al (2004) The peculiar nature of unfolding of the human prion protein. Protein Sci 13:586-595 (Pubitemid 38252555)
    • (2004) Protein Science , vol.13 , Issue.3 , pp. 586-595
    • Baskakov, I.V.1    Legname, G.2    Gryczynski, Z.3    Prusiner, S.B.4
  • 134
    • 28544443624 scopus 로고    scopus 로고
    • Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231
    • DOI 10.1021/bi051455+
    • Apetri AC, Vanik DL, SurewiczWK (2005) Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231. Biochemistry 44:15880-15888 (Pubitemid 41746918)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15880-15888
    • Apetri, A.C.1    Vanik, D.L.2    Surewicz, W.K.3
  • 135
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova OV, Breydo L, Parfenov AS et al (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). 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
  • 137
    • 58049199406 scopus 로고    scopus 로고
    • Prion protein amyloid formation under nativelike conditions involves refolding of the C-terminal alpha-helical domain
    • Cobb NJ, Apetri AC, Surewicz WK (2008) Prion protein amyloid formation under nativelike conditions involves refolding of the C-terminal alpha-helical domain. J Biol Chem 283: 34704-34711
    • (2008) J Biol Chem , vol.283 , pp. 34704-34711
    • Cobb, N.J.1    Apetri, A.C.2    Surewicz, W.K.3
  • 138
    • 17744379376 scopus 로고    scopus 로고
    • Sc from sporadic Creutzfeldt-Jakob disease
    • DOI 10.1110/ps.041186605
    • Bocharova OV, Breydo L, Salnikov VV et al (2005) Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob disease. Protein Sci 14:1222-1232 (Pubitemid 40577802)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1222-1232
    • Bocharova, O.V.1    Breydo, L.2    Salnikov, V.V.3    Gill, A.C.4    Baskakov, I.V.5
  • 140
    • 77449142074 scopus 로고    scopus 로고
    • Recombinant prion protein induces a new transmissible prion disease in wild-type animals
    • Makarava N, Kovacs GG, Bocharova O et al (2010) Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 119:177-187
    • (2010) Acta Neuropathol , vol.119 , pp. 177-187
    • Makarava, N.1    Kovacs, G.G.2    Bocharova, O.3
  • 142
    • 69949142350 scopus 로고    scopus 로고
    • Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange
    • Smirnovas V, Kim J, Lu X et al (2009) Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange. J Biol Chem 284:24233-24241
    • (2009) J Biol Chem , vol.284 , pp. 24233-24241
    • Smirnovas, V.1    Kim, J.2    Lu, X.3
  • 144
    • 77953427821 scopus 로고    scopus 로고
    • Prion protein amyloid formation involves structural rearrangements in the C-terminal domain
    • Kumar J, Sreeramulu S, Schmidt TL et al (2010) Prion protein amyloid formation involves structural rearrangements in the C-terminal domain. Chembiochem 11:1208-1213
    • (2010) Chembiochem , vol.11 , pp. 1208-1213
    • Kumar, J.1    Sreeramulu, S.2    Schmidt, T.L.3
  • 145
    • 78149307698 scopus 로고    scopus 로고
    • The a-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel b-sheet structure in PrP fibrils: Evidence from solid state nuclear magnetic resonance
    • Tycko R, Savtchenko R, Ostapchenko VG et al (2010) The a-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel b-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry 49:9488-9497
    • (2010) Biochemistry , vol.49 , pp. 9488-9497
    • Tycko, R.1    Savtchenko, R.2    Ostapchenko, V.G.3
  • 147
    • 61449258353 scopus 로고    scopus 로고
    • Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein
    • Walsh P, Simonetti K, Sharpe S (2009) Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein. Structure 17:417-426
    • (2009) Structure , vol.17 , pp. 417-426
    • Walsh, P.1    Simonetti, K.2    Sharpe, S.3
  • 148
    • 42649108674 scopus 로고    scopus 로고
    • Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein
    • Lee S, Mou Y, Lin S et al (2008) Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein. J Mol Biol 378:1142-1154
    • (2008) J Mol Biol , vol.378 , pp. 1142-1154
    • Lee, S.1    Mou, Y.2    Lin, S.3
  • 151
    • 77956941468 scopus 로고    scopus 로고
    • Crystallographic studies of PrP segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease
    • Apostol MI, Sawaya MR, Cascio D et al (2010) Crystallographic studies of PrP segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem 285:29671-29675
    • (2010) J Biol Chem , vol.285 , pp. 29671-29675
    • Apostol, M.I.1    Sawaya, M.R.2    Cascio, D.3
  • 152
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • DOI 10.1126/science.1138718
    • Collinge J, Clarke AR (2007) A general model of prion strains and their pathogenicity. Science 318:930-936 (Pubitemid 350098981)
    • (2007) Science , vol.318 , Issue.5852 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 153
    • 78651240044 scopus 로고    scopus 로고
    • Molecular biology and pathology of prion strains in sporadic human prion diseases
    • Gambetti P, Cali I, Notari S et al (2011) Molecular biology and pathology of prion strains in sporadic human prion diseases. Acta Neuropathol 121:79-90
    • (2011) Acta Neuropathol , vol.121 , pp. 79-90
    • Gambetti, P.1    Cali, I.2    Notari, S.3
  • 154
    • 76749109480 scopus 로고    scopus 로고
    • Darwinian evolution of prions in cell culture
    • Li J, Browning S, Mahal SP et al (2010) Darwinian evolution of prions in cell culture. Science 327:869-872
    • (2010) Science , vol.327 , pp. 869-872
    • Li, J.1    Browning, S.2    Mahal, S.P.3
  • 155
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen RA, Marsh RF (1992) Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66:2096-2101
    • (1992) J Virol , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 156
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen RA, Marsh RF (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68:7859-7868 (Pubitemid 24362673)
    • (1994) Journal of Virology , vol.68 , Issue.12 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 157
    • 0033610870 scopus 로고    scopus 로고
    • Strain-dependent differences in β-sheet conformations of abnormal prion protein
    • DOI 10.1074/jbc.273.48.32230
    • Caughey B, Raymond GJ, Bessen RA (1998) Strain-dependent differences in beta-sheet conformations of abnormal prion protein. J Biol Chem 273:32230-32235 (Pubitemid 29177169)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.48 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 159
    • 70349937836 scopus 로고    scopus 로고
    • Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: Its effect on the phenotype and prion-type characteristics
    • Cali I, Castellani R, Alshekhlee A et al (2009) Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics. Brain 132:2643-2658
    • (2009) Brain , vol.132 , pp. 2643-2658
    • Cali, I.1    Castellani, R.2    Alshekhlee, A.3
  • 160
    • 3042665537 scopus 로고    scopus 로고
    • Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study
    • DOI 10.1110/ps.03607204
    • Dzwolak W, Smirnovas V, Jansen R et al (2004) Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study. Protein Sci 13:1927-1932 (Pubitemid 38822132)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1927-1932
    • Dzwolak, W.1    Smirnovas, V.2    Jansen, R.3    Winter, R.4
  • 161
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • DOI 10.1126/science.1105850
    • Petkova AT, Leapman RD, Guo Z et al (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307:262-265 (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , 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
  • 162
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • DOI 10.1038/nature03679
    • Krishnan R, Lindquist SL (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435:765-772 (Pubitemid 40839721)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 163
    • 34548615995 scopus 로고    scopus 로고
    • The structural basis of yeast prion strain variants
    • DOI 10.1038/nature06108, PII NATURE06108
    • Toyama BH, Kelly MJS, Gross JD et al (2007) The structural basis of yeast prion strain variants. Nature 449:233-237 (Pubitemid 47402368)
    • (2007) Nature , vol.449 , Issue.7159 , pp. 233-237
    • Toyama, B.H.1    Kelly, M.J.S.2    Gross, J.D.3    Weissman, J.S.4
  • 164
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • DOI 10.1021/bi051952q
    • Petkova AT, Yau W, Tycko R (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 45:498-512 (Pubitemid 43100415)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 498-512
    • Petkova, A.T.1    Yau, W.-M.2    Tycko, R.3
  • 165
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structure of the prion protein yields two distinct self-propagating states
    • Makarava N, Baskakov IV (2008) The same primary structure of the prion protein yields two distinct self-propagating states. J Biol Chem 283:15988-15996
    • (2008) J Biol Chem , vol.283 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 166
    • 77954382827 scopus 로고    scopus 로고
    • Two amyloid states of the prion protein display significantly different folding patterns
    • Ostapchenko VG, Sawaya MR, Makarava N et al (2010) Two amyloid states of the prion protein display significantly different folding patterns. J Mol Biol 400:908-921
    • (2010) J Mol Biol , vol.400 , pp. 908-921
    • Ostapchenko, V.G.1    Sawaya, M.R.2    Makarava, N.3
  • 167
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • DOI 10.1016/S1097-2765(04)00155-8, PII S1097276504001558
    • Vanik DL, Surewicz KA, Surewicz WK (2004) Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol Cell 14:139-145 (Pubitemid 38469916)
    • (2004) Molecular Cell , vol.14 , Issue.1 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3
  • 168
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species-and straindependent seeding specificity of mammalian prion amyloids
    • Jones EM, Surewicz WK (2005) Fibril conformation as the basis of species-and straindependent seeding specificity of mammalian prion amyloids. Cell 121:63-72
    • (2005) Cell , vol.121 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2
  • 169
    • 0033600407 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease
    • DOI 10.1016/S0140-6736(99)05128-4
    • Collinge J (1999) Variant Creutzfeldt-Jakob disease. Lancet 354:317-323 (Pubitemid 29348751)
    • (1999) Lancet , vol.354 , Issue.9175 , pp. 317-323
    • Collinge, J.1
  • 170
    • 0023205075 scopus 로고
    • Biological evidence that scrapie agent has an independent genome
    • Bruce ME, Dickinson AG (1987) Biological evidence that scrapie agent has an independent genome. J Gen Virol 68(Pt 1):79-89 (Pubitemid 17207190)
    • (1987) Journal of General Virology , vol.68 , Issue.1 , pp. 79-89
    • Bruce, M.E.1    Dickinson, A.G.2
  • 172
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: The kiss of death?
    • DOI 10.1016/S0968-0004(01)01792-3, PII S0968000401017923
    • Caughey B (2001) Interactions between prion protein isoforms: the kiss of death? Trends Biochem Sci 26:235-242 (Pubitemid 32289242)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.4 , pp. 235-242
    • Caughey, B.1
  • 173
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • Hill AF, Antoniou M, Collinge J (1999) Protease-resistant prion protein produced in vitro lacks detectable infectivity. J Gen Virol 80(Pt 1):11-14 (Pubitemid 29041673)
    • (1999) Journal of General Virology , vol.80 , Issue.1 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge, J.3
  • 174
    • 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
  • 175
    • 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 et al (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
  • 176
    • 53549095695 scopus 로고    scopus 로고
    • Cell-free propagation of prion strains
    • Castilla J, Morales R, Saá P et al (2008) Cell-free propagation of prion strains. EMBO J 27:2557-2566
    • (2008) EMBO J , vol.27 , pp. 2557-2566
    • Castilla, J.1    Morales, R.2    Saá, P.3
  • 177
    • 67249123069 scopus 로고    scopus 로고
    • De novo generation of infectious prions in vitro produces a new disease phenotype
    • Barria MA, Mukherjee A, Gonzalez-Romero D et al (2009) De novo generation of infectious prions in vitro produces a new disease phenotype. PLoS Pathog 5:e1000421
    • (2009) PLoS Pathog , vol.5
    • Barria, M.A.1    Mukherjee, A.2    Gonzalez-Romero, D.3
  • 181
    • 73949160065 scopus 로고    scopus 로고
    • Design and construction of diverse mammalian prion strains
    • Colby DW, Giles K, Legname G et al (2009) Design and construction of diverse mammalian prion strains. Proc Natl Acad Sci USA 106:20417-20422
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20417-20422
    • Colby, D.W.1    Giles, K.2    Legname, G.3
  • 182
    • 22744435641 scopus 로고    scopus 로고
    • Birth of a prion: Spontaneous generation revisited
    • DOI 10.1016/j.cell.2005.07.001, PII S0092867405006598
    • Weissmann C (2005) Birth of a prion: spontaneous generation revisited. Cell 122:165-168 (Pubitemid 41032981)
    • (2005) Cell , vol.122 , Issue.2 , pp. 165-168
    • Weissmann, C.1
  • 184
    • 71749087690 scopus 로고    scopus 로고
    • The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro
    • Kim J, Surewicz K, Gambetti P et al (2009) The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro. FEBS Lett 583:3671-3675
    • (2009) FEBS Lett , vol.583 , pp. 3671-3675
    • Kim, J.1    Surewicz, K.2    Gambetti, P.3
  • 185
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang X, Yuan C et al (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.3
  • 186
    • 77951979579 scopus 로고    scopus 로고
    • Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors
    • Kim J, Cali I, Surewicz K et al (2010) Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 285: 14083-14087
    • (2010) J Biol Chem , vol.285 , pp. 14083-14087
    • Kim, J.1    Cali, I.2    Surewicz, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.