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Volumn 4, Issue 4, 2010, Pages 235-243

Structural requirements for efficient prion protein conversion: Cofactors may promote a conversion-competent structure for PrPC

Author keywords

Cell free conversion assay; Cofactor; Fibrillization; Loop region; Stability; Structure

Indexed keywords

PRION PROTEIN;

EID: 78650196956     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.4.4.13394     Document Type: Note
Times cited : (13)

References (75)
  • 1
    • 68849112731 scopus 로고    scopus 로고
    • Thoughts on mammalian prion strains
    • Weissmann C. Thoughts on mammalian prion strains. Folia Neuropathol 2009; 47:5-8.
    • (2009) Folia Neuropathol , vol.47 , pp. 5-8
    • Weissmann, C.1
  • 2
    • 33750576527 scopus 로고    scopus 로고
    • Prions: Protein only or something more? Overview of potential prion cofactors
    • DOI 10.1385/JMN:29:3:195, PII JMN293195
    • Fasano C, Campana V, Zurzolo C. Prions: protein only or something more? Overview of potential prion cofactors. J Mol Neurosci 2006; 29:195-214. (Pubitemid 44684495)
    • (2006) Journal of Molecular Neuroscience , vol.29 , Issue.3 , pp. 195-214
    • Fasano, C.1    Campana, V.2    Zurzolo, C.3
  • 4
    • 77952956256 scopus 로고    scopus 로고
    • Cellular factors implicated in prion replication
    • Abid K, Morales R, Soto C. Cellular factors implicated in prion replication. Febs Lett 2010; 584:2409-14.
    • (2010) Febs Lett , vol.584 , pp. 2409-2414
    • Abid, K.1    Morales, R.2    Soto, C.3
  • 8
    • 77951979579 scopus 로고    scopus 로고
    • Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors
    • Kim JI, Cali I, Surewicz K, Kong Q, Raymond GJ, Atarashi R, et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 2010; 285:14083-7.
    • (2010) J Biol Chem , vol.285 , pp. 14083-14087
    • Kim, J.I.1    Cali, I.2    Surewicz, K.3    Kong, Q.4    Raymond, G.J.5    Atarashi, R.6
  • 9
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • DOI 10.1074/jbc.M503973200
    • Deleault NR, Geoghegan JC, Nishina K, Kascsak R, Williamson RA, Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J Biol Chem 2005; 280:26873-9. (Pubitemid 41040721)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 11
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault NR, Lucassen RW, Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003; 425:717-20.
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 12
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang F, Wang XH, Yuan CG, Ma JY. Generating a prion with bacterially expressed recombinant prion protein. Science 2010; 327:1132-5.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.H.2    Yuan, C.G.3    Ma, J.Y.4
  • 13
    • 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. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001; 411:810-3. (Pubitemid 32588105)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 14
    • 9944257937 scopus 로고    scopus 로고
    • Breakage of PrP aggregates is essential for efficient autocatalytic propagation of misfolded prion protein
    • Piening N, Weber P, Giese A, Kretzschmar H. Breakage of PrP aggregates is essential for efficient autocatalytic propagation of misfolded prion protein. Biochem Bioph Res Co 2005; 326:339-43.
    • (2005) Biochem Bioph Res Co , vol.326 , pp. 339-343
    • Piening, N.1    Weber, P.2    Giese, A.3    Kretzschmar, H.4
  • 15
    • 25444512708 scopus 로고    scopus 로고
    • Ultrasonication-induced amyloid fibril formation of beta(2)-microglobulin
    • Ohhashi Y, Kihara M, Naiki H, Goto Y. Ultrasonication-induced amyloid fibril formation of beta(2)-microglobulin. J Biol Chem 2005; 280:32843-8.
    • (2005) J Biol Chem , vol.280 , pp. 32843-32848
    • Ohhashi, Y.1    Kihara, M.2    Naiki, H.3    Goto, Y.4
  • 19
    • 0037385673 scopus 로고    scopus 로고
    • In vitro cell-free conversion of bacterial recombinant PrP to Prp(res) as a model for conversion
    • Kirby L, Birkett CR, Rudyk H, Gilbert IH, Hope J. In vitro cell-free conversion of bacterial recombinant PrP to Prp(res) as a model for conversion. J Gen Virol 2003; 84:1013-20.
    • (2003) J Gen Virol , vol.84 , pp. 1013-1020
    • Kirby, L.1    Birkett, C.R.2    Rudyk, H.3    Gilbert, I.H.4    Hope, J.5
  • 20
  • 21
    • 77449100647 scopus 로고    scopus 로고
    • Inverse correlation of thermal lability and conversion efficiency for five prion protein polymorphic variants
    • Kirby L, Agarwal S, Graham JF, Goldmann W, Gill AC. Inverse correlation of thermal lability and conversion efficiency for five prion protein polymorphic variants. Biochemistry-US 2010; 49:1448-59.
    • (2010) Biochemistry-US , vol.49 , pp. 1448-1459
    • Kirby, L.1    Agarwal, S.2    Graham, J.F.3    Goldmann, W.4    Gill, A.C.5
  • 22
    • 0035796463 scopus 로고    scopus 로고
    • Scrapie strains maintain biological phenotypes on propagation in a cell line in culture
    • Birkett CR, Hennion RM, Bembridge DA, Clarke MC, Chree A, Bruce ME, et al. Scrapie strains maintain biological phenotypes on propagation in a cell line in culture. EMBO J 2001; 20:3351-8.
    • (2001) EMBO J , vol.20 , pp. 3351-3358
    • Birkett, C.R.1    Hennion, R.M.2    Bembridge, D.A.3    Clarke, M.C.4    Chree, A.5    Bruce, M.E.6
  • 23
    • 84934442254 scopus 로고    scopus 로고
    • Methods for conversion of prion protein into amyloid fibrils
    • Breydo L, Makarava N, Baskakov IV. Methods for conversion of prion protein into amyloid fibrils. Methods Mol Biol 2008; 459:105-15.
    • (2008) Methods Mol Biol , vol.459 , pp. 105-115
    • Breydo, L.1    Makarava, N.2    Baskakov, I.V.3
  • 24
    • 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
  • 25
    • 0032479890 scopus 로고    scopus 로고
    • The importance of the disulfide bond in prion protein conversion
    • Herrmann LM, Caughey B. The importance of the disulfide bond in prion protein conversion. Neuroreport 1998; 9:2457-61. (Pubitemid 28387130)
    • (1998) NeuroReport , vol.9 , Issue.11 , pp. 2457-2461
    • Herrmann, L.M.1    Caughey, B.2
  • 28
    • 50049084036 scopus 로고    scopus 로고
    • PrP genetics in ruminant transmissible spongiform encephalopathies
    • Goldmann W. PrP genetics in ruminant transmissible spongiform encephalopathies. Vet Res 2008; 39.
    • (2008) Vet Res , vol.39
    • Goldmann, W.1
  • 29
    • 33751412846 scopus 로고    scopus 로고
    • Ovine prion protein variant A(136) R(154)L(168)Q(171) increases resistance to experimental challenge with bovine spongiform encephalopathy agent
    • Goldmann W, Houston F, Stewart P, Perucchini M, Foster J, Hunter N. Ovine prion protein variant A(136) R(154)L(168)Q(171) increases resistance to experimental challenge with bovine spongiform encephalopathy agent. J Gen Virol 2006; 87:3741-5.
    • (2006) J Gen Virol , vol.87 , pp. 3741-3745
    • Goldmann, W.1    Houston, F.2    Stewart, P.3    Perucchini, M.4    Foster, J.5    Hunter, N.6
  • 31
    • 14744284214 scopus 로고    scopus 로고
    • Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities
    • Rezaei H, Eghiaian F, Perez J, Doublet B, Choiset Y, Haertle T, et al. Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities. J Mol Biol 2005; 347:665-79.
    • (2005) J Mol Biol , vol.347 , pp. 665-679
    • Rezaei, H.1    Eghiaian, F.2    Perez, J.3    Doublet, B.4    Choiset, Y.5    Haertle, T.6
  • 32
    • 70149110670 scopus 로고    scopus 로고
    • The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier
    • Robinson PJ, Pinheiro TJT. The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier. Biochemistry-US 2009; 48:8551-8.
    • (2009) Biochemistry-US , vol.48 , pp. 8551-8558
    • Robinson, P.J.1    Pinheiro, T.J.T.2
  • 33
    • 38749113941 scopus 로고    scopus 로고
    • The stability and aggregation of ovine prion protein associated with classical and atypical scrapie correlates with the ease of unwinding of helix-2
    • DOI 10.1042/BJ20071122
    • Fitzmaurice TJ, Burke DF, Hopkins L, Yang SJ, Yu SL, Sy MS, et al. The stability and aggregation of ovine prion protein associated with classical and atypical scrapie correlates with the ease of unwinding of helix-2. Biochem J 2008; 409:367-75. (Pubitemid 351184955)
    • (2008) Biochemical Journal , vol.409 , Issue.2 , pp. 367-375
    • Fitzmaurice, T.J.1    Burke, D.F.2    Hopkins, L.3    Yang, S.4    Yu, S.5    Sy, M.-S.6    Thackray, A.M.7    Bujdoso, R.8
  • 34
    • 28644432876 scopus 로고    scopus 로고
    • Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations
    • Bujdoso R, Burke DF, Thackray AM. Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations. Proteins 2005; 61:840-9.
    • (2005) Proteins , vol.61 , pp. 840-849
    • Bujdoso, R.1    Burke, D.F.2    Thackray, A.M.3
  • 37
    • 52949137870 scopus 로고    scopus 로고
    • NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171
    • Christen B, Perez DR, Hornemann S, Wuthrich K. NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171. J Mol Biol 2008; 383:306-12.
    • (2008) J Mol Biol , vol.383 , pp. 306-312
    • Christen, B.1    Perez, D.R.2    Hornemann, S.3    Wuthrich, K.4
  • 39
    • 33646931017 scopus 로고    scopus 로고
    • Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo
    • DOI 10.1074/jbc.M512239200
    • Piening N, Nonno R, Di Bari M, Walter S, Windl O, Agrimi U, et al. Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo. J Biol Chem 2006; 281:9373-84. (Pubitemid 43864654)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9373-9384
    • Piening, N.1    Nonno, R.2    Di Bari, M.3    Walter, S.4    Windl, O.5    Agrimi, U.6    Kretzschmar, H.A.7    Bertsch, U.8
  • 40
    • 48249132090 scopus 로고    scopus 로고
    • Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles
    • Agrimi U, Nonno R, Dell'Omo G, Di Bari MA, Conte M, Chiappini B, et al. Prion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and voles. PloS Patho 2008; 4:1000113.
    • (2008) PloS Patho , vol.4 , pp. 1000113
    • Agrimi, U.1    Nonno, R.2    Dell'Omo, G.3    Di Bari, M.A.4    Conte, M.5    Chiappini, B.6
  • 43
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko K, Zulianello L, Scott M, Cooper CM, Wallace AC, James TL, et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 1997; 94:10069-74.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3    Cooper, C.M.4    Wallace, A.C.5    James, T.L.6
  • 44
    • 13144275223 scopus 로고    scopus 로고
    • Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice
    • Scott MR, Safar J, Telling G, Nguyen O, Groth D, Torchia M, et al. Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc Natl Acad Sci USA 1997; 94:14279-84.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14279-14284
    • Scott, M.R.1    Safar, J.2    Telling, G.3    Nguyen, O.4    Groth, D.5    Torchia, M.6
  • 45
    • 77950608292 scopus 로고    scopus 로고
    • Electrostatics in the stability and misfolding of the prion protein: Salt bridges, self energy and solvation
    • Guest WC, Cashman NR, Plotkin SS. Electrostatics in the stability and misfolding of the prion protein: salt bridges, self energy and solvation. Biochem Cell Biol 2010; 88:371-81.
    • (2010) Biochem Cell Biol , vol.88 , pp. 371-381
    • Guest, W.C.1    Cashman, N.R.2    Plotkin, S.S.3
  • 46
    • 70049109405 scopus 로고    scopus 로고
    • Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor
    • Geoghegan JC, Miller MB, Kwak AH, Harris BT, Supattapone S. Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor. PLoS Pathog 2009; 5:1000535.
    • (2009) PLoS Pathog , vol.5 , pp. 1000535
    • Geoghegan, J.C.1    Miller, M.B.2    Kwak, A.H.3    Harris, B.T.4    Supattapone, S.5
  • 47
    • 70349195971 scopus 로고    scopus 로고
    • The consequences of pathogenic mutations to the human prion protein
    • van der Kamp MW, Daggett V. The consequences of pathogenic mutations to the human prion protein. Protein Eng Des Sel 2009; 22:461-8.
    • (2009) Protein Eng des Sel , vol.22 , pp. 461-468
    • Van Der Kamp, M.W.1    Daggett, V.2
  • 48
    • 33847281383 scopus 로고    scopus 로고
    • Epidemiological and genetical differences between classical and atypical scrapie cases
    • Luhken G, Buschmann A, Brandt H, Eiden M, Groschup MH, Erhardt G. Epidemiological and genetical differences between classical and atypical scrapie cases. Vet Res 2007; 38:65-80.
    • (2007) Vet Res , vol.38 , pp. 65-80
    • Luhken, G.1    Buschmann, A.2    Brandt, H.3    Eiden, M.4    Groschup, M.H.5    Erhardt, G.6
  • 50
    • 45549098509 scopus 로고    scopus 로고
    • Atypical scrapie in a sheep in a closed UK flock with endemic classical natural scrapie
    • Foster J, Toovey L, McKenzie C, Chong A, Parnham D, Drummond D, et al. Atypical scrapie in a sheep in a closed UK flock with endemic classical natural scrapie. Vet Rec 2008; 162:723-4.
    • (2008) Vet Rec , vol.162 , pp. 723-724
    • Foster, J.1    Toovey, L.2    McKenzie, C.3    Chong, A.4    Parnham, D.5    Drummond, D.6
  • 51
    • 17744379376 scopus 로고    scopus 로고
    • Scfrom sporadic Creutzfeldt-Jakob disease
    • DOI 10.1110/ps.041186605
    • Bocharova OV, Breydo L, Salnikov VV, Gill AC, Baskakov IV. Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob disease. Protein Sci 2005; 14:1222-32. (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
  • 52
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • DOI 10.1073/pnas.011578098
    • Ma J, Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci USA 2001; 98:14955-60. (Pubitemid 34013951)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.26 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 54
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • DOI 10.1038/nm1297-1383
    • Rieger R, Edenhofer F, Lasmezas CI, Weiss S. The human 37 kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nature Med 1997; 3:1383-8. (Pubitemid 28011039)
    • (1997) Nature Medicine , vol.3 , Issue.12 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmezas, C.I.3    Weiss, S.4
  • 56
    • 73549083896 scopus 로고    scopus 로고
    • Glypican-1 mediates both prion protein lipid raft association and disease isoform formation
    • Taylor DR, Whitehouse IJ, Hooper NM. Glypican-1 mediates both prion protein lipid raft association and disease isoform formation. PLoS Pathog 2009; 5:e1000666.
    • (2009) PLoS Pathog , vol.5
    • Taylor, D.R.1    Whitehouse, I.J.2    Hooper, N.M.3
  • 58
    • 0035815107 scopus 로고    scopus 로고
    • The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein
    • Gabus C, Auxilien S, Pechoux C, Dormont D, Swietnicki W, Morillas M, et al. The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. J Mol Biol 2001; 307:1011-21.
    • (2001) J Mol Biol , vol.307 , pp. 1011-1021
    • Gabus, C.1    Auxilien, S.2    Pechoux, C.3    Dormont, D.4    Swietnicki, W.5    Morillas, M.6
  • 59
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera N, Pinheiro TJ. Binding of prion protein to lipid membranes and implications for prion conversion. J Mol Biol 2002; 315:1241-56.
    • (2002) J Mol Biol , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 62
    • 77956267613 scopus 로고    scopus 로고
    • Interactions of prion protein with intracellular proteins: So many partners and no consequences?
    • Nieznanski K. Interactions of prion protein with intracellular proteins: so many partners and no consequences? Cell Mol Neurobiol 2010; 30:653-66.
    • (2010) Cell Mol Neurobiol , vol.30 , pp. 653-666
    • Nieznanski, K.1
  • 63
    • 28244481850 scopus 로고    scopus 로고
    • The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of alpha-linked polyglucose
    • DOI 10.1515/BC.2005.131
    • Dumpitak C, Beekes M, Weinmann N, Metzger S, Winklhofer KF, Tatzelt J, et al. The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of alpha-linked polyglucose. Biol Chem 2005; 386:1149-55. (Pubitemid 41705369)
    • (2005) Biological Chemistry , vol.386 , Issue.11 , pp. 1149-1155
    • Dumpitak, C.1    Beekes, M.2    Weinmann, N.3    Metzger, S.4    Winklhofer, K.F.5    Tatzelt, J.6    Riesner, D.7
  • 64
    • 42649106136 scopus 로고    scopus 로고
    • Aggregation and amyloid fibril formation of the prion protein is accelerated in the presence of glycogen
    • Panza G, Stohr J, Birkmann E, Riesner D, Willbold D, Baba O, et al. Aggregation and amyloid fibril formation of the prion protein is accelerated in the presence of glycogen. Rejuvenation Res 2008; 11:365-9.
    • (2008) Rejuvenation Res , vol.11 , pp. 365-369
    • Panza, G.1    Stohr, J.2    Birkmann, E.3    Riesner, D.4    Willbold, D.5    Baba, O.6
  • 65
    • 68549096430 scopus 로고    scopus 로고
    • Proteomic profiling of PrP27-30-enriched preparations extracted from the brain of hamsters with experimental scrapie
    • Giorgi A, Di Francesco L, Principe S, Mignogna G, Sennels L, Mancone C, et al. Proteomic profiling of PrP27-30-enriched preparations extracted from the brain of hamsters with experimental scrapie. Proteomics 2009; 9:3802-14.
    • (2009) Proteomics , vol.9 , pp. 3802-3814
    • Giorgi, A.1    Di Francesco, L.2    Principe, S.3    Mignogna, G.4    Sennels, L.5    Mancone, C.6
  • 66
    • 63649115218 scopus 로고    scopus 로고
    • Identification of proteins co-purifying with scrapie infectivity
    • Petrakis S, Malinowska A, Dadlez M, Sklaviadis T. Identification of proteins co-purifying with scrapie infectivity. J Proteomics 2009; 72:690-4.
    • (2009) J Proteomics , vol.72 , pp. 690-694
    • Petrakis, S.1    Malinowska, A.2    Dadlez, M.3    Sklaviadis, T.4
  • 67
    • 77955117634 scopus 로고    scopus 로고
    • Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations
    • Moore RA, Timmes A, Wilmarth PA, Priola SA. Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations. Proteomics 2010; 10:2858-69.
    • (2010) Proteomics , vol.10 , pp. 2858-2869
    • Moore, R.A.1    Timmes, A.2    Wilmarth, P.A.3    Priola, S.A.4
  • 68
    • 77951923337 scopus 로고    scopus 로고
    • Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro
    • Deleault NR, Kascsak R, Geoghegan JC, Supattapone S. Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry-US 2010; 49:3928-34.
    • (2010) Biochemistry-US , vol.49 , pp. 3928-3934
    • Deleault, N.R.1    Kascsak, R.2    Geoghegan, J.C.3    Supattapone, S.4
  • 69
    • 0035253848 scopus 로고    scopus 로고
    • Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein
    • Wong C, Xiong LW, Horiuchi M, Raymond L, Wehrly K, Chesebro B, et al. Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. EMBO J 2001; 20:377-86.
    • (2001) EMBO J , vol.20 , pp. 377-386
    • Wong, C.1    Xiong, L.W.2    Horiuchi, M.3    Raymond, L.4    Wehrly, K.5    Chesebro, B.6
  • 70
    • 70349479050 scopus 로고    scopus 로고
    • Insight into early events in the aggregation of the prion protein on lipid membranes
    • Sanghera N, Swann MJ, Ronan G, Pinheiro TJ. Insight into early events in the aggregation of the prion protein on lipid membranes. Biochim Biophys Acta 2009; 1788:2245-51.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2245-2251
    • Sanghera, N.1    Swann, M.J.2    Ronan, G.3    Pinheiro, T.J.4
  • 72
    • 0042970474 scopus 로고    scopus 로고
    • Protein stabilisation by compatible solutes: Effect of mannosylglycerate on unfolding thermodynamics and activity of ribonuclease A
    • Faria TQ, Knapp S, Ladenstein R, Macanita AL, Santos H. Protein stabilisation by compatible solutes: effect of mannosylglycerate on unfolding thermodynamics and activity of ribonuclease A. Chembiochem 2003; 4:734-41.
    • (2003) Chembiochem , vol.4 , pp. 734-741
    • Faria, T.Q.1    Knapp, S.2    Ladenstein, R.3    Macanita, A.L.4    Santos, H.5
  • 75
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman SK, Raymond GJ, Caughey B, Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc Natl Acad Sci USA 1997; 94:13938-43.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13938-13943
    • DebBurman, S.K.1    Raymond, G.J.2    Caughey, B.3    Lindquist, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.