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Volumn 8, Issue 5, 2013, Pages

N-Terminal Helix-Cap in α-Helix 2 Modulates β-State Misfolding in Rabbit and Hamster Prion Proteins

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; PRION PROTEIN; SERINE;

EID: 84877609635     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0063047     Document Type: Article
Times cited : (17)

References (46)
  • 1
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: one century of evolving concepts
    • Aguzzi A, Polymenidou M, (2004) Mammalian prion biology: one century of evolving concepts. Cell 116: 313-327 Available: http://www.ncbi.nlm.nih.gov/pubmed/14744440.
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 2
    • 0017336439 scopus 로고
    • Characteristics of a short incubation model of scrapie in the golden hamster
    • Available:. Accessed 12 September 2012
    • Kimberlin RH, Walker C (1977) Characteristics of a short incubation model of scrapie in the golden hamster. The Journal of general virology 34: 295-304. Available: http://www.ncbi.nlm.nih.gov/pubmed/402439. Accessed 12 September 2012.
    • (1977) The Journal of general virology , vol.34 , pp. 295-304
    • Kimberlin, R.H.1    Walker, C.2
  • 3
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Available. Accessed 12 September 2012
    • Bessen RA, Marsh RF (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. Journal of virology 68: 7859-7868. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=237248&tool=pmcentrez&rendertype=abstract. Accessed 12 September 2012.
    • (1994) Journal of virology , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 4
    • 33645778583 scopus 로고    scopus 로고
    • Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles
    • Available. Accessed 11 January 2011
    • Nonno R, Di Bari MA, Cardone F, Vaccari G, Fazzi P, et al. (2006) Efficient transmission and characterization of Creutzfeldt-Jakob disease strains in bank voles. PLoS pathogens 2: e12. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1383487&tool=pmcentrez&rendertype=abstract. Accessed 11 January 2011.
    • (2006) PLoS pathogens , vol.2
    • Nonno, R.1    Di Bari, M.A.2    Cardone, F.3    Vaccari, G.4    Fazzi, P.5
  • 5
    • 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
    • Available:. Accessed 11 October 2010
    • Piening N, Nonno R, Di Bari M, Walter S, Windl O, et al. (2006) 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. The Journal of biological chemistry 281: 9373-9384. Available: http://www.ncbi.nlm.nih.gov/pubmed/16455657. Accessed 11 October 2010.
    • (2006) The Journal of biological chemistry , vol.281 , pp. 9373-9384
    • Piening, N.1    Nonno, R.2    Di Bari, M.3    Walter, S.4    Windl, O.5
  • 6
    • 0015803185 scopus 로고
    • Experimental subacute spongiform virus encephalopathies in primates and other laboratory animals
    • Available:. Accessed 12 September 2012
    • Gibbs CJ, Gajdusek DC (1973) Experimental subacute spongiform virus encephalopathies in primates and other laboratory animals. Science (New York, NY) 182: 67-68. Available: http://www.ncbi.nlm.nih.gov/pubmed/4199733. Accessed 12 September 2012.
    • (1973) Science (New York, NY) , vol.182 , pp. 67-68
    • Gibbs, C.J.1    Gajdusek, D.C.2
  • 7
    • 0031030396 scopus 로고    scopus 로고
    • Characterization of a prion protein (PrP) gene from rabbit; a species with apparent resistance to infection by prions
    • Available:. Accessed 23 May 2011
    • Loftus B, Rogers M (1997) Characterization of a prion protein (PrP) gene from rabbit; a species with apparent resistance to infection by prions. Gene 184: 215-219. Available: http://www.ncbi.nlm.nih.gov/pubmed/9031631. Accessed 23 May 2011.
    • (1997) Gene , vol.184 , pp. 215-219
    • Loftus, B.1    Rogers, M.2
  • 8
    • 81155138316 scopus 로고    scopus 로고
    • Studies of the transmissibility of the agent of bovine spongiform encephalopathy to the domestic chicken
    • Available
    • Moore J, Hawkins SA, Austin AR, Konold T, Green RB, et al. (2011) Studies of the transmissibility of the agent of bovine spongiform encephalopathy to the domestic chicken. BMC research notes 4: 501. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3341577&tool=pmcentrez&rendertype=abstract. Accessed 12 September 2012.
    • (2011) BMC research notes , vol.4 , pp. 501
    • Moore, J.1    Hawkins, S.A.2    Austin, A.R.3    Konold, T.4    Green, R.B.5
  • 9
    • 0025244011 scopus 로고
    • Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
    • Available:. Accessed 12 September 2012
    • Prusiner SB, Scott M, Foster D, Pan KM, Groth D, et al. (1990) Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63: 673-686. Available: http://www.ncbi.nlm.nih.gov/pubmed/1977523. Accessed 12 September 2012.
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.B.1    Scott, M.2    Foster, D.3    Pan, K.M.4    Groth, D.5
  • 10
    • 0028364192 scopus 로고
    • Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells
    • Available
    • Priola SA, Caughey B, Race RE, Chesebro B (1994) Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cells. Journal of virology 68: 4873-4878. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=236427&tool=pmcentrez&rendertype=abstract. Accessed 12 September 2012.
    • (1994) Journal of virology , vol.68 , pp. 4873-4878
    • Priola, S.A.1    Caughey, B.2    Race, R.E.3    Chesebro, B.4
  • 11
    • 0037301367 scopus 로고    scopus 로고
    • Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
    • Available
    • Vorberg I, Groschup MH, Pfaff E, Priola SA (2003) Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. Journal of virology 77: 2003-2009. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=140934&tool=pmcentrez&rendertype=abstract. Accessed 23 May 2011.
    • (2003) Journal of virology , vol.77 , pp. 2003-2009
    • Vorberg, I.1    Groschup, M.H.2    Pfaff, E.3    Priola, S.A.4
  • 12
    • 0029937271 scopus 로고    scopus 로고
    • NMR structure of the mouse prion protein domain PrP(121-321)
    • Available:. Accessed 23 May 2011
    • Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, et al. (1996) NMR structure of the mouse prion protein domain PrP(121-321). Nature 382: 180-182. Available: http://www.ncbi.nlm.nih.gov/pubmed/8700211. Accessed 23 May 2011.
    • (1996) Nature , vol.382 , pp. 180-182
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Billeter, M.4    Glockshuber, R.5
  • 13
    • 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, Mehlhorn I, James TL, et al. (1997) Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proceedings of the National Academy of Sciences of the United States of America 94: 13452-13457 Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=28326&tool=pmcentrez&rendertype=abstract.
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 13452-13457
    • Donne, D.G.1    Viles, J.H.2    Groth, D.3    Mehlhorn, I.4    James, T.L.5
  • 18
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Available
    • Kaneko K, Zulianello L, Scott M, Cooper CM, Wallace AC, et al. (1997) Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proceedings of the National Academy of Sciences of the United States of America 94: 10069-10074. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=23307&tool=pmcentrez&rendertype=abstract. Accessed 8 June 2011.
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 10069-10074
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3    Cooper, C.M.4    Wallace, A.C.5
  • 20
    • 0030781922 scopus 로고    scopus 로고
    • pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231)
    • Available:. Accessed 25 May 2011
    • Swietnicki W, Petersen R, Gambetti P, Surewicz WK (1997) pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). The Journal of biological chemistry 272: 27517-27520. Available: http://www.ncbi.nlm.nih.gov/pubmed/9346881. Accessed 25 May 2011.
    • (1997) The Journal of biological chemistry , vol.272 , pp. 27517-27520
    • Swietnicki, W.1    Petersen, R.2    Gambetti, P.3    Surewicz, W.K.4
  • 21
    • 0032568592 scopus 로고    scopus 로고
    • A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH
    • Available
    • Hornemann S, Glockshuber R (1998) A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proceedings of the National Academy of Sciences of the United States of America 95: 6010-6014. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=27576&tool=pmcentrez&rendertype=abstract. Accessed 25 May 2011.
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , pp. 6010-6014
    • Hornemann, S.1    Glockshuber, R.2
  • 22
    • 0033583190 scopus 로고    scopus 로고
    • Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
    • Available:. Accessed 25 May 2011
    • Jackson GS, Hosszu LL, Power A, Hill AF, Kenney J, et al. (1999) Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science (New York, NY) 283: 1935-1937. Available: http://www.ncbi.nlm.nih.gov/pubmed/10082469. Accessed 25 May 2011.
    • (1999) Science (New York, NY) , vol.283 , pp. 1935-1937
    • Jackson, G.S.1    Hosszu, L.L.2    Power, A.3    Hill, A.F.4    Kenney, J.5
  • 23
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • Available:. Accessed 1 July 2010
    • Baskakov IV, Legname G, Prusiner SB, Cohen FE (2001) Folding of prion protein to its native alpha-helical conformation is under kinetic control. The Journal of biological chemistry 276: 19687-19690. Available: http://www.ncbi.nlm.nih.gov/pubmed/11306559. Accessed 1 July 2010.
    • (2001) The Journal of biological chemistry , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 24
    • 0037077234 scopus 로고    scopus 로고
    • Pathway complexity of prion protein assembly into amyloid
    • Available:. Accessed 29 April 2011
    • Baskakov IV, Legname G, Baldwin MA, Prusiner SB, Cohen FE (2002) Pathway complexity of prion protein assembly into amyloid. The Journal of biological chemistry 277: 21140-21148. Available: http://www.ncbi.nlm.nih.gov/pubmed/11912192. Accessed 29 April 2011.
    • (2002) The Journal of biological chemistry , vol.277 , pp. 21140-21148
    • Baskakov, I.V.1    Legname, G.2    Baldwin, M.A.3    Prusiner, S.B.4    Cohen, F.E.5
  • 25
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Available:. Accessed 13 July 2010
    • Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV (2006) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. The Journal of biological chemistry 281: 13828-13836. Available: http://www.ncbi.nlm.nih.gov/pubmed/16554307. Accessed 13 July 2010.
    • (2006) The Journal of biological chemistry , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 27
    • 78650575242 scopus 로고    scopus 로고
    • Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP
    • Available
    • Khan MQ, Sweeting B, Mulligan VK, Arslan PE, Cashman NR, et al. (2010) Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 107: 19808-19813. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2993331&tool=pmcentrez&rendertype=abstract. Accessed 23 March 2011.
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , pp. 19808-19813
    • Khan, M.Q.1    Sweeting, B.2    Mulligan, V.K.3    Arslan, P.E.4    Cashman, N.R.5
  • 28
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding
    • Available:. Accessed 23 May 2011
    • Zahn R, Von Schroetter C, Wüthrich K (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS letters 417: 400-404. Available: http://www.ncbi.nlm.nih.gov/pubmed/9409760. Accessed 23 May 2011.
    • (1997) FEBS letters , vol.417 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wüthrich, K.3
  • 29
    • 76449099287 scopus 로고    scopus 로고
    • XDS
    • Available
    • Kabsch W (2010) XDS. Acta crystallographica Section D, Biological crystallography 66: 125-132. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2815665&tool=pmcentrez&rendertype=abstract. Accessed 12 July 2012.
    • (2010) Acta crystallographica Section D, Biological crystallography , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 32
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • Available
    • Adams PD, Afonine P V, Bunkóczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta crystallographica Section D, Biological crystallography 66: 213-221. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2815670&tool=pmcentrez&rendertype=abstract. Accessed 13 July 2012.
    • (2010) Acta crystallographica Section D, Biological crystallography , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkóczi, G.3    Chen, V.B.4    Davis, I.W.5
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Available:. Accessed 18 July 2012
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta crystallographica Section D, Biological crystallography 60: 2126-2132. Available: http://www.ncbi.nlm.nih.gov/pubmed/15572765. Accessed 18 July 2012.
    • (2004) Acta crystallographica Section D, Biological crystallography , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 34
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Available:. Accessed 12 September 2012
    • Presta LG, Rose GD (1988) Helix signals in proteins. Science (New York, NY) 240: 1632-1641. Available: http://www.ncbi.nlm.nih.gov/pubmed/2837824. Accessed 12 September 2012.
    • (1988) Science (New York, NY) , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 35
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Available:. Accessed 23 July 2012
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. Journal of molecular biology 372: 774-797. Available: http://www.ncbi.nlm.nih.gov/pubmed/17681537. Accessed 23 July 2012.
    • (2007) Journal of molecular biology , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 36
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Available:. Accessed 15 October 2010
    • Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS letters 413: 282-288. Available: http://www.ncbi.nlm.nih.gov/pubmed/9280298. Accessed 15 October 2010.
    • (1997) FEBS letters , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüthrich, K.5
  • 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
    • Available:. Accessed 28 June 2010
    • Christen B, Pérez DR, Hornemann S, Wüthrich K (2008) NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171. Journal of molecular biology 383: 306-312. Available: http://www.ncbi.nlm.nih.gov/pubmed/18773909. Accessed 28 June 2010.
    • (2008) Journal of molecular biology , vol.383 , pp. 306-312
    • Christen, B.1    Pérez, D.R.2    Hornemann, S.3    Wüthrich, K.4
  • 38
    • 77957793037 scopus 로고    scopus 로고
    • Unique structural characteristics of the rabbit prion protein
    • Available
    • Wen Y, Li J, Yao W, Xiong M, Hong J, et al. (2010) Unique structural characteristics of the rabbit prion protein. The Journal of biological chemistry 285: 31682-31693. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2951240&tool=pmcentrez&rendertype=abstract. Accessed 18 February 2011.
    • (2010) The Journal of biological chemistry , vol.285 , pp. 31682-31693
    • Wen, Y.1    Li, J.2    Yao, W.3    Xiong, M.4    Hong, J.5
  • 39
    • 77953315370 scopus 로고    scopus 로고
    • Residues surrounding the glycosylphosphatidylinositol anchor attachment site of PrP modulate prion infection: insight from the resistance of rabbits to prion disease
    • Available
    • Nisbet RM, Harrison CF, Lawson VA, Masters CL, Cappai R, et al. (2010) Residues surrounding the glycosylphosphatidylinositol anchor attachment site of PrP modulate prion infection: insight from the resistance of rabbits to prion disease. Journal of virology 84: 6678-6686. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2903296&tool=pmcentrez&rendertype=abstract. Accessed 5 February 2013.
    • (2010) Journal of virology , vol.84 , pp. 6678-6686
    • Nisbet, R.M.1    Harrison, C.F.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5
  • 40
    • 77958611177 scopus 로고    scopus 로고
    • Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins
    • Available:. Accessed 5 February 2013
    • Zhang J (2011) Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins. Journal of theoretical biology 269: 88-95. Available: http://www.ncbi.nlm.nih.gov/pubmed/20970434. Accessed 5 February 2013.
    • (2011) Journal of theoretical biology , vol.269 , pp. 88-95
    • Zhang, J.1
  • 41
    • 77649237972 scopus 로고    scopus 로고
    • Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants
    • Available:. Accessed 5 February 2013
    • Zhang J (2010) Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants. Journal of theoretical biology 264: 119-122. Available: http://www.ncbi.nlm.nih.gov/pubmed/20109469. Accessed 5 February 2013.
    • (2010) Journal of theoretical biology , vol.264 , pp. 119-122
    • Zhang, J.1
  • 42
    • 70349454224 scopus 로고    scopus 로고
    • Differential stability of the bovine prion protein upon urea unfolding
    • Available
    • Julien O, Chatterjee S, Thiessen A, Graether SP, Sykes BD (2009) Differential stability of the bovine prion protein upon urea unfolding. Protein science: a publication of the Protein Society 18: 2172-2182. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2786980&tool=pmcentrez&rendertype=abstract. Accessed 30 June 2010.
    • (2009) Protein science: A publication of the Protein Society , vol.18 , pp. 2172-2182
    • Julien, O.1    Chatterjee, S.2    Thiessen, A.3    Graether, S.P.4    Sykes, B.D.5
  • 43
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Available
    • Wang F, Wang X, Yuan C-G, Ma J (2010) Generating a prion with bacterially expressed recombinant prion protein. Science (New York, NY) 327: 1132-1135. Available: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2893558&tool=pmcentrez&rendertype=abstract. Accessed 22 July 2012.
    • (2010) Science (New York, NY) , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.-G.3    Ma, J.4
  • 44
    • 84869015437 scopus 로고    scopus 로고
    • Isolation of novel synthetic prion strains by amplification in transgenic mice co-expressing wild-type and anchorless prion proteins
    • Available:. Accessed 12 September 2012
    • Raymond GJ, Race B, Hollister JR, Offerdahl DK, Moore RA, et al. (2012) Isolation of novel synthetic prion strains by amplification in transgenic mice co-expressing wild-type and anchorless prion proteins. Journal of virology. Available: http://www.ncbi.nlm.nih.gov/pubmed/22915801. Accessed 12 September 2012.
    • (2012) Journal of virology
    • Raymond, G.J.1    Race, B.2    Hollister, J.R.3    Offerdahl, D.K.4    Moore, R.A.5
  • 45
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Available:. Accessed 23 February 2011
    • Sandberg MK, Al-Doujaily H, Sharps B, Clarke AR, Collinge J (2011) Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 470: 540-542. Available: http://www.ncbi.nlm.nih.gov/pubmed/21350487. Accessed 23 February 2011.
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1    Al-Doujaily, H.2    Sharps, B.3    Clarke, A.R.4    Collinge, J.5


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