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Bamborough P, Wille H, Telling GC, Yehiely F, Prusiner SB, Cohen FE. Prion protein structure and scrapie replication: theoretical, spectroscopic and genetic investigations. of special interest Cold Spring Harb Symp Quant Biol. 61:1996; A comprehensive review of many aspects of prion biology that also contains kinetic analysis of the two prion-propagation models (template-assistance and nucleated-polymerization). In addition, a striking sequence similarity between the putative H1 region and a repeat in a fibrous spider-silk protein is discussed.
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Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
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Stahl N, Baldwin MA, Teplow DB, Hood L, Gibson BW, Burlingame AL, Prusiner SB. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry. 32:1993;1991-2002.
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Oesch B, Westaway D, Walchli M, McKinley MP, Kent SBH, Aebersold R, Barry RA, Tempst P, Teplow DB, Hood LE, et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell. 40:1985;735-746.
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Huang Z, Gabriel J-M, Baldwin MA, Fletterick RJ, Prusiner SB, Cohen FE. Proposed three-dimensional structure for the cellular prion protein. Proc Natl Acad Sci USA. 91:1994;7139-7143.
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Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein: Implications for scrapie formation
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Kazmirski SL, Alonso DOV, Cohen FE, Prusiner SB, Daggett V. Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein: implications for scrapie formation. Chem Biol. 2:1995;305-315.
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Kazmirski, S.L.1
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Gasset M, Baldwin MA, Lloyd DH, Gabriel J-M, Holtzman DM, Cohen FE, Fletterick R, Prusiner SB. Predicted α-helical regions of the prion protein when synthesized as peptides form amyloid. Proc Natl Acad Sci USA. 89:1992;10940-10944.
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19
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20
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Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
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Prusiner SB, Scott M, Foster D, Pan K-M, Groth D, Mirenda C, Torchia M, Yang S-L, Serban D, Carlson GA, et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell. 63:1990;673-686.
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Nguyen J, Baldwin MA, Cohen FE, Prusiner SB. Prion protein peptides induce α-helix to β-sheet conformational transitions. Biochemistry. 34:1995;4186-4192.
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T.P. Kaumaya, Hodges R. Leiden: ESCOM
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23
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Heller J, Kolbert A, Larsen R, Ernst M, Bekker T, Baldwin MA, Prusiner SB, Pines A, Wemmer DE. Solid-state studies of the prion protein H1 fragment. Protein Sci. 5:1996;1655-1661.
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Zhang H, Kaneko K, Nguyen JT, Livshits TL, Baldwin MA, Cohen FE, James TL, Prusiner SB. Conformational transitions in peptides containing two putative α-helices of the prion protein. J Mol Biol. 250:1995;514-526.
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26
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Nguyen JT, Inouye H, Baldwin MA, Fletterick RJ, Cohen FE, Prusiner SB, Kirschner DA. X-ray diffraction of scrapie prion rods and PrP peptides. J Mol Biol. 252:1995;412-422.
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Kaneko K, Peretz D, Pan K-M, Blochberger TC, Wille H, Gabizon R, Griffith OH, Cohen FE, Baldwin MA, Prusiner SB. Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proc Natl Acad Sci USA. 92:1995;11160-11164.
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28
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of special interest. The NMR structure of a substantial PrP fragment that does not contain the putative H1 region is reported. Proteolytic degradation in the E. coli periplasm limited the possibility of studying N-terminal extensions of this fragment. This fragment folded reversibly and was stable.
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Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K. NMR structure of the mouse prion protein domain PrP(121-231). of special interest Nature. 382:1996;180-182 The NMR structure of a substantial PrP fragment that does not contain the putative H1 region is reported. Proteolytic degradation in the E. coli periplasm limited the possibility of studying N-terminal extensions of this fragment. This fragment folded reversibly and was stable.
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Pan K-M, Stahl N, Prusiner SB. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1:1992;1343-1352.
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34
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of special interest. This article provides strong evidence for a host-specific phenomenon in prion propagation and a convincing line of reasoning that this phenomenon is a prion-binding protein required for conversion to the scrapie isoform. As the conversion of PrP must involve substantial refolding, the hypothesis that this protein is a molecular chaperone (which may be required in the normal processing of cellular PrP) is favoured.
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Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, DeArmond SJ, Prusiner SB. Prion propagation in mice expressing human and chimaeric PrP transgenes implicates the interaction of cellular PrP with another protein. of special interest Cell. 83:1995;79-90 This article provides strong evidence for a host-specific phenomenon in prion propagation and a convincing line of reasoning that this phenomenon is a prion-binding protein required for conversion to the scrapie isoform. As the conversion of PrP must involve substantial refolding, the hypothesis that this protein is a molecular chaperone (which may be required in the normal processing of cellular PrP) is favoured.
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Turk EY, Teplow DB, Hood LE, Prusiner SB. Purification and properties of the cellular and scrapie hamster prion forms. Eur J Biochem. 176:1988;21-30.
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Nicholl D, Windl O, De Silva R, Sawcer S, Dempster M, Ironside JW, Estibeiro JP, Yuill GM, Lathe R, Will RG. Inherited Creutzfeldt - Jakob disease in a British family associated with a novel 144-base pair insertion of the prion protein gene. J Neurol Neurosurg Psychiatry. 58:1995;65-69.
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