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3. Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Wildegger G; Liemann S; Glockshuber R Nat Struct Biol; 1999 Jun; 6(6):550-3. PubMed ID: 10360358 [TBL] [Abstract][Full Text] [Related]
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10. The peculiar nature of unfolding of the human prion protein. Baskakov IV; Legname G; Gryczynski Z; Prusiner SB Protein Sci; 2004 Mar; 13(3):586-95. PubMed ID: 14767078 [TBL] [Abstract][Full Text] [Related]
11. Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion protein. Hornemann S; Glockshuber R J Mol Biol; 1996 Sep; 261(5):614-9. PubMed ID: 8800210 [TBL] [Abstract][Full Text] [Related]
12. Stability and conformational properties of doppel, a prion-like protein, and its single-disulphide mutant. Whyte SM; Sylvester ID; Martin SR; Gill AC; Wopfner F; Schätzl HM; Dodson GG; Bayley PM Biochem J; 2003 Jul; 373(Pt 2):485-94. PubMed ID: 12665426 [TBL] [Abstract][Full Text] [Related]
13. Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils. Nazabal A; Hornemann S; Aguzzi A; Zenobi R J Mass Spectrom; 2009 Jun; 44(6):965-77. PubMed ID: 19283723 [TBL] [Abstract][Full Text] [Related]
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16. Isolation of isoforms of mouse prion protein with PrP(SC)-like structural properties. Lu BY; Chang JY Biochemistry; 2001 Nov; 40(44):13390-6. PubMed ID: 11683649 [TBL] [Abstract][Full Text] [Related]
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18. Production, purification and oxidative folding of the mouse recombinant prion protein. Pavlícek A; Bednárová L; Holada K Folia Microbiol (Praha); 2007; 52(4):391-7. PubMed ID: 18062188 [TBL] [Abstract][Full Text] [Related]
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