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Proceedings of the National Academy of Sciences of the United States of America|May 30, 1998
A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pHS Hornemann, R GlockshuberJournal of Molecular Biology|September 6, 1996
Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion proteinS Hornemann, R GlockshuberFEBS Letters|August 18, 1997
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)R Riek, S Hornemann, G Wider, et al.Nature|July 11, 1996
NMR structure of the mouse prion protein domain PrP(121-231)R Riek, S Hornemann, G Wider, et al.FEBS Letters|May 26, 1998
Prion protein structural features indicate possible relations to signal peptidasesR Glockshuber, S Hornemann, M Billeter, et al.Proceedings of the National Academy of Sciences of the United States of America|July 8, 1997
Prion protein NMR structure and species barrier for prion diseasesM Billeter, R Riek, G Wider, et al.Biopolymers|July 9, 1999
Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopyA Liu, R Riek, R Zahn, et al.Proceedings of the National Academy of Sciences of the United States of America|September 30, 1998
Prion protein NMR structure and familial human spongiform encephalopathiesR Riek, G Wider, M Billeter, et al.FEBS Letters|August 18, 1997
Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterizationS Hornemann, C Korth, B Oesch, et al.The Journal of Biological Chemistry|March 30, 2001
Prion protein binds copper within the physiological concentration rangeM L Kramer, H D Kratzin, B Schmidt, et al.Pageof 2