Structure of the recombinant full-length Syrian hamster prion protein PrP(29-231): the N-terminus is highly flexible. D.G. Donne, J.H. Viles, J. Chung, D. Groth, I. Mehlhorn, F.E. Cohen, S.B. Prusiner, P.E. Wright & H.J. Dyson (1997) Proc. Natl. Acad. Sci. USA 94, 13452-13457.
Copper binding to the prion protein. Structural implications of four identical cooperative binding sites. J.H. Viles, S.B. Prusiner, F.E. Cohen, D.D. Goodin, P.E. Wright and H.J. Dyson (1999) Proc. Natl Acad. Sci. USA 96, 2042-2047.
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. J.H. Viles, D. Donne, G.J.A. Kroon, S.B. Prusiner, F.E. Cohen, H.J. Dyson and P.E. Wright (2001) Biochemistry 40, 2743-2753.
Two different neurodegenerative diseases caused by proteins with similar structures. H. Mo, R.C. Moore, F.E. Cohen, D. Westaway, S.B. Prusiner, P.E. Wright and H.J. Dyson (2001) Proc. Natl. Acad. Sci. USA 98, 2352-2357.
NMR solution structure of the peptide fragment 1-30, derived from mouse Doppel protein, in DHPC micelles. E. Papadopoulos, K. Oglęcka, L. Mäler, J. Jarvet, P.E. Wright, H.J. Dyson, A. Gräslund (2006). Biochemistry 45, 159-166.
Prion proteins with pathogenic and protective mutations show similar structure and dynamics. S.-H. Bae, G. Legname, A. Serban, S.B. Prusiner, P.E. Wright and H.J. Dyson (2009) Biochemistry 48, 8120-8128.