ADNP - Donne,D.G.; Viles,J.H.; Groth,D.; Mehlhorn,I.; James,T.L.; Cohen,F.E.; Prusiner,S.B.; Wright,P.E.; Dyson,H.J. - 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 1997 Dec 9; 94(25): 13452-7
AUHL - Garnett,A.P.; Jones,C.E.; Viles,J.H. - A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat. - Dalton Transactions 2006 Jan 21(3): 509-18
AELD - Garnett,A.P.; Viles,J.H. - Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism. - The Journal of Biological Chemistry 2003 Feb 28; 278(9): 6795-802
ARQM - Jones,C.E.; Klewpatinond,M.; Abdelraheim,S.R.; Brown,D.R.; Viles,J.H. - Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: the unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations. - Journal of Molecular Biology 2005 Mar 11; 346(5): 1393-407
AQLB - Jones,C.E.; Abdelraheim,S.R.; Brown,D.R.; Viles,J.H. - Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein - The Journal of Biological Chemistry 2004 Jul 30; 279(31): 32018-27
AXCT - Klewpatinond,M.; Viles,J.H. - Fragment length influences affinity for Cu2+ and Ni2+ binding to His96 or His111 of the prion protein and spectroscopic evidence for a multiple histidine binding only at low pH - Biochemical Journal 2007 Jun 15; 404(3): 393-402
AWZL - Klewpatinond,M.; Viles,J.H. - Empirical rules for rationalising visible circular dichroism of Cu2+ and Ni2+ histidine complexes: applications to the prion protein. - FEBS Letters 2007 Apr 3; 581(7): 1430-4
AVXV - Nadal,R.C.; Abdelraheim,S.R.; Brazier,M.W.; Rigby,S.E.; Brown,D.R.; Viles,J.H. - Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals - Free Radical Biology and Medicine 2007 Jan 1; 42(1): 79-89
AVRF - O'Sullivan,D.B.; Jones,C.E.; Abdelraheim,S.R.; Thompsett,A.R.; Brazier,M.W.; Toms,H.; Brown,D.R.; Viles,J.H. - NMR characterization of the pH 4 beta-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility. - Biochemical Journal 2007 Jan 15; 401(2): 533-40
ATAC - Viles,J.H. - Copper and the prion protein - function and dysfunction - The Biochemist 2005 Aug; 27(4)
AMAQ - Viles,J.H.; Donne,D.; Kroon,G.; Prusiner,S.B.; Cohen,F.E.; Dyson,H.J.; Wright,P.E. - Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. - Biochemistry 2001 Mar 6; 40(9): 2743-53
AMAR - Viles,J.H.; Cohen,F.E.; Prusiner,S.B.; Goodin,D.B.; Wright,P.E.; Dyson,H.J. - Copper binding to the prion protein: structural implications of four identical cooperative binding sites. - Proceedings of the National Academy of Sciences of the United States of America 1999 Mar 2; 96(5): 2042-7