Structure of the recombinant full-length hamster prion protein PrP (29–231): the N terminus is highly flexible DG Donne, JH Viles, D Groth, I Mehlhorn, TL James, FE Cohen, ... Proceedings of the National Academy of Sciences 94 (25), 13452-13457, 1997 | 880 | 1997 |
Copper binding to the prion protein: structural implications of four identical cooperative binding sites JH Viles, FE Cohen, SB Prusiner, DB Goodin, PE Wright, HJ Dyson Proceedings of the National Academy of Sciences 96 (5), 2042-2047, 1999 | 716 | 1999 |
Amyloid β protein and Alzheimer’s disease: When computer simulations complement experimental studies J Nasica-Labouze, PH Nguyen, F Sterpone, O Berthoumieu, NV Buchete, ... Chemical reviews 115 (9), 3518-3563, 2015 | 633 | 2015 |
Copper binding to the amyloid-β (Aβ) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Aβ-(1–28 … CD Syme, RC Nadal, SEJ Rigby, JH Viles Journal of Biological Chemistry 279 (18), 18169-18177, 2004 | 565 | 2004 |
Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases JH Viles Coordination Chemistry Reviews 256 (19-20), 2271-2284, 2012 | 443 | 2012 |
Preferential Cu2+ coordination by His96 and His111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein CE Jones, SR Abdelraheim, DR Brown, JH Viles Journal of Biological Chemistry 279 (31), 32018-32027, 2004 | 293 | 2004 |
Involvement of a lysine residue in the N‐terminal Ni2+ and Cu2+ binding site of serum albumins: Comparison with Co2+, Cd2+ and Al3+ PJ Sadler, A Tucker, JH Viles European Journal of Biochemistry 220 (1), 193-200, 1994 | 293 | 1994 |
Copper (II) binding to amyloid-β fibrils of Alzheimer’s disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Aβ oligomeric form CJ Sarell, CD Syme, SEJ Rigby, JH Viles Biochemistry 48 (20), 4388-4402, 2009 | 251 | 2009 |
Copper binding to the octarepeats of the prion protein: affinity, specificity, folding, and cooperativity: insights from circular dichroism AP Garnett, JH Viles Journal of Biological Chemistry 278 (9), 6795-6802, 2003 | 249 | 2003 |
Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease CJ Sarell, SR Wilkinson, JH Viles Journal of biological chemistry 285 (53), 41533-41540, 2010 | 227 | 2010 |
Ion channel formation by amyloid-β42 oligomers but not amyloid-β40 in cellular membranes DC Bode, MD Baker, JH Viles Journal of Biological Chemistry 292 (4), 1404-1413, 2017 | 226 | 2017 |
Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease CD Syme, JH Viles Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1764 (2), 246-256, 2006 | 217 | 2006 |
1H and 113Cd NMR investigations of Cd2+ and Zn2+ binding sites on serum albumin: competition with Ca2+, Ni2+, Cu2+, and Zn2+ PJ Sadler, JH Viles Inorganic Chemistry 35 (15), 4490-4496, 1996 | 214 | 1996 |
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics JH Viles, D Donne, G Kroon, SB Prusiner, FE Cohen, HJ Dyson, ... Biochemistry 40 (9), 2743-2753, 2001 | 210 | 2001 |
A comparison of three fluorophores for the detection of amyloid fibers and prefibrillar oligomeric assemblies. ThT (thioflavin T); ANS (1-anilinonaphthalene-8-sulfonic acid … ND Younan, JH Viles Biochemistry 54 (28), 4297-4306, 2015 | 195 | 2015 |
Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease HF Stanyon, JH Viles Journal of Biological Chemistry 287 (33), 28163-28168, 2012 | 187 | 2012 |
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 … CE Jones, M Klewpatinond, SR Abdelraheim, DR Brown, JH Viles Journal of Molecular Biology 346 (5), 1393-1407, 2005 | 181 | 2005 |
Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy DC Bode, M Freeley, J Nield, M Palma, JH Viles Journal of biological chemistry 294 (19), 7566-7572, 2019 | 145 | 2019 |
Amyloid β−Cu2+ Complexes in both Monomeric and Fibrillar Forms Do Not Generate H2O2 Catalytically but Quench Hydroxyl Radicals RC Nadal, SEJ Rigby, JH Viles Biochemistry 47 (44), 11653-11664, 2008 | 141 | 2008 |
Deconvoluting the Cu2+ binding modes of full-length prion protein M Klewpatinond, P Davies, S Bowen, DR Brown, JH Viles Journal of Biological Chemistry 283 (4), 1870-1881, 2008 | 121 | 2008 |