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Publications:  Dr John Viles

Tian Y, Stanyon HF, Barritt JD, Mayet U, Patel P, Karamani E, Fusco G, Viles JH(2019). Copper2+ Binding to α-Synuclein. Histidine50 Can Form a Ternary Complex with Cu2+ at the N-Terminus but Not a Macrochelate. Inorganic Chemistry: including bioinorganic chemistry vol. 58, (22) 15580-15589.
Bode DC, Freeley M, Nield J, Palma M, Viles JH(2019). Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy. J Biol Chem vol. 294, (19) 7566-7572.
VILES JH(2018). Copper Redox Cycling Inhibits Aβ Fibre Formation and Promotes Fibre Fragmentation, while Generating a Dityrosine Aβ Dimer. Scientific Reports
Younan ND, Chen K-F, Rose R-S, Crowther DC, Viles JH(2018). Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a Drosophila model of Alzheimer's disease. J Biol Chem vol. 293, (34) 13090-13099.
Bode DC, Stanyon HF, Hirani T, Baker MD, Nield J, Viles JH(2018). Serum Albumin's Protective Inhibition of Amyloid-β Fibre Formation Is Suppressed by Cholesterol, Fatty Acids and Warfarin. J Mol Biol
Barritt JD, Younan ND, Viles JH(2017). N-Terminally Truncated Amyloid-β(11-40/42) Cofibrillizes with its Full-Length Counterpart: Implications for Alzheimer's Disease. Angew Chem Int Ed Engl vol. 56, (33) 9816-9819.
BAKER MD(2016). Ion Channel Formation by Amyloid-β42 Oligomers but not Amyloid-β40 in Cellular Membranes. Journal of Biological Chemistry
Shahzad R, Jones MR, Viles JH, Jones CE(2016). Endocytosis of the tachykinin neuropeptide, neurokinin B, in astrocytes and its role in cellular copper uptake. Journal of Inorganic Biochemistry vol. 162, 319-325.
Matheou CJ, Younan ND, Viles JH(2016). The Rapid Exchange of Zinc2+ Enables Trace Levels to Profoundly Influence Amyloid-β Misfolding and Dominates Assembly Outcomes in Cu2+/Zn2+ Mixtures. Journal of Molecular Biology vol. 428, (14) 2832-2846.
Gu M, Viles JH(2016). Methionine oxidation reduces lag-times for Amyloid-β(1–40) fibre formation but generates highly fragmented fibres. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Barritt JD, Viles JH(2015). Truncated amyloid-β<inf>(11-40/42)</inf> from Alzheimer disease binds Cu<sup>2+</sup> with a femtomolar affinity and influences fiber assembly. Journal of Biological Chemistry vol. 290, (46) 27791-27802.
Younan ND, Viles JH(2015). A Comparison of Three Fluorophores for the Detection of Amyloid Fibers and Prefibrillar Oligomeric Assemblies. ThT (Thioflavin T); ANS (1-Anilinonaphthalene-8-sulfonic Acid); and bisANS (4,4′-Dianilino-1,1′-binaphthyl-5,5′-disulfonic Acid). Biochemistry vol. 54, (28) 4297-4306.
Matheou CJ, Younan ND, Viles JH(2015). Cu<sup>2+</sup> accentuates distinct misfolding of Aβ<inf>(1-40)</inf> and Aβ<inf>(1-42)</inf> peptides, and potentiates membrane disruption. Biochemical Journal vol. 466, 233-242.
Nasica-Labouze J, Nguyen PH, Sterpone F, Berthoumieu O, Buchete NV, Coté S, De Simone A, Doig AJ et al.(2015). Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies. Chemical Reviews vol. 115, (9) 3518-3563.
Jones CE, Otara CB, Younan ND, Viles JH, Elphick MR(2014). Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2. Biochim Biophys Acta vol. 1844, (10) 1842-1850.
Stanyon HF, Cong X, Chen Y, Shahidullah N, Rossetti G, Dreyer J, Papamokos G, Carloni P et al.(2014). Developing predictive rules for coordination geometry from visible circular dichroism of copper(II) and nickel(II) ions in histidine and amide main-chain complexes. FEBS J vol. 281, (17) 3945-3954.
Stanyon HF, Patel K, Begum N, Viles JH(2014). Copper(II) sequentially loads onto the N-terminal amino group of the cellular prion protein before the individual octarepeats. Biochemistry vol. 53, (24) 3934-3999.
Otara CB, Jones CE, Younan ND, Viles JH, Elphick MR(2014). Structural analysis of the starfish SALMFamide neuropeptides S1 and S2: the N-terminal region of S2 facilitates self-association. Biochim Biophys Acta vol. 1844, (2) 358-365.
Younan ND, Sarell CJ, Davies P, Brown DR, Viles JH(2013). The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers. FASEB J vol. 27, (5) 1847-1858.
Viles JH(2012). Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases. COORDINATION CHEMISTRY REVIEWS vol. 256, (19-20) 2271-2284.
Younan ND, Nadal RC, Davies P, Brown DR, Viles JH(2012). Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway. J Biol Chem vol. 287, (34) 28263-28275.
Stanyon HF, Viles JH(2012). Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease. J Biol Chem vol. 287, (33) 28163-28168.
Younan ND, Klewpatinond M, Davies P, Ruban AV, Brown DR, Viles JH(2011). Copper(II)-induced secondary structure changes and reduced folding stability of the prion protein. J Mol Biol vol. 410, (3) 369-382.
Davies P, Wang X, Sarell CJ, Drewett A, Marken F, Viles JH, Brown DR(2011). The synucleins are a family of redox-active copper binding proteins. Biochemistry vol. 50, (1) 37-47.
Sarell CJ, Wilkinson SR, Viles JH(2010). Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-{beta} from Alzheimer disease. J Biol Chem vol. 285, (53) 41533-41540.
Wright HM, Wyatt PB, Viles JH(2010). Is oxidation the trigger of the Amyloid Cascade?: A synthesis of 2-oxo-histidine for incorporation into the Amyloid beta sequence. J PEPT SCI vol. 16, 66-66.
Nadal RC, Davies P, Brown DR, Viles JH(2009). Evaluation of copper2+ affinities for the prion protein. Biochemistry vol. 48, (38) 8929-8931.
Sarell CJ, Syme CD, Rigby SEJ, Viles JH(2009). Copper(II) binding to amyloid-beta fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Abeta oligomeric form. Biochemistry vol. 48, (20) 4388-4402.
O'Sullivan DBD, Jones CE, Abdelraheim SR, Brazier MW, Toms H, Brown DR, Viles JH(2009). Dynamics of a truncated prion protein, PrP(113-231), from (15)N NMR relaxation: order parameters calculated and slow conformational fluctuations localized to a distinct region. Protein Sci vol. 18, (2) 410-423.
Viles JH, Klewpatinond M, Nadal RC(2008). Copper and the structural biology of the prion protein. Biochem Soc Trans vol. 36, (Pt 6) 1288-1292.
Nadal RC, Rigby SEJ, Viles JH(2008). Amyloid beta-Cu2+ complexes in both monomeric and fibrillar forms do not generate H2O2 catalytically but quench hydroxyl radicals. Biochemistry vol. 47, (44) 11653-11664.
Brazier MW, Davies P, Player E, Marken F, Viles JH, Brown DR(2008). Manganese binding to the prion protein. J Biol Chem vol. 283, (19) 12831-12839.
Klewpatinond M, Davies P, Bowen S, Brown DR, Viles JH(2008). Deconvoluting the Cu2+ binding modes of full-length prion protein. J BIOL CHEM vol. 283, (4) 1870-1881.
Klewpatinond M, Viles JH(2007). Fragment length influences affinity for Cu2+ and Ni2+ binding to His(96) or His(111) of the prion protein and spectroscopic evidence for a multiple histidine binding only at low pH. BIOCHEM J vol. 404, 393-402.
Klewpatinond M, Viles JH(2007). Empirical rules for rationalising visible circular dichroism of Cu2+ and Ni2+ histidine complexes: Applications to the prion protein. FEBS LETT vol. 581, (7) 1430-1434.
O'Sullivan DBD, Jones CE, Abdelraheim SR, Thompsett AR, Brazier MW, Toms H, Brown DR, Viles JH(2007). 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. Biochem J vol. 401, (2) 533-540.
Nadal RC, Abdelraheim SR, Brazier MW, Rigby SEJ, Brown DR, Viles JH(2007). Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals. Free Radic Biol Med vol. 42, (1) 79-89.
Syme CD, Viles JH(2006). Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Abeta) of Alzheimer's disease. Biochim Biophys Acta vol. 1764, (2) 246-256.
Garnett AP, Jones CE, Viles JH(2006). A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat. Dalton Trans (3) 509-518.
Otara CB, Jones CE, Melarange R, Viles JH, Elphick MR(2005). Tertiary structure and activity of SALMFamide neuropeptides. COMP BIOCHEM PHYS A vol. 141, (3) S161-S161.
Jones CE, Klewpatinond M, Abdelraheim SR, Brown DR, Viles JH(2005). 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. J Mol Biol vol. 346, (5) 1393-1407.
Jones CE, Abdelraheim SR, Brown DR, Viles JH(2004). Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein. J Biol Chem vol. 279, (31) 32018-32027.
Syme CD, Nadal RC, Rigby SEJ, Viles JH(2004). Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques. J Biol Chem vol. 279, (18) 18169-18177.
Garnett AP, Viles JH(2003). Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism. J Biol Chem vol. 278, (9) 6795-6802.
Dyson HJ, Wright PE, Mo HP, Viles JH(2002). Structure and dynamics of prion and doppel proteins. ABSTR PAP AM CHEM S vol. 223, C35-C35.
Dyson HJ, Mo HP, Viles JH, Wright PE, Prusiner SB, Cohen FE(2002). Structure and dynamics of prion and Doppel proteins. BIOPHYS J vol. 82, (1) 169A-169A.
Viles JH, Duggan BM, Zaborowski E, Schwarzinger S, Huntley JJA, Kroon GJA, Dyson HJ, Wright PE(2001). Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods. J BIOMOL NMR vol. 21, (1) 1-9.
Viles JH, Donne D, Kroon G, Prusiner SB, Cohen FE, Dyson HJ, Wright PE(2001). Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. BIOCHEMISTRY-US vol. 40, (9) 2743-2753.
Viles JH, Cohen FE, Prusiner SB, Goodin DB, Wright PE, Dyson HJ(1999). Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc Natl Acad Sci U S A vol. 96, (5) 2042-2047.
Viles JH, Patel SU, Mitchell JB, Moody CM, Justice DE, Uppenbrink J, Doyle PM, Harris CJ et al.(1998). Design, synthesis and structure of a zinc finger with an artificial beta-turn. J Mol Biol vol. 279, (4) 973-986.
Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE et al.(1997). Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci U S A vol. 94, (25) 13452-13457.
Viles JH, Mitchell JB, Gough SL, Doyle PM, Harris CJ, Sadler PJ, Thornton JM(1996). Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-). Analysis of the (phi, psi) space available to cyclic pentapeptides. Eur J Biochem vol. 242, (2) 352-362.
Sadler PJ, Viles JH(1996). 1H and (113)Cd NMR Investigations of Cd(2+) and Zn(2+) Binding Sites on Serum Albumin: Competition with Ca(2+), Ni(2+), Cu(2+), and Zn(2+). Inorg Chem vol. 35, (15) 4490-4496.
Harris R, Patel SU, Sadler PJ, Viles JH(1996). Observation of albumin resonances in proton nuclear magnetic resonance spectra of human blood plasma: N-terminal assignments aided by use of modified recombinant albumin. Analyst vol. 121, (7) 913-922.
Doyle PM, Harris JC, Moody CM, Sadler PJ, Sims M, Thornton JM, Uppenbrink J, Viles JH(1996). Solution structure of a biologically active cyclic LDV peptide analogue containing a type II' beta-turn mimetic. Int J Pept Protein Res vol. 47, (6) 427-436.
Jones DT, Moody CM, Uppenbrink J, Viles JH, Doyle PM, Harris CJ, Pearl LH, Sadler PJ et al.(1996). Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein. Proteins: Structure, Function and Genetics vol. 24, (4) 502-513.
Jones DT, Moody CM, Uppenbrink J, Viles JH, Doyle PM, Harris CJ, Pearl LH, Sadler PJ et al.(1996). Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an alpha-helical protein with over 50% sequence identity to an all-beta protein. Proteins vol. 24, (4) 502-513.
Sadler PJ, Viles JH(1996). <sup>1</sup>H and <sup>113</sup>Cd NMR Investigations of Cd<sup>2+</sup> and Zn<sup>2+</sup> Binding Sites on Serum Albumin: Competition with Ca<sup>2+</sup>, Ni<sup>2+</sup>, Cu<sup>2+</sup>, and Zn<sup>2+</sup>. Inorganic Chemistry vol. 35, (15) 4490-4496.
Sadler PJ, Tucker A, Viles JH(1994). Involvement of a lysine residue in the N-terminal Ni2+ and Cu2+ binding site of serum albumins. Comparison with Co2+, Cd2+ and Al3+. Eur J Biochem vol. 220, (1) 193-200.
Patel SU, Sadler PJ, Tucker A, Viles JH(1993). Direct Detection of Albumin in Human Blood Plasma by <sup>1</sup>H NMR Spectroscopy. Complexation of Nickel<sup>2+</sup>. Journal of the American Chemical Society vol. 115, (20) 9285-9286.
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