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Publications:  Dr John Viles

Bode DC, Stanyon HF, Hirani T et al.(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.
Bode DC, Baker MD, Viles JH(2017). Ion channel formation by amyloid-β<inf>42</inf>oligomers but not amyloid-β<inf>40</inf>in cellular membranes. Journal of Biological Chemistry vol. 292, (4) 144-1413.
Shahzad R, Jones MR, Viles JH et al.(2016). Endocytosis of the tachykinin neuropeptide, neurokinin B, in astrocytes and its role in cellular copper uptake. J Inorg Biochem 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(11-40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly. J Biol Chem 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.
Nasica-Labouze J, Nguyen PH, Sterpone F et al.(2015). Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies. Chem Rev vol. 115, (9) 3518-3563.
Matheou CJ, Younan ND, Viles JH(2015). Cu²⁺ accentuates distinct misfolding of Aβ₁₋₄₀ and Aβ₁₋₄₂ peptides, and potentiates membrane disruption. Biochem J vol. 466, (2) 233-242.
Jones CE, Otara CB, Younan ND et al.(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 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 et al.(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 et al.(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 et al.(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 et al.(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 et al.(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 et al.(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 et al.(2009). Evaluation of copper2+ affinities for the prion protein. Biochemistry vol. 48, (38) 8929-8931.
Sarell CJ, Syme CD, Rigby SEJ et al.(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 et al.(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 et al.(2008). Manganese binding to the prion protein. J Biol Chem vol. 283, (19) 12831-12839.
Klewpatinond M, Davies P, Bowen S et al.(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 et al.(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 et al.(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 et al.(2005). Tertiary structure and activity of SALMFamide neuropeptides. COMP BIOCHEM PHYS A vol. 141, (3) S161-S161.
Jones CE, Klewpatinond M, Abdelraheim SR et al.(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 et al.(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 et al.(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 et al.(2002). Structure and dynamics of prion and doppel proteins. ABSTR PAP AM CHEM S vol. 223, C35-C35.
Dyson HJ, Mo HP, Viles JH et al.(2002). Structure and dynamics of prion and Doppel proteins. BIOPHYS J vol. 82, (1) 169A-169A.
Viles JH, Duggan BM, Zaborowski E et al.(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 et al.(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 et al.(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 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 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.
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.
Viles JH, Mitchell JB, Gough SL et al.(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 et al.(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 et al.(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 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 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, 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 et al.(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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