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Publications:  Dr John Viles

Younan ND, Chen K-F, Rose R-S et al.(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.
10.1074/jbc.RA118.003319
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
10.1016/j.jmb.2018.01.008
http://qmro.qmul.ac.uk/xmlui/handle/123456789/33744
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.
10.1002/anie.201704618
http://qmro.qmul.ac.uk/xmlui/handle/123456789/25927
Bode DC, Baker MD, Viles JH(2017). Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes. J Biol Chem vol. 292, (4) 1404-1413.
10.1074/jbc.M116.762526
http://qmro.qmul.ac.uk/xmlui/handle/123456789/21600
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.
10.1016/j.jinorgbio.2016.02.027
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.
10.1016/j.jmb.2016.05.017
http://qmro.qmul.ac.uk/xmlui/handle/123456789/13507
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
10.1016/j.bbapap.2016.04.009
http://qmro.qmul.ac.uk/xmlui/handle/123456789/12385
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.
10.1074/jbc.M115.684084
http://qmro.qmul.ac.uk/xmlui/handle/123456789/11005
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.
10.1021/acs.biochem.5b00309
http://qmro.qmul.ac.uk/xmlui/handle/123456789/11006
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.
10.1021/cr500638n
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.
10.1042/BJ20141168
http://qmro.qmul.ac.uk/xmlui/handle/123456789/11007
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.
10.1016/j.bbapap.2014.08.001
http://qmro.qmul.ac.uk/xmlui/handle/123456789/6407
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.
10.1111/febs.12934
http://qmro.qmul.ac.uk/xmlui/handle/123456789/11008
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.
10.1021/bi500643b
http://qmro.qmul.ac.uk/xmlui/handle/123456789/11269
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.
10.1016/j.bbapap.2013.10.013
http://qmro.qmul.ac.uk/xmlui/handle/123456789/6403
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.
10.1096/fj.12-222588
http://qmro.qmul.ac.uk/xmlui/handle/123456789/17639
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.
10.1016/j.ccr.2012.05.003
http://qmro.qmul.ac.uk/xmlui/handle/123456789/11270
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.
10.1074/jbc.M112.354779
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.
10.1074/jbc.C112.360800
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.
10.1016/j.jmb.2011.05.013
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.
10.1021/bi101582p
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.
10.1074/jbc.M110.171355
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.
10.1021/bi9011397
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.
10.1021/bi900254n
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.
10.1002/pro.44
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.
10.1042/BST0361288
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.
10.1021/bi8011093
Brazier MW, Davies P, Player E et al.(2008). Manganese binding to the prion protein. J Biol Chem vol. 283, (19) 12831-12839.
10.1074/jbc.M709820200
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.
10.1074/jbc.M708472200
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.
10.1042/BJ20061893
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.
10.1016/j.febslet.2007.02.068
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.
10.1042/BJ20060668
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.
10.1016/j.freeradbiomed.2006.09.019
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.
10.1016/j.bbapap.2005.09.012
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.
10.1039/b511553a
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.
10.1016/j.jmb.2004.12.043
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.
10.1074/jbc.M403467200
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.
10.1074/jbc.M313572200
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.
10.1074/jbc.M209280200
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.
10.1023/A:1011966718826
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.
10.1021/bi002898a
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.
10.1073/pnas.96.5.2042
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.
10.1006/jmbi.1998.1764
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.
10.1073/pnas.94.25.13452
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.
10.1111/j.1432-1033.1996.0352r.x
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.
10.1021/ic951005d
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.
10.1039/an9962100913
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.
10.1111/j.1399-3011.1996.tb01093.x
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.
10.1002/(SICI)1097-0134(199604)24:4<502::AID-PROT9>3.0.CO;2-F
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.
10.1002/(SICI)1097-0134(199604)24:4<502::AID-PROT9>3.0.CO;2-F
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.
10.1111/j.1432-1033.1994.tb18614.x
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.
10.1021/ja00073a053
PATEL SU, SADLER PJ, TUCKER A et al. (1993). PROTON NMR DETECTION OF ALBUMIN IN INTACT HUMAN BLOOD-PLASMA. JOURNAL OF CELLULAR BIOCHEMISTRY. 298-298.
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