Publications: Dr John Viles
Tian Y, Shang Q, Liang R, Viles JH
(
2024
)
.
Copper(II) Can Kinetically Trap Arctic and Italian Amyloid‑β40 as Toxic Oligomers, Mimicking Cu(II) Binding to Wild-Type Amyloid‑β42: Implications for Familial Alzheimer’s Disease
.
JACS Au
vol.
4
,
(
2
)
578
-
591
.
Khursheed A, Viles JH
(
2024
)
.
Impact of Membrane Phospholipids and Exosomes on the Kinetics of Amyloid-β Fibril Assembly
.
Journal of Molecular Biology
vol.
436
,
(
6
)
Viles JH
(
2023
)
.
Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease
.
Angewandte Chemie
vol.
135
,
(
25
)
Tian Y, Viles JH
(
2022
)
.
pH Dependence of Amyloid-β Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes
.
Angewandte Chemie International Edition
Tian Y, Viles JH
(
2022
)
.
pH Dependence of Amyloid‐β Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes
.
Angewandte Chemie
Liang R, Tian Y, Viles JH
(
2022
)
.
Cross-seeding of WT amyloid-β with Arctic but not Italian familial mutants accelerates fibril formation in Alzheimer's disease
.
Journal of Biological Chemistry
vol.
298
,
(
7
)
Tian Y, Liu J, Yang F, Lian C, Zhang H, Viles JH, Li Z
(
2022
)
.
Therapeutic potential for amyloid surface inhibitor: only amyloid-β oligomers formed by secondary nucleation disrupt lipid membrane integrity
.
FEBS Journal
Tian Y, Liang R, Kumar A, Szwedziak P, Viles JH
(
2021
)
.
3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography
.
Chemical Science
vol.
12
,
(
20
)
6896
-
6907
.
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
.
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
.
Angewandte Chemie
vol.
129
,
(
33
)
9948
-
9951
.
BAKER MD
(
2016
)
.
Ion Channel Formation by Amyloid-β42 Oligomers but not Amyloid-β40 in Cellular Membranes
.
Journal of Biological Chemistry
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
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
.
Barritt JD, Viles JH
(
2015
)
.
Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ 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
.
Nasica-Labouze J, Nguyen PH, Sterpone F, Berthoumieu O, Buchete N-V, 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
.
Matheou CJ, Younan ND, Viles JH
(
2015
)
.
Cu²⁺ accentuates distinct misfolding of Aβ₁₋₄₀ and Aβ₁₋₄₂ peptides, and potentiates membrane disruption
.
Biochemical Journal
vol.
466
,
(
2
)
233
-
242
.
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
.
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
.
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, 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
.
Viles JH
(
2005
)
.
Copper and the prion protein: Function and dysfunction
.
The Biochemist
vol.
27
,
(
4
)
9
-
12
.
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
.
Patel SU, Sadler PJ, Tucker A, Viles JH
(
2002
)
.
Direct detection of albumin in human blood plasma by proton NMR spectroscopy. Complexation of nickel2+
.
Journal of the American Chemical Society
vol.
115
,
(
20
)
9285
-
9286
.
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
)
.
PROTON NMR DETECTION OF ALBUMIN IN INTACT HUMAN BLOOD-PLASMA
.
JOURNAL OF CELLULAR BIOCHEMISTRY
.
298
-
298
.