John H. Viles

6.9k total citations · 1 hit paper
66 papers, 5.5k citations indexed

About

John H. Viles is a scholar working on Molecular Biology, Physiology and Nutrition and Dietetics. According to data from OpenAlex, John H. Viles has authored 66 papers receiving a total of 5.5k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 33 papers in Physiology and 23 papers in Nutrition and Dietetics. Recurrent topics in John H. Viles's work include Alzheimer's disease research and treatments (33 papers), Prion Diseases and Protein Misfolding (25 papers) and Trace Elements in Health (23 papers). John H. Viles is often cited by papers focused on Alzheimer's disease research and treatments (33 papers), Prion Diseases and Protein Misfolding (25 papers) and Trace Elements in Health (23 papers). John H. Viles collaborates with scholars based in United Kingdom, United States and Australia. John H. Viles's co-authors include Christopher D. Syme, Stephen E. J. Rigby, David R. Brown, Nadine D. Younan, Peter E. Wright, H. Jane Dyson, Fred E. Cohen, Stanley B. Prusiner, Peter J. Sadler and Claire J. Sarell and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

John H. Viles

66 papers receiving 5.4k citations

Hit Papers

Structure of the recombinant full-length hamster prion pr... 1997 2026 2006 2016 1997 100 200 300 400 500
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Structure of the recombinant full-length hamster prion protein PrP(29–231): The N terminus is highly flexible
    1997 568 citations John H. Viles et al. profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
John H. Viles United Kingdom 36 3.6k 2.3k 2.2k 1.1k 647 66 5.5k
Daniela Valensin Italy 35 2.4k 0.7× 1.5k 0.6× 1.6k 0.7× 362 0.3× 772 1.2× 122 5.3k
Per Hammarström Sweden 45 4.5k 1.3× 3.2k 1.4× 433 0.2× 514 0.5× 361 0.6× 145 7.2k
Leonid Breydo United States 30 3.0k 0.8× 2.1k 0.9× 595 0.3× 721 0.7× 136 0.2× 74 4.8k
Claudio O. Fernández Argentina 39 1.9k 0.5× 2.4k 1.0× 532 0.2× 512 0.5× 308 0.5× 86 5.3k
Joseph T. Jarrett United States 29 3.6k 1.0× 3.0k 1.3× 399 0.2× 551 0.5× 312 0.5× 47 5.9k
Gianni Valensin Italy 29 2.1k 0.6× 1.0k 0.4× 1.2k 0.5× 269 0.2× 629 1.0× 155 4.5k
Elena Gaggelli Italy 27 1.8k 0.5× 905 0.4× 1.1k 0.5× 250 0.2× 532 0.8× 127 4.0k
Monica Bucciantini Italy 31 3.7k 1.0× 2.5k 1.1× 325 0.1× 320 0.3× 206 0.3× 87 5.6k
Wolfgang Hoyer Germany 31 2.8k 0.8× 3.4k 1.5× 229 0.1× 364 0.3× 152 0.2× 73 5.8k
Yi Liang China 38 2.6k 0.7× 798 0.3× 431 0.2× 203 0.2× 246 0.4× 122 4.1k

Countries citing papers authored by John H. Viles

Since Specialization
Citations

This map shows the geographic impact of John H. Viles's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by John H. Viles with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites John H. Viles more than expected).

Fields of papers citing papers by John H. Viles

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John H. Viles. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by John H. Viles. The network helps show where John H. Viles may publish in the future.

Co-authorship network of co-authors of John H. Viles

This figure shows the co-authorship network connecting the top 25 collaborators of John H. Viles. A scholar is included among the top collaborators of John H. Viles based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with John H. Viles. John H. Viles is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Tian, Yao, Qi Shang, Hui Zhang, et al.. (2025). The p3 peptides (Aβ17-40/42) rapidly form amyloid fibrils that cross-seed with full-length Aβ. Nature Communications. 16(1). 2040–2040. 3 indexed citations
2.
3.
Khursheed, Anum & John H. Viles. (2024). Impact of Membrane Phospholipids and Exosomes on the Kinetics of Amyloid-β Fibril Assembly. Journal of Molecular Biology. 436(6). 168464–168464. 7 indexed citations
4.
Tian, Yao, et al.. (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. 298(7). 102071–102071. 12 indexed citations
5.
Younan, Nadine D., Ko‐Fan Chen, Ruth‐Sarah Rose, Damian C. Crowther, & John H. Viles. (2018). Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a Drosophila model of Alzheimer's disease. Journal of Biological Chemistry. 293(34). 13090–13099. 29 indexed citations
6.
Viles, John H., et al.. (2016). Methionine oxidation reduces lag-times for amyloid-β(1–40) fiber formation but generates highly fragmented fibers. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1864(9). 1260–1269. 27 indexed citations
7.
Jones, Mark R., et al.. (2016). Endocytosis of the tachykinin neuropeptide, neurokinin B, in astrocytes and its role in cellular copper uptake. Journal of Inorganic Biochemistry. 162. 319–325. 16 indexed citations
8.
Barritt, Joseph D. & John H. Viles. (2015). Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly. Journal of Biological Chemistry. 290(46). 27791–27802. 53 indexed citations
9.
Jones, Christopher E., et al.. (2014). Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844(10). 1842–1850. 4 indexed citations
10.
Jones, Christopher E., et al.. (2013). Structural analysis of the starfish SALMFamide neuropeptides S1 and S2: The N-terminal region of S2 facilitates self-association. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844(2). 358–365. 6 indexed citations
11.
Younan, Nadine D., et al.. (2012). Methionine Oxidation Perturbs the Structural Core of the Prion Protein and Suggests a Generic Misfolding Pathway. Journal of Biological Chemistry. 287(34). 28263–28275. 40 indexed citations
12.
Sarell, Claire J., Shane R. Wilkinson, & John H. Viles. (2010). Substoichiometric Levels of Cu2+ Ions Accelerate the Kinetics of Fiber Formation and Promote Cell Toxicity of Amyloid-β from Alzheimer Disease. Journal of Biological Chemistry. 285(53). 41533–41540. 172 indexed citations
13.
Brazier, Marcus W., et al.. (2008). Manganese Binding to the Prion Protein. Journal of Biological Chemistry. 283(19). 12831–12839. 81 indexed citations
14.
Abdelraheim, Salama R., et al.. (2006). Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals. Free Radical Biology and Medicine. 42(1). 79–89. 64 indexed citations
15.
Syme, Christopher D. & John H. Viles. (2005). Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(2). 246–256. 157 indexed citations
16.
Jones, Christopher E., et al.. (2005). A survey of diamagnetic probes for copper2+binding to the prion protein.1H NMR solution structure of the palladium2+bound single octarepeat. Dalton Transactions. 509–518. 24 indexed citations
17.
18.
Syme, Christopher D., et al.. (2004). Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease. Journal of Biological Chemistry. 279(18). 18169–18177. 401 indexed citations
19.
20.
Jones, David T., Claire M. Moody, Julia Uppenbrink, 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 Bioinformatics. 24(4). 502–513. 27 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Daniela Valensin Breakdown of academic impact, for papers by Per Hammarström Breakdown of academic impact, for papers by Leonid Breydo Breakdown of academic impact, for papers by Claudio O. Fernández Breakdown of academic impact, for papers by Joseph T. Jarrett Breakdown of academic impact, for papers by Gianni Valensin Breakdown of academic impact, for papers by Elena Gaggelli Breakdown of academic impact, for papers by Monica Bucciantini Breakdown of academic impact, for papers by Wolfgang Hoyer Breakdown of academic impact, for papers by Yi Liang
Rankless by CCL
2026