Claire J. Sarell

887 total citations
12 papers, 665 citations indexed

About

Claire J. Sarell is a scholar working on Physiology, Molecular Biology and Biomaterials. According to data from OpenAlex, Claire J. Sarell has authored 12 papers receiving a total of 665 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Physiology, 9 papers in Molecular Biology and 3 papers in Biomaterials. Recurrent topics in Claire J. Sarell's work include Alzheimer's disease research and treatments (10 papers), Prion Diseases and Protein Misfolding (6 papers) and Trace Elements in Health (3 papers). Claire J. Sarell is often cited by papers focused on Alzheimer's disease research and treatments (10 papers), Prion Diseases and Protein Misfolding (6 papers) and Trace Elements in Health (3 papers). Claire J. Sarell collaborates with scholars based in United Kingdom, United States and Ireland. Claire J. Sarell's co-authors include John H. Viles, Shane R. Wilkinson, Stephen E. J. Rigby, Christopher D. Syme, Paul Davies, David R. Brown, Sheena E. Radford, Peter G. Stockley, Nadine D. Younan and Robert G. Griffin and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Claire J. Sarell

12 papers receiving 664 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Claire J. Sarell United Kingdom 9 513 325 206 84 76 12 665
Timothy Johanssen Australia 7 452 0.9× 235 0.7× 118 0.6× 89 1.1× 122 1.6× 8 585
Wei‐Hui Wu China 14 568 1.1× 303 0.9× 186 0.9× 84 1.0× 126 1.7× 19 803
Nadine D. Younan United Kingdom 9 325 0.6× 309 1.0× 136 0.7× 49 0.6× 41 0.5× 11 508
Daniela Kaden Germany 11 571 1.1× 433 1.3× 127 0.6× 86 1.0× 83 1.1× 12 742
Paolo De Bona Italy 11 504 1.0× 314 1.0× 71 0.3× 59 0.7× 121 1.6× 16 665
Axel Abelein Sweden 19 664 1.3× 654 2.0× 130 0.6× 137 1.6× 143 1.9× 36 1.1k
Anna K. Tickler Australia 10 426 0.8× 450 1.4× 87 0.4× 64 0.8× 75 1.0× 10 848
William D. Bush United States 7 184 0.4× 196 0.6× 180 0.9× 60 0.7× 50 0.7× 8 609
Sungsu Lim South Korea 15 345 0.7× 280 0.9× 60 0.3× 34 0.4× 68 0.9× 39 684
Samer Salamekh United States 5 561 1.1× 429 1.3× 82 0.4× 105 1.3× 85 1.1× 8 785

Countries citing papers authored by Claire J. Sarell

Since Specialization
Citations

This map shows the geographic impact of Claire J. Sarell'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 Claire J. Sarell with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Claire J. Sarell more than expected).

Fields of papers citing papers by Claire J. Sarell

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Claire J. Sarell. 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 Claire J. Sarell. The network helps show where Claire J. Sarell may publish in the future.

Co-authorship network of co-authors of Claire J. Sarell

This figure shows the co-authorship network connecting the top 25 collaborators of Claire J. Sarell. A scholar is included among the top collaborators of Claire J. Sarell 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 Claire J. Sarell. Claire J. Sarell is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

12 of 12 papers shown
1.
2.
Purro, Silvia A., Michael Farmer, Claire J. Sarell, et al.. (2023). Two mouse models of Alzheimer’s disease accumulate amyloid at different rates and have distinct Aβ oligomer profiles unaltered by ablation of cellular prion protein. PLoS ONE. 18(11). e0294465–e0294465. 2 indexed citations
3.
Zhang, Dainan, Yingjie Qi, Igor Klyubin, et al.. (2017). Targeting glutamatergic and cellular prion protein mechanisms of amyloid β-mediated persistent synaptic plasticity disruption: Longitudinal studies. Neuropharmacology. 121. 231–246. 23 indexed citations
4.
Sarell, Claire J., Cassandra Terry, Andrew J. Nicoll, et al.. (2017). Soluble Aβ aggregates can inhibit prion propagation. Open Biology. 7(11). 8 indexed citations
5.
Su, Yongchao, Claire J. Sarell, Matthew T. Eddy, et al.. (2014). Secondary Structure in the Core of Amyloid Fibrils Formed from Human β2m and its Truncated Variant ΔN6. Journal of the American Chemical Society. 136(17). 6313–6325. 41 indexed citations
6.
Sarell, Claire J., Theodoros K. Karamanos, Simon J. White, et al.. (2014). Distinguishing Closely Related Amyloid Precursors Using an RNA Aptamer. Journal of Biological Chemistry. 289(39). 26859–26871. 6 indexed citations
7.
Sarell, Claire J., Lucy A. Woods, Yongchao Su, et al.. (2013). Expanding the Repertoire of Amyloid Polymorphs by Co-polymerization of Related Protein Precursors. Journal of Biological Chemistry. 288(10). 7327–7337. 36 indexed citations
8.
Sarell, Claire J., Peter G. Stockley, & Sheena E. Radford. (2013). Assessing the causes and consequences of co-polymerization in amyloid formation. Prion. 7(5). 359–368. 40 indexed citations
9.
Younan, Nadine D., Claire J. Sarell, Paul Davies, David R. Brown, & John H. Viles. (2013). The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers. The FASEB Journal. 27(5). 1847–1858. 86 indexed citations
10.
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
11.
Davies, Paul, Xiaoyan Wang, Claire J. Sarell, et al.. (2010). The Synucleins Are a Family of Redox-Active Copper Binding Proteins. Biochemistry. 50(1). 37–47. 62 indexed citations
12.
Sarell, Claire J., Christopher D. Syme, Stephen E. J. Rigby, & John H. Viles. (2009). Copper(II) Binding to Amyloid-β Fibrils of Alzheimer’s Disease Reveals a Picomolar Affinity: Stoichiometry and Coordination Geometry Are Independent of Aβ Oligomeric Form. Biochemistry. 48(20). 4388–4402. 185 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.

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2026