Alexander J. Dear

1.8k total citations · 1 hit paper
40 papers, 1.3k citations indexed

About

Alexander J. Dear is a scholar working on Physiology, Molecular Biology and Biomaterials. According to data from OpenAlex, Alexander J. Dear has authored 40 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Physiology, 25 papers in Molecular Biology and 9 papers in Biomaterials. Recurrent topics in Alexander J. Dear's work include Alzheimer's disease research and treatments (26 papers), Protein Structure and Dynamics (17 papers) and Prion Diseases and Protein Misfolding (14 papers). Alexander J. Dear is often cited by papers focused on Alzheimer's disease research and treatments (26 papers), Protein Structure and Dynamics (17 papers) and Prion Diseases and Protein Misfolding (14 papers). Alexander J. Dear collaborates with scholars based in United Kingdom, United States and Sweden. Alexander J. Dear's co-authors include Tuomas P. J. Knowles, Thomas C. T. Michaels, Christopher M. Dobson, Sara Linse, Georg Meisl, David Klenerman, Anđela Šarić, Michele Vendruscolo, Samuel I. A. Cohen and Sarah Perrett and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Physical Review Letters.

In The Last Decade

Alexander J. Dear

38 papers receiving 1.3k citations

Hit Papers

Dynamics of oligomer populations formed during the aggreg... 2020 2026 2022 2024 2020 50 100 150 200 250

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alexander J. Dear United Kingdom 20 806 775 256 178 164 40 1.3k
Sean Chia United Kingdom 21 916 1.1× 929 1.2× 221 0.9× 129 0.7× 233 1.4× 46 1.5k
Luke Rajah United Kingdom 9 994 1.2× 962 1.2× 281 1.1× 113 0.6× 193 1.2× 9 1.5k
Therése Klingstedt Sweden 16 616 0.8× 444 0.6× 138 0.5× 152 0.9× 134 0.8× 33 1.1k
Tadato Ban Japan 14 985 1.2× 1.0k 1.3× 297 1.2× 94 0.5× 126 0.8× 16 1.6k
Marten Beeg Italy 23 949 1.2× 1.0k 1.3× 188 0.7× 120 0.7× 209 1.3× 47 1.8k
Henrik Biverstål Sweden 18 1.1k 1.3× 1.0k 1.3× 272 1.1× 113 0.6× 231 1.4× 35 1.6k
Sofie Nyström Sweden 24 1.2k 1.5× 1.0k 1.3× 222 0.9× 192 1.1× 229 1.4× 51 2.1k
Rabia Sarroukh Belgium 9 850 1.1× 779 1.0× 296 1.2× 248 1.4× 147 0.9× 10 1.4k
Samuel A. Kotler United States 13 908 1.1× 924 1.2× 293 1.1× 96 0.5× 166 1.0× 18 1.4k
Axel Abelein Sweden 19 664 0.8× 654 0.8× 171 0.7× 75 0.4× 143 0.9× 36 1.1k

Countries citing papers authored by Alexander J. Dear

Since Specialization
Citations

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

Fields of papers citing papers by Alexander J. Dear

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Alexander J. Dear

This figure shows the co-authorship network connecting the top 25 collaborators of Alexander J. Dear. A scholar is included among the top collaborators of Alexander J. Dear 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 Alexander J. Dear. Alexander J. Dear 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.
Scheidt, Tom, Stefan Wennmalm, Samo Curk, et al.. (2026). Structural defects in amyloid-β fibrils drive secondary nucleation. Nature Communications. 17(1).
2.
Dear, Alexander J., et al.. (2025). Kinetics of seeded protein aggregation: Theory and application. The Journal of Chemical Physics. 163(4). 1 indexed citations
3.
Dear, Alexander J. & L. Mahadevan. (2025). Approximate Lie symmetries and singular perturbation theory. Proceedings of the Royal Society A Mathematical Physical and Engineering Sciences. 481(2312). 1 indexed citations
4.
Dear, Alexander J., Georg Meisl, Tuomas P. J. Knowles, et al.. (2025). Global kinetic model of lipid-induced α -synuclein aggregation and its inhibition by small molecules. Proceedings of the National Academy of Sciences. 122(26). e2422427122–e2422427122. 2 indexed citations
5.
Dear, Alexander J., Xiangyu Teng, J. Lewin, et al.. (2024). Molecular mechanism of α-synuclein aggregation on lipid membranes revealed. Chemical Science. 15(19). 7229–7242. 8 indexed citations
6.
Dear, Alexander J., et al.. (2024). The role of shear forces in primary and secondary nucleation of amyloid fibrils. Proceedings of the National Academy of Sciences. 121(25). e2322572121–e2322572121. 18 indexed citations
7.
Dear, Alexander J., Stefan Wennmalm, Ewa Andrzejewska, et al.. (2024). Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces. ACS Chemical Neuroscience. 15(11). 2296–2307. 4 indexed citations
8.
Dear, Alexander J., Georg Meisl, Christopher G. Taylor, et al.. (2024). Surface effects on functional amyloid formation. Nanoscale. 16(34). 16172–16182. 2 indexed citations
9.
Xu, Catherine K., Georg Meisl, Georg Krainer, et al.. (2024). α-Synuclein oligomers form by secondary nucleation. Nature Communications. 15(1). 7083–7083. 21 indexed citations
10.
Dear, Alexander J., Gonzalo Garcia, Georg Meisl, et al.. (2024). Maximum entropy determination of mammalian proteome dynamics. Proceedings of the National Academy of Sciences. 121(18). e2313107121–e2313107121.
11.
Dear, Alexander J., et al.. (2022). Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation. Chemical Science. 13(8). 2423–2439. 34 indexed citations
12.
Michaels, Thomas C. T., Alexander J. Dear, Samuel I. A. Cohen, Michele Vendruscolo, & Tuomas P. J. Knowles. (2022). Kinetic profiling of therapeutic strategies for inhibiting the formation of amyloid oligomers. The Journal of Chemical Physics. 156(16). 164904–164904. 21 indexed citations
13.
Dear, Alexander J., Thomas C. T. Michaels, Tuomas P. J. Knowles, & L. Mahadevan. (2021). Feedback control of protein aggregation. The Journal of Chemical Physics. 155(6). 64102–64102. 5 indexed citations
14.
Flagmeier, Patrick, Suman De, Thomas C. T. Michaels, et al.. (2020). Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation. Nature Structural & Molecular Biology. 27(10). 886–891. 47 indexed citations
15.
Dear, Alexander J., Georg Meisl, Anđela Šarić, et al.. (2020). Identification of on- and off-pathway oligomers in amyloid fibril formation. Chemical Science. 11(24). 6236–6247. 92 indexed citations
16.
Yang, Jie, Alexander J. Dear, Zhenyan Liu, et al.. (2020). Amelioration of aggregate cytotoxicity by catalytic conversion of protein oligomers into amyloid fibrils. Nanoscale. 12(36). 18663–18672. 16 indexed citations
17.
Dear, Alexander J., et al.. (2020). The catalytic nature of protein aggregation. The Journal of Chemical Physics. 152(4). 45101–45101. 41 indexed citations
18.
Dear, Alexander J., Thomas C. T. Michaels, Georg Meisl, et al.. (2020). Kinetic diversity of amyloid oligomers. Proceedings of the National Academy of Sciences. 117(22). 12087–12094. 133 indexed citations
19.
Michaels, Thomas C. T., Alexander J. Dear, Julius B. Kirkegaard, et al.. (2016). Fluctuations in the Kinetics of Linear Protein Self-Assembly. Physical Review Letters. 116(25). 258103–258103. 32 indexed citations
20.
Tosatto, Laura, Mathew H. Horrocks, Alexander J. Dear, et al.. (2015). Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants. Scientific Reports. 5(1). 16696–16696. 86 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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