David R. Boyer

3.9k total citations · 2 hit papers
32 papers, 2.6k citations indexed

About

David R. Boyer is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, David R. Boyer has authored 32 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 14 papers in Physiology and 8 papers in Materials Chemistry. Recurrent topics in David R. Boyer's work include Alzheimer's disease research and treatments (14 papers), RNA Research and Splicing (9 papers) and Protein Structure and Dynamics (8 papers). David R. Boyer is often cited by papers focused on Alzheimer's disease research and treatments (14 papers), RNA Research and Splicing (9 papers) and Protein Structure and Dynamics (8 papers). David R. Boyer collaborates with scholars based in United States, China and Netherlands. David R. Boyer's co-authors include M.R. Sawaya, David Eisenberg, Duilio Cascio, P. Ge, Qin Cao, José A. Rodríguez, Tamir Gonen, Kevin A. Murray, Michael P. Hughes and Binsen Li and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

David R. Boyer

31 papers receiving 2.6k citations

Hit Papers

align trajectories

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.

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

2018 470 citations Binsen Li, P. Ge et al. Nature Communications profile →
Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks

2018 343 citations Michael P. Hughes, M.R. Sawaya et al. Science profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
David R. Boyer United States	19	1.7k	1.2k	766	317	316	32	2.6k
Hisashi Yagi Japan	33	1.8k 1.1×	1.6k 1.4×	507 0.7×	445 1.4×	354 1.1×	78	2.9k
Céline Galvagnion United Kingdom	21	1.5k 0.9×	1.7k 1.5×	1.5k 2.0×	436 1.4×	210 0.7×	28	3.2k
Mathew H. Horrocks United Kingdom	27	1.5k 0.9×	997 0.9×	847 1.1×	131 0.4×	209 0.7×	68	3.0k
Silvia Campioni Switzerland	20	1.6k 1.0×	1.7k 1.4×	1.3k 1.7×	407 1.3×	252 0.8×	32	3.3k
Leila M. Luheshi United Kingdom	19	2.0k 1.2×	2.0k 1.7×	519 0.7×	495 1.6×	233 0.7×	26	3.1k
Ashutosh Kumar India	19	709 0.4×	875 0.8×	848 1.1×	253 0.8×	133 0.4×	64	1.9k
Larissa A. Munishkina United States	16	1.1k 0.7×	969 0.8×	963 1.3×	132 0.4×	223 0.7×	18	2.3k
Erik Hellstrand Sweden	12	1.6k 0.9×	1.7k 1.5×	321 0.4×	616 1.9×	297 0.9×	14	2.6k
Benedetta Mannini United Kingdom	22	1.3k 0.8×	1.2k 1.0×	189 0.2×	223 0.7×	191 0.6×	43	2.1k
Jan Stöhr United States	22	1.8k 1.1×	1.1k 1.0×	274 0.4×	482 1.5×	244 0.8×	32	2.5k

Countries citing papers authored by David R. Boyer

Since Specialization

Citations

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

Fields of papers citing papers by David R. Boyer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David R. Boyer. 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 David R. Boyer. The network helps show where David R. Boyer may publish in the future.

Co-authorship network of co-authors of David R. Boyer

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

All Works

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20 of 20 papers shown

Hou, Ke, P. Ge, M.R. Sawaya, et al.. (2025). How short peptides disassemble tau fibrils in Alzheimer’s disease. Nature. 644(8078). 1020–1027. 3 indexed citations

Lu, Jiahui, P. Ge, M.R. Sawaya, et al.. (2023). Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation. Journal of Biological Chemistry. 300(2). 105531–105531. 4 indexed citations

Rosenberg, Gregory M., Romany Abskharon, David R. Boyer, et al.. (2023). Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method. PNAS Nexus. 2(12). pgad402–pgad402. 2 indexed citations

Sawaya, M.R., et al.. (2022). Micro-electron diffraction structure of the aggregation-driving N terminus of Drosophila neuronal protein Orb2A reveals amyloid-like β-sheets. Journal of Biological Chemistry. 298(10). 102396–102396. 6 indexed citations

Seidler, Paul M., Kevin A. Murray, David R. Boyer, et al.. (2022). Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro. Nature Communications. 13(1). 5451–5451. 117 indexed citations

Cao, Qin, David R. Boyer, M.R. Sawaya, et al.. (2021). Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores. Nature Structural & Molecular Biology. 28(9). 724–730. 57 indexed citations

Boyer, David R., Binsen Li, Chuanqi Sun, et al.. (2020). The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure. Proceedings of the National Academy of Sciences. 117(7). 3592–3602. 137 indexed citations

Kelly, H. Ray, Peter Dahl, Sophia M. Yi, et al.. (2020). Intrinsic electronic conductivity of individual atomically resolved amyloid crystals reveals micrometer-long hole hopping via tyrosines. Proceedings of the National Academy of Sciences. 118(2). 52 indexed citations

Lu, Jiahui, Qin Cao, Michael P. Hughes, et al.. (2020). CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Nature Communications. 11(1). 4090–4090. 78 indexed citations

10.

Boyer, David R., Chih-Te Zee, M.R. Sawaya, et al.. (2019). Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface. Nature Communications. 10(1). 3357–3357. 43 indexed citations

11.

Gallagher-Jones, Marcus, Colin Ophus, Karen C. Bustillo, et al.. (2019). Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction. Communications Biology. 2(1). 53 indexed citations

12.

Cao, Qin, David R. Boyer, M.R. Sawaya, P. Ge, & David Eisenberg. (2019). Cryo-EM structures of four polymorphic TDP-43 amyloid cores. Nature Structural & Molecular Biology. 26(7). 619–627. 180 indexed citations

13.

Seidler, Paul M., David R. Boyer, Kevin A. Murray, et al.. (2019). Structure-based inhibitors halt prion-like seeding by Alzheimer’s disease–and tauopathy–derived brain tissue samples. Journal of Biological Chemistry. 294(44). 16451–16464. 47 indexed citations

14.

Guenther, E.L., Qin Cao, Hamilton Trinh, et al.. (2019). Author Correction: Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. Nature Structural & Molecular Biology. 26(10). 988–988. 1 indexed citations

15.

Gallagher-Jones, Marcus, Calina Glynn, David R. Boyer, et al.. (2018). Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp. Nature Structural & Molecular Biology. 25(2). 131–134. 67 indexed citations

16.

Hughes, Michael P., M.R. Sawaya, David R. Boyer, et al.. (2018). Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks. Science. 359(6376). 698–701. 343 indexed citations breakdown →

17.

Li, Binsen, P. Ge, Kevin A. Murray, et al.. (2018). Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel. Nature Communications. 9(1). 3609–3609. 470 indexed citations breakdown →

18.

Guenther, E.L., Qin Cao, Hamilton Trinh, et al.. (2018). Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. Nature Structural & Molecular Biology. 25(6). 463–471. 183 indexed citations

19.

Seidler, Paul M., David R. Boyer, José A. Rodríguez, et al.. (2017). Structure-based inhibitors of tau aggregation. Nature Chemistry. 10(2). 170–176. 251 indexed citations

20.

Boyer, David R., et al.. (1986). Characterization of maternal haemoglobins in the eggs and embryos of Chironomus thummi. Journal of Insect Physiology. 32(11). 963–969. 7 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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