David R. Boyer

Pilot corpus only

This score is computed over theSindex pilot corpus and does not cover the full scientific literature. Scores are relative to papers we have ingested — papers, authors, and institutions outside the pilot are not represented. Methodology.

Top 100%percentile

0Author DataRank

Indexed papers

0in pilot corpus

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Papers

Driven by 24 papers. Top paper: “The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure”.

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

Proceedings of the National Academy of Sciences(2020)10.1073/pnas.1917914117

N/A

4.3DataRank · unranked

183 citations

Binsen Li, Chuanqi Sun, Weijia Fan, Kang Zhou, Michael P. Hughes +4 more

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

Nature Structural & Molecular Biology(2020)10.1038/s41594-020-0435-3

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0DataRank · unranked

149 citations

David R. Boyer, M.R. Sawaya, P. Ge, David Eisenberg, Qin Cao

CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

Nature Communications(2020)10.1038/s41467-020-17905-y

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0DataRank · unranked

116 citations

Qin Cao, Michael P. Hughes, M.R. Sawaya, David R. Boyer, Duilio Cascio +2 more

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.05.25.114967

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0DataRank · unranked

3 citations

David R. Boyer, M.R. Sawaya, P. Ge, David Eisenberg, Qin Cao

The cryoEM structure of the fibril-forming low-complexity domain of hnRNPA2 reveals distinct differences from pathogenic amyloid and shows how mutation converts it to the pathogenic form

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.05.24.113621

N/A

0DataRank · unranked

1 citations

Qin Cao, Michael P. Hughes, M.R. Sawaya, David R. Boyer, Duilio Cascio +2 more

Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores

Nature Structural & Molecular Biology(2021)10.1038/s41594-021-00646-x

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0DataRank · unranked

90 citations

David R. Boyer, M.R. Sawaya, Romany Abskharon, Lorena Saelices, Binh A. Nguyen +5 more

Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2

bioRxiv (Cold Spring Harbor Laboratory)(2021)10.1101/2021.03.05.434000

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0DataRank · unranked

24 citations

Xinyi Cheng, Christen E. Tai, Jeannette T. Bowler, Sarah L. Griner, M.R. Sawaya +19 more

Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro

Nature Communications(2022)10.1038/s41467-022-32951-4

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0DataRank · unranked

187 citations

Kevin A. Murray, David R. Boyer, P. Ge, M.R. Sawaya, Carolyn J. Hu +9 more

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

Proceedings of the National Academy of Sciences(2022)10.1073/pnas.2119952119

N/A

0DataRank · unranked

98 citations

M.R. Sawaya, David R. Boyer, Qin Cao, Binh A. Nguyen, Duilio Cascio +2 more

The rippled β-sheet layer configuration—a novel supramolecular architecture based on predictions by Pauling and Corey

Chemical Science(2022)10.1039/d2sc02531k

N/A

0DataRank · unranked

16 citations

M.R. Sawaya, Niko Vlahakis, Timothy C. Johnstone, David R. Boyer, José A. Rodríguez +3 more

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.01.28.478258

N/A

0DataRank · unranked

11 citations

M.R. Sawaya, David R. Boyer, Qin Cao, Binh A. Nguyen, Duilio Cascio +2 more

Structural polymorphism of amyloid fibrils in cardiac transthyretin amyloidosis revealed by cryo-electron microscopy

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.06.21.496949

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0DataRank · unranked

8 citations

Shumaila Afrin, Virender Singh, Yasmin Ahmed, Rose Pedretti, María del Carmen Fernández‐Ramírez +12 more

Structure of a reversible amyloid fibril formed by the CPEB3 prion-like domain reveals a core sequence involved in translational regulation

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.12.07.519389

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0DataRank · unranked

8 citations

M.R. Sawaya, David R. Boyer, Samantha Zink, Susanna Tovmasyan, Adrian Saucedo +5 more

Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils

Nature Communications(2023)10.1038/s41467-023-37865-3

N/A

0DataRank · unranked

27 citations

Jeannette T. Bowler, Christen E. Tai, M.R. Sawaya, Yi Xiao Jiang, Gustavo Garcia +23 more

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(2023)10.1016/j.jbc.2023.105531

N/A

0DataRank · unranked

5 citations

P. Ge, M.R. Sawaya, Michael P. Hughes, David R. Boyer, Qin Cao +5 more

Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method

PNAS Nexus(2023)10.1093/pnasnexus/pgad402

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0DataRank · unranked

4 citations

Romany Abskharon, David R. Boyer, P. Ge, M.R. Sawaya, David Eisenberg +1 more

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.03.06.531355

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0DataRank · unranked

8 citations

Elizaveta Ustyantseva, David R. Boyer, Aydé Mendoza‐Oliva, Mikołaj I. Kuska, Paweł M. Wydorski +7 more

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity

Structure(2024)10.1016/j.str.2024.02.015

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0DataRank · unranked

17 citations

Elizaveta Ustyantseva, David R. Boyer, Aydé Mendoza‐Oliva, Mikołaj I. Kuska, Paweł M. Wydorski +7 more

How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism

bioRxiv (Cold Spring Harbor Laboratory)(2024)10.1101/2024.03.25.586668

N/A

0DataRank · unranked

3 citations

P. Ge, M.R. Sawaya, Joshua L. Dolinsky, Yuan Yang, Yi Xiao Jiang +11 more

How short peptides can disassemble ultra-stable tau fibrils extracted from Alzheimer’s disease brain by a strain-relief mechanism

Research Square(2024)10.21203/rs.3.rs-4152095/v1

N/A

0DataRank · unranked

3 citations

Ke Hou, P. Ge, M.R. Sawaya, Joshua L. Dolinsky, Yuan Yang +11 more

How short peptides disassemble tau fibrils in Alzheimer’s disease

Nature(2025)10.1038/s41586-025-09244-z

N/A

0DataRank · unranked

17 citations

P. Ge, M.R. Sawaya, Liisa Lutter, Joshua L. Dolinsky, Yuan Yang +12 more

Structural and molecular homogeneity of ATTRv-T60A amyloid fibrils across patients and organs

Structure(2025)10.1016/j.str.2025.09.008

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0DataRank · unranked

2 citations

Binh A. Nguyen, Shumaila Afrin, Virender Singh, Bret M. Evers, John M. Shelton +15 more

Structural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment

Structure(2025)10.1016/j.str.2025.05.007

N/A

0DataRank · unranked

2 citations

M.R. Sawaya, David R. Boyer, Samantha Zink, Susanna Tovmasyan, Adrian Saucedo +6 more

How Sup35 monomer conformation and amyloid fibril polymorphism determine yeast strain phenotypes

Research Square(2025)10.21203/rs.3.rs-7945345/v1

N/A

0DataRank · unranked

0 citations

Takashi Nomura, David R. Boyer, Yusuke Komi, P. Ge, Rodrigo A. Maillard +7 more