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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

High-throughput cryo-EM structure determination of amyloids
Sofia Lövestam, Sjors H. W. Scheres
Faraday Discussions (2022) Vol. 240, pp. 243-260
Open Access | Times Cited: 46

Showing 1-25 of 46 citing articles:

Assembly of recombinant tau into filaments identical to those of Alzheimer’s disease and chronic traumatic encephalopathy
Sofia Lövestam, Fujiet Adrian Koh, Bart van Knippenberg, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 203
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Sjors H. W. Scheres, Benjamin Falcon, Michel Goedert
Nature (2023) Vol. 621, Iss. 7980, pp. 701-710
Closed Access | Times Cited: 110
Disease-specific tau filaments assemble via polymorphic intermediates
Sofia Lövestam, David Li, Jane L. Wagstaff, et al.
Nature (2023) Vol. 625, Iss. 7993, pp. 119-125
Open Access | Times Cited: 74
Cryo-EM of prion strains from the same genotype of host identifies conformational determinants
Forrest Hoyt, Parvez Alam, Efrosini Artikis, et al.
PLoS Pathogens (2022) Vol. 18, Iss. 11, pp. e1010947-e1010947
Open Access | Times Cited: 39
New Pathways Identify Novel Drug Targets for the Prevention and Treatment of Alzheimer’s Disease
Botond Penke, Mária Szűcs, Ferenc Bogár
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 6, pp. 5383-5383
Open Access | Times Cited: 23
Cryo-EM structure of Alzheimer’s disease tau filaments with PET ligand MK-6240
Peter Kunach, Jaime Vaquer‐Alicea, Matthew S. Smith, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 14
Twelve phosphomimetic mutations induce the assembly of recombinant full-length human tau into paired helical filaments
Sofia Lövestam, Jane L. Wagstaff, Panagiotis Katsinelos, et al.
(2025)
Open Access | Times Cited: 1
Structural insights into the role of reduced cysteine residues in SOD1 amyloid filament formation
Yeongjin Baek, Hyunmin Kim, Dukwon Lee, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 5
Open Access | Times Cited: 1
Cryo-EM structure of Alzheimer’s disease tau filaments with PET ligand MK-6240
Peter Kunach, Jaime Vaquer‐Alicea, Matthew S. Smith, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 17
Structure of the nonhelical filament of the Alzheimer’s disease tau core
Pu Duan, Aurelio J. Dregni, Nadia El Mammeri, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 44
Open Access | Times Cited: 17
Alzheimer’s disease seeded tau forms paired helical filaments yet lacks seeding potential
Pu Duan, Aurelio J. Dregni, Hong Xu, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 9, pp. 107730-107730
Open Access | Times Cited: 8
Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer
Parvez Alam, Forrest Hoyt, Efrosini Artikis, et al.
Acta Neuropathologica (2024) Vol. 148, Iss. 1
Open Access | Times Cited: 7
Disease-specific tau filaments assemble via polymorphic intermediates
Sofia Lövestam, David Li, Jane L. Wagstaff, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13
Mutations in human prion-like domains: pathogenic but not always amyloidogenic
Andrea Bartolomé-Nafría, Javier García‐Pardo, Salvador Ventura
Prion (2024) Vol. 18, Iss. 1, pp. 28-39
Open Access | Times Cited: 4
Mimicking kidney flow shear efficiently induces aggregation of LECT2, a protein involved in renal amyloidosis
Jeung‐Hoi Ha, Yikang Xu, Harsimranjit Sekhon, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 5, pp. 107231-107231
Open Access | Times Cited: 4
In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils
Shoyab Ansari, Dominique Lagasca, Rania Dumarieh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Twelve phosphomimetic mutations induce the assembly of recombinant full-length human tau into paired helical filaments
Sofia Lövestam, Jane L. Wagstaff, Panagiotis Katsinelos, et al.
(2025)
Open Access
Functional classification of tauopathy strains reveals the role of protofilament core residues
Jaime Vaquer‐Alicea, V Manon, Vaibhav Bommareddy, et al.
Science Advances (2025) Vol. 11, Iss. 4
Open Access
Cotadutide reversible self-assembly based long-acting injectable depot for sustained delivery of GLP-1 glucagon receptor agonists with controlled burst release
Bin Yang, Durga Devalla, Silvia Sonzini, et al.
Journal of Controlled Release (2025) Vol. 380, pp. 647-663
Closed Access
Structural and Functional Versatility of the Amyloidogenic Antimicrobial Peptide Citropin 1.3
Fabio Strati, Mariana P. Cali, Yehudi Bloch, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Artificial intelligence and deep learning in electron microscopy
Kevin P. Treder, Chen Huang, Judy S. Kim, et al.
Advances in imaging and electron physics (2025)
Closed Access
Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms
Xian Xia, Michelle M. Shimogawa, Hui Wang, et al.
Science (2025) Vol. 387, Iss. 6739
Closed Access
Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins
Alexander Stevens, S. K. Kashyap, Ethan Crofut, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Cryo-EM structures of functional and pathological amyloid ribonucleoprotein assemblies
Javier García‐Pardo, Salvador Ventura
Trends in Biochemical Sciences (2023) Vol. 49, Iss. 2, pp. 119-133
Open Access | Times Cited: 10
Cryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research
Tiffany W. Todd, Naeyma N. Islam, Casey Cook, et al.
Neuron (2024) Vol. 112, Iss. 14, pp. 2269-2288
Closed Access | Times Cited: 3
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