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:

Tau filaments from multiple cases of sporadic and inherited Alzheimer’s disease adopt a common fold
Benjamin Falcon, Wenjuan Zhang, Manuel Schweighauser, et al.
Acta Neuropathologica (2018) Vol. 136, Iss. 5, pp. 699-708
Open Access | Times Cited: 303

Showing 1-25 of 303 citing articles:

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules
Benjamin Falcon, Jasenko Zivanov, Wenjuan Zhang, et al.
Nature (2019) Vol. 568, Iss. 7752, pp. 420-423
Open Access | Times Cited: 629

Structure-based classification of tauopathies
Yang Shi, Wenjuan Zhang, Yang Yang, et al.
Nature (2021) Vol. 598, Iss. 7880, pp. 359-363
Open Access | Times Cited: 619

Structures of α-synuclein filaments from multiple system atrophy
Manuel Schweighauser, Yang Shi, Airi Tarutani, et al.
Nature (2020) Vol. 585, Iss. 7825, pp. 464-469
Open Access | Times Cited: 601

Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease
Hendrik Wesseling, Waltraud Mair, Mukesh Kumar, et al.
Cell (2020) Vol. 183, Iss. 6, pp. 1699-1713.e13
Open Access | Times Cited: 522

Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases
Wenjuan Zhang, Benjamin Falcon, Alexey G. Murzin, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 416

Cryo-EM structures of amyloid-β 42 filaments from human brains
Yang Yang, Diana Arseni, Wenjuan Zhang, et al.
Science (2022) Vol. 375, Iss. 6577, pp. 167-172
Open Access | Times Cited: 352

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains
Tamta Arakhamia, Christina E. Lee, Yari Carlomagno, et al.
Cell (2020) Vol. 180, Iss. 4, pp. 633-644.e12
Open Access | Times Cited: 347

Hypothesis: Tau pathology is an initiating factor in sporadic Alzheimer's disease
Amy F.T. Arnsten, Dibyadeep Datta, Kelly Del Tredici, et al.
Alzheimer s & Dementia (2020) Vol. 17, Iss. 1, pp. 115-124
Open Access | Times Cited: 273

The expanding amyloid family: Structure, stability, function, and pathogenesis
M.R. Sawaya, Michael P. Hughes, José A. Rodríguez, et al.
Cell (2021) Vol. 184, Iss. 19, pp. 4857-4873
Open Access | Times Cited: 272

Phosphorylated tau interactome in the human Alzheimer’s disease brain
Eleanor Drummond, Geoffrey Pires, Claire MacMurray, et al.
Brain (2020) Vol. 143, Iss. 9, pp. 2803-2817
Open Access | Times Cited: 264

Amyloid structure determination in RELION-3.1
Sjors H. W. Scheres
Acta Crystallographica Section D Structural Biology (2020) Vol. 76, Iss. 2, pp. 94-101
Open Access | Times Cited: 229

Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Qin Cao, David R. Boyer, M.R. Sawaya, et al.
Nature Structural & Molecular Biology (2019) Vol. 26, Iss. 7, pp. 619-627
Open Access | Times Cited: 228

Cryo-EM structures of tau filaments
Sjors H. W. Scheres, Wenjuan Zhang, Benjamin Falcon, et al.
Current Opinion in Structural Biology (2020) Vol. 64, pp. 17-25
Closed Access | Times Cited: 223

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: 206

Amyloid-beta peptide and tau protein crosstalk in Alzheimer’s disease
Sandra Villegas, AlejandroR Roda, Gabriel Serra-Mir, et al.
Neural Regeneration Research (2021) Vol. 17, Iss. 8, pp. 1666-1666
Open Access | Times Cited: 182

Amyloid structures: much more than just a cross-β fold
Rodrigo Gallardo, Neil A. Ranson, Sheena E. Radford
Current Opinion in Structural Biology (2019) Vol. 60, pp. 7-16
Open Access | Times Cited: 180

From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy
Morvane Colin, Simon Dujardin, Susanna Schraen‐Maschke, et al.
Acta Neuropathologica (2019) Vol. 139, Iss. 1, pp. 3-25
Open Access | Times Cited: 157

Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Dieter Willbold, Birgit Strodel, Gunnar F. Schröder, et al.
Chemical Reviews (2021) Vol. 121, Iss. 13, pp. 8285-8307
Open Access | Times Cited: 154

Cryo-EM structures of tau filaments from Alzheimer’s disease with PET ligand APN-1607
Yang Shi, Alexey G. Murzin, Benjamin Falcon, et al.
Acta Neuropathologica (2021) Vol. 141, Iss. 5, pp. 697-708
Open Access | Times Cited: 147

Cellular and pathological heterogeneity of primary tauopathies
Dah‐eun Chloe Chung, Shanu F. Roemer, Leonard Petrucelli, et al.
Molecular Neurodegeneration (2021) Vol. 16, Iss. 1
Open Access | Times Cited: 140

MEG3 activates necroptosis in human neuron xenografts modeling Alzheimer’s disease
Sriram Balusu, Katrien Horré, Nicola Thrupp, et al.
Science (2023) Vol. 381, Iss. 6663, pp. 1176-1182
Open Access | Times Cited: 126

Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro
Paul M. Seidler, Kevin A. Murray, David R. Boyer, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 123

Tau strains shape disease
Jaime Vaquer‐Alicea, Marc I. Diamond, Łukasz A. Joachimiak
Acta Neuropathologica (2021) Vol. 142, Iss. 1, pp. 57-71
Open Access | Times Cited: 115

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: 115

Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 12, pp. 912-933
Closed Access | Times Cited: 113

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