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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:

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: 348

Showing 1-25 of 348 citing articles:

The molecular basis for cellular function of intrinsically disordered protein regions
Alex S. Holehouse, Birthe B. Kragelund
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 187-211
Open Access | Times Cited: 227
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
Age-dependent formation of TMEM106B amyloid filaments in human brains
Manuel Schweighauser, Diana Arseni, Mehtap Bacioglu, et al.
Nature (2022) Vol. 605, Iss. 7909, pp. 310-314
Open Access | Times Cited: 142
Alzheimer's disease: From immunotherapy to immunoprevention
Mathias Jucker, Lary C. Walker
Cell (2023) Vol. 186, Iss. 20, pp. 4260-4270
Open Access | Times Cited: 125
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
2.7 Å cryo-EM structure of ex vivo RML prion fibrils
Szymon W. Manka, Wenjuan Zhang, Adam Wenborn, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 107
If amyloid drives Alzheimer disease, why have anti-amyloid therapies not yet slowed cognitive decline?
Christian Haass, Dennis J. Selkoe
PLoS Biology (2022) Vol. 20, Iss. 7, pp. e3001694-e3001694
Open Access | Times Cited: 107
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: 105
Conformational strains of pathogenic amyloid proteins in neurodegenerative diseases
Dan Li, Cong Liu
Nature reviews. Neuroscience (2022) Vol. 23, Iss. 9, pp. 523-534
Closed Access | Times Cited: 75
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
Is Alzheimer disease a disease?
Amos D. Korczyn, Lea T. Grinberg
Nature Reviews Neurology (2024) Vol. 20, Iss. 4, pp. 245-251
Closed Access | Times Cited: 65
Cryo-EM structures of amyloid-β filaments with the Arctic mutation (E22G) from human and mouse brains
Yang Yang, Wenjuan Zhang, Alexey G. Murzin, et al.
Acta Neuropathologica (2023) Vol. 145, Iss. 3, pp. 325-333
Open Access | Times Cited: 50
Iatrogenic Alzheimer’s disease in recipients of cadaveric pituitary-derived growth hormone
Gargi Banerjee, Simon F. Farmer, Harpreet Hyare, et al.
Nature Medicine (2024)
Open Access | Times Cited: 47
Abundant Aβ fibrils in ultracentrifugal supernatants of aqueous extracts from Alzheimer’s disease brains
Andrew M. Stern, Yang Yang, Shan‐Xue Jin, et al.
Neuron (2023) Vol. 111, Iss. 13, pp. 2012-2020.e4
Open Access | Times Cited: 44
Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
Dillon J. Rinauro, Fabrizio Chiti, Michele Vendruscolo, et al.
Molecular Neurodegeneration (2024) Vol. 19, Iss. 1
Open Access | Times Cited: 43
Molecular Crowding: The History and Development of a Scientific Paradigm
Caterina Alfano, Yann Fichou, Klaus Huber, et al.
Chemical Reviews (2024) Vol. 124, Iss. 6, pp. 3186-3219
Open Access | Times Cited: 37
Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy
Binh A. Nguyen, Virender Singh, Shumaila Afrin, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 31
Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy
Qiuyang Zheng, Xin Wang
Protein & Cell (2024)
Open Access | Times Cited: 24
CryoET of β-amyloid and tau within postmortem Alzheimer’s disease brain
Madeleine A. G. Gilbert, Nayab Fatima, Joshua Jenkins, et al.
Nature (2024) Vol. 631, Iss. 8022, pp. 913-919
Open Access | Times Cited: 22
Cryo-EM structures of amyloid-β and tau filaments in Down syndrome
Anllely Fernández, Md Rejaul Hoq, Grace I. Hallinan, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 6, pp. 903-909
Open Access | Times Cited: 18
Ultrastructure of human brain tissue vitrified from autopsy revealed by cryo-ET with cryo-plasma FIB milling
Benjamin C. Creekmore, Kathryn Kixmoeller, Ben E. Black, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
Human and mouse proteomics reveals the shared pathways in Alzheimer’s disease and delayed protein turnover in the amyloidome
Jay M. Yarbro, Xian Han, Abhijit Dasgupta, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2
The 3D structure of lipidic fibrils of α-synuclein
Benedikt Frieg, Leif Antonschmidt, Christian Dienemann, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 65
Medin co-aggregates with vascular amyloid-β in Alzheimer’s disease
Jessica Wagner, Karoline Degenhardt, Marleen Veit, et al.
Nature (2022) Vol. 612, Iss. 7938, pp. 123-131
Open Access | Times Cited: 62
Current Concepts of Mixed Pathologies in Neurodegenerative Diseases
Shelley L. Forrest, Gábor G. Kovács
Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques (2022) Vol. 50, Iss. 3, pp. 329-345
Open Access | Times Cited: 57
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