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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:

RNA induces unique tau strains and stabilizes Alzheimer’s disease seeds
Amy N. Zwierzchowski-Zarate, Aydé Mendoza‐Oliva, Omar M. Kashmer, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 8, pp. 102132-102132
Open Access | Times Cited: 33

Showing 1-25 of 33 citing articles:

Chronic RNA G-quadruplex accumulation in aging and Alzheimer’s disease
Lena Kallweit, Eric D. Hamlett, Hannah Saternos, et al.
eLife (2025) Vol. 14
Open Access | Times Cited: 4
A New Role for RNA G-quadruplexes in Aging and Alzheimer’s Disease
Lena Kallweit, Eric D. Hamlett, Hannah Saternos, et al.
eLife (2025) Vol. 14
Open Access | Times Cited: 2
Bioactive Compounds of the Mediterranean Diet as Nutritional Support to Fight Neurodegenerative Disease
Gianluca Antonio Franco, Livia Interdonato, Marika Cordaro, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 8, pp. 7318-7318
Open Access | Times Cited: 38
Neurodegenerative Disease Tauopathies
Benjamin C. Creekmore, Ryohei Watanabe, Edward B. Lee
Annual Review of Pathology Mechanisms of Disease (2023) Vol. 19, Iss. 1, pp. 345-370
Open Access | Times Cited: 29
Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures
Kerry Sun, Sue‐Ann Mok
Neurotherapeutics (2025), pp. e00512-e00512
Closed Access | Times Cited: 1
Nanoscale observation of heparin-mediated self-assembly of chiral tau enantiomers
Wei Chen, Yunhao Chen, Yunjiao Wang, et al.
Materials Today Physics (2024) Vol. 42, pp. 101370-101370
Closed Access | Times Cited: 6
The Role of Tau Pathology in Alzheimer’s Disease and Down Syndrome
Ann‐Charlotte Granholm, Eric D. Hamlett
Journal of Clinical Medicine (2024) Vol. 13, Iss. 5, pp. 1338-1338
Open Access | Times Cited: 5
Dysfunctional microglia and tau pathology in Alzheimer’s disease
Gunel Ayyubova
Reviews in the Neurosciences (2022) Vol. 34, Iss. 4, pp. 443-458
Closed Access | Times Cited: 20
FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation
Dailu Chen, Sofia Bali, Ruhar Singh, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 13
Aggregation, Transmission, and Toxicity of the Microtubule-Associated Protein Tau: A Complex Comprehension
Jiaxin Hu, Wenchi Sha, Shuangshuang Yuan, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 19, pp. 15023-15023
Open Access | Times Cited: 12
Disease-associated patterns of acetylation stabilize tau fibril formation
Li Li, Binh A. Nguyen, Vishruth Mullapudi, et al.
Structure (2023) Vol. 31, Iss. 9, pp. 1025-1037.e4
Open Access | Times Cited: 10
A New Role for RNA G-quadruplexes in Aging and Alzheimer’s Disease
Lena Kallweit, Eric D. Hamlett, Hannah Saternos, et al.
(2025)
Open Access
Chronic RNA G-quadruplex Accumulation in Aging and Alzheimer’s Disease
Lena Kallweit, Eric D. Hamlett, Hannah Saternos, et al.
(2025)
Open Access
Chemical Synthesis Reveals Pathogenic Role of N-Glycosylation in Microtubule-Associated Protein Tau
Wyatt C. Powell, Ruiheng Jing, Morgane Herlory, et al.
Journal of the American Chemical Society (2025)
Closed Access
A role for RNA knots in Alzheimer’s disease
Silvia Galli, Marco Di Antonio
eLife (2025) Vol. 14
Open Access
Making tau amyloid models in vitro: a crucial and underestimated challenge
Julien Broc, Clara Piersson, Yann Fichou
FEBS Letters (2025)
Open Access
Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease
Theodore J. Litberg, Scott Horowitz
ACS Chemical Biology (2024) Vol. 19, Iss. 4, pp. 809-823
Closed Access | Times Cited: 3
RNA sequestration driven by amyloid formation: the alpha synuclein case
Jakob Rupert, Michele Monti, Elsa Zacco, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 21, pp. 11466-11478
Open Access | Times Cited: 8
Cell redistribution of G quadruplex‐structured DNA is associated with morphological changes of nuclei and nucleoli in neurons during tau pathology progression
Thomas Comptdaer, Meryem Tardivel, Claire Schirmer, et al.
Brain Pathology (2024)
Open Access | Times Cited: 2
Tau seeding without tauopathy
Michael LaCroix, Efrosini Artikis, Brian D. Hitt, et al.
Journal of Biological Chemistry (2023) Vol. 300, Iss. 1, pp. 105545-105545
Open Access | Times Cited: 6
Tau, RNA, and RNA-Binding Proteins: Complex Interactions in Health and Neurodegenerative Diseases
Evan Lester, Roy Parker
The Neuroscientist (2023) Vol. 30, Iss. 4, pp. 458-472
Closed Access | Times Cited: 5
A New Role for RNA G-quadruplexes in Aging and Alzheimer’s Disease
Lena Kallweit, Eric D. Hamlett, Hannah Saternos, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
Chemical Imaging of RNA‐Tau Amyloid Fibrils at the Nanoscale Using Tip‐Enhanced Raman Spectroscopy
Gary Sean Cooney, David Talaga, Vicky Ury‐Thiery, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 50
Open Access | Times Cited: 4
Elucidating the Mechanism of Recognition and Binding of Heparin to Amyloid Fibrils of Serum Amyloid A
Conor B. Abraham, Emily Lewkowicz, Olga Gursky, et al.
Biochemistry (2024) Vol. 64, Iss. 1, pp. 266-276
Closed Access | Times Cited: 1
Tau: More than a microtubule‐binding protein in neurons
Alejandra del C. Alonso, Abdeslem El Idrissi, Robert F. Candia, et al.
Cytoskeleton (2023)
Open Access | Times Cited: 3
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