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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.

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Showing 1-25 of 113 citing articles:

Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson’s disease and other synucleinopathies
Pedro Magalhães, Hilal A. Lashuel
npj Parkinson s Disease (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 92
Oxidative damage in neurodegeneration: roles in the pathogenesis and progression of Alzheimer disease
Marzia Perluigi, Fabio Di Domenico, D. Allan Butterfield
Physiological Reviews (2023) Vol. 104, Iss. 1, pp. 103-197
Closed Access | Times Cited: 71
Heterotypic electrostatic interactions control complex phase separation of tau and prion into multiphasic condensates and co-aggregates
K. Sandeep, Roopali Khanna, Anamika Avni, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 2
Open Access | Times Cited: 44
Mitochondria in Alzheimer’s Disease Pathogenesis
Allison B. Reiss, Shelly Gulkarov, Benna Jacob, et al.
Life (2024) Vol. 14, Iss. 2, pp. 196-196
Open Access | Times Cited: 25
Quercetin-functionalized nanomaterials: Innovative therapeutic avenues for Alzheimer's disease management
Jinjin Pei, Ranil Vikraman Kumarasamy, Selvaraj Jayaraman, et al.
Ageing Research Reviews (2025), pp. 102665-102665
Closed Access | Times Cited: 3
Targeting protein kinases for the treatment of Alzheimer's disease: Recent progress and future perspectives
Zhijia Li, Bo Yin, Shuangqian Zhang, et al.
European Journal of Medicinal Chemistry (2023) Vol. 261, pp. 115817-115817
Closed Access | Times Cited: 29
Chemical Features of Polyanions Modulate Tau Aggregation and Conformational States
Kelly M. Montgomery, Emma C. Carroll, Aye C. Thwin, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 7, pp. 3926-3936
Open Access | Times Cited: 25
Sensitive label-free detection of the biomarker phosphorylated tau−217 protein in Alzheimer's disease using a graphene-based solution-gated field effect transistor
Sian-Hong Ciou, Ao-Ho Hsieh, Yu-Xiu Lin, et al.
Biosensors and Bioelectronics (2023) Vol. 228, pp. 115174-115174
Closed Access | Times Cited: 24
Alzheimer's disease: The role of proteins in formation, mechanisms, and new therapeutic approaches
Amirreza Gholami
Neuroscience Letters (2023) Vol. 817, pp. 137532-137532
Closed Access | Times Cited: 22
Nasal tau immunotherapy clears intracellular tau pathology and improves cognitive functions in aged tauopathy mice
Sagar Gaikwad, Nicha Puangmalai, Minal Sonawane, et al.
Science Translational Medicine (2024) Vol. 16, Iss. 754
Closed Access | Times Cited: 10
Hydrogen-Bonded Network of Water in Phase-Separated Biomolecular Condensates
Ashish Joshi, Anamika Avni, Anuja Walimbe, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 30, pp. 7724-7734
Closed Access | Times Cited: 10
Exploring the clinical transition of engineered exosomes designed for intracellular delivery of therapeutic proteins
Minseong Kim, Hojun Choi, Deok-Jin Jang, et al.
Stem Cells Translational Medicine (2024) Vol. 13, Iss. 7, pp. 637-647
Open Access | Times Cited: 9
Current Progress and Future Directions in Non-Alzheimer’s Disease Tau PET Tracers
Hendris Wongso, Ryuichi Harada, Shozo Furumoto
ACS Chemical Neuroscience (2025) Vol. 16, Iss. 2, pp. 111-127
Closed Access | Times Cited: 1
Phosphorylation of Tau R2 Repeat Destabilizes Its Binding to Microtubules: A Molecular Dynamics Simulation Study
Viet Hoang Man, Xibing He, Jie Gao, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 3, pp. 458-467
Open Access | Times Cited: 20
Nature's toolbox against tau aggregation: An updated review of current research
Sumaiya Khan, Md. Imtaiyaz Hassan, Mohammad Shahid, et al.
Ageing Research Reviews (2023) Vol. 87, pp. 101924-101924
Closed Access | Times Cited: 18
Tau–RNA complexes inhibit microtubule polymerization and drive disease-relevant conformation change
Pamela J. McMillan, Sarah J. Benbow, Rikki L. Uhrich, et al.
Brain (2023) Vol. 146, Iss. 8, pp. 3206-3220
Open Access | Times Cited: 17
Neuroprotective Roles of the Biliverdin Reductase-A/Bilirubin Axis in the Brain
Bindu D. Paul, Andrew A. Pieper
Biomolecules (2024) Vol. 14, Iss. 2, pp. 155-155
Open Access | Times Cited: 7
Post-Translational Modifications in Tau and Their Roles in Alzheimer's Pathology
Subha Kalyaanamoorthy, Stanley Opare, Xiaoxiao Xu, et al.
Current Alzheimer Research (2024) Vol. 21, Iss. 1, pp. 24-49
Closed Access | Times Cited: 6
Electrochemical Monitoring of Real‐Time Vesicle Dynamics Induced by Tau in a Confined Nanopipette
Kele Chen, Ru‐Jia Yu, Cheng-Bing Zhong, et al.
Angewandte Chemie International Edition (2024)
Closed Access | Times Cited: 6
Tau protein quantification in skin biopsies differentiates tauopathies from alpha-synucleinopathies
Elena Vacchi, Edoardo Lazzarini, Sandra Pinton, et al.
Brain (2022) Vol. 145, Iss. 8, pp. 2755-2768
Open Access | Times Cited: 24
Portable Vertical Graphene@Au-Based Electrochemical Aptasensing Platform for Point-of-Care Testing of Tau Protein in the Blood
Yibiao Liu, Xingyun Liu, Mifang Li, et al.
Biosensors (2022) Vol. 12, Iss. 8, pp. 564-564
Open Access | Times Cited: 24
An inhibitor with GSK3β and DYRK1A dual inhibitory properties reduces Tau hyperphosphorylation and ameliorates disease in models of Alzheimer's disease
Xin Liu, Lingyun Lai, Jiang-xia Chen, et al.
Neuropharmacology (2023) Vol. 232, pp. 109525-109525
Closed Access | Times Cited: 15
Phosphorylation at Ser289 Enhances the Oligomerization of Tau Repeat R2
Viet Hoang Man, Xibing He, Fengyang Han, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 4, pp. 1351-1361
Open Access | Times Cited: 13
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
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: 5
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