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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:

Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43
Anukool A. Bhopatkar, Vladimir N. Uversky, Vijayaraghavan Rangachari
Journal of Biological Chemistry (2020) Vol. 295, Iss. 8, pp. 2506-2519
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 384
Fluid biomarkers in frontotemporal dementia: past, present and future
Imogen J. Swift, Aitana Sogorb‐Esteve, Carolin Heller, et al.
Journal of Neurology Neurosurgery & Psychiatry (2020) Vol. 92, Iss. 2, pp. 204-215
Open Access | Times Cited: 102
Liquid–liquid phase separation of tau: From molecular biophysics to physiology and disease
K. Sandeep, Adriana Savastano, Priyanka Singh, et al.
Protein Science (2021) Vol. 30, Iss. 7, pp. 1294-1314
Open Access | Times Cited: 93
Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils
Shailendra Dhakal, Courtney E. Wyant, Hannah E. George, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 10, pp. 166953-166953
Open Access | Times Cited: 58
Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau
Pablo Gracia, David Polanco, Jorge Tarancón-Díez, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 52
Secreted Chaperones in Neurodegeneration
Kriti Chaplot, Timothy S. Jarvela, Iris Lindberg
Frontiers in Aging Neuroscience (2020) Vol. 12
Open Access | Times Cited: 57
TDP-43 condensates and lipid droplets regulate the reactivity of microglia and regeneration after traumatic brain injury
Alessandro Zambusi, Klara Tereza Novoselc, Saskia Hutten, et al.
Nature Neuroscience (2022) Vol. 25, Iss. 12, pp. 1608-1625
Closed Access | Times Cited: 37
Peptide-based coacervates in therapeutic applications
Lilusi Ma, Xiaocui Fang, Chen Wang
Frontiers in Bioengineering and Biotechnology (2023) Vol. 10
Open Access | Times Cited: 17
Synaptopathy: presynaptic convergence in frontotemporal dementia and amyotrophic lateral sclerosis
Emma L. Clayton, Laura Huggon, Michael A. Cousin, et al.
Brain (2024) Vol. 147, Iss. 7, pp. 2289-2307
Open Access | Times Cited: 7
Progranulin in neurodegenerative dementia
Xiaoming Wang, Peng Zeng, Ying‐Yan Fang, et al.
Journal of Neurochemistry (2021) Vol. 158, Iss. 2, pp. 119-137
Open Access | Times Cited: 30
The pathogenic mechanism of TAR DNA-binding protein 43 (TDP-43) in amyotrophic lateral sclerosis
Xinxin Wang, Yushu Hu, Renshi Xu
Neural Regeneration Research (2023) Vol. 19, Iss. 4, pp. 800-806
Open Access | Times Cited: 13
Progranulin haploinsufficiency mediates cytoplasmic TDP-43 aggregation with lysosomal abnormalities in human microglia
Wonjae Sung, Min‐Young Noh, Minyeop Nahm, et al.
Journal of Neuroinflammation (2024) Vol. 21, Iss. 1
Open Access | Times Cited: 5
Charge and redox states modulate granulin—TDP-43 coacervation toward phase separation or aggregation
Anukool A. Bhopatkar, Shailendra Dhakal, Hannah G. Abernathy, et al.
Biophysical Journal (2022) Vol. 121, Iss. 11, pp. 2107-2126
Open Access | Times Cited: 19
Shapeshifter TDP-43: Molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators
Abhilasha A. Doke, Santosh Kumar Jha
Biophysical Chemistry (2023) Vol. 295, pp. 106972-106972
Closed Access | Times Cited: 10
Surface hydrophobic clusters modulate the folding stability and molecular recognition of the disintegrin Jarastatin
Ariana A. Vasconcelos, Russolina B. Zingali, Fábio C. L. Almeida
Journal of Biological Chemistry (2025), pp. 108294-108294
Closed Access
Targeting redox-sensitive MBD2–NuRD condensate in cancer cells
Heyang Wei, Hongdan Zheng, Siqing Wang, et al.
Nature Cell Biology (2025)
Closed Access
FTLD‐TDP assemblies seed neoaggregates with subtype‐specific features via a prion‐like cascade
Pierre De Rossi, Amanda J. Lewis, Johanna Furrer, et al.
EMBO Reports (2021) Vol. 22, Iss. 12
Open Access | Times Cited: 22
In silico design of Mycobacterium tuberculosis multi-epitope adhesin protein vaccines
Koobashnee Pillay, Thamsanqa E. Chiliza, Sibusiso Senzani, et al.
Heliyon (2024) Vol. 10, Iss. 18, pp. e37536-e37536
Open Access | Times Cited: 3
Roles of intrinsically disordered protein regions in transcriptional regulation and genome organization
Jiapei Miao, Shasha Chong
Current Opinion in Genetics & Development (2024) Vol. 90, pp. 102285-102285
Closed Access | Times Cited: 3
Protein phase separation and its role in chromatin organization and diseases
Jiaqi Li, Yao Zhang, Xi Chen, et al.
Biomedicine & Pharmacotherapy (2021) Vol. 138, pp. 111520-111520
Open Access | Times Cited: 17
Heterotypic liquid-liquid phase separation of tau and α-synuclein: Implications for overlapping neuropathologies
Nahuel N. Foressi, Leandro Cruz Rodríguez, M. Soledad Celej
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2023) Vol. 1871, Iss. 6, pp. 140950-140950
Closed Access | Times Cited: 7
Identifying and Diagnosing TDP-43 Neurodegenerative Diseases in Psychiatry
Simon Ducharme, Yolande A.L. Pijnenburg, Jonathan D. Rohrer, et al.
American Journal of Geriatric Psychiatry (2023) Vol. 32, Iss. 1, pp. 98-113
Open Access | Times Cited: 7
Reversible Disulfide Bond Cross-Links as Tunable Levers of Phase Separation in Designer Biomolecular Condensates
Malay Mondal, Penelope E. Jankoski, L. Lee, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 36, pp. 25299-25311
Open Access | Times Cited: 2
The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils
Hung-Ming Chien, Chi-Chang Lee, Joseph Jen‐Tse Huang
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 15, pp. 8213-8213
Open Access | Times Cited: 13
Tryptophan Probes of TDP-43 C-Terminal Domain Amyloid Formation
Sydney O. Shuster, Jennifer C. Lee
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 15, pp. 3781-3789
Open Access | Times Cited: 8
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