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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:

Pathomechanisms of TDP‐43 in neurodegeneration
Ju Gao, Luwen Wang, Mikayla L. Huntley, et al.
Journal of Neurochemistry (2018) Vol. 146, Iss. 1, pp. 7-20
Open Access | Times Cited: 203

Showing 1-25 of 203 citing articles:

TDP-43 proteinopathies: a new wave of neurodegenerative diseases
Eva M. J. de Boer, Viyanti K Orie, Timothy L. Williams, et al.
Journal of Neurology Neurosurgery & Psychiatry (2020) Vol. 92, Iss. 1, pp. 86-95
Open Access | Times Cited: 276
Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation
W. Michael Babinchak, Witold K. Surewicz
Journal of Molecular Biology (2020) Vol. 432, Iss. 7, pp. 1910-1925
Open Access | Times Cited: 231
Microglial phagocytosis of neurons in neurodegeneration, and its regulation
Claire A. Butler, Alma S. Popescu, Emily J. A. Kitchener, et al.
Journal of Neurochemistry (2021) Vol. 158, Iss. 3, pp. 621-639
Open Access | Times Cited: 196
TDP-43 Pathology in Alzheimer’s Disease
Axel Meneses, Shunsuke Koga, Justin O’Leary, et al.
Molecular Neurodegeneration (2021) Vol. 16, Iss. 1
Open Access | Times Cited: 182
Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Paraskevi Tziortzouda, Ludo Van Den Bosch, Frank Hirth
Nature reviews. Neuroscience (2021) Vol. 22, Iss. 4, pp. 197-208
Closed Access | Times Cited: 171
Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis
Jessica Root, Paola Merino, Austin Nuckols, et al.
Neurobiology of Disease (2021) Vol. 154, pp. 105360-105360
Open Access | Times Cited: 165
Neurodegenerative Disease and the NLRP3 Inflammasome
Jonathan Holbrook, Heledd Jarosz-Griffiths, Emily A. Caseley, et al.
Frontiers in Pharmacology (2021) Vol. 12
Open Access | Times Cited: 149
Progranulin as a therapeutic target in neurodegenerative diseases
Hervé Rhinn, Nadine Tatton, Stella McCaughey, et al.
Trends in Pharmacological Sciences (2022) Vol. 43, Iss. 8, pp. 641-652
Open Access | Times Cited: 123
Neurodegenerative disorders: Mechanisms of degeneration and therapeutic approaches with their clinical relevance
Dnyandev Gadhave, Vrashabh V. Sugandhi, Saurav Kumar Jha, et al.
Ageing Research Reviews (2024) Vol. 99, pp. 102357-102357
Open Access | Times Cited: 33
Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
Luke McAlary, Steven S. Plotkin, Justin J. Yerbury, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 136
Extracellular Vesicle as a Source of Alzheimer’s Biomarkers: Opportunities and Challenges
Seongju Lee, Sakulrat Mankhong, Ju‐Hee Kang
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 7, pp. 1728-1728
Open Access | Times Cited: 106
Nuclear accumulation of CHMP7 initiates nuclear pore complex injury and subsequent TDP-43 dysfunction in sporadic and familial ALS
Alyssa N. Coyne, Victoria Baskerville, Benjamin L. Zaepfel, et al.
Science Translational Medicine (2021) Vol. 13, Iss. 604
Open Access | Times Cited: 101
Proteomics in cerebrospinal fluid and spinal cord suggests UCHL1, MAP2 and GPNMB as biomarkers and underpins importance of transcriptional pathways in amyotrophic lateral sclerosis
Patrick Oeckl, Patrick Weydt, Dietmar Rudolf Thal, et al.
Acta Neuropathologica (2019) Vol. 139, Iss. 1, pp. 119-134
Closed Access | Times Cited: 98
Impaired NHEJ repair in amyotrophic lateral sclerosis is associated with TDP-43 mutations
Anna Konopka, Donna R. Whelan, Md Shafi Jamali, et al.
Molecular Neurodegeneration (2020) Vol. 15, Iss. 1
Open Access | Times Cited: 83
Physiological and pathological functions of TMEM106B: a gene associated with brain aging and multiple brain disorders
Tuancheng Feng, Alexander Lacrampe, Fenghua Hu
Acta Neuropathologica (2021) Vol. 141, Iss. 3, pp. 327-339
Open Access | Times Cited: 76
TDP-43 and Tau Oligomers in Alzheimer's Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia
Mauro Montalbano, Salomé McAllen, Filippa Lo Cascio, et al.
Neurobiology of Disease (2020) Vol. 146, pp. 105130-105130
Open Access | Times Cited: 73
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD
Alistair Wood, Yuval Gurfinkel, Nicole Polain, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 9, pp. 4705-4705
Open Access | Times Cited: 70
Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43
Jorge García Morato, Friederike Hans, Felix von Zweydorf, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 67
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
The Role of TDP-43 in Neurodegenerative Disease
Yan-Zhe Liao, Jing Ma, Jie-Zhi Dou
Molecular Neurobiology (2022) Vol. 59, Iss. 7, pp. 4223-4241
Closed Access | Times Cited: 53
RNA binding proteins (RBPs) and their role in DNA damage and radiation response in cancer
Meghna Mehta, Rajeswari Raguraman, Rajagopal Ramesh, et al.
Advanced Drug Delivery Reviews (2022) Vol. 191, pp. 114569-114569
Open Access | Times Cited: 39
Astrocytic TDP-43 dysregulation impairs memory by modulating antiviral pathways and interferon-inducible chemokines
Avital Licht-Murava, Samantha M. Meadows, Fernando Palaguachi, et al.
Science Advances (2023) Vol. 9, Iss. 16
Open Access | Times Cited: 27
Limbic-predominant age-related TDP43 encephalopathy (LATE) neuropathological change in neurodegenerative diseases
Sukriti Nag, Julie A. Schneider
Nature Reviews Neurology (2023) Vol. 19, Iss. 9, pp. 525-541
Closed Access | Times Cited: 25
Ergothioneine promotes longevity and healthy aging in male mice
Makoto Katsube, Takahiro Ishimoto, Yutaro Fukushima, et al.
GeroScience (2024) Vol. 46, Iss. 4, pp. 3889-3909
Open Access | Times Cited: 12
Endothelial TDP-43 controls sprouting angiogenesis and vascular barrier integrity, and its deletion triggers neuroinflammation
Víctor Arribas, Yara Onetti, Marina Ramiro‐Pareta, et al.
JCI Insight (2024)
Open Access | Times Cited: 11
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