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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:

TDP-43 regulation of stress granule dynamics in neurodegenerative disease-relevant cell types
Yousra Khalfallah, Rachel Kuta, Camille Grasmuck, et al.
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 142

Showing 1-25 of 142 citing articles:

Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death
F. Gasset-Rosa, Shan Lu, Haiyang Yu, et al.
Neuron (2019) Vol. 102, Iss. 2, pp. 339-357.e7
Open Access | Times Cited: 442
The role of TDP-43 mislocalization in amyotrophic lateral sclerosis
Terry R. Suk, Maxime W.C. Rousseaux
Molecular Neurodegeneration (2020) Vol. 15, Iss. 1
Open Access | Times Cited: 304
The Overlapping Genetics of Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Yevgeniya Abramzon, Pietro Fratta, Bryan J. Traynor, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 203
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: 183
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
Amyotrophic lateral sclerosis: translating genetic discoveries into therapies
Fulya Akçimen, Elia R. Lopez, John E. Landers, et al.
Nature Reviews Genetics (2023) Vol. 24, Iss. 9, pp. 642-658
Open Access | Times Cited: 115
Axonal TDP-43 condensates drive neuromuscular junction disruption through inhibition of local synthesis of nuclear encoded mitochondrial proteins
Topaz Altman, Ariel Ionescu, Amjad Ibraheem, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 109
Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases
Jenny L. Carey, Lin Guo
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 103
Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion
Maura E. Charette, Carolyn Rosenblum, Olivia Shade, et al.
Chemical Reviews (2025)
Open Access | Times Cited: 2
Cytoplasmic functions of TDP-43 and FUS and their role in ALS
Nicol Birsa, Matthew P. Bentham, Pietro Fratta
Seminars in Cell and Developmental Biology (2019) Vol. 99, pp. 193-201
Open Access | Times Cited: 106
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: 85
Sexually dimorphic RNA helicases DDX3X and DDX3Y differentially regulate RNA metabolism through phase separation
Hui Shen, Amber Yanas, Michael C. Owens, et al.
Molecular Cell (2022) Vol. 82, Iss. 14, pp. 2588-2603.e9
Open Access | Times Cited: 64
Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration
Tomohiro Nakamura, Chang-ki Oh, Xu Zhang, et al.
Free Radical Biology and Medicine (2021) Vol. 172, pp. 562-577
Open Access | Times Cited: 60
Emerging Therapies and Novel Targets for TDP-43 Proteinopathy in ALS/FTD
Lindsey R. Hayes, Petr Kaláb
Neurotherapeutics (2022) Vol. 19, Iss. 4, pp. 1061-1084
Open Access | Times Cited: 43
Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43
Sean S. Keating, Adekunle T. Bademosi, Rebecca San Gil, et al.
Cellular and Molecular Life Sciences (2023) Vol. 80, Iss. 4
Open Access | Times Cited: 33
Friend or foe: The role of stress granule in neurodegenerative disease
Qinqin Cui, Zhongyi Liu, Ge Bai
Neuron (2024) Vol. 112, Iss. 15, pp. 2464-2485
Closed Access | Times Cited: 15
Copper toxicity and deficiency: the vicious cycle at the core of protein aggregation in ALS
Jin Hong Min, Heela Sarlus, Robert A. Harris
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access | Times Cited: 9
Stress granule formation helps to mitigate neurodegeneration
M. Rebecca Glineburg, Evrim Yildirim, Nicolás Gómez, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 16, pp. 9745-9759
Open Access | Times Cited: 9
Graphene Quantum Dots Attenuate TDP-43 Proteinopathy in Amyotrophic Lateral Sclerosis
Na-Young Park, Yunseok Heo, Ji Won Yang, et al.
ACS Nano (2025)
Closed Access | Times Cited: 1
A stress-dependent TDP-43 SUMOylation program preserves neuronal function
Terry R. Suk, Caroline E. Part, Jenny L. Zhang, et al.
Molecular Neurodegeneration (2025) Vol. 20, Iss. 1
Open Access | Times Cited: 1
Pathogenic TDP-43 in amyotrophic lateral sclerosis
Zhao Zhong Chong, Nizar Souayah
Drug Discovery Today (2025), pp. 104351-104351
Open Access | Times Cited: 1
Glial Cells—The Strategic Targets in Amyotrophic Lateral Sclerosis Treatment
Tereza Filipi, Zuzana Heřmanová, Jana Turečková, et al.
Journal of Clinical Medicine (2020) Vol. 9, Iss. 1, pp. 261-261
Open Access | Times Cited: 70
Selective Autophagy Receptors in Neuronal Health and Disease
Owen Conway, Hafize Aysin Akpinar, Vladimir V. Rogov, et al.
Journal of Molecular Biology (2019) Vol. 432, Iss. 8, pp. 2483-2509
Closed Access | Times Cited: 64
Traffic jam at the nuclear pore: All roads lead to nucleocytoplasmic transport defects in ALS/FTD
Claudia Fallini, Bilal Khalil, Courtney L. Smith, et al.
Neurobiology of Disease (2020) Vol. 140, pp. 104835-104835
Open Access | Times Cited: 63
Small Molecule Targeting TDP-43’s RNA Recognition Motifs Reduces Locomotor Defects in a Drosophila Model of Amyotrophic Lateral Sclerosis (ALS)
Liberty François‐Moutal, Razaz Felemban, David D. Scott, et al.
ACS Chemical Biology (2019) Vol. 14, Iss. 9, pp. 2006-2013
Open Access | Times Cited: 60
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