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 controls lysosomal pathways thereby determining its own clearance and cytotoxicity
Christine Leibiger, Jana Deisel, Andreas Aufschnaiter, et al.
Human Molecular Genetics (2018) Vol. 27, Iss. 9, pp. 1593-1607
Open Access | Times Cited: 61

Showing 1-25 of 61 citing articles:

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
A. Aditya Prasad, Vidhya Bharathi, Vishwanath Sivalingam, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 636

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 emerging mechanisms and functions of microautophagy
Liming Wang, Daniel J. Klionsky, Han‐Ming Shen
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 3, pp. 186-203
Closed Access | Times Cited: 258

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

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

Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress
Annika Höhn, Antonella Tramutola, Roberta Cascella
Oxidative Medicine and Cellular Longevity (2020) Vol. 2020, pp. 1-21
Open Access | Times Cited: 141

C9orf72 ALS-FTD: recent evidence for dysregulation of the autophagy-lysosome pathway at multiple levels
Jimmy Beckers, Arun Kumar Tharkeshwar, Philip Van Damme
Autophagy (2021) Vol. 17, Iss. 11, pp. 3306-3322
Open Access | Times Cited: 88

TDP-43 pathology: From noxious assembly to therapeutic removal
Sean S. Keating, Rebecca San Gil, Molly E. V. Swanson, et al.
Progress in Neurobiology (2022) Vol. 211, pp. 102229-102229
Closed Access | Times Cited: 55

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

Pathogenic TDP-43 in amyotrophic lateral sclerosis
Zhao Zhong Chong, Nizar Souayah
Drug Discovery Today (2025), pp. 104351-104351
Open Access | Times Cited: 1

TDP-43 interacts with amyloid-β, inhibits fibrillization, and worsens pathology in a model of Alzheimer’s disease
Yao‐Hsiang Shih, Ling‐Hsien Tu, T.-Y. Chang, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 66

TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Fiona Bright, Gabriella Chan, Annika van Hummel, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 15, pp. 7781-7781
Open Access | Times Cited: 43

The endolysosomal pathway and ALS/FTD
Tiffany W. Todd, Wei Shao, Yong‐Jie Zhang, et al.
Trends in Neurosciences (2023) Vol. 46, Iss. 12, pp. 1025-1041
Closed Access | Times Cited: 18

Identification of TMEM106B amyloid fibrils provides an updated view of TMEM106B biology in health and disease
Jolien Perneel, Rosa Rademakers
Acta Neuropathologica (2022) Vol. 144, Iss. 5, pp. 807-819
Open Access | Times Cited: 27

Heat shock protein Grp78/BiP/HspA5 binds directly to TDP-43 and mitigates toxicity associated with disease pathology
Liberty François‐Moutal, David D. Scott, Andrew J. Ambrose, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 24

TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: From pathomechanisms to therapeutic strategies
Pei‐Chuan Ho, Tsung‐Chi Hsieh, Kuen‐Jer Tsai
Ageing Research Reviews (2024) Vol. 100, pp. 102441-102441
Open Access | Times Cited: 6

Calcium Dyshomeostasis and Lysosomal Ca2+ Dysfunction in Amyotrophic Lateral Sclerosis
Valentina Tedeschi, Tiziana Petrozziello, Agnese Secondo
Cells (2019) Vol. 8, Iss. 10, pp. 1216-1216
Open Access | Times Cited: 38

Application of yeast to studying amyloid and prion diseases
Yury O. Chernoff, Anastasia V. Grizel, Aleksandr A. Rubel, et al.
Advances in genetics (2020), pp. 293-380
Open Access | Times Cited: 36

Stress Granule Assembly Can Facilitate but Is Not Required for TDP-43 Cytoplasmic Aggregation
Nikita Fernandes, Luke Nero, Shawn M. Lyons, et al.
Biomolecules (2020) Vol. 10, Iss. 10, pp. 1367-1367
Open Access | Times Cited: 33

Lysosome quality control in health and neurodegenerative diseases
Veronica Ferrari, B. Tedesco, Marta Cozzi, et al.
Cellular & Molecular Biology Letters (2024) Vol. 29, Iss. 1
Open Access | Times Cited: 4

Studying Spatial Protein Quality Control, Proteopathies, and Aging Using Different Model Misfolding Proteins in S. cerevisiae
Kara L. Schneider, Thomas Nyström, Per O. Widlund
Frontiers in Molecular Neuroscience (2018) Vol. 11
Open Access | Times Cited: 34

Studying Huntington’s Disease in Yeast: From Mechanisms to Pharmacological Approaches
Sebastian J. Hofer, Katharina Kainz, Andreas Zimmermann, et al.
Frontiers in Molecular Neuroscience (2018) Vol. 11
Open Access | Times Cited: 33

Cdc48/VCP and Endocytosis Regulate TDP-43 and FUS Toxicity and Turnover
Guangbo Liu, Aaron Byrd, Amanda N. Warner, et al.
Molecular and Cellular Biology (2019) Vol. 40, Iss. 4
Open Access | Times Cited: 30

Microglial progranulin differently regulates hypothalamic lysosomal function in lean and obese conditions via cleavage-dependent mechanisms
Chae Beom Park, Chan Hee Lee, Gil Myoung Kang, et al.
Journal of Neuroinflammation (2025) Vol. 22, Iss. 1
Open Access

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