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:

Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins
Antonia Ratti, Emanuele Buratti
Journal of Neurochemistry (2016) Vol. 138, Iss. S1, pp. 95-111
Open Access | Times Cited: 325

Showing 1-25 of 325 citing articles:

Pathology of Neurodegenerative Diseases
Brittany N. Dugger, Dennis W. Dickson
Cold Spring Harbor Perspectives in Biology (2017) Vol. 9, Iss. 7, pp. a028035-a028035
Open Access | Times Cited: 1300

Amyotrophic lateral sclerosis
Orla Hardiman, Ammar Al‐Chalabi, Adriano Chiò, et al.
Nature Reviews Disease Primers (2017) Vol. 3, Iss. 1
Open Access | Times Cited: 1110

ALS Genetics, Mechanisms, and Therapeutics: Where Are We Now?
Rita Mejzini, Loren L. Flynn, Ianthe Pitout, et al.
Frontiers in Neuroscience (2019) Vol. 13
Open Access | Times Cited: 658

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

FUS and TDP-43 Phases in Health and Disease
Bede Portz, Bo Lim Lee, James Shorter
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 7, pp. 550-563
Open Access | Times Cited: 230

TDP-43 induces mitochondrial damage and activates the mitochondrial unfolded protein response
Peng Wang, Jianwen Deng, Jie Dong, et al.
PLoS Genetics (2019) Vol. 15, Iss. 5, pp. e1007947-e1007947
Open Access | Times Cited: 227

Genetic mutations in RNA-binding proteins and their roles in ALS
Katannya Kapeli, Fernando J. Martínez, G Yeo
Human Genetics (2017) Vol. 136, Iss. 9, pp. 1193-1214
Open Access | Times Cited: 190

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
Lara A. Gruijs da Silva, Francesca Simonetti, Saskia Hutten, et al.
The EMBO Journal (2022) Vol. 41, Iss. 8
Open Access | Times Cited: 128

Antisense Oligonucleotides for the Study and Treatment of ALS
Benjamin D. Boros, Kathleen M. Schoch, Collin J. Kreple, et al.
Neurotherapeutics (2022) Vol. 19, Iss. 4, pp. 1145-1158
Open Access | Times Cited: 73

Emerging regulatory mechanisms and functions of biomolecular condensates: implications for therapeutic targets
Soyoung Jeon, Yong‐Duck Chung, Jae‐Sung Lim, et al.
Signal Transduction and Targeted Therapy (2025) Vol. 10, Iss. 1
Open Access | Times Cited: 3

The roles of intrinsically disordered proteins in neurodegeneration
Kagistia Hana Utami, Satoru Morimoto, Yasue Mitsukura, et al.
Biochimica et Biophysica Acta (BBA) - General Subjects (2025), pp. 130772-130772
Open Access | Times Cited: 2

Gene-specific mitochondria dysfunctions in human TARDBP and C9ORF72 fibroblasts
Elisa Onesto, Claudia Colombrita, Valentina Gumina, et al.
Acta Neuropathologica Communications (2016) Vol. 4, Iss. 1
Open Access | Times Cited: 158

TDP‐43 and FUS en route from the nucleus to the cytoplasm
Helena Ederle, Dorothee Dormann
FEBS Letters (2017) Vol. 591, Iss. 11, pp. 1489-1507
Open Access | Times Cited: 150

TDP-43 post-translational modifications in health and disease
Emanuele Buratti
Expert Opinion on Therapeutic Targets (2018) Vol. 22, Iss. 3, pp. 279-293
Closed Access | Times Cited: 150

Mice with endogenous TDP ‐43 mutations exhibit gain of splicing function and characteristics of amyotrophic lateral sclerosis
Pietro Fratta, Prasanth Sivakumar, Jack Humphrey, et al.
The EMBO Journal (2018) Vol. 37, Iss. 11
Open Access | Times Cited: 148

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1
Helena Ederle, Christina Funk, Claudia Abou‐Ajram, et al.
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 137

From animal models to human disease: a genetic approach for personalized medicine in ALS
Vincent Picher‐Martel, Paul N. Valdmanis, Peter V. Gould, et al.
Acta Neuropathologica Communications (2016) Vol. 4, Iss. 1
Open Access | Times Cited: 135

Small Non-coding RNAs: New Class of Biomarkers and Potential Therapeutic Targets in Neurodegenerative Disease
Callum N. Watson, Antonio Belli, Valentina Di Pietro
Frontiers in Genetics (2019) Vol. 10
Open Access | Times Cited: 130

Review: Neuropathology of non‐tau frontotemporal lobar degeneration
Manuela Neumann, Ian R. Mackenzie
Neuropathology and Applied Neurobiology (2018) Vol. 45, Iss. 1, pp. 19-40
Closed Access | Times Cited: 123

Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 123

ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles
Haiyan An, Lucy Skelt, Antonietta Notaro, et al.
Acta Neuropathologica Communications (2019) Vol. 7, Iss. 1
Open Access | Times Cited: 122

Linking hnRNP Function to ALS and FTD Pathology
Maria D. Purice, J. Paul Taylor
Frontiers in Neuroscience (2018) Vol. 12
Open Access | Times Cited: 109

FUS interacts with ATP synthase beta subunit and induces mitochondrial unfolded protein response in cellular and animal models
Jianwen Deng, Peng Wang, Xiaoping Chen, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 41
Open Access | Times Cited: 106

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

The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis
Alexander Bampton, Lauren M. Gittings, Pietro Fratta, et al.
Acta Neuropathologica (2020) Vol. 140, Iss. 5, pp. 599-623
Open Access | Times Cited: 97

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