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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 cryptic exons are highly variable between cell types
Yun Ha Jeong, Jonathan P. Ling, Sophie Lin, et al.
Molecular Neurodegeneration (2017) Vol. 12, Iss. 1
Open Access | Times Cited: 79

Showing 1-25 of 79 citing articles:

Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration
Ze’ev Melamed, Jone López‐Erauskin, Michael W. Baughn, et al.
Nature Neuroscience (2019) Vol. 22, Iss. 2, pp. 180-190
Open Access | Times Cited: 477
TDP-43 represses cryptic exon inclusion in the FTD–ALS gene UNC13A
X. Rosa, Mercedes Prudencio, Yuka Koike, et al.
Nature (2022) Vol. 603, Iss. 7899, pp. 124-130
Open Access | Times Cited: 332
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: 295
Truncated stathmin-2 is a marker of TDP-43 pathology in frontotemporal dementia
Mercedes Prudencio, Jack Humphrey, Sarah Pickles, et al.
Journal of Clinical Investigation (2020) Vol. 130, Iss. 11, pp. 6080-6092
Open Access | Times Cited: 168
Mechanism of STMN2 cryptic splice-polyadenylation and its correction for TDP-43 proteinopathies
Michael W. Baughn, Ze’ev Melamed, Jone López‐Erauskin, et al.
Science (2023) Vol. 379, Iss. 6637, pp. 1140-1149
Open Access | Times Cited: 112
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: 108
The era of cryptic exons: implications for ALS-FTD
Puja R. Mehta, Anna‐Leigh Brown, Michael E. Ward, et al.
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 58
A fluid biomarker reveals loss of TDP-43 splicing repression in presymptomatic ALS–FTD
Katherine E. Irwin, Pei Jasin, Kerstin E. Braunstein, et al.
Nature Medicine (2024) Vol. 30, Iss. 2, pp. 382-393
Open Access | Times Cited: 58
Skeletal muscle in amyotrophic lateral sclerosis
Jeremy M. Shefner, Antonio Musarò, Shyuan T. Ngo, et al.
Brain (2023) Vol. 146, Iss. 11, pp. 4425-4436
Open Access | Times Cited: 44
Dysregulated molecular pathways in amyotrophic lateral sclerosis–frontotemporal dementia spectrum disorder
Fen‐Biao Gao, Sandra Almeida, Rodrigo López‐González
The EMBO Journal (2017) Vol. 36, Iss. 20, pp. 2931-2950
Open Access | Times Cited: 166
Neurons selectively targeted in frontotemporal dementia reveal early stage TDP-43 pathobiology
Alissa L. Nana, Manu Sidhu, Stephanie E. Gaus, et al.
Acta Neuropathologica (2018) Vol. 137, Iss. 1, pp. 27-46
Open Access | Times Cited: 108
RNA-binding proteins in neurological development and disease
Shavanie Prashad, Pallavi P. Gopal
RNA Biology (2020) Vol. 18, Iss. 7, pp. 972-987
Open Access | Times Cited: 93
TDP-43 proteinopathy and mitochondrial abnormalities in neurodegeneration
Ju Gao, Luwen Wang, Tingxiang Yan, et al.
Molecular and Cellular Neuroscience (2019) Vol. 100, pp. 103396-103396
Open Access | Times Cited: 89
DeepCLIP: predicting the effect of mutations on protein–RNA binding with deep learning
Alexander G. B. Grønning, Thomas Koed Doktor, Simon J. Larsen, et al.
Nucleic Acids Research (2020)
Open Access | Times Cited: 83
Splicing repression is a major function of TDP-43 in motor neurons
Aneesh Donde, Mingkuan Sun, Jonathan P. Ling, et al.
Acta Neuropathologica (2019) Vol. 138, Iss. 5, pp. 813-826
Open Access | Times Cited: 79
Loss of TDP-43 function and rimmed vacuoles persist after T cell depletion in a xenograft model of sporadic inclusion body myositis
Kyla A. Britson, Jonathan P. Ling, Kerstin E. Braunstein, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 628
Open Access | Times Cited: 50
Cell environment shapes TDP-43 function with implications in neuronal and muscle disease
Urša Šušnjar, Neva Škrabar, Anna‐Leigh Brown, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 40
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: 40
A fluid biomarker reveals loss of TDP-43 splicing repression in pre-symptomatic ALS
Katherine E. Irwin, Pei Jasin, Kerstin E. Braunstein, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 35
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: 31
TDP-43 and other hnRNPs regulate cryptic exon inclusion of a key ALS/FTD risk gene, UNC13A
Yuka Koike, Sarah Pickles, Virginia Estades Ayuso, et al.
PLoS Biology (2023) Vol. 21, Iss. 3, pp. e3002028-e3002028
Open Access | Times Cited: 27
A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration
Rebecca San Gil, Dana Pascovici, Juliana Venturato, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9
Loss of TDP‐43 Splicing Repression Occurs in Myonuclei of Inclusion Body Myositis Patients
Chiseko Ikenaga, Andrew B. Wilson, Katherine E. Irwin, et al.
Annals of Neurology (2025)
Closed Access | Times Cited: 1
C9orf72-FTD/ALS pathogenesis: evidence from human neuropathological studies
Sarat C. Vatsavayai, Alissa L. Nana, Jennifer S. Yokoyama, et al.
Acta Neuropathologica (2018) Vol. 137, Iss. 1, pp. 1-26
Open Access | Times Cited: 67
Synaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic Functions
Shuo‐Chien Ling
Neural Plasticity (2018) Vol. 2018, pp. 1-13
Open Access | Times Cited: 65
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