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:

Loss of Nuclear TDP-43 Is Associated with Decondensation of LINE Retrotransposons
Elaine Y. Liu, Jenny Russ, Christopher P. Cali, et al.
Cell Reports (2019) Vol. 27, Iss. 5, pp. 1409-1421.e6
Open Access | Times Cited: 184

Showing 26-50 of 184 citing articles:

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

Cryptic exon detection and transcriptomic changes revealed in single-nuclei RNA sequencing of C9ORF72 patients spanning the ALS-FTD spectrum
Lauren M. Gittings, Eric Alsop, Jerry Antone, et al.
Acta Neuropathologica (2023) Vol. 146, Iss. 3, pp. 433-450
Open Access | Times Cited: 28

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: 26

TDP-43 loss induces extensive cryptic polyadenylation in ALS/FTD
Sam Bryce-Smith, Anna‐Leigh Brown, Puja R. Mehta, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 13

TDP-43 nuclear loss in FTD/ALS causes widespread alternative polyadenylation changes
Yi Zeng, Anastasiia Lovchykova, Tetsuya Akiyama, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 12

TDP-43 dysregulation of polyadenylation site selection is a defining feature of RNA misprocessing in ALS/FTD and related disorders
Frederick J. Arnold, Ya Cui, Sebastian Michels, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 11

RNA-mediated ribonucleoprotein assembly controls TDP-43 nuclear retention
Patricia M. dos Passos, Erandika H. Hemamali, Lohany D. Mamede, et al.
PLoS Biology (2024) Vol. 22, Iss. 2, pp. e3002527-e3002527
Open Access | Times Cited: 10

RNA-binding properties orchestrate TDP-43 homeostasis through condensate formation in vivo
Natalie M. Scherer, Cindy Maurel, Matthew S. Graus, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 9, pp. 5301-5319
Open Access | Times Cited: 8

The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders
Bess Frost, Josh Dubnau
Annual Review of Neuroscience (2024) Vol. 47, Iss. 1, pp. 123-143
Closed Access | Times Cited: 8

Whole blood transcriptome profile identifies motor neurone disease RNA biomarker signatures
Sulev Kõks, Karin Rallmann, Mari Muldmaa, et al.
Experimental Biology and Medicine (2025) Vol. 249
Open Access | Times Cited: 1

TDP43 autoregulation gives rise to dominant negative isoforms that are tightly controlled by transcriptional and post-translational mechanisms
Megan M. Dykstra, Kaitlin Weskamp, Nicolás Gómez, et al.
Cell Reports (2025) Vol. 44, Iss. 1, pp. 115113-115113
Open Access | Times Cited: 1

Aberrantly High Levels of Somatic LINE-1 Expression and Retrotransposition in Human Neurological Disorders
Diane Terry, Scott E. Devine
Frontiers in Genetics (2020) Vol. 10
Open Access | Times Cited: 66

The SINEB1 element in the long non-coding RNA Malat1 is necessary for TDP-43 proteostasis
Tuan M. Nguyen, Elena B. Kabotyanski, Lucas C. Reineke, et al.
Nucleic Acids Research (2019) Vol. 48, Iss. 5, pp. 2621-2642
Open Access | Times Cited: 55

G-quadruplexes originating from evolutionary conserved L1 elements interfere with neuronal gene expression in Alzheimer’s disease
Roy Hanna, Anthony Flamier, A Barabino, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 46

Induction of autophagy mitigates TDP-43 pathology and translational repression of neurofilament mRNAs in mouse models of ALS/FTD
Sunny Kumar, Daniel J. Phaneuf, Pierre Cordeau, et al.
Molecular Neurodegeneration (2021) Vol. 16, Iss. 1
Open Access | Times Cited: 43

Transposable elements as new players in neurodegenerative diseases
Camille Ravel‐Godreuil, Rania Znaidi, Tom Bonnifet, et al.
FEBS Letters (2021) Vol. 595, Iss. 22, pp. 2733-2755
Open Access | Times Cited: 41

TDP-43 Oligomerization and Phase Separation Properties Are Necessary for Autoregulation
Lydia C. Koehler, Zachary R. Grese, Alliny C.S. Bastos, et al.
Frontiers in Neuroscience (2022) Vol. 16
Open Access | Times Cited: 38

Synaptic dysfunction in ALS and FTD: anatomical and molecular changes provide insights into mechanisms of disease
Pauline A. Gelon, Paul A. Dutchak, Chantelle F. Sephton
Frontiers in Molecular Neuroscience (2022) Vol. 15
Open Access | Times Cited: 35

LINE-1 activation in the cerebellum drives ataxia
Takehiro Takahashi, Milan Stoiljković, Eric Song, et al.
Neuron (2022) Vol. 110, Iss. 20, pp. 3278-3287.e8
Open Access | Times Cited: 33

Retrotransposons as a Source of DNA Damage in Neurodegeneration
Eugénie Pezé-Heidsieck, Tom Bonnifet, Rania Znaidi, et al.
Frontiers in Aging Neuroscience (2022) Vol. 13
Open Access | Times Cited: 29

A retrotransposon storm marks clinical phenoconversion to late-onset Alzheimer’s disease
Fabìo Macciardi, Maria Giulia Bacalini, Ricardo Miramontes, et al.
GeroScience (2022) Vol. 44, Iss. 3, pp. 1525-1550
Open Access | Times Cited: 28

Astroglial toxicity promotes synaptic degeneration in the thalamocortical circuit in frontotemporal dementia with GRN mutations
Elise Marsan, Dmitry Velmeshev, Marina Ramsey, et al.
Journal of Clinical Investigation (2023) Vol. 133, Iss. 6
Open Access | Times Cited: 20

Creation of de novo cryptic splicing for ALS and FTD precision medicine
Oscar G. Wilkins, Max Z. Y. J. Chien, Josette J Wlaschin, et al.
Science (2024) Vol. 386, Iss. 6717, pp. 61-69
Closed Access | Times Cited: 8

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