OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Cryptic splicing of stathmin-2 and UNC13A mRNAs is a pathological hallmark of TDP-43-associated Alzheimer’s disease
Ana Rita Agra de Almeida Quadros, Zhaozhi Li, Xue Wang, et al.
Acta Neuropathologica (2024) Vol. 147, Iss. 1
Open Access | Times Cited: 23

Showing 23 citing articles:

RNA dysregulation in neurodegenerative diseases
Yini Li, Shuying Sun
The EMBO Journal (2025) Vol. 44, Iss. 3, pp. 613-638
Open Access | Times Cited: 3

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

Structural insights and milestones in TDP-43 research: A comprehensive review of its pathological and therapeutic advances
Mei Dang, Longjiang Wu, Xiaoying Zhang
International Journal of Biological Macromolecules (2025), pp. 141677-141677
Open Access | Times Cited: 1

Large-scale RNA-seq mining reveals ciclopirox triggers TDP-43 cryptic exons
Irika Sinha, Parker S. Sandal, G Burns, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5

ALS-Associated TDP-43 Dysfunction Compromises UPF1-Dependent mRNA Metabolism Pathways Including Alternative Polyadenylation and 3’UTR Length
Francesco Alessandrini, Matthew Wright, Tatsuaki Kurosaki, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4

The potential impact of RNA splicing abnormalities on immune regulation in endometrial cancer
M D Cao, Jiayu Yan, Yan Ding, et al.
Cell Death and Disease (2025) Vol. 16, Iss. 1
Open Access

C9ORF72 poly-PR disrupts expression of ALS/FTD-implicated STMN2 through SRSF7
Karen S. Wang, Julie Smeyers, Kevin Eggan, et al.
Acta Neuropathologica Communications (2025) Vol. 13, Iss. 1
Open Access

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

To splice or not to splice: pseudoexons in neurological disease and opportunities for intervention
Sue Fletcher, Niall P. Keegan, Rita Mejzini, et al.
Current Opinion in Genetics & Development (2025) Vol. 92, pp. 102343-102343
Open Access

Progranulin deficiency in the brain: the interplay between neuronal and non-neuronal cells
Katarzyna Gaweda‐Walerych, Vanessa Aragona, Simona Lodato, et al.
Translational Neurodegeneration (2025) Vol. 14, Iss. 1
Open Access

Updates on Disease Mechanisms and Therapeutics for Amyotrophic Lateral Sclerosis
Lien Nguyen
Cells (2024) Vol. 13, Iss. 11, pp. 888-888
Open Access | Times Cited: 3

Understanding age-related pathologic changes in TDP-43 functions and the consequence on RNA splicing and signalling in health and disease
Flora Cheng, Tyler Chapman, Selina Zhang, et al.
Ageing Research Reviews (2024) Vol. 96, pp. 102246-102246
Open Access | Times Cited: 2

An atlas of expressed transcripts in the prenatal and postnatal human cortex
Rosemary A. Bamford, Szi Kay Leung, V. Kartik Chundru, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

Protein disulfide isomerase disassembles stress granules and blocks cytoplasmic aggregation of TDP-43 in ALS
Jiaqi Liu, Hao Liu, Yuying Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

hnRNPs: roles in neurodevelopment and implication for brain disorders
Pierre Tilliole, Simon Fix, Juliette D. Godin
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access | Times Cited: 1

Stathmin 2 is a potential treatment target for TDP-43 proteinopathy in amyotrophic lateral sclerosis
Yunqing Liu, Dejun Yan, Lin Yang, et al.
Translational Neurodegeneration (2024) Vol. 13, Iss. 1
Open Access

TDP43 autoregulation gives rise to shortened isoforms that are tightly controlled by both transcriptional and post-translational mechanisms
Megan M. Dykstra, Kaitlin Weskamp, Nicolás Gómez, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Cryptic exon inclusion in TDP-43 proteinopathies: opportunities and challenges
Lorena Decker, Sonja Menge, Axel Freischmidt
Neural Regeneration Research (2024) Vol. 20, Iss. 7, pp. 2003-2004
Open Access

Microtubules, Membranes, and Movement: New Roles for Stathmin‐2 in Axon Integrity
Emma J. C. Thornburg‐Suresh, Daniel W. Summers
Journal of Neuroscience Research (2024) Vol. 102, Iss. 9
Open Access

HDGFL2 cryptic protein: a portal to detection and diagnosis in neurodegenerative disease
Ellen A. Albagli, Anna Calliari, Tania F. Gendron, et al.
Molecular Neurodegeneration (2024) Vol. 19, Iss. 1
Open Access

Decoding TDP-43: the molecular chameleon of neurodegenerative diseases
Jixiang Zeng, Can Luo, Yang Jiang, et al.
Acta Neuropathologica Communications (2024) Vol. 12, Iss. 1
Open Access

Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration
Katie E. Copley, Jocelyn C. Mauna, Helen L. Danielson, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Page 1

Scroll to top