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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 condensation properties specify its RNA-binding and regulatory repertoire
Martina Hallegger, Anob M. Chakrabarti, Flora Lee, et al.
Cell (2021) Vol. 184, Iss. 18, pp. 4680-4696.e22
Open Access | Times Cited: 190

Showing 51-75 of 190 citing articles:

The kinesin-3 KIF1C undergoes liquid-liquid phase separation for accumulation of specific transcripts at the cell periphery
Qi Geng, Jakia Jannat Keya, Takashi Hotta, et al.
The EMBO Journal (2024) Vol. 43, Iss. 15, pp. 3192-3213
Open Access | Times Cited: 7
Structural details of helix-mediated TDP-43 C-terminal domain multimerization
Azamat Rizuan, Jayakrishna Kanhangad Shenoy, Priyesh Mohanty, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
TDP-43 Proteinopathy Specific Biomarker Development
Isabell Cordts, Annika Wachinger, Carlo Scialò, et al.
Cells (2023) Vol. 12, Iss. 4, pp. 597-597
Open Access | Times Cited: 17
Towards in silico CLIP-seq: predicting protein-RNA interaction via sequence-to-signal learning
Marc Horlacher, Nils Wagner, Lambert Moyon, et al.
Genome biology (2023) Vol. 24, Iss. 1
Open Access | Times Cited: 16
The RBPome of influenza A virus NP-mRNA reveals a role for TDP-43 in viral replication
Maud Dupont, Tim Krischuns, Quentin Giai Gianetto, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 12, pp. 7188-7210
Open Access | Times Cited: 6
Multivalent GU-rich oligonucleotides sequester TDP-43 in the nucleus by inducing high molecular weight RNP complexes
Xi Zhang, Tanuza Das, Tiffany F. Chao, et al.
iScience (2024) Vol. 27, Iss. 6, pp. 110109-110109
Open Access | Times Cited: 5
Assessing the clinical utility of protein structural analysis in genomic variant classification: experiences from a diagnostic laboratory
Richard Caswell, Adam C. Gunning, Martina Owens, et al.
Genome Medicine (2022) Vol. 14, Iss. 1
Open Access | Times Cited: 23
A Feedback Regulatory Loop Involving dTrbd/dTak1 in Controlling IMD Signaling in Drosophila Melanogaster
Yongzhi Hua, Yangyang Zhu, Yixuan Hu, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 20
Beyond gene expression: how MYC relieves transcription stress
Dimitrios Papadopoulos, Leonie Uhl, Stefanie Anh Ha, et al.
Trends in cancer (2023) Vol. 9, Iss. 10, pp. 805-816
Open Access | Times Cited: 13
Oxidative regulation of TDP-43 self-association by a β-to-α conformational switch
Jinge Gu, Xiaoming Zhou, Lillian B. Sutherland, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 41
Open Access | Times Cited: 13
Poised PABP–RNA hubs implement signal-dependent mRNA decay in development
Miha Modic, Klara Kuret, Sebastian Steinhauser, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 9, pp. 1439-1447
Open Access | Times Cited: 4
Pathological Involvement of Protein Phase Separation and Aggregation in Neurodegenerative Diseases
Y. Wu, Biao Ma, Chang Yu Liu, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 18, pp. 10187-10187
Open Access | Times Cited: 4
From computational models of the splicing code to regulatory mechanisms and therapeutic implications
Charlotte Capitanchik, Oscar G. Wilkins, Nils Wagner, et al.
Nature Reviews Genetics (2024)
Closed Access | Times Cited: 4
RBPWorld for exploring functions and disease associations of RNA-binding proteins across species
Jian‐You Liao, Bing Yang, Chuan-Ping Shi, et al.
Nucleic Acids Research (2024) Vol. 53, Iss. D1, pp. D220-D232
Open Access | Times Cited: 4
Pathogenic Mutation of TDP-43 Impairs RNA Processing in a Cell Type-Specific Manner: Implications for the Pathogenesis of ALS/FTLD
Kent Imaizumi, Hirosato Ideno, Tsukika Sato, et al.
eNeuro (2022) Vol. 9, Iss. 3, pp. ENEURO.0061-22.2022
Open Access | Times Cited: 17
Current insights in the molecular genetic pathogenesis of amyotrophic lateral sclerosis
Zhou Wan, Renshi Xu
Frontiers in Neuroscience (2023) Vol. 17
Open Access | Times Cited: 11
RNA-binding deficient TDP-43 drives cognitive decline in a mouse model of TDP-43 proteinopathy
Julie Necarsulmer, Jeremy M. Simon, Baggio Evangelista, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 10
RNA sequestration driven by amyloid formation: the alpha synuclein case
Jakob Rupert, Michele Monti, Elsa Zacco, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 21, pp. 11466-11478
Open Access | Times Cited: 10
Long way up: rethink diseases in light of phase separation and phase transition
Mingrui Ding, Weifan Xu, Gaofeng Pei, et al.
Protein & Cell (2023) Vol. 15, Iss. 7, pp. 475-492
Open Access | Times Cited: 10
TDP-43 in nuclear condensates: where, how, and why
Ruaridh Lang, Rachel E. Hodgson, Tatyana A. Shelkovnikova
Biochemical Society Transactions (2024) Vol. 52, Iss. 4, pp. 1809-1825
Closed Access | Times Cited: 4
The levels of the long non-coding RNA MALAT1 affect cell viability and modulate TDP-43 binding to mRNA in the nucleus
Adarsh Balaji, A. Button, Simone D. Hall, et al.
Journal of Biological Chemistry (2025), pp. 108207-108207
Open Access
A simple method for mapping the location of cross-β forming regions within protein domains of low sequence complexity
J. H. Gu, Xiaoming Zhou, Lillian B. Sutherland, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
catGRANULE 2.0: accurate predictions of liquid-liquid phase separating proteins at single amino acid resolution
Michele Monti, Jonathan Fiorentino, Dimitrios Miltiadis-Vrachnos, et al.
Genome biology (2025) Vol. 26, Iss. 1
Open Access
Testosterone Supplementation: A Potential Therapeutic Strategy for Amyotrophic Lateral Sclerosis
Wenzhi Yang, Wendi Xiao, Xiangyi Liu, et al.
Biomedicines (2025) Vol. 13, Iss. 3, pp. 622-622
Open Access
TDP-43 seeding induces cytoplasmic aggregation heterogeneity and nuclear loss of function of TDP-43
JL Rummens, Bilal Khalil, Günseli Yıldırım, et al.
Neuron (2025)
Open Access

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