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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:

Transcriptome–pathology correlation identifies interplay between TDP-43 and the expression of its kinase CK1E in sporadic ALS
Florian Krach, Ranjan Batra, Emily C. Wheeler, et al.
Acta Neuropathologica (2018) Vol. 136, Iss. 3, pp. 405-423
Open Access | Times Cited: 88

Showing 1-25 of 88 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: 487
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: 300
Small-Molecule Modulation of TDP-43 Recruitment to Stress Granules Prevents Persistent TDP-43 Accumulation in ALS/FTD
Mark Y. Fang, Sebastian Markmiller, Anthony Q. Vu, et al.
Neuron (2019) Vol. 103, Iss. 5, pp. 802-819.e11
Open Access | Times Cited: 220
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
TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance in ALS
Xinxin Zuo, Jie Zhou, Yin‐Ming Li, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 2, pp. 132-142
Closed Access | Times Cited: 146
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: 115
Identification of Therapeutic Targets for Amyotrophic Lateral Sclerosis Using PandaOmics – An AI-Enabled Biological Target Discovery Platform
Frank W. Pun, Bonnie Hei Man Liu, Xi Long, et al.
Frontiers in Aging Neuroscience (2022) Vol. 14
Open Access | Times Cited: 73
Gasdermin-E mediates mitochondrial damage in axons and neurodegeneration
Dylan V. Neel, Himanish Basu, Georgia Gunner, et al.
Neuron (2023) Vol. 111, Iss. 8, pp. 1222-1240.e9
Open Access | Times Cited: 66
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
TDP-43-stratified single-cell proteomics of postmortem human spinal motor neurons reveals protein dynamics in amyotrophic lateral sclerosis
Amanda J. Guise, Santosh A. Misal, Richard H. Carson, et al.
Cell Reports (2024) Vol. 43, Iss. 1, pp. 113636-113636
Open Access | Times Cited: 23
Shortened TDP43 isoforms upregulated by neuronal hyperactivity drive TDP43 pathology in ALS
Kaitlin Weskamp, Elizabeth M. H. Tank, Roberto Miguez, et al.
Journal of Clinical Investigation (2019) Vol. 130, Iss. 3, pp. 1139-1155
Open Access | Times Cited: 107
Regulation of TDP-43 phosphorylation in aging and disease
Randall J. Eck, Brian C. Kraemer, Nicole F. Liachko
GeroScience (2021) Vol. 43, Iss. 4, pp. 1605-1614
Open Access | Times Cited: 63
Transcriptome-wide identification of RNA-binding protein binding sites using seCLIP-seq
Steven M. Blue, Brian A. Yee, Gabriel A. Pratt, et al.
Nature Protocols (2022) Vol. 17, Iss. 5, pp. 1223-1265
Open Access | Times Cited: 50
Stathmin-2 loss leads to neurofilament-dependent axonal collapse driving motor and sensory denervation
Jone López‐Erauskin, Mariana Bravo‐Hernández, Maximiliano Presa, et al.
Nature Neuroscience (2023) Vol. 27, Iss. 1, pp. 34-47
Open Access | Times Cited: 25
Neuronal STING activation in amyotrophic lateral sclerosis and frontotemporal dementia
Christine Marques, Aaron Held, Katherine Dorfman, et al.
Acta Neuropathologica (2024) Vol. 147, Iss. 1
Open Access | Times Cited: 16
Proteomics Approaches for Biomarker and Drug Target Discovery in ALS and FTD
Thomas J. Hedl, Rebecca San Gil, Flora Cheng, et al.
Frontiers in Neuroscience (2019) Vol. 13
Open Access | Times Cited: 75
A multi-ethnic meta-analysis identifies novel genes, including ACSL5, associated with amyotrophic lateral sclerosis
Ryoichi Nakamura, Kazuharu Misawa, Genki Tohnai, et al.
Communications Biology (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 56
Motor neuron preservation and decrease of in vivo TDP-43 phosphorylation by protein CK-1δ kinase inhibitor treatment
Loreto Martínez-González, Carmen Rodríguez‐Cueto, Diego Cabezudo, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 54
Novel STMN2 Variant Linked to Amyotrophic Lateral Sclerosis Risk and Clinical Phenotype
Frances Theunissen, Ryan S. Anderton, Frank Mastaglia, et al.
Frontiers in Aging Neuroscience (2021) Vol. 13
Open Access | Times Cited: 44
Whole-genome sequencing reveals that variants in the Interleukin 18 Receptor Accessory Protein 3′UTR protect against ALS
Chen Eitan, Aviad Siany, Elad Barkan, et al.
Nature Neuroscience (2022) Vol. 25, Iss. 4, pp. 433-445
Open Access | Times Cited: 29
The molecular genetics of nELAVL in brain development and disease
Meghan R. Mulligan, Louise S. Bicknell
European Journal of Human Genetics (2023) Vol. 31, Iss. 11, pp. 1209-1217
Open Access | Times Cited: 21
Human genetics and neuropathology suggest a link between miR-218 and amyotrophic lateral sclerosis pathophysiology
Irit Reichenstein, Chen Eitan, Sandra Díaz-García, et al.
Science Translational Medicine (2019) Vol. 11, Iss. 523
Open Access | Times Cited: 49
TDP-43: A Key Therapeutic Target beyond Amyotrophic Lateral Sclerosis
Valle Palomo, Carlota Tosat‐Bitrián, Vanesa Nozal, et al.
ACS Chemical Neuroscience (2019) Vol. 10, Iss. 3, pp. 1183-1196
Open Access | Times Cited: 44
Changes to the TDP-43 and FUS Interactomes Induced by DNA Damage
Tetsuya Kawaguchi, Matthew G. Rollins, Mahta Moinpour, et al.
Journal of Proteome Research (2019) Vol. 19, Iss. 1, pp. 360-370
Open Access | Times Cited: 43
TDP-43 stabilizes G3BP1 mRNA: relevance to amyotrophic lateral sclerosis/frontotemporal dementia
Hadjara Sidibé, Yousra Khalfallah, Shangxi Xiao, et al.
Brain (2021) Vol. 144, Iss. 11, pp. 3461-3476
Open Access | Times Cited: 37
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