Open Access Helper

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:

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

Showing 1-25 of 477 citing articles:

Stress granules and neurodegeneration
Benjamin Wolozin, Pavel Ivanov
Nature reviews. Neuroscience (2019) Vol. 20, Iss. 11, pp. 649-666
Open Access | Times Cited: 588
Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death
F. Gasset-Rosa, Shan Lu, Haiyang Yu, et al.
Neuron (2019) Vol. 102, Iss. 2, pp. 339-357.e7
Open Access | Times Cited: 430
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
TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of UNC13A
Anna‐Leigh Brown, Oscar G. Wilkins, Matthew J. Keuss, et al.
Nature (2022) Vol. 603, Iss. 7899, pp. 131-137
Open Access | Times Cited: 305
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
ALS Genetics: Gains, Losses, and Implications for Future Therapies
Garam Kım, Olivia Gautier, Eduardo Tassoni-Tsuchida, et al.
Neuron (2020) Vol. 108, Iss. 5, pp. 822-842
Open Access | Times Cited: 291
HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells
Haiyang Yu, Shan Lu, Kelsey Gasior, et al.
Science (2021) Vol. 371, Iss. 6529
Open Access | Times Cited: 290
TDP-43 proteinopathies: a new wave of neurodegenerative diseases
Eva M. J. de Boer, Viyanti K Orie, Timothy L. Williams, et al.
Journal of Neurology Neurosurgery & Psychiatry (2020) Vol. 92, Iss. 1, pp. 86-95
Open Access | Times Cited: 267
Programmed axon degeneration: from mouse to mechanism to medicine
Michael P. Coleman, Ahmet Höke
Nature reviews. Neuroscience (2020) Vol. 21, Iss. 4, pp. 183-196
Open Access | Times Cited: 258
Disruption of RNA Metabolism in Neurological Diseases and Emerging Therapeutic Interventions
Julia K. Nussbacher, Ricardos Tabet, G Yeo, et al.
Neuron (2019) Vol. 102, Iss. 2, pp. 294-320
Open Access | Times Cited: 229
TDP-43 Pathology in Alzheimer’s Disease
Axel Meneses, Shunsuke Koga, Justin O’Leary, et al.
Molecular Neurodegeneration (2021) Vol. 16, Iss. 1
Open Access | Times Cited: 179
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
Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Paraskevi Tziortzouda, Ludo Van Den Bosch, Frank Hirth
Nature reviews. Neuroscience (2021) Vol. 22, Iss. 4, pp. 197-208
Closed Access | Times Cited: 167
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: 144
Gene therapy for ALS: A review
Defne A. Amado, Beverly L. Davidson
Molecular Therapy (2021) Vol. 29, Iss. 12, pp. 3345-3358
Open Access | Times Cited: 134
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
Axonal TDP-43 condensates drive neuromuscular junction disruption through inhibition of local synthesis of nuclear encoded mitochondrial proteins
Topaz Altman, Ariel Ionescu, Amjad Ibraheem, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 105
Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases
Jenny L. Carey, Lin Guo
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 99
Genome-wide identification of the genetic basis of amyotrophic lateral sclerosis
Sai Zhang, Johnathan Cooper‐Knock, Annika K. Weimer, et al.
Neuron (2022) Vol. 110, Iss. 6, pp. 992-1008.e11
Open Access | Times Cited: 96
Genetics of amyotrophic lateral sclerosis: seeking therapeutic targets in the era of gene therapy
Naoki Suzuki, Ayumi Nishiyama, Hitoshi Warita, et al.
Journal of Human Genetics (2022) Vol. 68, Iss. 3, pp. 131-152
Open Access | Times Cited: 92
Constitutively active SARM1 variants that induce neuropathy are enriched in ALS patients
A. Joseph Bloom, Xianrong Mao, Amy Strickland, et al.
Molecular Neurodegeneration (2022) Vol. 17, Iss. 1
Open Access | Times Cited: 85
Cerebrospinal fluid proteomics in patients with Alzheimer’s disease reveals five molecular subtypes with distinct genetic risk profiles
Betty M. Tijms, Eleonora M. Vromen, Olav Mjaavatten, et al.
Nature Aging (2024) Vol. 4, Iss. 1, pp. 33-47
Open Access | Times Cited: 80
Alternative splicing in neurodegenerative disease and the promise of RNA therapies
David Nikom, Sika Zheng
Nature reviews. Neuroscience (2023) Vol. 24, Iss. 8, pp. 457-473
Closed Access | Times Cited: 77
Integrative transcriptomic analysis of the amyotrophic lateral sclerosis spinal cord implicates glial activation and suggests new risk genes
Jack Humphrey, Sanan Venkatesh, Rahat Hasan, et al.
Nature Neuroscience (2022) Vol. 26, Iss. 1, pp. 150-162
Open Access | Times Cited: 76
Formation, function, and pathology of RNP granules
Nina Ripin, Roy Parker
Cell (2023) Vol. 186, Iss. 22, pp. 4737-4756
Closed Access | Times Cited: 74
Page 1 - Next Page

Scroll to top