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 and RNA form amyloid-like myo-granules in regenerating muscle
Thomas O. Vogler, Joshua R. Wheeler, Éric Nguyen, et al.
Nature (2018) Vol. 563, Iss. 7732, pp. 508-513
Open Access | Times Cited: 197

Showing 1-25 of 197 citing articles:

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
A. Aditya Prasad, Vidhya Bharathi, Vishwanath Sivalingam, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 636

Stress granules and neurodegeneration
Benjamin Wolozin, Pavel Ivanov
Nature reviews. Neuroscience (2019) Vol. 20, Iss. 11, pp. 649-666
Open Access | Times Cited: 599

RNA contributions to the form and function of biomolecular condensates
Christine Roden, Amy S. Gladfelter
Nature Reviews Molecular Cell Biology (2020) Vol. 22, Iss. 3, pp. 183-195
Open Access | Times Cited: 527

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: 442

Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 384

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: 304

A guide to membraneless organelles and their various roles in gene regulation
Tetsuro Hirose, Kensuke Ninomiya, Shinichi Nakagawa, et al.
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 288-304
Closed Access | Times Cited: 297

The expanding amyloid family: Structure, stability, function, and pathogenesis
M.R. Sawaya, Michael P. Hughes, José A. Rodríguez, et al.
Cell (2021) Vol. 184, Iss. 19, pp. 4857-4873
Open Access | Times Cited: 274

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum
G Elif Karagöz, Diego Acosta‐Alvear, Peter Walter
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 9, pp. a033886-a033886
Open Access | Times Cited: 266

Endoplasmic reticulum contact sites regulate the dynamics of membraneless organelles
Jason E. Lee, Peter I. Cathey, Haoxi Wu, et al.
Science (2020) Vol. 367, Iss. 6477
Open Access | Times Cited: 251

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: 230

FUS and TDP-43 Phases in Health and Disease
Bede Portz, Bo Lim Lee, James Shorter
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 7, pp. 550-563
Open Access | Times Cited: 230

Bridging biophysics and neurology: aberrant phase transitions in neurodegenerative disease
Natalia B. Nedelsky, J. Paul Taylor
Nature Reviews Neurology (2019) Vol. 15, Iss. 5, pp. 272-286
Closed Access | Times Cited: 187

Higher-order organization of biomolecular condensates
Charlotte M. Fare, Alexis Villani, Lauren E. Drake, et al.
Open Biology (2021) Vol. 11, Iss. 6
Open Access | Times Cited: 143

Skeletal muscle in amyotrophic lateral sclerosis
Jeremy M. Shefner, Antonio Musarò, Shyuan T. Ngo, et al.
Brain (2023) Vol. 146, Iss. 11, pp. 4425-4436
Open Access | Times Cited: 45

Neuropathogenesis-on-chips for neurodegenerative diseases
Sarnai Amartumur, Huong Mai Nguyen, Thuy Huynh, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 32

Tissue-specific landscape of protein aggregation and quality control in an aging vertebrate
Yiwen R. Chen, Itamar Harel, Param Priya Singh, et al.
Developmental Cell (2024) Vol. 59, Iss. 14, pp. 1892-1911.e13
Open Access | Times Cited: 19

Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
Luke McAlary, Steven S. Plotkin, Justin J. Yerbury, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 137

Neurotoxic microglia promote TDP-43 proteinopathy in progranulin deficiency
Jiasheng Zhang, Dmitry Velmeshev, Kei Hashimoto, et al.
Nature (2020) Vol. 588, Iss. 7838, pp. 459-465
Open Access | Times Cited: 130

Cryo-EM of amyloid fibrils and cellular aggregates
Anthony Fitzpatrick, Helen R. Saibil
Current Opinion in Structural Biology (2019) Vol. 58, pp. 34-42
Open Access | Times Cited: 126

RNA Droplets
Kevin Rhine, Velinda Vidaurre, Sua Myong
Annual Review of Biophysics (2020) Vol. 49, Iss. 1, pp. 247-265
Open Access | Times Cited: 126

A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids
Jian Kang, Liangzhong Lim, Yimei Lu, et al.
PLoS Biology (2019) Vol. 17, Iss. 6, pp. e3000327-e3000327
Open Access | Times Cited: 125

Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 123

Molecular and Cellular Mechanisms Affected in ALS
Laura Le Gall, Ekene Anakor, Owen Connolly, et al.
Journal of Personalized Medicine (2020) Vol. 10, Iss. 3, pp. 101-101
Open Access | Times Cited: 112

Cytoplasmic functions of TDP-43 and FUS and their role in ALS
Nicol Birsa, Matthew P. Bentham, Pietro Fratta
Seminars in Cell and Developmental Biology (2019) Vol. 99, pp. 193-201
Open Access | Times Cited: 106

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