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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:

Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains
Lin Guo, Hong Joo Kim, Hejia Wang, et al.
Cell (2018) Vol. 173, Iss. 3, pp. 677-692.e20
Open Access | Times Cited: 427

Showing 1-25 of 427 citing articles:

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Simon Alberti, Anthony A. Hyman
Nature Reviews Molecular Cell Biology (2021) Vol. 22, Iss. 3, pp. 196-213
Closed Access | Times Cited: 871
Liquid–Liquid Phase Separation in Disease
Simon Alberti, Dorothee Dormann
Annual Review of Genetics (2019) Vol. 53, Iss. 1, pp. 171-194
Open Access | Times Cited: 772
The molecular language of membraneless organelles
Edward Gomes, James Shorter
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7115-7127
Open Access | Times Cited: 711
A framework for understanding the functions of biomolecular condensates across scales
Andrew S. Lyon, William B. Peeples, Michael K. Rosen
Nature Reviews Molecular Cell Biology (2020) Vol. 22, Iss. 3, pp. 215-235
Open Access | Times Cited: 686
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
Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation
Mario Hofweber, Saskia Hutten, Benjamin Bourgeois, et al.
Cell (2018) Vol. 173, Iss. 3, pp. 706-719.e13
Open Access | Times Cited: 584
RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43
Jacob R. Mann, Amanda M. Gleixner, Jocelyn C. Mauna, et al.
Neuron (2019) Vol. 102, Iss. 2, pp. 321-338.e8
Open Access | Times Cited: 480
Liquid–liquid phase separation in human health and diseases
Bin Wang, Lei Zhang, Tong Dai, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 460
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
Beyond aggregation: Pathological phase transitions in neurodegenerative disease
Cécile Mathieu, Rohit V. Pappu, J. Paul Taylor
Science (2020) Vol. 370, Iss. 6512, pp. 56-60
Open Access | Times Cited: 334
Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation
Brian Tsang, Jason Arsenault, Robert M. Vernon, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 10, pp. 4218-4227
Open Access | Times Cited: 316
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
Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites
Takuya Yoshizawa, Rustam Ali, Jenny Jiou, et al.
Cell (2018) Vol. 173, Iss. 3, pp. 693-705.e22
Open Access | Times Cited: 303
TDP-43 proteinopathies: a new wave of neurodegenerative diseases
Eva Maria Johanna 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: 277
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
Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases
Hong Zhang, Ji Xiong, Pilong Li, et al.
Science China Life Sciences (2020) Vol. 63, Iss. 7, pp. 953-985
Closed Access | Times Cited: 262
Modulating biomolecular condensates: a novel approach to drug discovery
Diana M. Mitrea, Matthäus Mittasch, Beatriz Ferreira Gomes, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 11, pp. 841-862
Open Access | Times Cited: 236
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
Phase separation at the synapse
Xudong Chen, Xiandeng Wu, Haowei Wu, et al.
Nature Neuroscience (2020) Vol. 23, Iss. 3, pp. 301-310
Closed Access | Times Cited: 218
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M. Franzmann, Simon Alberti
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7128-7136
Open Access | Times Cited: 208
Chromatin-associated RNAs as facilitators of functional genomic interactions
Xiao Li, Xiang‐Dong Fu
Nature Reviews Genetics (2019) Vol. 20, Iss. 9, pp. 503-519
Open Access | Times Cited: 198
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
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