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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:

C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles
Kyung‐Ha Lee, Peipei Zhang, Hong Joo Kim, et al.
Cell (2016) Vol. 167, Iss. 3, pp. 774-788.e17
Open Access | Times Cited: 670

Showing 1-25 of 670 citing articles:

Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates
Simon Alberti, Amy Gladfelter, Tanja Mittag
Cell (2019) Vol. 176, Iss. 3, pp. 419-434
Open Access | Times Cited: 2381
Protein Phase Separation: A New Phase in Cell Biology
Steven Boeynaems, Simon Alberti, Nicolas L. Fawzi, et al.
Trends in Cell Biology (2018) Vol. 28, Iss. 6, pp. 420-435
Open Access | Times Cited: 1836
Decoding ALS: from genes to mechanism
J. Paul Taylor, Robert H. Brown, Don W. Cleveland
Nature (2016) Vol. 539, Iss. 7628, pp. 197-206
Open Access | Times Cited: 1821
A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins
Jie Wang, Jeong‐Mo Choi, Alex S. Holehouse, et al.
Cell (2018) Vol. 174, Iss. 3, pp. 688-699.e16
Open Access | Times Cited: 1817
The proteostasis network and its decline in ageing
Mark S. Hipp, Prasad Kasturi, F. Ulrich Hartl
Nature Reviews Molecular Cell Biology (2019) Vol. 20, Iss. 7, pp. 421-435
Open Access | Times Cited: 1211
Tau protein liquid–liquid phase separation can initiate tau aggregation
Susanne Wegmann, Bahareh Eftekharzadeh, Katharina Tepper, et al.
The EMBO Journal (2018) Vol. 37, Iss. 7
Open Access | Times Cited: 929
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
Hallmarks of neurodegenerative diseases
David M. Wilson, Mark Cookson, Ludo Van Den Bosch, et al.
Cell (2023) Vol. 186, Iss. 4, pp. 693-714
Open Access | Times Cited: 827
Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules
Sebastian Markmiller, Sahar Soltanieh, Kari L. Server, et al.
Cell (2018) Vol. 172, Iss. 3, pp. 590-604.e13
Open Access | Times Cited: 815
Pi-Pi contacts are an overlooked protein feature relevant to phase separation
Robert M. Vernon, P. Andrew Chong, Brian Tsang, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 797
The nucleolus as a multiphase liquid condensate
Denis L. J. Lafontaine, Joshua A. Riback, Rümeyza Bascetin, et al.
Nature Reviews Molecular Cell Biology (2020) Vol. 22, Iss. 3, pp. 165-182
Open Access | Times Cited: 784
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
Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins
Tyler S. Harmon, Alex S. Holehouse, Michael K. Rosen, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 657
Biomimetic peptide self-assembly for functional materials
Aviad Levin, Tuuli A. Hakala, Lee Schnaider, et al.
Nature Reviews Chemistry (2020) Vol. 4, Iss. 11, pp. 615-634
Closed Access | Times Cited: 646
Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
Zachary Monahan, Veronica H. Ryan, Abigail M. Janke, et al.
The EMBO Journal (2017) Vol. 36, Iss. 20, pp. 2951-2967
Open Access | Times Cited: 636
C9orf72-mediated ALS and FTD: multiple pathways to disease
Rubika Balendra, Adrian M. Isaacs
Nature Reviews Neurology (2018) Vol. 14, Iss. 9, pp. 544-558
Open Access | Times Cited: 616
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
TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics
Ian R. Mackenzie, Alexandra M. Nicholson, Mohona Sarkar, et al.
Neuron (2017) Vol. 95, Iss. 4, pp. 808-816.e9
Open Access | Times Cited: 570
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
Ching-Chieh Chou, Yi Zhang, Mfon Umoh, et al.
Nature Neuroscience (2018) Vol. 21, Iss. 2, pp. 228-239
Open Access | Times Cited: 511
Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics
Steven Boeynaems, Elke Bogaert, Dénes Kovács, et al.
Molecular Cell (2017) Vol. 65, Iss. 6, pp. 1044-1055.e5
Open Access | Times Cited: 507
Spontaneous driving forces give rise to protein−RNA condensates with coexisting phases and complex material properties
Steven Boeynaems, Alex S. Holehouse, Venera Weinhardt, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 16, pp. 7889-7898
Open Access | Times Cited: 469
The nucleolus functions as a phase-separated protein quality control compartment
Frédéric Frottin, Florian Schueder, Shivani Tiwary, et al.
Science (2019) Vol. 365, Iss. 6451, pp. 342-347
Open Access | Times Cited: 441
Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers
Yi Lin, Eiichiro Mori, Masato Kato, et al.
Cell (2016) Vol. 167, Iss. 3, pp. 789-802.e12
Open Access | Times Cited: 431
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