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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:

Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS
Zhihui Sun, Zamia Diaz, Xiao‐Dong Fang, et al.
PLoS Biology (2011) Vol. 9, Iss. 4, pp. e1000614-e1000614
Open Access | Times Cited: 446

Showing 1-25 of 446 citing articles:

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Avinash Patel, Hyun O. Lee, Louise Jawerth, et al.
Cell (2015) Vol. 162, Iss. 5, pp. 1066-1077
Open Access | Times Cited: 2712
Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles
Timothy J. Nott, Evangelia Petsalaki, Patrick Farber, et al.
Molecular Cell (2015) Vol. 57, Iss. 5, pp. 936-947
Open Access | Times Cited: 1728
Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Shuo‐Chien Ling, Magdalini Polymenidou, Don W. Cleveland
Neuron (2013) Vol. 79, Iss. 3, pp. 416-438
Open Access | Times Cited: 1603
Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
Yuan Lin, David S.W. Protter, Michael K. Rosen, et al.
Molecular Cell (2015) Vol. 60, Iss. 2, pp. 208-219
Open Access | Times Cited: 1507
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Hong Joo Kim, Nam Chul Kim, Yong‐Dong Wang, et al.
Nature (2013) Vol. 495, Iss. 7442, pp. 467-473
Open Access | Times Cited: 1391
RNA buffers the phase separation behavior of prion-like RNA binding proteins
Shovamayee Maharana, Jie Wang, Dimitrios K. Papadopoulos, et al.
Science (2018) Vol. 360, Iss. 6391, pp. 918-921
Open Access | Times Cited: 1022
The changing scene of amyotrophic lateral sclerosis
Wim Robberecht, Thomas Philips
Nature reviews. Neuroscience (2013) Vol. 14, Iss. 4, pp. 248-264
Closed Access | Times Cited: 933
Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II
Kathleen A. Burke, Abigail M. Janke, Christy L. Rhine, et al.
Molecular Cell (2015) Vol. 60, Iss. 2, pp. 231-241
Open Access | Times Cited: 880
Stress granules as crucibles of ALS pathogenesis
Leslie A. Lange, Oliver D. King, James Shorter, et al.
The Journal of Cell Biology (2013) Vol. 201, Iss. 3, pp. 361-372
Open Access | Times Cited: 874
Cell-free Formation of RNA Granules: Bound RNAs Identify Features and Components of Cellular Assemblies
Tina W. Han, Masato Kato, Shanhai Xie, et al.
Cell (2012) Vol. 149, Iss. 4, pp. 768-779
Open Access | Times Cited: 762
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
Molecular interactions underlying liquid−liquid phase separation of the FUS low-complexity domain
Anastasia C. Murthy, Gregory L. Dignon, Yelena Kan, et al.
Nature Structural & Molecular Biology (2019) Vol. 26, Iss. 7, pp. 637-648
Open Access | Times Cited: 638
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
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
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Edward B. Lee, Virginia M.‐Y. Lee, John Q. Trojanowski
Nature reviews. Neuroscience (2011) Vol. 13, Iss. 1, pp. 38-50
Open Access | Times Cited: 619
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
Oliver D. King, Aaron D. Gitler, James Shorter
Brain Research (2012) Vol. 1462, pp. 61-80
Open Access | Times Cited: 613
Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS
Ana Jovičić, Jérôme Mertens, Steven Boeynaems, et al.
Nature Neuroscience (2015) Vol. 18, Iss. 9, pp. 1226-1229
Open Access | Times Cited: 593
Altered Ribostasis: RNA-Protein Granules in Degenerative Disorders
Mani Ramaswami, J. Paul Taylor, Roy Parker
Cell (2013) Vol. 154, Iss. 4, pp. 727-736
Open Access | Times Cited: 592
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
Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
Sonja Kroschwald, Shovamayee Maharana, Daniel Matějů, et al.
eLife (2015) Vol. 4
Open Access | Times Cited: 539
Protein aggregation in amyotrophic lateral sclerosis
Anna M. Blokhuis, Ewout J. N. Groen, Max Koppers, et al.
Acta Neuropathologica (2013) Vol. 125, Iss. 6, pp. 777-794
Open Access | Times Cited: 519
The Yeast Deletion Collection: A Decade of Functional Genomics
Guri Giaever, Corey Nislow
Genetics (2014) Vol. 197, Iss. 2, pp. 451-465
Open Access | Times Cited: 471
Gene Overexpression: Uses, Mechanisms, and Interpretation
Gregory Prelich
Genetics (2012) Vol. 190, Iss. 3, pp. 841-854
Open Access | Times Cited: 446
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
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
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