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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:

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

Showing 1-25 of 874 citing articles:

Biomolecular condensates: organizers of cellular biochemistry
Salman F. Banani, Hyun O. Lee, Anthony A. Hyman, et al.
Nature Reviews Molecular Cell Biology (2017) Vol. 18, Iss. 5, pp. 285-298
Open Access | Times Cited: 5061
Liquid-Liquid Phase Separation in Biology
Anthony A. Hyman, Christoph A. Weber, Frank Jülicher
Annual Review of Cell and Developmental Biology (2014) Vol. 30, Iss. 1, pp. 39-58
Closed Access | Times Cited: 2837
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 Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization
Amandine Molliex, Jamshid Temirov, Jihun Lee, et al.
Cell (2015) Vol. 163, Iss. 1, pp. 123-133
Open Access | Times Cited: 2432
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
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Daniel J. Klionsky, Amal Kamal Abdel‐Aziz, Sara Abdelfatah, et al.
Autophagy (2021) Vol. 17, Iss. 1, pp. 1-382
Open Access | Times Cited: 1998
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: 1831
Amyotrophic Lateral Sclerosis
Robert H. Brown, Ammar Al‐Chalabi
New England Journal of Medicine (2017) Vol. 377, Iss. 2, pp. 162-172
Open Access | Times Cited: 1704
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
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Mathias Jucker, Lary C. Walker
Nature (2013) Vol. 501, Iss. 7465, pp. 45-51
Open Access | Times Cited: 1492
Principles and Properties of Stress Granules
David S.W. Protter, Roy Parker
Trends in Cell Biology (2016) Vol. 26, Iss. 9, pp. 668-679
Open Access | Times Cited: 1473
ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure
Saumya Jain, Joshua R. Wheeler, Robert W. Walters, et al.
Cell (2016) Vol. 164, Iss. 3, pp. 487-498
Open Access | Times Cited: 1471
Polymer physics of intracellular phase transitions
Clifford P. Brangwynne, Péter Tompa, Rohit V. Pappu
Nature Physics (2015) Vol. 11, Iss. 11, pp. 899-904
Closed Access | Times Cited: 1451
Context-dependent control of alternative splicing by RNA-binding proteins
Xiang‐Dong Fu, Manuel Ares
Nature Reviews Genetics (2014) Vol. 15, Iss. 10, pp. 689-701
Open Access | Times Cited: 961
Spatiotemporal Control of Intracellular Phase Transitions Using Light-Activated optoDroplets
Yongdae Shin, Joel Berry, Nicole L. Pannucci, et al.
Cell (2016) Vol. 168, Iss. 1-2, pp. 159-171.e14
Open Access | Times Cited: 866
ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function
Tetsuro Murakami, Seema Qamar, Julie Qiaojin Lin, et al.
Neuron (2015) Vol. 88, Iss. 4, pp. 678-690
Open Access | Times Cited: 818
Distinct stages in stress granule assembly and disassembly
Joshua R. Wheeler, Tyler Matheny, Saumya Jain, et al.
eLife (2016) Vol. 5
Open Access | Times Cited: 748
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
The Stress Granule Transcriptome Reveals Principles of mRNA Accumulation in Stress Granules
Anthony Khong, Tyler Matheny, Saumya Jain, et al.
Molecular Cell (2017) Vol. 68, Iss. 4, pp. 808-820.e5
Open Access | Times Cited: 697
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
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
The small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assembly
Carmela Sidrauski, Anna McGeachy, Nicholas T. Ingolia, et al.
eLife (2015) Vol. 4
Open Access | Times Cited: 576
Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)
Matthias Altmeyer, Kai J. Neelsen, Federico Teloni, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 544
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