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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:

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

Showing 51-75 of 1728 citing articles:

Sequence determinants of protein phase behavior from a coarse-grained model
Gregory L. Dignon, Wenwei Zheng, Young C. Kim, et al.
PLoS Computational Biology (2018) Vol. 14, Iss. 1, pp. e1005941-e1005941
Open Access | Times Cited: 587
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
m6A enhances the phase separation potential of mRNA
Ryan J. Ries, Sara Zaccara, Pierre Klein, et al.
Nature (2019) Vol. 571, Iss. 7765, pp. 424-428
Open Access | Times Cited: 582
Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles
Ming-Tzo Wei, Shana Elbaum‐Garfinkle, Alex S. Holehouse, et al.
Nature Chemistry (2017) Vol. 9, Iss. 11, pp. 1118-1125
Open Access | Times Cited: 568
Phosphorylation-mediated RNA/peptide complex coacervation as a model for intracellular liquid organelles
William Aumiller, Christine D. Keating
Nature Chemistry (2015) Vol. 8, Iss. 2, pp. 129-137
Closed Access | Times Cited: 557
Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties
Gregory L. Dignon, Robert B. Best, Jeetain Mittal
Annual Review of Physical Chemistry (2020) Vol. 71, Iss. 1, pp. 53-75
Open Access | Times Cited: 552
Evaluating phase separation in live cells: diagnosis, caveats, and functional consequences
David T. McSwiggen, Mustafa Mir, Xavier Darzacq, et al.
Genes & Development (2019) Vol. 33, Iss. 23-24, pp. 1619-1634
Open Access | Times Cited: 543
Recent progress in the science of complex coacervation
Charles E. Sing, Sarah L. Perry
Soft Matter (2020) Vol. 16, Iss. 12, pp. 2885-2914
Closed Access | Times Cited: 530
P-Bodies: Composition, Properties, and Functions
Yang Luo, Zhenkun Na, Sarah A. Slavoff
Biochemistry (2018) Vol. 57, Iss. 17, pp. 2424-2431
Open Access | Times Cited: 529
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
Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation
Jacob P. Brady, Patrick Farber, Ashok Sekhar, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 39
Open Access | Times Cited: 519
Regulation by 3′-Untranslated Regions
Christine Mayr
Annual Review of Genetics (2017) Vol. 51, Iss. 1, pp. 171-194
Open Access | Times Cited: 516
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
A conceptual framework for understanding phase separation and addressing open questions and challenges
Tanja Mittag, Rohit V. Pappu
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2201-2214
Open Access | Times Cited: 500
Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications
Alaji Bah, Julie D. Forman‐Kay
Journal of Biological Chemistry (2016) Vol. 291, Iss. 13, pp. 6696-6705
Open Access | Times Cited: 496
RNA transcription modulates phase transition-driven nuclear body assembly
Joel Berry, Stephanie C. Weber, Nilesh Vaidya, et al.
Proceedings of the National Academy of Sciences (2015) Vol. 112, Iss. 38
Open Access | Times Cited: 484
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
RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome
Briana Van Treeck, David S.W. Protter, Tyler Matheny, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 11, pp. 2734-2739
Open Access | Times Cited: 474
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
CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins
Alex S. Holehouse, Rahul K. Das, James Ahad, et al.
Biophysical Journal (2017) Vol. 112, Iss. 1, pp. 16-21
Open Access | Times Cited: 467
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Vladimir N. Uversky
Frontiers in Physics (2019) Vol. 7
Open Access | Times Cited: 466
RNA-Mediated Feedback Control of Transcriptional Condensates
Jonathan E. Henninger, Ozgur Oksuz, Krishna Shrinivas, et al.
Cell (2020) Vol. 184, Iss. 1, pp. 207-225.e24
Open Access | Times Cited: 457
Methods for mapping 3D chromosome architecture
Rieke Kempfer, Ana Pombo
Nature Reviews Genetics (2019) Vol. 21, Iss. 4, pp. 207-226
Closed Access | Times Cited: 452
Nuclear speckles: molecular organization, biological function and role in disease
Łukasz Gałgański, Martyna O. Urbanek, Włodzimierz J. Krzyżosiak
Nucleic Acids Research (2017) Vol. 45, Iss. 18, pp. 10350-10368
Open Access | Times Cited: 434
Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation
Daxiao Sun, Rongbo Wu, Jingxiang Zheng, et al.
Cell Research (2018) Vol. 28, Iss. 4, pp. 405-415
Open Access | Times Cited: 422

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