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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 1-25 of 1728 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 phase condensation in cell physiology and disease
Yongdae Shin, Clifford P. Brangwynne
Science (2017) Vol. 357, Iss. 6357
Closed Access | Times Cited: 3617
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
Coactivator condensation at super-enhancers links phase separation and gene control
Benjamin R. Sabari, Alessandra Dall’Agnese, Ann Boija, et al.
Science (2018) Vol. 361, Iss. 6400
Open Access | Times Cited: 2174
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
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
Coexisting Liquid Phases Underlie Nucleolar Subcompartments
Marina Feric, Nilesh Vaidya, Tyler S. Harmon, et al.
Cell (2016) Vol. 165, Iss. 7, pp. 1686-1697
Open Access | Times Cited: 1790
Phase separation drives heterochromatin domain formation
Amy R. Strom, Alexander Emelyanov, Mustafa Mir, et al.
Nature (2017) Vol. 547, Iss. 7662, pp. 241-245
Open Access | Times Cited: 1698
Transcription Factors Activate Genes through the Phase-Separation Capacity of Their Activation Domains
Ann Boija, Isaac A. Klein, Benjamin R. Sabari, et al.
Cell (2018) Vol. 175, Iss. 7, pp. 1842-1855.e16
Open Access | Times Cited: 1581
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
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: 1480
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
The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics
Shana Elbaum‐Garfinkle, Younghoon Kim, Krzysztof Szczepaniak, et al.
Proceedings of the National Academy of Sciences (2015) Vol. 112, Iss. 23, pp. 7189-7194
Open Access | Times Cited: 1219
Compositional Control of Phase-Separated Cellular Bodies
Salman F. Banani, Allyson M. Rice, William B. Peeples, et al.
Cell (2016) Vol. 166, Iss. 3, pp. 651-663
Open Access | Times Cited: 1173
PIWI-interacting RNAs: small RNAs with big functions
Deniz M. Özata, Ildar Gainetdinov, Ansgar Zoch, et al.
Nature Reviews Genetics (2018) Vol. 20, Iss. 2, pp. 89-108
Open Access | Times Cited: 1010
Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
Erik Martin, Alex S. Holehouse, Ivan Peran, et al.
Science (2020) Vol. 367, Iss. 6478, pp. 694-699
Open Access | Times Cited: 995
G3BP1 Is a Tunable Switch that Triggers Phase Separation to Assemble Stress Granules
Peiguo Yang, Cécile Mathieu, Regina‐Maria Kolaitis, et al.
Cell (2020) Vol. 181, Iss. 2, pp. 325-345.e28
Open Access | Times Cited: 993
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
Imaging dynamic and selective low-complexity domain interactions that control gene transcription
Shasha Chong, Claire Dugast‐Darzacq, Zhe Liu, et al.
Science (2018) Vol. 361, Iss. 6400
Open Access | Times Cited: 911
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
ATP as a biological hydrotrope
Avinash Patel, Liliana Malinovska, Shambaditya Saha, et al.
Science (2017) Vol. 356, Iss. 6339, pp. 753-756
Closed Access | Times Cited: 875
Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation
Huan‐Xiang Zhou, Xiaodong Pang
Chemical Reviews (2018) Vol. 118, Iss. 4, pp. 1691-1741
Open Access | Times Cited: 874
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
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