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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:

Protein condensates as aging Maxwell fluids
Louise Jawerth, Elisabeth Fischer‐Friedrich, Suropriya Saha, et al.
Science (2020) Vol. 370, Iss. 6522, pp. 1317-1323
Closed Access | Times Cited: 391

Showing 1-25 of 391 citing articles:

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
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
Phase Transitions of Associative Biomacromolecules
Rohit V. Pappu, Samuel R. Cohen, Furqan Dar, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 8945-8987
Closed Access | Times Cited: 236
Extreme dynamics in a biomolecular condensate
Nicola Galvanetto, Miloš T. Ivanović, Aritra Chowdhury, et al.
Nature (2023) Vol. 619, Iss. 7971, pp. 876-883
Open Access | Times Cited: 190
Regulation of biomolecular condensates by interfacial protein clusters
Andrew W. Folkmann, Andrea Putnam, Chiu Fan Lee, et al.
Science (2021) Vol. 373, Iss. 6560, pp. 1218-1224
Open Access | Times Cited: 189
Programmable viscoelasticity in protein-RNA condensates with disordered sticker-spacer polypeptides
Ibraheem Alshareedah, Mahdi Muhammad Moosa, Matthew Pham, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 183
On the role of phase separation in the biogenesis of membraneless compartments
Andrea Musacchio
The EMBO Journal (2022) Vol. 41, Iss. 5
Open Access | Times Cited: 158
Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Dieter Willbold, Birgit Strodel, Gunnar F. Schröder, et al.
Chemical Reviews (2021) Vol. 121, Iss. 13, pp. 8285-8307
Open Access | Times Cited: 154
Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by expanded conformations
Mina Farag, Samuel R. Cohen, Wade M. Borcherds, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 150
Higher-order organization of biomolecular condensates
Charlotte M. Fare, Alexis Villani, Lauren E. Drake, et al.
Open Biology (2021) Vol. 11, Iss. 6
Open Access | Times Cited: 143
Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry
Anton Abyzov, Martin Blackledge, Markus Zweckstetter
Chemical Reviews (2022) Vol. 122, Iss. 6, pp. 6719-6748
Open Access | Times Cited: 137
Tau liquid–liquid phase separation in neurodegenerative diseases
Solomiia Boyko, Witold K. Surewicz
Trends in Cell Biology (2022) Vol. 32, Iss. 7, pp. 611-623
Open Access | Times Cited: 113
Liquid-to-solid phase transition of oskar ribonucleoprotein granules is essential for their function in Drosophila embryonic development
Mainak Bose, Marko Lampe, Julia Mahamid, et al.
Cell (2022) Vol. 185, Iss. 8, pp. 1308-1324.e23
Open Access | Times Cited: 101
High shear rate propulsion of acoustic microrobots in complex biological fluids
Amirreza Aghakhani, Abdon Pena‐Francesch, Ugur Bozuyuk, et al.
Science Advances (2022) Vol. 8, Iss. 10
Open Access | Times Cited: 91
Expanding the molecular language of protein liquid–liquid phase separation
Shiv Rekhi, Cristobal Garcia Garcia, Mayur Barai, et al.
Nature Chemistry (2024) Vol. 16, Iss. 7, pp. 1113-1124
Open Access | Times Cited: 85
The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils
Miriam Linsenmeier, Lenka Faltova, Chiara Morelli, et al.
Nature Chemistry (2023) Vol. 15, Iss. 10, pp. 1340-1349
Open Access | Times Cited: 80
Synthetic protein condensates for cellular and metabolic engineering
Zhi‐Gang Qian, Sheng-Chen Alex Huang, Xiao‐Xia Xia
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1330-1340
Closed Access | Times Cited: 79
Molecular and environmental determinants of biomolecular condensate formation
José A. Villegas, Meta Heidenreich, Emmanuel D. Levy
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1319-1329
Closed Access | Times Cited: 77
Aging can transform single-component protein condensates into multiphase architectures
Adiran Garaizar, Jorge R. Espinosa, Jerelle A. Joseph, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 26
Open Access | Times Cited: 76
Wetting and complex remodeling of membranes by biomolecular condensates
Agustín Mangiarotti, Nannan Chen, Ziliang Zhao, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 75
The liquid-to-solid transition of FUS is promoted by the condensate surface
Yi Shen, Anqi Chen, Wenyun Wang, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 33
Open Access | Times Cited: 75
A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules
Seán Millar, Jie Huang, Karl J. Schreiber, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9036-9064
Open Access | Times Cited: 63
RNA granules: functional compartments or incidental condensates?
Andrea Putnam, Laura Thomas, Géraldine Seydoux
Genes & Development (2023) Vol. 37, Iss. 9-10, pp. 354-376
Open Access | Times Cited: 57
Phase Separation in Biology and Disease; Current Perspectives and Open Questions
Steven Boeynaems, Shasha Chong, Jörg Gsponer, et al.
Journal of Molecular Biology (2023) Vol. 435, Iss. 5, pp. 167971-167971
Open Access | Times Cited: 53
Coacervate Droplets for Synthetic Cells
Zi Lin, Thomas Beneyton, Jean‐Christophe Baret, et al.
Small Methods (2023) Vol. 7, Iss. 12
Open Access | Times Cited: 53
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