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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:

Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior
Benjamin S. Schuster, Gregory L. Dignon, Wai Shing Tang, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 21, pp. 11421-11431
Open Access | Times Cited: 286

Showing 1-25 of 286 citing articles:

Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains
Anne Bremer, Mina Farag, Wade M. Borcherds, et al.
Nature Chemistry (2021) Vol. 14, Iss. 2, pp. 196-207
Open Access | Times Cited: 400
Peptide-based coacervates as biomimetic protocells
Manzar Abbas, Wojciech P. Lipiński, Jiahua Wang, et al.
Chemical Society Reviews (2021) Vol. 50, Iss. 6, pp. 3690-3705
Open Access | Times Cited: 334
Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
Giulio Tesei, Thea K. Schulze, Ramón Crehuet, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 44
Open Access | Times Cited: 289
Physics-driven coarse-grained model for biomolecular phase separation with near-quantitative accuracy
Jerelle A. Joseph, Aleks Reinhardt, Anne Aguirre, et al.
Nature Computational Science (2021) Vol. 1, Iss. 11, pp. 732-743
Open Access | Times Cited: 260
Comparative roles of charge, π , and hydrophobic interactions in sequence-dependent phase separation of intrinsically disordered proteins
Suman Das, Yi‐Hsuan Lin, Robert M. Vernon, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 46, pp. 28795-28805
Open Access | Times Cited: 256
How do intrinsically disordered protein regions encode a driving force for liquid–liquid phase separation?
Wade M. Borcherds, Anne Bremer, Madeleine B. Borgia, et al.
Current Opinion in Structural Biology (2020) Vol. 67, pp. 41-50
Open Access | Times Cited: 252
Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof
Erik Martin, Alex S. Holehouse
Emerging Topics in Life Sciences (2020) Vol. 4, Iss. 3, pp. 307-329
Closed Access | Times Cited: 225
Molecular Details of Protein Condensates Probed by Microsecond Long Atomistic Simulations
Wenwei Zheng, Gregory L. Dignon, Nina Jovic, et al.
The Journal of Physical Chemistry B (2020) Vol. 124, Iss. 51, pp. 11671-11679
Open Access | Times Cited: 192
Improved coarse‐grained model for studying sequence dependent phase separation of disordered proteins
Roshan Mammen Regy, J Thompson, Young C. Kim, et al.
Protein Science (2021) Vol. 30, Iss. 7, pp. 1371-1379
Open Access | Times Cited: 183
A short peptide synthon for liquid–liquid phase separation
Manzar Abbas, Wojciech P. Lipiński, Karina K. Nakashima, et al.
Nature Chemistry (2021) Vol. 13, Iss. 11, pp. 1046-1054
Open Access | Times Cited: 183
Unraveling Molecular Interactions in Liquid–Liquid Phase Separation of Disordered Proteins by Atomistic Simulations
Matteo Paloni, Rémy Bailly, Luca Ciandrini, et al.
The Journal of Physical Chemistry B (2020) Vol. 124, Iss. 41, pp. 9009-9016
Open Access | Times Cited: 141
The living interface between synthetic biology and biomaterial design
Allen P. Liu, Eric A. Appel, Paul D. Ashby, et al.
Nature Materials (2022) Vol. 21, Iss. 4, pp. 390-397
Open Access | Times Cited: 141
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
Physics-based computational and theoretical approaches to intrinsically disordered proteins
Joan‐Emma Shea, Robert B. Best, Jeetain Mittal
Current Opinion in Structural Biology (2021) Vol. 67, pp. 219-225
Open Access | Times Cited: 134
Learning the chemical grammar of biomolecular condensates
Henry R. Kilgore, Richard A. Young
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1298-1306
Open Access | Times Cited: 116
Molecular interactions contributing to FUS SYGQ LC-RGG phase separation and co-partitioning with RNA polymerase II heptads
Anastasia C. Murthy, Wai Shing Tang, Nina Jovic, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 11, pp. 923-935
Open Access | Times Cited: 109
Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions
Mina Farag, Wade M. Borcherds, Anne Bremer, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 98
Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins
Yuri Hong, Saeed Najafi, Thomas M. Casey, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 97
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
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
Giulio Tesei, Kresten Lindorff‐Larsen
Open Research Europe (2023) Vol. 2, pp. 94-94
Open Access | Times Cited: 83
Minimalist Design of an Intrinsically Disordered Protein-Mimicking Scaffold for an Artificial Membraneless Organelle
Jianhui Liu, Fariza Zhorabek, Xin Dai, et al.
ACS Central Science (2022) Vol. 8, Iss. 4, pp. 493-500
Open Access | Times Cited: 77
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
Liquid–Liquid Phase Separation Modifies the Dynamic Properties of Intrinsically Disordered Proteins
Serafima Guseva, Vincent Schnapka, Wiktor Adamski, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 19, pp. 10548-10563
Open Access | Times Cited: 59
Stress-related biomolecular condensates in plants
Jorge Solís-Miranda, Monika Chodasiewicz, Aleksandra Skirycz, et al.
The Plant Cell (2023) Vol. 35, Iss. 9, pp. 3187-3204
Open Access | Times Cited: 48
Sequence-dependent material properties of biomolecular condensates and their relation to dilute phase conformations
Dinesh Sundaravadivelu Devarajan, Jiahui Wang, Beata Szała-Mendyk, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 47
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