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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:

Principles Governing the Phase Separation of Multidomain Proteins
Priyesh Mohanty, Utkarsh Kapoor, Dinesh Sundaravadivelu Devarajan, et al.
Biochemistry (2022) Vol. 61, Iss. 22, pp. 2443-2455
Open Access | Times Cited: 66

Showing 1-25 of 66 citing articles:

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: 76
Heterotypic electrostatic interactions control complex phase separation of tau and prion into multiphasic condensates and co-aggregates
K. Sandeep, Roopali Khanna, Anamika Avni, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 2
Open Access | Times Cited: 44
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: 41
Determinants that enable disordered protein assembly into discrete condensed phases
Rachel M. Welles, Kandarp A. Sojitra, Mikael V. Garabedian, et al.
Nature Chemistry (2024) Vol. 16, Iss. 7, pp. 1062-1072
Closed Access | Times Cited: 37
Analytical Formulation and Field-Theoretic Simulation of Sequence-Specific Phase Separation of Protein-Like Heteropolymers with Short- and Long-Spatial-Range Interactions
Jonas Wessén, Suman Das, Tanmoy Pal, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 45, pp. 9222-9245
Open Access | Times Cited: 46
A synergy between site-specific and transient interactions drives the phase separation of a disordered, low-complexity domain
Priyesh Mohanty, Jayakrishna Shenoy, Azamat Rizuan, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 34
Open Access | Times Cited: 34
Expanding the molecular language of protein liquid-liquid phase separation
Shiv Rekhi, Cristobal Garcia Garcia, Mayur Barai, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 33
Role of Strong Localized vs Weak Distributed Interactions in Disordered Protein Phase Separation
Shiv Rekhi, Dinesh Sundaravadivelu Devarajan, Michael P. Howard, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 17, pp. 3829-3838
Open Access | Times Cited: 31
Conformational Properties of Polymers at Droplet Interfaces as Model Systems for Disordered Proteins
Jiahui Wang, Dinesh Sundaravadivelu Devarajan, Arash Nikoubashman, et al.
ACS Macro Letters (2023) Vol. 12, Iss. 11, pp. 1472-1478
Open Access | Times Cited: 24
Multiscale simulations reveal TDP-43 molecular-level interactions driving condensation
Helgi I. Ingólfsson, Azamat Rizuan, Xikun Liu, et al.
Biophysical Journal (2023) Vol. 122, Iss. 22, pp. 4370-4381
Open Access | Times Cited: 23
Coiled-coil domains are sufficient to drive liquid-liquid phase separation in protein models
Dominique Ramirez, Loren E. Hough, Michael R. Shirts
Biophysical Journal (2024) Vol. 123, Iss. 6, pp. 703-717
Open Access | Times Cited: 15
Phase separation as a new form of regulation in innate immunity
Lei Wang, Wen Zhou
Molecular Cell (2024) Vol. 84, Iss. 13, pp. 2410-2422
Closed Access | Times Cited: 11
Interplay between charge distribution and DNA in shaping HP1 paralog phase separation and localization
Tien M. Phan, Young C. Kim, Galia T. Debelouchina, et al.
eLife (2024) Vol. 12
Open Access | Times Cited: 9
Molecular interactions underlying the phase separation of HP1α: role of phosphorylation, ligand and nucleic acid binding
Cheenou Her, Tien M. Phan, Nina Jovic, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. 22, pp. 12702-12722
Open Access | Times Cited: 37
A Zn‐dependent structural transition of SOD1 modulates its ability to undergo phase separation
Bidisha Das, Sumangal Roychowdhury, Priyesh Mohanty, et al.
The EMBO Journal (2022) Vol. 42, Iss. 2
Open Access | Times Cited: 33
Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins
Dinesh Sundaravadivelu Devarajan, Shiv Rekhi, Arash Nikoubashman, et al.
Macromolecules (2022) Vol. 55, Iss. 20, pp. 8987-8997
Open Access | Times Cited: 29
A complex network of interdomain interactions underlies the conformational ensemble of monomeric TDP‐43 and modulates its phase behavior
Priyesh Mohanty, Azamat Rizuan, Young C. Kim, et al.
Protein Science (2023) Vol. 33, Iss. 2
Open Access | Times Cited: 18
Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations
Beata Szała-Mendyk, Tien M. Phan, Priyesh Mohanty, et al.
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102333-102333
Open Access | Times Cited: 16
Kinetic trapping organizes actin filaments within liquid-like protein droplets
Aravind Chandrasekaran, Kristin Graham, Jeanne C. Stachowiak, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Protein conformation and biomolecular condensates
Diego S. Vazquez, Pamela L. Toledo, Alejo R. Gianotti, et al.
Current Research in Structural Biology (2022) Vol. 4, pp. 285-307
Open Access | Times Cited: 24
Programmable de novo designed coiled coil-mediated phase separation in mammalian cells
Maruša Ramšak, Dominique Ramirez, Loren E. Hough, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Recent advances in the synthesis and application of biomolecular condensates
Zhongyue Li, Wei Tan, Guoping Zhao, et al.
Journal of Biological Chemistry (2025), pp. 108188-108188
Closed Access
Optimal scaling of protein-water interactions coupled with targeted torsional refinements yields balanced force fields suitable for simulations of single-chain folded proteins, disordered polypeptides, and protein-protein complexes
Jeetain Mittal, Tien Phan, Priyesh Mohanty
Research Square (Research Square) (2025)
Closed Access
The mechanobiology of biomolecular condensates
Neus Sanfeliu-Cerdán, Michael Krieg
Biophysics Reviews (2025) Vol. 6, Iss. 1
Open Access
Determinants of Disordered Protein Co-Assembly Into Discrete Condensed Phases
Rachel M. Welles, Kandarp A. Sojitra, Mikael V. Garabedian, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 12
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