Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins
Xiangze Zeng, Alex S. Holehouse, Ashutosh Chilkoti, et al.
Biophysical Journal (2020) Vol. 119, Iss. 2, pp. 402-418
Open Access | Times Cited: 113

Showing 1-25 of 113 citing articles:

The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA
Jasmine Cubuk, Jhullian J. Alston, J. Jeremías Incicco, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 502
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
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
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
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: 254
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
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
Phase-separating RNA-binding proteins form heterogeneous distributions of clusters in subsaturated solutions
Mrityunjoy Kar, Furqan Dar, Timothy J. Welsh, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 28
Open Access | Times Cited: 210
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
A multi-step nucleation process determines the kinetics of prion-like domain phase separation
Erik Martin, Tyler S. Harmon, Jesse B. Hopkins, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 110
Sequence grammar underlying the unfolding and phase separation of globular proteins
Kiersten M. Ruff, Yoon Hee Choi, Dezerae Cox, et al.
Molecular Cell (2022) Vol. 82, Iss. 17, pp. 3193-3208.e8
Open Access | Times Cited: 83
Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate
Ian Seim, Ammon E. Posey, Wilton T. Snead, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 13
Open Access | Times Cited: 80
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
RNAs undergo phase transitions with lower critical solution temperatures
Gable M. Wadsworth, Walter J. Zahurancik, Xiangze Zeng, et al.
Nature Chemistry (2023) Vol. 15, Iss. 12, pp. 1693-1704
Open Access | Times Cited: 72
Fundamental Aspects of Phase-Separated Biomolecular Condensates
Huan‐Xiang Zhou, Divya Kota, Sanbo Qin, et al.
Chemical Reviews (2024) Vol. 124, Iss. 13, pp. 8550-8595
Closed Access | Times Cited: 23
Biomolecular condensates form spatially inhomogeneous network fluids
Furqan Dar, Samuel R. Cohen, Diana M. Mitrea, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 21
Prediction of phase separation propensities of disordered proteins from sequence
Sören von Bülow, Giulio Tesei, Kresten Lindorff‐Larsen
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 18
Prediction of phase-separation propensities of disordered proteins from sequence
Sören von Bülow, Giulio Tesei, Fatima Zaidi, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 13
Open Access | Times Cited: 2
Generalized models for bond percolation transitions of associative polymers
Jeong‐Mo Choi, Anthony A. Hyman, Rohit V. Pappu
Physical review. E (2020) Vol. 102, Iss. 4
Open Access | Times Cited: 122
Clustering of Aromatic Residues in Prion-like Domains Can Tune the Formation, State, and Organization of Biomolecular Condensates
Alex S. Holehouse, Garrett M. Ginell, Daniel Griffith, et al.
Biochemistry (2021) Vol. 60, Iss. 47, pp. 3566-3581
Open Access | Times Cited: 92
The Protein Folding Problem: The Role of Theory
Roy Nassar, Gregory L. Dignon, Rostam M. Razban, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 20, pp. 167126-167126
Open Access | Times Cited: 86
Intrinsically disordered proteins and biomolecular condensates as drug targets
Mateusz Biesaga, Marta Frigolé‐Vivas, Xavier Salvatella
Current Opinion in Chemical Biology (2021) Vol. 62, pp. 90-100
Open Access | Times Cited: 85
Molecular dynamics simulations of DNA–DNA and DNA–protein interactions
Jejoong Yoo, David Winogradoff, Aleksei Aksimentiev
Current Opinion in Structural Biology (2020) Vol. 64, pp. 88-96
Open Access | Times Cited: 84
Phase separation vs aggregation behavior for model disordered proteins
Ushnish Rana, Clifford P. Brangwynne, Athanassios Z. Panagiotopoulos
The Journal of Chemical Physics (2021) Vol. 155, Iss. 12
Open Access | Times Cited: 81
Page 1 - Next Page

Scroll to top