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:

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: 262

Showing 1-25 of 262 citing articles:

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: 226

The molecular basis for cellular function of intrinsically disordered protein regions
Alex S. Holehouse, Birthe B. Kragelund
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 187-211
Open Access | Times Cited: 180

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: 130

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: 124

Improving Martini 3 for Disordered and Multidomain Proteins
F. Emil Thomasen, Francesco Pesce, Mette Ahrensback Roesgaard, et al.
Journal of Chemical Theory and Computation (2022) Vol. 18, Iss. 4, pp. 2033-2041
Open Access | Times Cited: 115

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
Lara A. Gruijs da Silva, Francesca Simonetti, Saskia Hutten, et al.
The EMBO Journal (2022) Vol. 41, Iss. 8
Open Access | Times Cited: 114

Conformational ensembles of the human intrinsically disordered proteome
Giulio Tesei, Anna Ida Trolle, Nicolas Jonsson, et al.
Nature (2024) Vol. 626, Iss. 8000, pp. 897-904
Closed Access | Times Cited: 103

Direct prediction of intrinsically disordered protein conformational properties from sequence
Jeffrey M. Lotthammer, Garrett M. Ginell, Daniel Griffith, et al.
Nature Methods (2024) Vol. 21, Iss. 3, pp. 465-476
Open Access | Times Cited: 82

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: 74

Competing interactions give rise to two-state behavior and switch-like transitions in charge-rich intrinsically disordered proteins
Xiangze Zeng, Kiersten M. Ruff, Rohit V. Pappu
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 19
Open Access | Times Cited: 67

Visualizing the disordered nuclear transport machinery in situ
Miao Yu, Maziar Heidari, Sofya Mikhaleva, et al.
Nature (2023) Vol. 617, Iss. 7959, pp. 162-169
Open Access | Times Cited: 67

Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins
F. Emil Thomasen, Kresten Lindorff‐Larsen
Biochemical Society Transactions (2022) Vol. 50, Iss. 1, pp. 541-554
Open Access | Times Cited: 66

Sequence-specific interactions determine viscoelasticity and ageing dynamics of protein condensates
Ibraheem Alshareedah, Wade M. Borcherds, Samuel R. Cohen, et al.
Nature Physics (2024) Vol. 20, Iss. 9, pp. 1482-1491
Open Access | Times Cited: 26

Active learning of the thermodynamics-dynamics trade-off in protein condensates
Yaxin An, Michael Webb, William M. Jacobs
Science Advances (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 16

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: 12

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: 12

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: 64

Intrinsically disordered regions that drive phase separation form a robustly distinct protein class
Ayyam Y. Ibrahim, Nathan P. Khaodeuanepheng, Dhanush L. Amarasekara, et al.
Journal of Biological Chemistry (2022) Vol. 299, Iss. 1, pp. 102801-102801
Open Access | Times Cited: 48

Kinase regulation by liquid–liquid phase separation
Tania P. López-Palacios, Joshua L. Andersen
Trends in Cell Biology (2022) Vol. 33, Iss. 8, pp. 649-666
Open Access | Times Cited: 48

Rules of Physical Mathematics Govern Intrinsically Disordered Proteins
Kingshuk Ghosh, Jonathan Huihui, Michael W. Phillips, et al.
Annual Review of Biophysics (2022) Vol. 51, Iss. 1, pp. 355-376
Open Access | Times Cited: 42

Protein structural transitions critically transform the network connectivity and viscoelasticity of RNA-binding protein condensates but RNA can prevent it
Andrés R. Tejedor, Ignacio Sanchez‐Burgos, Maria Estevez-Espinosa, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 40

On the stability and layered organization of protein-DNA condensates
Andrew P. Latham, Bin Zhang
Biophysical Journal (2022) Vol. 121, Iss. 9, pp. 1727-1737
Open Access | Times Cited: 39

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: 38

Modeling Concentration-dependent Phase Separation Processes Involving Peptides and RNA via Residue-Based Coarse-Graining
Gilberto Valdés‐García, Lim Heo, Lisa J. Lapidus, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 2, pp. 669-678
Open Access | Times Cited: 25

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