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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:

How does solvation in the cell affect protein folding and binding?
Caitlin M. Davis, Martin Gruebele, Shahar Sukenik
Current Opinion in Structural Biology (2017) Vol. 48, pp. 23-29
Open Access | Times Cited: 63

Showing 1-25 of 63 citing articles:

Intrinsically disordered regions are poised to act as sensors of cellular chemistry
David Moses, Garrett M. Ginell, Alex S. Holehouse, et al.
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 12, pp. 1019-1034
Open Access | Times Cited: 56
When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates
Paulette S. Romero-Pérez, Yanniv Dorone, Eduardo Flores, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9010-9035
Open Access | Times Cited: 43
Structural biases in disordered proteins are prevalent in the cell
David Moses, Karina Guadalupe, Feng Yu, et al.
Nature Structural & Molecular Biology (2024)
Open Access | Times Cited: 38
Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions
Alex S. Holehouse, Rohit V. Pappu
Annual Review of Biophysics (2018) Vol. 47, Iss. 1, pp. 19-39
Open Access | Times Cited: 118
Colloidal stability of the living cell
Håkan Wennerström, Eloy Vallina Estrada, Jens Danielsson, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 19, pp. 10113-10121
Open Access | Times Cited: 109
Protein shape modulates crowding effects
Alex J. Guseman, Gerardo M. Perez Goncalves, Shannon L. Speer, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 43, pp. 10965-10970
Open Access | Times Cited: 87
Revealing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment
David Moses, Feng Yu, Garrett M. Ginell, et al.
The Journal of Physical Chemistry Letters (2020) Vol. 11, Iss. 23, pp. 10131-10136
Open Access | Times Cited: 78
Weak, specific chemical interactions dictate barnase stability in diverse cellular environments
Ume Tahir, Caitlin M. Davis
Protein Science (2025) Vol. 34, Iss. 5
Open Access | Times Cited: 1
Polymer effects modulate binding affinities in disordered proteins
Renée Vancraenenbroeck, Yair Shalom Harel, Wenwei Zheng, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 39, pp. 19506-19512
Open Access | Times Cited: 75
Viewing SARS-CoV-2 Nucleocapsid Protein in Terms of Molecular Flexibility
Tatsuhito Matsuo
Biology (2021) Vol. 10, Iss. 6, pp. 454-454
Open Access | Times Cited: 34
Sequence-ensemble-function relationships for disordered proteins in live cells
Ryan J. Emenecker, Karina Guadalupe, Nora M. Shamoon, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 12
Protein Folding as a Jamming Transition
Alex T. Grigas, Zhuoyi Liu, Jack A. Logan, et al.
PRX Life (2025) Vol. 3, Iss. 1
Open Access
Hydrophobic Solvation and Liquid Water: A Theoretical Investigation Using Thermodynamic Perturbation and Integral Equations Theory
Umesh C. Roy, Pradipta Bandyopadhyay, Tomaž Urbič
Journal of Molecular Liquids (2025), pp. 127408-127408
Open Access
A hybrid, bottom-up, structurally accurate, Go¯-like coarse-grained protein model
Tanmoy Sanyal, Jeetain Mittal, M. Scott Shell
The Journal of Chemical Physics (2019) Vol. 151, Iss. 4
Open Access | Times Cited: 26
Protein folding and quinary interactions: creating cellular organisation through functional disorder
Sara S. Ribeiro, Simon Ebbinghaus, João Carlos Marcos
FEBS Letters (2018) Vol. 592, Iss. 18, pp. 3040-3053
Open Access | Times Cited: 24
Structural biases in disordered proteins are prevalent in the cell
David Moses, Karina Guadalupe, Feng Yu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 18
The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly
Premila P. Samuel, Mark A. White, William C. Ou, et al.
Biophysical Journal (2020) Vol. 118, Iss. 6, pp. 1381-1400
Open Access | Times Cited: 20
The Study of Molecules and Processes in Solution: An Overview of Questions, Approaches and Applications
Neani Tshilande, Лилиана Маммино, Mireille K. Bilonda
(2024)
Open Access | Times Cited: 2
The Study of Molecules and Processes in Solution: An Overview of Questions, Approaches and Applications
Neani Tshilande, Лилиана Маммино, Mireille K. Bilonda
Computation (2024) Vol. 12, Iss. 4, pp. 78-78
Open Access | Times Cited: 2
Inhibition of Microtubule Depolymerization by Osmolytes
George D. Bachand, Rishi K. Jain, Randy Ko, et al.
Biomacromolecules (2018) Vol. 19, Iss. 7, pp. 2401-2408
Closed Access | Times Cited: 18
Polyanions Cause Protein Destabilization Similar to That in Live Cells
Therese Sörensen, Sarah Leeb, Jens Danielsson, et al.
Biochemistry (2021) Vol. 60, Iss. 10, pp. 735-746
Open Access | Times Cited: 14
Presenting B-DNA as macromolecular crowding agent to improve efficacy of cytochrome c under various stresses
Sachin M. Shet, Pranav Bharadwaj, Meena Bisht, et al.
International Journal of Biological Macromolecules (2022) Vol. 215, pp. 184-191
Closed Access | Times Cited: 9
Solvent Organization and Electrostatics Tuned by Solute Electronic Structure: Amide versus Non-Amide Carbonyls
Steven D.E. Fried, Chu Zheng, Yuezhi Mao, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 31, pp. 5876-5886
Open Access | Times Cited: 9
Does macromolecular crowding compatible with enzyme stem bromelain structure and stability?
Kavya Bhakuni, Pannuru Venkatesu
International Journal of Biological Macromolecules (2019) Vol. 131, pp. 527-535
Closed Access | Times Cited: 15
Application of circular dichroism spectroscopy in studying protein folding, stability, and interaction
Md. Anzarul Haque, Punit Kaur, Asimul Islam, et al.
Elsevier eBooks (2022), pp. 213-224
Closed Access | Times Cited: 9
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