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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 51-75 of 63 citing articles:

Identifying Native and Non-native Membrane Protein Loops by Using Stabilizing Energetic Terms of Three Popular Force Fields
Konda Mani Saravanan, Haiping Zhang, Yanjie Wei
Current Chinese Science (2020) Vol. 1, Iss. 1, pp. 14-21
Closed Access | Times Cited: 3
Research progress of molecular structure and dynamics of biological water
Shuji Ye, Li Chuan-Zhao, Jiahui Zhang, et al.
Acta Physica Sinica (2019) Vol. 68, Iss. 1, pp. 013101-013101
Open Access | Times Cited: 3
Sequence-ensemble-function relationships for disordered proteins in live cells
Alex S. Holehouse, Ryan J. Emenecker, Karina Guadalupe, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 1
A Tale of Two Chains: Geometries of a Chain Model and Protein Native State Structures
Tatjana Škrbić, Achille Giacometti, Trinh Xuan Hoang, et al.
Polymers (2024) Vol. 16, Iss. 4, pp. 502-502
Open Access
Coordinate-Dependent Drift-Diffusion Reveals the Kinetic Intermediate Traps of Top7-Based Proteins
Ronaldo Junio de Oliveira
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 51, pp. 10854-10869
Closed Access | Times Cited: 2
Probing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment
David Moses, Feng Yu, Garrett M. Ginell, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 2
The interplay between molten globules and heme disassociation defines human hemoglobin disassembly
Premila P. Samuel, Mark A. White, W.C. Ou, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 1
Protein folding: how, why, and beyond
Athi N. Naganathan
Elsevier eBooks (2020), pp. 3-22
Closed Access | Times Cited: 1
A theoretical study on the effects of interdomain flexibility on drug encounter rate for coronavirus nucleocapsid-type proteins
Tatsuhito Matsuo
Biophysical Chemistry (2021) Vol. 272, pp. 106574-106574
Open Access | Times Cited: 1
Protein stabilisation by polymersome entrapment
Denis Cecchin, Giuseppe Battaglia
arXiv (Cornell University) (2016)
Closed Access
Protein structure, activity and thermal stability within nanoscopic compartments
Denis Cecchin Luca Chierico, Xiaohe Tian, Katharina Kluthe, et al.
arXiv (Cornell University) (2016)
Open Access
TMAO: Protecting Proteins from Feeling the Heat
Mayank Boob, Shahar Sukenik, Martin Gruebele, et al.
(2020)
Open Access
TMAO: Protecting Proteins from Feeling the Heat
Mayank Boob, Shahar Sukenik, Martin Gruebele, et al.
(2020)
Open Access
Solvent Organization and Electrostatics Tuned by Solute Electronic Structure: Amide vs. Non-Amide Carbonyls
Steven D.E. Fried, Chu Zheng, Yuezhi Mao, et al.
(2022)
Open Access
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