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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:

Interplay between Conformational Entropy and Solvation Entropy in Protein–Ligand Binding
Maria Luisa Verteramo, Olof Stenström, Majda Misini Ignjatović, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 5, pp. 2012-2026
Open Access | Times Cited: 114

Showing 1-25 of 114 citing articles:

Ligand binding remodels protein side-chain conformational heterogeneity
Stephanie A. Wankowicz, Saulo H de Oliveira, Daniel W. Hogan, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 73
Overview of Recent Strategic Advances in Medicinal Chemistry
Gaochan Wu, Tong Zhao, Dongwei Kang, et al.
Journal of Medicinal Chemistry (2019) Vol. 62, Iss. 21, pp. 9375-9414
Open Access | Times Cited: 144
Assessing the Binding Performance of Amyloid–Carbon Membranes toward Heavy Metal Ions
Mohammad Peydayesh, Sreenath Bolisetty, Toraj Mohammadi, et al.
Langmuir (2019) Vol. 35, Iss. 11, pp. 4161-4170
Closed Access | Times Cited: 93
Peptide-based inhibitors of protein–protein interactions: biophysical, structural and cellular consequences of introducing a constraint
Hongshuang Wang, Robert S. Dawber, Peiyu Zhang, et al.
Chemical Science (2021) Vol. 12, Iss. 17, pp. 5977-5993
Open Access | Times Cited: 88
Interplay of halogen bonding and solvation in protein–ligand binding
Maria Luisa Verteramo, Majda Misini Ignjatović, Rohit Kumar, et al.
iScience (2024) Vol. 27, Iss. 4, pp. 109636-109636
Open Access | Times Cited: 10
Minimizing the Entropy Penalty for Ligand Binding: Lessons from the Molecular Recognition of the Histo Blood‐Group Antigens by Human Galectin‐3
Ana Gimeno, Sandra Delgado, Pablo Valverde, et al.
Angewandte Chemie International Edition (2019) Vol. 58, Iss. 22, pp. 7268-7272
Open Access | Times Cited: 65
Entropy–Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C
Johan Wallerstein, Vilhelm Ekberg, Majda Misini Ignjatović, et al.
JACS Au (2021) Vol. 1, Iss. 4, pp. 484-500
Open Access | Times Cited: 40
Prediction of Protein–ATP Binding Residues Based on Ensemble of Deep Convolutional Neural Networks and LightGBM Algorithm
Jiazhi Song, Guixia Liu, Jingqing Jiang, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 2, pp. 939-939
Open Access | Times Cited: 34
Harnessing the cyclization strategy for new drug discovery
Kai Tang, Shu Wang, Wenshuo Gao, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 12, Iss. 12, pp. 4309-4326
Open Access | Times Cited: 25
Spatially Resolved Hydration Thermodynamics in Biomolecular Systems
Saumyak Mukherjee, Lars V. Schäfer
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 20, pp. 3619-3631
Open Access | Times Cited: 24
Ligand Strain and Its Conformational Complexity Is a Major Factor in the Binding of Cyclic Dinucleotides to STING Protein
Miroslav Smola, Ondrej Gutten, Milan Dejmek, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 18, pp. 10172-10178
Open Access | Times Cited: 31
Applications of isothermal titration calorimetry in pure and applied research from 2016 to 2020
Robert J. Falconer, Boelo Schuur, Anthony Mittermaier
Journal of Molecular Recognition (2021) Vol. 34, Iss. 10
Open Access | Times Cited: 28
Cellular and molecular responses of earthworm coelomocytes and antioxidant enzymes to naphthalene and a major metabolite (1-naphthol)
Mingyang Jing, Guangye Han, Yuze Li, et al.
Journal of Molecular Liquids (2022) Vol. 350, pp. 118563-118563
Closed Access | Times Cited: 20
Discovery of Novel Inhibitors of BRD4 for Treating Prostate Cancer: A Comprehensive Case Study for Considering Water Networks in Virtual Screening and Drug Design
Haiyang Zhong, Xinyue Wang, Shicheng Chen, et al.
Journal of Medicinal Chemistry (2023) Vol. 67, Iss. 1, pp. 138-151
Closed Access | Times Cited: 12
Ligand-induced protein transition state stabilization switches the binding pathway from conformational selection to induced fit
Olof Stenström, Carl Diehl, Kristofer Modig, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 14
Open Access | Times Cited: 4
PPDock: Pocket Prediction-Based Protein–Ligand Blind Docking
Jie Du, Mingzhi Yuan, Ao Shen, et al.
Journal of Chemical Information and Modeling (2025)
Closed Access
Uncovering The Pharmacological Mechanism of Ficus elastica as Anti-hyperlipidemia Candidate: LC-HRMS, Network Pharmacology, In vitro and In vivo Studies
Gita Susanti, Yufri Aldi, Dian Handayani, et al.
Journal of Multidisciplinary Applied Natural Science (2025) Vol. 5, Iss. 1, pp. 332-351
Closed Access
Inhibitory Potential and Binding Thermodynamics of Scyllatoxin‐Based BH3 Domain Mimetics Targeting Repressor BCL2 Proteins
H. A. D. B. Amarasiri, Danushka Arachchige, Matthew J. K. Vince, et al.
Journal of Molecular Recognition (2025) Vol. 38, Iss. 2
Open Access
Integrated Network Pharmacology, Molecular Modeling, LC–MS Profiling, and Semisynthetic Approach for the Roots of Rubia tinctorum L. Metabolites in Cancer Treatment
Alaa A. El‐Banna, Enas E. Eltamany, Asmaa S. A. Yassen, et al.
ACS Omega (2025)
Open Access
Advances in uncovering the mechanisms of macromolecular conformational entropy
Stephanie A. Wankowicz, James S. Fraser
Nature Chemical Biology (2025)
Closed Access
Galectin-3: is this member of a large family of multifunctional lectins (already) a therapeutic target?
Antonio Romero, Hans‐Joachim Gabius
Expert Opinion on Therapeutic Targets (2019) Vol. 23, Iss. 10, pp. 819-828
Open Access | Times Cited: 34
19F Fast Magic-Angle Spinning NMR Spectroscopy on Microcrystalline Complexes of Fluorinated Ligands and the Carbohydrate Recognition Domain of Galectin-3
Roza Kalabekova, Caitlin M. Quinn, Kumar Tekwani Movellan, et al.
Biochemistry (2024) Vol. 63, Iss. 17, pp. 2207-2216
Closed Access | Times Cited: 3
Strong Adverse Contribution of Conformational Dynamics to Streptavidin–Biotin Binding
Mona Sarter, Doreen Niether, Bernd W. Koenig, et al.
The Journal of Physical Chemistry B (2019) Vol. 124, Iss. 2, pp. 324-335
Closed Access | Times Cited: 26
Predicting NMR relaxation of proteins from molecular dynamics simulations with accurate methyl rotation barriers
Falk Hoffmann, Frans A. A. Mulder, Lars V. Schäfer
The Journal of Chemical Physics (2020) Vol. 152, Iss. 8
Open Access | Times Cited: 26
Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation
Xinyao Xiang, Alexandar L. Hansen, Lei Yu, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 34, pp. 13593-13604
Open Access | Times Cited: 22
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