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:

Perspectives on Ligand/Protein Binding Kinetics Simulations: Force Fields, Machine Learning, Sampling, and User-Friendliness
Paolo Conflitti, Stefano Raniolo, Vittorio Limongelli
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 18, pp. 6047-6061
Open Access | Times Cited: 16

Showing 16 citing articles:

Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery
Paolo Conflitti, Edward Lyman, Mark S.P. Sansom, et al.
Nature Reviews Drug Discovery (2025)
Closed Access | Times Cited: 3

Investigating the effects of chitosan atomic ratio and drug type on mechanical properties of silica aerogel/chitosan nanocomposites using molecular dynamics approach
Saina Alasvandian, Mohamad Shahgholi, Arash Karimipour
Journal of Molecular Liquids (2024) Vol. 401, pp. 124639-124639
Closed Access | Times Cited: 14

Machine Learning Interatomic Potentials for Catalysis
Deqi Tang, Rangsiman Ketkaew, Sandra Luber
Chemistry - A European Journal (2024) Vol. 30, Iss. 60
Open Access | Times Cited: 8

The Open Force Field Initiative: Open Software and Open Science for Molecular Modeling
Lily Wang, Pavan Kumar Behara, Matthew W. Thompson, et al.
The Journal of Physical Chemistry B (2024)
Open Access | Times Cited: 7

Current Status of Computational Approaches for Small Molecule Drug Discovery
Weijun Xu
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 21, pp. 18633-18636
Open Access | Times Cited: 6

Trust the force, but pull wisely: Structural insights into non-equilibrium response forces from pulling MD simulations
Fabian Koch, Miriam Jäger, Victor Tänzel, et al.
The Journal of Chemical Physics (2025) Vol. 162, Iss. 14
Closed Access

Exploring Membrane Cholesterol Binding to the CB1 Receptor: A Computational Perspective
Manuela J. Vanegas, Sara Gómez, Chiara Cappelli, et al.
The Journal of Physical Chemistry B (2025)
Closed Access

Mechanism of Ligand Binding to Theophylline RNA Aptamer
Sana Akhter, Zhichao Tang, Jinan Wang, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 3, pp. 1017-1029
Open Access | Times Cited: 2

Host–Guest Binding Free Energies à la Carte: An Automated OneOPES Protocol
Pedro Febrer Martinez, Valerio Rizzi, Simone Aureli, et al.
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 22, pp. 10275-10287
Open Access | Times Cited: 2

Computational screening of the effects of mutations on protein-protein off-rates and dissociation mechanisms by τRAMD
Giulia D’Arrigo, Daria B. Kokh, Ariane Nunes‐Alves, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Computational screening of the effects of mutations on protein-protein off-rates and dissociation mechanisms by τRAMD
Giulia D’Arrigo, Daria B. Kokh, Ariane Nunes‐Alves, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 1

Increased throughput in methods for simulating protein ligand binding and unbinding
Syeda Rehana Zia, Adriana Coricello, Giovanni Bottegoni
Current Opinion in Structural Biology (2024) Vol. 87, pp. 102871-102871
Open Access

Host-Guest binding free energies à la carte: an automated OneOPES protocol
Pedro Febrer Martinez, Valerio Rizzi, Simone Aureli, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Pathway Specific Unbinding Free Energy Profiles of Ritonavir Dissociation From HIV-1 Protease
Emily Vig, Jianan Sun, Chia‐en A. Chang
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Detection of Putative Ligand Dissociation Pathways in Proteins Using Site-Identification by Ligand Competitive Saturation
Wenbo Yu, David J. Weber, Alexander D. MacKerell
Journal of Chemical Information and Modeling (2024)
Closed Access

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