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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 accurately do force fields represent protein side chain ensembles?
Dušan Petrović, Xue Wang, Birgit Strodel
Proteins Structure Function and Bioinformatics (2018) Vol. 86, Iss. 9, pp. 935-944
Closed Access | Times Cited: 19

Showing 19 citing articles:

Investigating Biomolecules in Deep Eutectic Solvents with Molecular Dynamics Simulations: Current State, Challenges and Future Perspectives
Jan Philipp Bittner, Ирина Смирнова, Sven Jakobtorweihen
Molecules (2024) Vol. 29, Iss. 3, pp. 703-703
Open Access | Times Cited: 20
Charge transfer from the carotenoid can quench chlorophyll excitation in antenna complexes of plants
Lorenzo Cupellini, Dario Calvani, Denis Jacquemin, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 115
Comparison and Validation of Force Fields for Deep Eutectic Solvents in Combination with Water and Alcohol Dehydrogenase
Jan Philipp Bittner, Lei Huang, Ningning Zhang, et al.
Journal of Chemical Theory and Computation (2021) Vol. 17, Iss. 8, pp. 5322-5341
Open Access | Times Cited: 26
Elastomeric behavior of the Bombyx mori fibroin (GAGAGS)n tandem motifs
Álvaro Ridruejo, Luis F. Pacios, Joseph Arguelles, et al.
Journal of the mechanical behavior of biomedical materials/Journal of mechanical behavior of biomedical materials (2025), pp. 107002-107002
Closed Access
AF2χ: Predicting protein side-chain rotamer distributions with AlphaFold2
Matteo Cagiada, F. Emil Thomasen, Sergey Ovchinnikov, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Pairwise-additive and polarizable atomistic force fields for molecular dynamics simulations of proteins
Justin A. Lemkul
Progress in molecular biology and translational science (2020), pp. 1-71
Closed Access | Times Cited: 25
Fitting Force Field Parameters to NMR Relaxation Data
Felix Kümmerer, Simone Orioli, Kresten Lindorff‐Larsen
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 12, pp. 3741-3751
Open Access | Times Cited: 8
Molecular Dynamics Simulations for Rationalizing Polymer Bioconjugation Strategies: Challenges, Recent Developments, and Future Opportunities
Josef Kehrein, Christoph Sotriffer
ACS Biomaterials Science & Engineering (2023) Vol. 10, Iss. 1, pp. 51-74
Closed Access | Times Cited: 6
Molecular Modeling in Drug Delivery: Polymer Protective Coatings as Case Study
Alex Bunker, Josef Kehrein
(2024), pp. 104-198
Closed Access | Times Cited: 2
Unraveling the Allosteric Cross-Talk between the Coactivator Peptide and the Ligand-Binding Site in the Glucocorticoid Receptor
Giuseppina La Sala, Anders Gunnarsson, K. A. P. Edman, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 7, pp. 3667-3680
Open Access | Times Cited: 14
In silico analysis of PFN1 related to amyotrophic lateral sclerosis
Gabriel Rodrigues Coutinho Pereira, Giovanni Henrique Almeida Silva Tellini, Joelma Freire De Mesquita
PLoS ONE (2019) Vol. 14, Iss. 6, pp. e0215723-e0215723
Open Access | Times Cited: 13
Rad5 HIRAN domain: Structural insights into its interaction with ssDNA through molecular modeling approaches
Bruno Marques Silva, Lucianna Helene Santos, João Paulo P. de Almeida, et al.
Journal of Biomolecular Structure and Dynamics (2022) Vol. 41, Iss. 7, pp. 3062-3075
Open Access | Times Cited: 3
A backbone‐dependent rotamer library with high (ϕ, ψ) coverage using metadynamics simulations
Jennifer C. Mortensen, Jovan Damjanovic, J. Miao, et al.
Protein Science (2022) Vol. 31, Iss. 12
Open Access | Times Cited: 3
Crystal structures of Streptomyces tsukubaensis sigma factor SigG1 and anti-sigma RsfG
José P. Leite, Frederico M. Lourenço, Rute Oliveira, et al.
Journal of Structural Biology (2023) Vol. 215, Iss. 4, pp. 108038-108038
Open Access | Times Cited: 1
Improving DNA Aptamers Against Heart Failure Protein Biomarker Using Structure-Guided Random Mutations Approaches for Colourimetric Biosensor Development
Donny Marcius, Bejo Ropii, Diah Safitri, et al.
Molecular Systems Design & Engineering (2024) Vol. 9, Iss. 10, pp. 1023-1035
Closed Access
Oncogenic Mutations in the DNA-Binding Domain of FOXO1 that Disrupt Folding: Quantitative Insights from Experiments and Molecular Simulations
Dylan Novack, Lei Qian, Gwyneth Acker, et al.
Biochemistry (2022) Vol. 61, Iss. 16, pp. 1669-1682
Open Access | Times Cited: 2
Fitting Force Field parameters to NMR Relaxation Data
Felix Kümmerer, Simone Orioli, Kresten Lindorff‐Larsen
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Unraveling the Allosteric Cross-Talk Between Coactivator Peptide and Ligand Binding Site in Glucocorticoid Receptor
Giuseppina La Sala, Anders Gunnarsson, K. A. P. Edman, et al.
(2021)
Open Access
Unraveling the Allosteric Cross-Talk Between Coactivator Peptide and Ligand Binding Site in Glucocorticoid Receptor
Giuseppina La Sala, Anders Gunnarsson, K. A. P. Edman, et al.
(2021)
Open Access
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