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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:

Computational prediction of protein–protein binding affinities
Till Siebenmorgen, Martin Zacharias
Wiley Interdisciplinary Reviews Computational Molecular Science (2019) Vol. 10, Iss. 3
Open Access | Times Cited: 148

Showing 1-25 of 148 citing articles:

The SARS-CoV-2 Spike variant D614G favors an open conformational state
Rachael A. Mansbach, Srirupa Chakraborty, Kien Nguyen, et al.
Science Advances (2021) Vol. 7, Iss. 16
Open Access | Times Cited: 190
Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry
Yuming Jiang, Rex Devasahayam Arokia Balaya, Dina Schuster, et al.
ACS Measurement Science Au (2024) Vol. 4, Iss. 4, pp. 338-417
Open Access | Times Cited: 21
MISATO: machine learning dataset of protein–ligand complexes for structure-based drug discovery
Till Siebenmorgen, Filipe Menezes, Sabrina Benassou, et al.
Nature Computational Science (2024) Vol. 4, Iss. 5, pp. 367-378
Open Access | Times Cited: 17
An Effective MM/GBSA Protocol for Absolute Binding Free Energy Calculations: A Case Study on SARS-CoV-2 Spike Protein and the Human ACE2 Receptor
Negin Forouzesh, Nikita Mishra
Molecules (2021) Vol. 26, Iss. 8, pp. 2383-2383
Open Access | Times Cited: 88
BFEE2: Automated, Streamlined, and Accurate Absolute Binding Free-Energy Calculations
Haohao Fu, Haochuan Chen, Wensheng Cai, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 5, pp. 2116-2123
Closed Access | Times Cited: 62
Machine learning solutions for predicting protein–protein interactions
Rita Casadio, Pier Luigi Martelli, Castrense Savojardo
Wiley Interdisciplinary Reviews Computational Molecular Science (2022) Vol. 12, Iss. 6
Open Access | Times Cited: 49
RosettaDDGPrediction for high‐throughput mutational scans: From stability to binding
Valentina Sora, Adrian Otamendi Laspiur, Kristine Degn, et al.
Protein Science (2022) Vol. 32, Iss. 1
Open Access | Times Cited: 40
How the ovalbumin modulates the conformation of zein through protein-protein interactions
Hujun Xie, Hao Li, Lei Liu, et al.
Food Hydrocolloids (2024), pp. 110696-110696
Closed Access | Times Cited: 8
Accuracy of Molecular Simulation-Based Predictions of koff Values: A Metadynamics Study
Riccardo Capelli, Wenping Lyu, Viacheslav Bolnykh, et al.
The Journal of Physical Chemistry Letters (2020) Vol. 11, Iss. 15, pp. 6373-6381
Open Access | Times Cited: 52
Building intuition for binding free energy calculations: Bound state definition, restraints, and symmetry
Élise Duboué-Dijon, Jérôme Hénin
The Journal of Chemical Physics (2021) Vol. 154, Iss. 20
Open Access | Times Cited: 47
In silico investigation of critical binding pattern in SARS-CoV-2 spike protein with angiotensin-converting enzyme 2
Farzaneh Jafary, Sepideh Jafari, Mohamad Reza Ganjalikhany
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 42
A highly accurate metadynamics-based Dissociation Free Energy method to calculate protein–protein and protein–ligand binding potencies
Jing Wang, Alexey Ishchenko, Wei Zhang, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 36
Binding affinity estimation from restrained umbrella sampling simulations
Vivek Govind Kumar, Adithya Polasa, Shilpi Agrawal, et al.
Nature Computational Science (2022) Vol. 3, Iss. 1, pp. 59-70
Open Access | Times Cited: 32
Towards design of drugs and delivery systems with the Martini coarse-grained model
Lisbeth R. Kjølbye, Gilberto P. Pereira, Alessio Bartocci, et al.
QRB Discovery (2022) Vol. 3
Open Access | Times Cited: 29
How the strength of proteins interactions affects the phase behavior of protein complexes
Qingbo Jiao, Haoxin Ye, Nan Lv, et al.
Food Hydrocolloids (2023) Vol. 149, pp. 109654-109654
Closed Access | Times Cited: 18
Exploring the Conformational Ensembles of Protein–Protein Complex with Transformer-Based Generative Model
Jianmin Wang, Xun Wang, Yanyi Chu, et al.
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 11, pp. 4469-4480
Closed Access | Times Cited: 6
Perspectives on High-Throughput Ligand/Protein Docking With Martini MD Simulations
Paulo C. T. Souza, Vittorio Limongelli, Sangwook Wu, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 38
Native or Non-Native Protein–Protein Docking Models? Molecular Dynamics to the Rescue
Zuzana Jandová, Attilio V. Vargiu, Alexandre M. J. J. Bonvin
Journal of Chemical Theory and Computation (2021) Vol. 17, Iss. 9, pp. 5944-5954
Open Access | Times Cited: 34
Predicting the mutation effects of protein–ligand interactions via end-point binding free energy calculations: strategies and analyses
Yang Yu, Zhe Wang, Lingling Wang, et al.
Journal of Cheminformatics (2022) Vol. 14, Iss. 1
Open Access | Times Cited: 26
The disordered N-terminal tail of SARS CoV-2 Nucleocapsid protein forms a dynamic complex with RNA
Jasmine Cubuk, Jhullian J. Alston, J. Jeremías Incicco, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 14
Comparative Binding Ability of Human Monoclonal Antibodies against Omicron Variants of SARS-CoV-2: An In Silico Investigation
Nabarun Chandra Das, Pritha Chakraborty, Jagadeesh Bayry, et al.
Antibodies (2023) Vol. 12, Iss. 1, pp. 17-17
Open Access | Times Cited: 14
Standard Binding Free-Energy Calculations: How Far Are We from Automation?
Haohao Fu, Christophe Chipot, Xueguang Shao, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 49, pp. 10459-10468
Closed Access | Times Cited: 13
The physical logic of protein machines
J. Michael McBride, Tsvi Tlusty
Journal of Statistical Mechanics Theory and Experiment (2024) Vol. 2024, Iss. 2, pp. 024001-024001
Open Access | Times Cited: 5
Computationally Derived Structural Insights into Rare Earth Selectivity in Lanmodulin and its Variants
Karuna Anna Sajeevan, Bibek Acharya, Sakib Ferdous, et al.
Computational and Structural Biotechnology Journal (2025) Vol. 27, pp. 639-648
Open Access
Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints
Evangelia Notari, Christopher W. Wood, Julien Michel
Journal of Chemical Theory and Computation (2025)
Open Access
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