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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:

Assessment of software methods for estimating protein-protein relative binding affinities
Tawny R. Gonzalez, Kyle P. Martin, Jonathan E. Barnes, et al.
PLoS ONE (2020) Vol. 15, Iss. 12, pp. e0240573-e0240573
Open Access | Times Cited: 20

Showing 20 citing articles:

Ensemble-Based Mutational Profiling and Network Analysis of the SARS-CoV-2 Spike Omicron XBB Lineages for Interactions with the ACE2 Receptor and Antibodies: Cooperation of Binding Hotspots in Mediating Epistatic Couplings Underlies Binding Mechanism and Immune Escape
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 8, pp. 4281-4281
Open Access | Times Cited: 6
Fast, accurate ranking of engineered proteins by target-binding propensity using structure modeling
Xiaozhe Ding, Xinhong Chen, Erin E. Sullivan, et al.
Molecular Therapy (2024) Vol. 32, Iss. 6, pp. 1687-1700
Open Access | Times Cited: 5
Statistical modeling to quantify the uncertainty of FoldX-predicted protein folding and binding stability
Yesol Sapozhnikov, Jagdish Suresh Patel, F. Marty Ytreberg, et al.
BMC Bioinformatics (2023) Vol. 24, Iss. 1
Open Access | Times Cited: 12
AlphaFold2-Enabled Atomistic Modeling of Structure, Conformational Ensembles, and Binding Energetics of the SARS-CoV-2 Omicron BA.2.86 Spike Protein with ACE2 Host Receptor and Antibodies: Compensatory Functional Effects of Binding Hotspots in Modulating Mechanisms of Receptor Binding and Immune Escape
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 5, pp. 1657-1681
Closed Access | Times Cited: 3
Molecular Modeling Predicts Novel Antibody Escape Mutations in the Respiratory Syncytial Virus Fusion Glycoprotein
Sierra S. Beach, McKenna A. Hull, F. Marty Ytreberg, et al.
Journal of Virology (2022) Vol. 96, Iss. 13
Open Access | Times Cited: 13
Exploring the ability of the MD+FoldX method to predict SARS-CoV-2 antibody escape mutations using large-scale data
L. América, Jonathan E. Barnes, Jagdish Suresh Patel, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2
Atomistic simulations reveal impacts of missense mutations on the structure and function of SynGAP1
Aliaa A. Ali, Lili Li, Michael J. Courtney, et al.
Briefings in Bioinformatics (2024) Vol. 25, Iss. 6
Open Access | Times Cited: 1
Atomistic Simulations and In Silico Mutational Profiling of Protein Stability and Binding in the SARS-CoV-2 Spike Protein Complexes with Nanobodies: Molecular Determinants of Mutational Escape Mechanisms
Gennady M. Verkhivker, Steve Agajanian, Deniz Yaşar Öztaş, et al.
ACS Omega (2021) Vol. 6, Iss. 40, pp. 26354-26371
Open Access | Times Cited: 11
Exploring the ability of the MD+FoldX method to predict SARS-CoV-2 antibody escape mutations using large-scale data
L. América, Jonathan E. Barnes, Jagdish Suresh Patel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
The effect of mutations on binding interactions between the SARS-CoV-2 receptor binding domain and neutralizing antibodies B38 and CB6
Jonathan E. Barnes, Peik K. Lund-Andersen, Jagdish Suresh Patel, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 7
Little Brown Bats (Myotis lucifugus) Support the Binding of SARS-CoV-2 Spike and Are Likely Susceptible to SARS-CoV-2 Infection
Shubhada K. Chothe, Padmaja Jakka, Veda Sheersh Boorla, et al.
Viruses (2023) Vol. 15, Iss. 5, pp. 1103-1103
Open Access | Times Cited: 3
Defining the HIV Capsid Binding Site of Nucleoporin 153
Shunji Li, Jagdish Suresh Patel, Jordan Yang, et al.
mSphere (2022) Vol. 7, Iss. 5
Open Access | Times Cited: 5
An optimized thermodynamics integration protocol for identifying beneficial mutations in antibody design
Zizhang Sheng, Jude Bimela, Maple Wang, et al.
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 2
Effect of identified non-synonymous mutations in DPP4 receptor binding residues among highly exposed human population in Morocco to MERS-CoV through computational approach
Anass Abbad, Latifa Anga, Abdellah Faouzi, et al.
PLoS ONE (2021) Vol. 16, Iss. 10, pp. e0258750-e0258750
Open Access | Times Cited: 5
Software for Predicting Binding Free Energy of Protein–Protein Complexes and Their Mutants
Małgorzata Jarończyk
Methods in molecular biology (2024), pp. 139-147
Closed Access
Leveraging neural networks to correct FoldX free energy estimates
Jonathan E. Barnes, L. América, F. Marty Ytreberg, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Integrative computational pipeline for identifying binding‐enhancing mutations targeting the MBD2–p66α interaction: Implications for therapeutic applications
Sargol Mazraedoost, Hadi Sedigh Malekroodi, Myunggi Yi, et al.
Bulletin of the Korean Chemical Society (2024)
Closed Access
Fast, accurate ranking of engineered proteins by receptor binding propensity using structure modeling
Xiaozhe Ding, Xinhong Chen, Erin E. Sullivan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Molecular modeling predicts novel antibody escape mutations in respiratory syncytial virus fusion glycoprotein
Sierra S. Beach, McKenna A. Hull, F. Marty Ytreberg, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
Defining the HIV Capsid Binding Site of Nucleoporin 153
Shunji Li, Jagdish Suresh Patel, Jordan Yang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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