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:

Structure-based dual affinity optimization of a SARS-CoV-1/2 cross-reactive single-domain antibody
Traian Sulea, Jason Baardsnes, Matthew Stuible, et al.
PLoS ONE (2022) Vol. 17, Iss. 3, pp. e0266250-e0266250
Open Access | Times Cited: 19

Showing 19 citing articles:

Arsenal of nanobodies shows broad-spectrum neutralization against SARS-CoV-2 variants of concern in vitro and in vivo in hamster models
Martín A. Rossotti, Henk van Faassen, Anh Tran, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 27

Enhanced potency of an IgM-like nanobody targeting conserved epitope in SARS-CoV-2 spike N-terminal domain
Bo Liu, Honghui Liu, Pu Han, et al.
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 5

Immunogenicity of SARS-CoV-2 spike antigens derived from Beta & Delta variants of concern
Bassel Akache, Tyler M. Renner, Matthew Stuible, et al.
npj Vaccines (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 21

Structure-guided mutations in CDRs for enhancing the affinity of neutralizing SARS-CoV-2 nanobody
Vishakha Singh, Mandar Bhutkar, Shweta Choudhary, et al.
Biochemical and Biophysical Research Communications (2024) Vol. 734, pp. 150746-150746
Closed Access | Times Cited: 4

Novel Strategy of Antibody Affinity Maturation and Enhancement of Nucleolin‐Mediated Antibody‐Dependent Cellular Cytotoxicity Against Triple‐Negative Breast Cancer
Rita Ribeiro, Jorge M. B. Vítor, Anastasiya Voronovska, et al.
Biotechnology Journal (2025) Vol. 20, Iss. 1
Closed Access

Modifying the glycosylation profile of SARS-CoV-2 spike-based subunit vaccines alters focusing of the humoral immune response in a mouse model
Tyler M. Renner, Matthew Stuible, Martín A. Rossotti, et al.
Communications Medicine (2025) Vol. 5, Iss. 1
Open Access

Design of nanobody targeting SARS-CoV-2 spike glycoprotein using CDR-grafting assisted by molecular simulation and machine learning
Matheus Ferraz, Wenny Camilla dos Santos Adan, Tayná Evily de Lima, et al.
PLoS Computational Biology (2025) Vol. 21, Iss. 4, pp. e1012921-e1012921
Open Access

Solvated interaction energy: from small-molecule to antibody drug design
Enrico O. Purisima, Christopher R. Corbeil, Francis Gaudreault, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 8

A selection and optimization strategy for single-domain antibodies targeting the PHF6 linear peptide within the tau intrinsically disordered protein
Justine Mortelecque, Orgeta Zejneli, Séverine Bégard, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 4, pp. 107163-107163
Open Access | Times Cited: 2

High-throughput ML-guided design of diverse single-domain antibodies against SARS-CoV-2
Christof Angermueller, Zelda Mariet, Benjamin W. Jester, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5

Structure-Based Optimization of One Neutralizing Antibody against SARS-CoV-2 Variants Bearing the L452R Mutation
Yamin Chen, Jialu Zha, Shiqi Xu, et al.
Viruses (2024) Vol. 16, Iss. 4, pp. 566-566
Open Access | Times Cited: 1

A Significant Contribution of the Classical Pathway of Complement in SARS-CoV-2 Neutralization of Convalescent and Vaccinee Sera
Patrick Budylowski, Serena Chau, Arinjay Banerjee, et al.
The Journal of Immunology (2024) Vol. 212, Iss. 12, pp. 1922-1931
Closed Access | Times Cited: 1

Enhancing affinity of neutralizing SARS-CoV-2 nanobody through facile structure-guided mutations in CDRs
Vishakha Singh, Mandar Bhutkar, Shweta Choudhary, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

AttABseq: an attention-based deep learning prediction method for antigen–antibody binding affinity changes based on protein sequences
Ruofan Jin, Qing Ye, Jike Wang, et al.
Briefings in Bioinformatics (2024) Vol. 25, Iss. 4
Open Access | Times Cited: 1

Evaluation of an Affinity-Enhanced Anti-SARS-CoV2 Nanobody Design Workflow Using Machine Learning and Molecular Dynamics
Zsolt Fazekas, Dóra Nagy‐Fazekas, Boglárka Mária Shilling-Tóth, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 19, pp. 7626-7638
Open Access | Times Cited: 1

Resistance-based directed evolution of nanobodies for higher affinity in prokaryotes
Yue Hu, Li Huo, Weiwei Chen, et al.
Biochimica et Biophysica Acta (BBA) - General Subjects (2024) Vol. 1868, Iss. 11, pp. 130710-130710
Closed Access

Rapid Transformation of Nanobodies Affinity Based on AlphaFold2's High-Accuracy Predictions and Interaction Analysis for Enrofloxacin Detection in Coastal Fish
Guoqiang Li, Chang Liu, Xinping Guo, et al.
Biosensors and Bioelectronics (2024) Vol. 267, pp. 116785-116785
Closed Access

Strategy of selection and optimization of single domain antibodies targeting the PHF6 linear peptide within the Tau intrinsically disordered protein
Justine Mortelecque, Orgeta Zejneli, Séverine Bégard, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

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