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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:

Structural basis for broad sarbecovirus neutralization by a human monoclonal antibody
M. Alejandra Tortorici, Nadine Czudnochowski, Tyler N. Starr, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 24

Showing 24 citing articles:

SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
Matthew McCallum, Jessica Bassi, Anna De Marco, et al.
Science (2021) Vol. 373, Iss. 6555, pp. 648-654
Open Access | Times Cited: 439
LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants
Kathryn Westendorf, Stefanie Žentelis, Lingshu Wang, et al.
Cell Reports (2022) Vol. 39, Iss. 7, pp. 110812-110812
Open Access | Times Cited: 396
Tackling COVID-19 with neutralizing monoclonal antibodies
Davide Corti, Lisa A. Purcell, Gyorgy Snell, et al.
Cell (2021) Vol. 184, Iss. 12, pp. 3086-3108
Open Access | Times Cited: 369
Broad betacoronavirus neutralization by a stem helix–specific human antibody
Dora Pinto, Maximilian M. Sauer, Nadine Czudnochowski, et al.
Science (2021) Vol. 373, Iss. 6559, pp. 1109-1116
Open Access | Times Cited: 351
SARS-CoV-2 Neutralizing Antibodies for COVID-19 Prevention and Treatment
Dapeng Li, Gregory D. Sempowski, Kevin O. Saunders, et al.
Annual Review of Medicine (2021) Vol. 73, Iss. 1, pp. 1-16
Closed Access | Times Cited: 130
Persistent immune imprinting occurs after vaccination with the COVID-19 XBB.1.5 mRNA booster in humans
M. Alejandra Tortorici, Amin Addetia, Albert J. Seo, et al.
Immunity (2024) Vol. 57, Iss. 4, pp. 904-911.e4
Open Access | Times Cited: 54
A potently neutralizing SARS-CoV-2 antibody inhibits variants of concern by utilizing unique binding residues in a highly conserved epitope
Laura A. VanBlargan, Lucas J. Adams, Zhuoming Liu, et al.
Immunity (2021) Vol. 54, Iss. 10, pp. 2399-2416.e6
Open Access | Times Cited: 94
LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants
Kathryn Westendorf, Stefanie Žentelis, Lingshu Wang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 83
Broadly-Neutralizing Antibodies Against Emerging SARS-CoV-2 Variants
Lok Bahadur Shrestha, Nicodemus Tedla, Rowena A. Bull
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 75
Stabilization of the SARS-CoV-2 Spike Receptor-Binding Domain Using Deep Mutational Scanning and Structure-Based Design
Daniel Ellis, Natalie Brunette, Katharine H. D. Crawford, et al.
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 45
A broadly neutralizing antibody protects against SARS-CoV, pre-emergent bat CoVs, and SARS-CoV-2 variants in mice
David R. Martinez, Alexandra Schaefer, S. Gobeil, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 43
Keep out! SARS-CoV-2 entry inhibitors: their role and utility as COVID-19 therapeutics
Lennox Chitsike, Penelope J. Duerksen-Hughes
Virology Journal (2021) Vol. 18, Iss. 1
Open Access | Times Cited: 41
Key Substitutions in the Spike Protein of SARS-CoV-2 Variants Can Predict Resistance to Monoclonal Antibodies, but Other Substitutions Can Modify the Effects
Sabrina Lusvarghi, Wei Wang, Rachel Herrup, et al.
Journal of Virology (2021) Vol. 96, Iss. 1
Open Access | Times Cited: 33
Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies
Claudia A. Jette, Alexander A. Cohen, Priyanthi N.P. Gnanapragasam, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 20
Elucidating important structural features for the binding affinity of spike ‐ SARS‐CoV‐2 neutralizing antibody complexes
Divya Sharma, Puneet Rawat, Janakiraman Vani, et al.
Proteins Structure Function and Bioinformatics (2021) Vol. 90, Iss. 3, pp. 824-834
Open Access | Times Cited: 18
A potently neutralizing anti-SARS-CoV-2 antibody inhibits variants of concern by binding a highly conserved epitope
Laura A. VanBlargan, Lucas J. Adams, Zhuoming Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 16
A human antibody that broadly neutralizes betacoronaviruses protects against SARS-CoV-2 by blocking the fusion machinery
Dora Pinto, Maximilian M. Sauer, Nadine Czudnochowski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Closed Access | Times Cited: 15
Multivalent designed proteins protect against SARS-CoV-2 variants of concern
Andrew C. Hunt, James Brett Case, Young‐Jun Park, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 15
Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
Mohamed Hendy, Samuel Kaufman, Mauricio Ponga
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 15
Key substitutions in the spike protein of SARS-CoV-2 variants can predict resistance to monoclonal antibodies, but other substitutions can modify the effects
Sabrina Lusvarghi, Wei Wang, Rachel Herrup, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Closed Access | Times Cited: 11
Targeted isolation of panels of diverse human protective broadly neutralizing antibodies against SARS-like viruses
Wanting He, Rami Musharrafieh, Ge Song, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 6
Stabilization of the SARS-CoV-2 Spike receptor-binding domain using deep mutational scanning and structure-based design
Daniel Ellis, Natalie Brunette, Katharine H. D. Crawford, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 2
Rapid screening methods for universal binding peptide aptamers against SARS-CoV-2 variant spikes, including omicron variants, and their application to diagnostic and therapeutic agents.
Nakanobu Hayashi
Research Square (Research Square) (2023)
Closed Access
Rapid screening methods for universal binding peptide aptamers against SARS-CoV-2 variant spikes, including omicron variants, and their application to diagnostic and therapeutic agents.
Nakanobu Hayashi, Chikako Abe, Jiro Kikuchi, et al.
Research Square (Research Square) (2023)
Closed Access
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