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:

Paired heavy- and light-chain signatures contribute to potent SARS-CoV-2 neutralization in public antibody responses
Bailey B. Banach, Gabriele Cerutti, Ahmed S. Fahad, et al.
Cell Reports (2021) Vol. 37, Iss. 1, pp. 109771-109771
Open Access | Times Cited: 56

Showing 1-25 of 56 citing articles:

Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
Nature (2021) Vol. 602, Iss. 7898, pp. 676-681
Open Access | Times Cited: 1255

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
Meng Yuan, Deli Huang, Chang‐Chun D. Lee, et al.
Science (2021) Vol. 373, Iss. 6556, pp. 818-823
Open Access | Times Cited: 362

Antibody Resistance of SARS-CoV-2 Variants B.1.351 and B.1.1.7
Pengfei Wang, Manoj S. Nair, Lihong Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 320

Broadly neutralizing antibodies to SARS-CoV-2 and other human coronaviruses
Yanjia Chen, Xiaoyu Zhao, Hao Zhou, et al.
Nature reviews. Immunology (2022) Vol. 23, Iss. 3, pp. 189-199
Open Access | Times Cited: 272

Monoclonal antibody therapies against SARS-CoV-2
Daniele Focosi, Scott A. McConnell, Arturo Casadevall, et al.
The Lancet Infectious Diseases (2022) Vol. 22, Iss. 11, pp. e311-e326
Open Access | Times Cited: 204

Monoclonal antibodies for COVID-19 therapy and SARS-CoV-2 detection
Yu‐Chyi Hwang, Ruei‐Min Lu, Shih-Chieh Su, et al.
Journal of Biomedical Science (2022) Vol. 29, Iss. 1
Open Access | Times Cited: 194

Increased Resistance of SARS-CoV-2 Variants B.1.351 and B.1.1.7 to Antibody Neutralization
David D. Ho, Pengfei Wang, Lihong Liu, et al.
Research Square (Research Square) (2021)
Open Access | Times Cited: 161

Structural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies
Daniel J. Sheward, Pradeepa Pushparaj, Hrishikesh Das, et al.
Cell Reports Medicine (2024) Vol. 5, Iss. 6, pp. 101577-101577
Open Access | Times Cited: 22

Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding
Dhiraj Mannar, James W. Saville, Xing Zhu, et al.
Cell Reports (2021) Vol. 37, Iss. 12, pp. 110156-110156
Open Access | Times Cited: 86

Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
Nature (2021)
Closed Access | Times Cited: 83

A structural view of the SARS-CoV-2 virus and its assembly
Nathan J. Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65

Molecular Aspects Concerning the Use of the SARS-CoV-2 Receptor Binding Domain as a Target for Preventive Vaccines
Yury Valdés-Balbín, Darielys Santana-Mederos, Françoise Paquet, et al.
ACS Central Science (2021) Vol. 7, Iss. 5, pp. 757-767
Open Access | Times Cited: 61

Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain
Timothy J.C. Tan, Meng Yuan, Kaylee Kuzelka, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 59

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants
Meng Yuan, Deli Huang, Chang‐Chun D. Lee, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 56

Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies
Gabriele Cerutti, Micah Rapp, Yicheng Guo, et al.
Structure (2021) Vol. 29, Iss. 7, pp. 655-663.e4
Open Access | Times Cited: 56

Structural basis of Omicron neutralization by affinity-matured public antibodies
Daniel J. Sheward, Pradeepa Pushparaj, Hrishikesh Das, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 37

Striking Antibody Evasion Manifested by the Omicron Variant of SARS-CoV-2
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 54

Integrative overview of antibodies against SARS-CoV-2 and their possible applications in COVID-19 prophylaxis and treatment
Norma A. Valdez‐Cruz, Enrique García‐Hernández, Clara Espitia, et al.
Microbial Cell Factories (2021) Vol. 20, Iss. 1
Open Access | Times Cited: 48

One-shot identification of SARS-CoV-2 S RBD escape mutants using yeast screening
Irene M. Francino-Urdániz, Paul J. Steiner, Monica B. Kirby, et al.
Cell Reports (2021) Vol. 36, Iss. 9, pp. 109627-109627
Open Access | Times Cited: 47

Epitope profiling using computational structural modelling demonstrated on coronavirus-binding antibodies
Sarah A. Robinson, Matthew I. J. Raybould, Constantin Schneider, et al.
PLoS Computational Biology (2021) Vol. 17, Iss. 12, pp. e1009675-e1009675
Open Access | Times Cited: 40

Retrospective SARS-CoV-2 human antibody development trajectories are largely sparse and permissive
Monica B. Kirby, Brian M. Petersen, Jonathan G. Faris, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 4
Open Access

Molecular probes of spike ectodomain and its subdomains for SARS-CoV-2 variants, Alpha through Omicron
I‐Ting Teng, Alexandra F. Nazzari, Misook Choe, et al.
PLoS ONE (2022) Vol. 17, Iss. 5, pp. e0268767-e0268767
Open Access | Times Cited: 23

Combating the SARS-CoV-2 Omicron (BA.1) and BA.2 with potent bispecific antibodies engineered from non-Omicron neutralizing antibodies
Ying-Dan Wang, Xiang Zhang, Yunping Ma, et al.
Cell Discovery (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 23

Therapeutic antibodies for COVID-19: is a new age of IgM, IgA and bispecific antibodies coming?
Jingjing Zhang, Han Zhang, Litao Sun
mAbs (2022) Vol. 14, Iss. 1
Open Access | Times Cited: 22

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