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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 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: 57

Showing 1-25 of 57 citing articles:

Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5
Qian Wang, Yicheng Guo, Sho Iketani, et al.
Nature (2022) Vol. 608, Iss. 7923, pp. 603-608
Open Access | Times Cited: 720
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: 402
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: 368
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: 284
Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies
Yifan Wang, Caixuan Liu, Chao Zhang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 158
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice
Phillip Pymm, Amy Adair, Li‐Jin Chan, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 19
Open Access | Times Cited: 143
Scientific rationale for developing potent RBD-based vaccines targeting COVID-19
Harry Kleanthous, Judith M. Silverman, Karen W. Makar, et al.
npj Vaccines (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 138
Cryo-EM structure of the SARS-CoV-2 Omicron spike
Gabriele Cerutti, Yicheng Guo, Lihong Liu, et al.
Cell Reports (2022) Vol. 38, Iss. 9, pp. 110428-110428
Open Access | Times Cited: 95
Reinfection in patients with COVID-19: a systematic review
Xiangying Ren, Jie Zhou, Jing Guo, et al.
Global Health Research and Policy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 94
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: 95
The success of SARS-CoV-2 vaccines and challenges ahead
Kanta Subbarao
Cell Host & Microbe (2021) Vol. 29, Iss. 7, pp. 1111-1123
Open Access | Times Cited: 90
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: 79
Structural Evaluation of the Spike Glycoprotein Variants on SARS-CoV-2 Transmission and Immune Evasion
Mohd Zulkifli Salleh, Jeremy P. Derrick, Zakuan Zainy Deris
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 14, pp. 7425-7425
Open Access | Times Cited: 78
Neutralizing antibody 5-7 defines a distinct site of vulnerability in SARS-CoV-2 spike N-terminal domain
Gabriele Cerutti, Yicheng Guo, Pengfei Wang, et al.
Cell Reports (2021) Vol. 37, Iss. 5, pp. 109928-109928
Open Access | Times Cited: 69
A structural view of the SARS-CoV-2 virus and its assembly
Nathan Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65
Impact of new variants on SARS-CoV-2 infectivity and neutralization: A molecular assessment of the alterations in the spike-host protein interactions
Mary Hongying Cheng, James Krieger, Anupam Banerjee, et al.
iScience (2022) Vol. 25, Iss. 3, pp. 103939-103939
Open Access | Times Cited: 47
A circular mRNA vaccine prototype producing VFLIP-X spike confers a broad neutralization of SARS-CoV-2 variants by mouse sera
Chotiwat Seephetdee, Kanit Bhukhai, Nattawut Buasri, et al.
Antiviral Research (2022) Vol. 204, pp. 105370-105370
Open Access | Times Cited: 44
Protective neutralizing epitopes in SARS‐CoV‐2
Hejun Liu, Ian A. Wilson
Immunological Reviews (2022) Vol. 310, Iss. 1, pp. 76-92
Open Access | Times Cited: 40
A third dose of inactivated vaccine augments the potency, breadth, and duration of anamnestic responses against SARS-CoV-2
Kang Wang, Yunlong Cao, Yunjiao Zhou, et al.
medRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 46
Passive Immunotherapy Against SARS-CoV-2: From Plasma-Based Therapy to Single Potent Antibodies in the Race to Stay Ahead of the Variants
William R. Strohl, Zhiqiang Ku, Zhiqiang An, et al.
BioDrugs (2022) Vol. 36, Iss. 3, pp. 231-323
Open Access | Times Cited: 32
Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4, and BA.5
Qian Wang, Yicheng Guo, Sho Iketani, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 32
Broadly neutralizing antibodies against COVID-19
Daming Zhou, Jingshan Ren, Elizabeth E. Fry, et al.
Current Opinion in Virology (2023) Vol. 61, pp. 101332-101332
Open Access | Times Cited: 20
The Development of SARS-CoV-2 Variants: The Gene Makes the Disease
Raquel Pérez-Gómez
Journal of Developmental Biology (2021) Vol. 9, Iss. 4, pp. 58-58
Open Access | Times Cited: 37
Structures of synthetic nanobody–SARS-CoV-2 receptor-binding domain complexes reveal distinct sites of interaction
Javeed Ahmad, Jiansheng Jiang, Lisa F. Boyd, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 4, pp. 101202-101202
Open Access | Times Cited: 36
A monoclonal antibody that neutralizes SARS-CoV-2 variants, SARS-CoV, and other sarbecoviruses
Pengfei Wang, Ryan G. Casner, Manoj S. Nair, et al.
Emerging Microbes & Infections (2021) Vol. 11, Iss. 1, pp. 147-157
Open Access | Times Cited: 36
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