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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 Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies
Daniel Wrapp, Dorien De Vlieger, Kizzmekia S. Corbett, et al.
Cell (2020) Vol. 181, Iss. 5, pp. 1004-1015.e15
Open Access | Times Cited: 629

Showing 1-25 of 629 citing articles:

UCSF ChimeraX: Structure visualization for researchers, educators, and developers
Eric F. Pettersen, Thomas D. Goddard, Conrad C. Huang, et al.
Protein Science (2020) Vol. 30, Iss. 1, pp. 70-82
Open Access | Times Cited: 6748
An mRNA Vaccine against SARS-CoV-2 — Preliminary Report
Lisa A. Jackson, Evan J. Anderson, Nadine Rouphael, et al.
New England Journal of Medicine (2020) Vol. 383, Iss. 20, pp. 1920-1931
Open Access | Times Cited: 3209
Coronavirus biology and replication: implications for SARS-CoV-2
Philip V’kovski, Annika Kratzel, Silvio Steiner, et al.
Nature Reviews Microbiology (2020) Vol. 19, Iss. 3, pp. 155-170
Open Access | Times Cited: 2794
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding
Tyler N. Starr, Allison J. Greaney, Sarah K. Hilton, et al.
Cell (2020) Vol. 182, Iss. 5, pp. 1295-1310.e20
Open Access | Times Cited: 2000
Immunology of COVID-19: Current State of the Science
Nicolas Vabret, Graham J. Britton, Conor Gruber, et al.
Immunity (2020) Vol. 52, Iss. 6, pp. 910-941
Open Access | Times Cited: 1654
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Xiangyang Chi, Renhong Yan, Jun Zhang, et al.
Science (2020) Vol. 369, Iss. 6504, pp. 650-655
Open Access | Times Cited: 1481
Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein
Lorenzo Casalino, Zied Gaieb, Jory A. Goldsmith, et al.
ACS Central Science (2020) Vol. 6, Iss. 10, pp. 1722-1734
Open Access | Times Cited: 929
Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity
Emma C. Thomson, Laura E. Rosen, James G. Shepherd, et al.
Cell (2021) Vol. 184, Iss. 5, pp. 1171-1187.e20
Open Access | Times Cited: 623
A systematic review of SARS-CoV-2 vaccine candidates
Yetian Dong, Tong Dai, Yujun Wei, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 538
Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite
Gabriele Cerutti, Yicheng Guo, Tongqing Zhou, et al.
Cell Host & Microbe (2021) Vol. 29, Iss. 5, pp. 819-833.e7
Open Access | Times Cited: 531
Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2
Jiandong Huo, Audrey Le Bas, Reinis R. Ruza, et al.
Nature Structural & Molecular Biology (2020) Vol. 27, Iss. 9, pp. 846-854
Open Access | Times Cited: 505
An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike
Michael Schoof, Bryan Faust, Reuben A. Saunders, et al.
Science (2020) Vol. 370, Iss. 6523, pp. 1473-1479
Open Access | Times Cited: 422
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
Yufei Xiang, Sham Nambulli, Zhengyun Xiao, et al.
Science (2020) Vol. 370, Iss. 6523, pp. 1479-1484
Open Access | Times Cited: 402
Structural biology of SARS-CoV-2 and implications for therapeutic development
Haitao Yang, Zihe Rao
Nature Reviews Microbiology (2021) Vol. 19, Iss. 11, pp. 685-700
Open Access | Times Cited: 399
Longitudinal Isolation of Potent Near-Germline SARS-CoV-2-Neutralizing Antibodies from COVID-19 Patients
Christoph Kreer, Matthias Zehner, Timm Weber, et al.
Cell (2020) Vol. 182, Iss. 4, pp. 843-854.e12
Open Access | Times Cited: 382
Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape
Paul-Albert Koenig, Hrishikesh Das, Hejun Liu, et al.
Science (2021) Vol. 371, Iss. 6530
Open Access | Times Cited: 365
An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction
Leo Hanke, Laura Perez Vidakovics, Daniel J. Sheward, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 322
Rapid single-molecule detection of COVID-19 and MERS antigens via nanobody-functionalized organic electrochemical transistors
Keying Guo, Shofarul Wustoni, Anil Koklu, et al.
Nature Biomedical Engineering (2021) Vol. 5, Iss. 7, pp. 666-677
Open Access | Times Cited: 312
Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient
Daming Zhou, Helen M. E. Duyvesteyn, Cheng‐Pin Chen, et al.
Nature Structural & Molecular Biology (2020) Vol. 27, Iss. 10, pp. 950-958
Open Access | Times Cited: 311
Molecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy
Qianqian Zhang, Rong Xiang, Shanshan Huo, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 300
In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies
Dapeng Li, Robert J. Edwards, Kartik Manne, et al.
Cell (2021) Vol. 184, Iss. 16, pp. 4203-4219.e32
Open Access | Times Cited: 277
STAT2 signaling restricts viral dissemination but drives severe pneumonia in SARS-CoV-2 infected hamsters
Robbert Boudewijns, Hendrik Jan Thibaut, Suzanne J. F. Kaptein, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 273
A materials-science perspective on tackling COVID-19
Zhongmin Tang, Na Kong, Xingcai Zhang, et al.
Nature Reviews Materials (2020) Vol. 5, Iss. 11, pp. 847-860
Open Access | Times Cited: 269
Favipiravir at high doses has potent antiviral activity in SARS-CoV-2−infected hamsters, whereas hydroxychloroquine lacks activity
Suzanne J. F. Kaptein, Sofie Jacobs, Lana Langendries, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 43, pp. 26955-26965
Open Access | Times Cited: 264
A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses
Tiong Kit Tan, Pramila Rijal, Rolle Rahikainen, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 248
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