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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:

Rapid isolation and profiling of a diverse panel of human monoclonal antibodies targeting the SARS-CoV-2 spike protein
Seth J. Zost, Pavlo Gilchuk, Rita E. Chen, et al.
Nature Medicine (2020) Vol. 26, Iss. 9, pp. 1422-1427
Open Access | Times Cited: 504

Showing 1-25 of 504 citing articles:

Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Yunlong Cao, Jing Wang, Fanchong Jian, et al.
Nature (2021) Vol. 602, Iss. 7898, pp. 657-663
Open Access | Times Cited: 1734
SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Christopher O. Barnes, Claudia A. Jette, Morgan E. Abernathy, et al.
Nature (2020) Vol. 588, Iss. 7839, pp. 682-687
Open Access | Times Cited: 1659
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Lihong Liu, Pengfei Wang, Manoj S. Nair, et al.
Nature (2020) Vol. 584, Iss. 7821, pp. 450-456
Open Access | Times Cited: 1515
Phase I/II study of COVID-19 RNA vaccine BNT162b1 in adults
Mark J. Mulligan, Kirsten E. Lyke, Nicholas Kitchin, et al.
Nature (2020) Vol. 586, Iss. 7830, pp. 589-593
Open Access | Times Cited: 1452
Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies
Allison J. Greaney, Andrea N. Loes, Katharine H. D. Crawford, et al.
Cell Host & Microbe (2021) Vol. 29, Iss. 3, pp. 463-476.e6
Open Access | Times Cited: 1212
Potently neutralizing and protective human antibodies against SARS-CoV-2
Seth J. Zost, Pavlo Gilchuk, James Brett Case, et al.
Nature (2020) Vol. 584, Iss. 7821, pp. 443-449
Open Access | Times Cited: 1107
Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition
Allison J. Greaney, Tyler N. Starr, Pavlo Gilchuk, et al.
Cell Host & Microbe (2020) Vol. 29, Iss. 1, pp. 44-57.e9
Open Access | Times Cited: 1062
Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies
Rita E. Chen, Xianwen Zhang, James Brett Case, et al.
Nature Medicine (2021) Vol. 27, Iss. 4, pp. 717-726
Open Access | Times Cited: 970
Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
Christopher O. Barnes, Anthony P. West, Kathryn E. Huey‐Tubman, et al.
Cell (2020) Vol. 182, Iss. 4, pp. 828-842.e16
Open Access | Times Cited: 823
An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies
Laura A. VanBlargan, John M. Errico, Peter Halfmann, et al.
Nature Medicine (2022) Vol. 28, Iss. 3, pp. 490-495
Open Access | Times Cited: 708
BNT162b vaccines protect rhesus macaques from SARS-CoV-2
Annette B. Vogel, Isis Kanevsky, Ye Che, et al.
Nature (2021) Vol. 592, Iss. 7853, pp. 283-289
Open Access | Times Cited: 633
Structural basis of a shared antibody response to SARS-CoV-2
Meng Yuan, Hejun Liu, Nicholas C. Wu, et al.
Science (2020) Vol. 369, Iss. 6507, pp. 1119-1123
Open Access | Times Cited: 628
Intramuscular AZD7442 (Tixagevimab–Cilgavimab) for Prevention of Covid-19
Myron J. Levin, Andrew Ustianowski, Stéphane De Wit, et al.
New England Journal of Medicine (2022) Vol. 386, Iss. 23, pp. 2188-2200
Open Access | Times Cited: 614
SARS-CoV-2 Omicron virus causes attenuated disease in mice and hamsters
Peter Halfmann, Shun Iida, Kiyoko Iwatsuki‐Horimoto, et al.
Nature (2022) Vol. 603, Iss. 7902, pp. 687-692
Open Access | Times Cited: 589
REGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters
Alina Baum, Dharani K. Ajithdoss, Richard Copin, et al.
Science (2020) Vol. 370, Iss. 6520, pp. 1110-1115
Open Access | Times Cited: 552
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: 532
A Single-Dose Intranasal ChAd Vaccine Protects Upper and Lower Respiratory Tracts against SARS-CoV-2
Ahmed O. Hassan, Natasha M. Kafai, Igor P. Dmitriev, et al.
Cell (2020) Vol. 183, Iss. 1, pp. 169-184.e13
Open Access | Times Cited: 529
Controlling the SARS-CoV-2 spike glycoprotein conformation
Rory Henderson, Robert J. Edwards, Katayoun Mansouri, et al.
Nature Structural & Molecular Biology (2020) Vol. 27, Iss. 10, pp. 925-933
Open Access | Times Cited: 441
The neutralizing antibody, LY-CoV555, protects against SARS-CoV-2 infection in nonhuman primates
Bryan E. Jones, Patricia Brown‐Augsburger, Kizzmekia S. Corbett, et al.
Science Translational Medicine (2021) Vol. 13, Iss. 593
Open Access | Times Cited: 426
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice
Alexander A. Cohen, Priyanthi N.P. Gnanapragasam, Yu E. Lee, et al.
Science (2021) Vol. 371, Iss. 6530, pp. 735-741
Open Access | Times Cited: 384
Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein
Naveenchandra Suryadevara, Swathi Shrihari, Pavlo Gilchuk, et al.
Cell (2021) Vol. 184, Iss. 9, pp. 2316-2331.e15
Open Access | Times Cited: 382
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
Human neutralizing antibodies against SARS-CoV-2 require intact Fc effector functions for optimal therapeutic protection
Emma S. Winkler, Pavlo Gilchuk, Jinsheng Yu, et al.
Cell (2021) Vol. 184, Iss. 7, pp. 1804-1820.e16
Open Access | Times Cited: 349
Distinguishing features of current COVID-19 vaccines: knowns and unknowns of antigen presentation and modes of action
Franz X. Heinz, Karin Stiasny
npj Vaccines (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 339
Antibody potency, effector function, and combinations in protection and therapy for SARS-CoV-2 infection in vivo
Alexandra Schäfer, Frauke Muecksch, Julio C. C. Lorenzi, et al.
The Journal of Experimental Medicine (2020) Vol. 218, Iss. 3
Open Access | Times Cited: 332
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