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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:

De novo design of picomolar SARS-CoV-2 miniprotein inhibitors
Longxing Cao, Inna Goreshnik, Brian Coventry, et al.
Science (2020) Vol. 370, Iss. 6515, pp. 426-431
Open Access | Times Cited: 594

Showing 1-25 of 594 citing articles:

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
SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution
Jiří Zahradník, Shir Marciano, Maya Shemesh, et al.
Nature Microbiology (2021) Vol. 6, Iss. 9, pp. 1188-1198
Open Access | Times Cited: 377
Design of protein-binding proteins from the target structure alone
Longxing Cao, Brian Coventry, Inna Goreshnik, et al.
Nature (2022) Vol. 605, Iss. 7910, pp. 551-560
Open Access | Times Cited: 327
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
De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2
Thomas W. Linsky, Renan Vergara, N. Codina-Castillo, et al.
Science (2020) Vol. 370, Iss. 6521, pp. 1208-1214
Open Access | Times Cited: 198
De novo design of modular and tunable protein biosensors
Alfredo Quijano‐Rubio, Hsien‐Wei Yeh, Jooyoung Park, et al.
Nature (2021) Vol. 591, Iss. 7850, pp. 482-487
Open Access | Times Cited: 198
Structural basis for broad coronavirus neutralization
Maximilian M. Sauer, M. Alejandra Tortorici, Young‐Jun Park, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 6, pp. 478-486
Open Access | Times Cited: 195
Intranasal fusion inhibitory lipopeptide prevents direct-contact SARS-CoV-2 transmission in ferrets
Rory D. de Vries, Katharina S. Schmitz, Francesca T. Bovier, et al.
Science (2021) Vol. 371, Iss. 6536, pp. 1379-1382
Open Access | Times Cited: 194
Structure of SARS-CoV-2 spike protein
Jun Zhang, Tianshu Xiao, Yongfei Cai, et al.
Current Opinion in Virology (2021) Vol. 50, pp. 173-182
Open Access | Times Cited: 190
Recent advances in de novo protein design: Principles, methods, and applications
Xingjie Pan, Tanja Kortemme
Journal of Biological Chemistry (2021) Vol. 296, pp. 100558-100558
Open Access | Times Cited: 177
Programmable icosahedral shell system for virus trapping
Christian Sigl, Elena M. Willner, Wouter Engelen, et al.
Nature Materials (2021) Vol. 20, Iss. 9, pp. 1281-1289
Open Access | Times Cited: 174
Peptide and peptide-based inhibitors of SARS-CoV-2 entry
Desirée Schütz, Yasser B. Ruiz‐Blanco, Jan Münch, et al.
Advanced Drug Delivery Reviews (2020) Vol. 167, pp. 47-65
Open Access | Times Cited: 167
Engineering protein-based therapeutics through structural and chemical design
Sasha B. Ebrahimi, Devleena Samanta
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 142
Protein Design: From the Aspect of Water Solubility and Stability
Rui Qing, Shilei Hao, Eva Smorodina, et al.
Chemical Reviews (2022) Vol. 122, Iss. 18, pp. 14085-14179
Open Access | Times Cited: 138
An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants
Kui K. Chan, Timothy J.C. Tan, Krishna K. Narayanan, et al.
Science Advances (2021) Vol. 7, Iss. 8
Open Access | Times Cited: 136
A trimeric human angiotensin-converting enzyme 2 as an anti-SARS-CoV-2 agent
Tianshu Xiao, Jianming Lü, Jun Zhang, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 2, pp. 202-209
Open Access | Times Cited: 127
A single intranasal dose of chimpanzee adenovirus-vectored vaccine protects against SARS-CoV-2 infection in rhesus macaques
Ahmed O. Hassan, Friederike Feldmann, Haiyan Zhao, et al.
Cell Reports Medicine (2021) Vol. 2, Iss. 4, pp. 100230-100230
Open Access | Times Cited: 122
An intranasal vaccine durably protects against SARS-CoV-2 variants in mice
Ahmed O. Hassan, Swathi Shrihari, Matthew J. Gorman, et al.
Cell Reports (2021) Vol. 36, Iss. 4, pp. 109452-109452
Open Access | Times Cited: 119
A Brief History of De Novo Protein Design: Minimal, Rational, and Computational
Derek N. Woolfson
Journal of Molecular Biology (2021) Vol. 433, Iss. 20, pp. 167160-167160
Open Access | Times Cited: 118
SARS-CoV-2 RBD in vitro evolution follows contagious mutation spread, yet generates an able infection inhibitor
Jiří Zahradník, Shir Marciano, Maya Shemesh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 116
De novo design of protein interactions with learned surface fingerprints
Pablo Gaínza, Sarah Wehrle, Alexandra Van Hall‐Beauvais, et al.
Nature (2023) Vol. 617, Iss. 7959, pp. 176-184
Open Access | Times Cited: 114
Human ACE2 peptide-mimics block SARS-CoV-2 pulmonary cells infection
Philippe Karoyan, Vincent Vieillard, Luis Gómez‐Morales, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 109
Multivalent designed proteins neutralize SARS-CoV-2 variants of concern and confer protection against infection in mice
Andrew C. Hunt, James Brett Case, Young‐Jun Park, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 646
Open Access | Times Cited: 97
Angiotensin-converting enzyme 2—at the heart of the COVID-19 pandemic
Gavin Y. Oudit, Kaiming Wang, Anissa Viveiros, et al.
Cell (2023) Vol. 186, Iss. 5, pp. 906-922
Open Access | Times Cited: 74
Machine learning for functional protein design
Pascal Notin, Nathan Rollins, Yarin Gal, et al.
Nature Biotechnology (2024) Vol. 42, Iss. 2, pp. 216-228
Closed Access | Times Cited: 72
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