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 antibody neutralization of SARS-CoV-2 variants including B.1.1.529
Tongqing Zhou, Lingshu Wang, John Misasi, et al.
Science (2022) Vol. 376, Iss. 6591
Open Access | Times Cited: 151
Tongqing Zhou, Lingshu Wang, John Misasi, et al.
Science (2022) Vol. 376, Iss. 6591
Open Access | Times Cited: 151
Showing 1-25 of 151 citing articles:
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
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
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
Yanjia Chen, Xiaoyu Zhao, Hao Zhou, et al.
Nature reviews. Immunology (2022) Vol. 23, Iss. 3, pp. 189-199
Open Access | Times Cited: 272
The SARS-CoV-2 monoclonal antibody combination, AZD7442, is protective in nonhuman primates and has an extended half-life in humans
Yueh–Ming Loo, Patrick M. McTamney, Rosalinda H. Arends, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 635
Open Access | Times Cited: 191
Yueh–Ming Loo, Patrick M. McTamney, Rosalinda H. Arends, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 635
Open Access | Times Cited: 191
Structural diversity of the SARS-CoV-2 Omicron spike
S. Gobeil, Rory Henderson, Victoria Stalls, et al.
Molecular Cell (2022) Vol. 82, Iss. 11, pp. 2050-2068.e6
Open Access | Times Cited: 171
S. Gobeil, Rory Henderson, Victoria Stalls, et al.
Molecular Cell (2022) Vol. 82, Iss. 11, pp. 2050-2068.e6
Open Access | Times Cited: 171
Antibody evasion of SARS-CoV-2 Omicron BA.1, BA.1.1, BA.2, and BA.3 sub-lineages
Jingwen Ai, Xun Wang, Xinyi He, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 8, pp. 1077-1083.e4
Open Access | Times Cited: 167
Jingwen Ai, Xun Wang, Xinyi He, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 8, pp. 1077-1083.e4
Open Access | Times Cited: 167
Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike
Qian Wang, Yicheng Guo, Liyuan Liu, et al.
Nature (2023) Vol. 624, Iss. 7992, pp. 639-644
Open Access | Times Cited: 150
Qian Wang, Yicheng Guo, Liyuan Liu, et al.
Nature (2023) Vol. 624, Iss. 7992, pp. 639-644
Open Access | Times Cited: 150
The humoral response and antibodies against SARS-CoV-2 infection
Hai Qi, Bo Liu, Xinquan Wang, et al.
Nature Immunology (2022) Vol. 23, Iss. 7, pp. 1008-1020
Open Access | Times Cited: 144
Hai Qi, Bo Liu, Xinquan Wang, et al.
Nature Immunology (2022) Vol. 23, Iss. 7, pp. 1008-1020
Open Access | Times Cited: 144
Enhanced evasion of neutralizing antibody response by Omicron XBB.1.5, CH.1.1, and CA.3.1 variants
Panke Qu, Julia N. Faraone, John P. Evans, et al.
Cell Reports (2023) Vol. 42, Iss. 5, pp. 112443-112443
Open Access | Times Cited: 144
Panke Qu, Julia N. Faraone, John P. Evans, et al.
Cell Reports (2023) Vol. 42, Iss. 5, pp. 112443-112443
Open Access | Times Cited: 144
Origin, virological features, immune evasion and intervention of SARS-CoV-2 Omicron sublineages
Shuai Xia, Lijue Wang, Yun Zhu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 134
Shuai Xia, Lijue Wang, Yun Zhu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 134
Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant
Jumpei Ito, Rigel Suzuki, Keiya Uriu, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 117
Jumpei Ito, Rigel Suzuki, Keiya Uriu, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 117
A critical overview of current progress for COVID-19: development of vaccines, antiviral drugs, and therapeutic antibodies
Monika Kumari, Ruei‐Min Lu, Mu‐Chun Li, et al.
Journal of Biomedical Science (2022) Vol. 29, Iss. 1
Open Access | Times Cited: 111
Monika Kumari, Ruei‐Min Lu, Mu‐Chun Li, et al.
Journal of Biomedical Science (2022) Vol. 29, Iss. 1
Open Access | Times Cited: 111
Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike
Victoria Stalls, Jared Lindenberger, S. Gobeil, et al.
Cell Reports (2022) Vol. 39, Iss. 13, pp. 111009-111009
Open Access | Times Cited: 91
Victoria Stalls, Jared Lindenberger, S. Gobeil, et al.
Cell Reports (2022) Vol. 39, Iss. 13, pp. 111009-111009
Open Access | Times Cited: 91
SARS-CoV-2 BA.1 variant is neutralized by vaccine booster–elicited serum but evades most convalescent serum and therapeutic antibodies
Sabrina Lusvarghi, Simon Pollett, Sabari Nath Neerukonda, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 645
Open Access | Times Cited: 87
Sabrina Lusvarghi, Simon Pollett, Sabari Nath Neerukonda, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 645
Open Access | Times Cited: 87
Susceptibility of SARS-CoV-2 Omicron Variants to Therapeutic Monoclonal Antibodies: Systematic Review and Meta-analysis
Kaiming Tao, Philip L. Tzou, Sergei L. Kosakovsky Pond, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 4
Open Access | Times Cited: 76
Kaiming Tao, Philip L. Tzou, Sergei L. Kosakovsky Pond, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 4
Open Access | Times Cited: 76
Sensitivity to Vaccines, Therapeutic Antibodies, and Viral Entry Inhibitors and Advances To Counter the SARS-CoV-2 Omicron Variant
Hao Zhou, Michelle Møhlenberg, Jigarji Chaturji Thakor, et al.
Clinical Microbiology Reviews (2022) Vol. 35, Iss. 3
Open Access | Times Cited: 67
Hao Zhou, Michelle Møhlenberg, Jigarji Chaturji Thakor, et al.
Clinical Microbiology Reviews (2022) Vol. 35, Iss. 3
Open Access | Times Cited: 67
Bench-to-bedside: Innovation of small molecule anti-SARS-CoV-2 drugs in China
Liyan Yang, Zhonglei Wang
European Journal of Medicinal Chemistry (2023) Vol. 257, pp. 115503-115503
Open Access | Times Cited: 63
Liyan Yang, Zhonglei Wang
European Journal of Medicinal Chemistry (2023) Vol. 257, pp. 115503-115503
Open Access | Times Cited: 63
The landscape of antibody binding affinity in SARS-CoV-2 Omicron BA.1 evolution
Alief Moulana, Thomas Dupic, Angela M. Phillips, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 46
Alief Moulana, Thomas Dupic, Angela M. Phillips, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 46
Spike deep mutational scanning helps predict success of SARS-CoV-2 clades
Bernadeta Dadonaite, Jack Brown, Teagan E. McMahon, et al.
Nature (2024) Vol. 631, Iss. 8021, pp. 617-626
Open Access | Times Cited: 38
Bernadeta Dadonaite, Jack Brown, Teagan E. McMahon, et al.
Nature (2024) Vol. 631, Iss. 8021, pp. 617-626
Open Access | Times Cited: 38
Neutralization escape, infectivity, and membrane fusion of JN.1-derived SARS-CoV-2 SLip, FLiRT, and KP.2 variants
Pei Li, Julia N. Faraone, Cheng Chih Hsu, et al.
Cell Reports (2024) Vol. 43, Iss. 8, pp. 114520-114520
Open Access | Times Cited: 27
Pei Li, Julia N. Faraone, Cheng Chih Hsu, et al.
Cell Reports (2024) Vol. 43, Iss. 8, pp. 114520-114520
Open Access | Times Cited: 27
Mutations in the SARS-CoV-2 spike receptor binding domain and their delicate balance between ACE2 affinity and antibody evasion
Song Xue, Yuru Han, Fan Wu, et al.
Protein & Cell (2024) Vol. 15, Iss. 6, pp. 403-418
Open Access | Times Cited: 18
Song Xue, Yuru Han, Fan Wu, et al.
Protein & Cell (2024) Vol. 15, Iss. 6, pp. 403-418
Open Access | Times Cited: 18
Characteristics of JN.1-derived SARS-CoV-2 subvariants SLip, FLiRT, and KP.2 in neutralization escape, infectivity and membrane fusion
Pei Li, Julia N. Faraone, Cheng Chih Hsu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 17
Pei Li, Julia N. Faraone, Cheng Chih Hsu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 17
A broad and potent neutralization epitope in SARS-related coronaviruses
Meng Yuan, Xueyong Zhu, Wanting He, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 29
Open Access | Times Cited: 60
Meng Yuan, Xueyong Zhu, Wanting He, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 29
Open Access | Times Cited: 60
Broadly neutralizing and protective nanobodies against SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.4/5 and diverse sarbecoviruses
Mingxi Li, Yifei Ren, Zhen Qin Aw, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 46
Mingxi Li, Yifei Ren, Zhen Qin Aw, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 46
Clinical grade ACE2 as a universal agent to block SARS‐CoV ‐2 variants
Vanessa Monteil, Brett Eaton, Elena Postnikova, et al.
EMBO Molecular Medicine (2022) Vol. 14, Iss. 8
Open Access | Times Cited: 45
Vanessa Monteil, Brett Eaton, Elena Postnikova, et al.
EMBO Molecular Medicine (2022) Vol. 14, Iss. 8
Open Access | Times Cited: 45
An antibody from single human V H -rearranging mouse neutralizes all SARS-CoV-2 variants through BA.5 by inhibiting membrane fusion
Sai Luo, Jun Zhang, Alex J.B. Kreutzberger, et al.
Science Immunology (2022) Vol. 7, Iss. 76
Open Access | Times Cited: 45
Sai Luo, Jun Zhang, Alex J.B. Kreutzberger, et al.
Science Immunology (2022) Vol. 7, Iss. 76
Open Access | Times Cited: 45
