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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:

Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study
Kathryn M. Hastie, Haoyang Li, Daniel Bedinger, et al.
Science (2021) Vol. 374, Iss. 6566, pp. 472-478
Open Access | Times Cited: 289

Showing 1-25 of 289 citing articles:

SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Wanwisa Dejnirattisai, Jiandong Huo, Daming Zhou, et al.
Cell (2022) Vol. 185, Iss. 3, pp. 467-484.e15
Open Access | Times Cited: 921
SARS-CoV-2 vaccination induces immunological T cell memory able to cross-recognize variants from Alpha to Omicron
Alison Tarke, Camila H. Coelho, Zeli Zhang, et al.
Cell (2022) Vol. 185, Iss. 5, pp. 847-859.e11
Open Access | Times Cited: 760
SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex
Dhiraj Mannar, James W. Saville, Xing Zhu, et al.
Science (2022) Vol. 375, Iss. 6582, pp. 760-764
Open Access | Times Cited: 610
Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron
Zhen Cui, Pan Liu, Nan Wang, et al.
Cell (2022) Vol. 185, Iss. 5, pp. 860-871.e13
Open Access | Times Cited: 379
Structural biology of SARS-CoV-2: open the door for novel therapies
Weizhu Yan, Yanhui Zheng, Xiao‐Tao Zeng, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 241
SARS-CoV-2 Omicron Variant Neutralization after mRNA-1273 Booster Vaccination
Rolando Pajón, Nicole A. Doria‐Rose, Xiaoying Shen, et al.
New England Journal of Medicine (2022) Vol. 386, Iss. 11, pp. 1088-1091
Open Access | Times Cited: 239
Memory B cell repertoire from triple vaccinees against diverse SARS-CoV-2 variants
Kang Wang, Zijing Jia, Linilin Bao, et al.
Nature (2022) Vol. 603, Iss. 7903, pp. 919-925
Open Access | Times Cited: 165
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
Heterologous immunization with inactivated vaccine followed by mRNA-booster elicits strong immunity against SARS-CoV-2 Omicron variant
Fanglei Zuo, Hassan Abolhassani, Likun Du, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 137
Broad neutralization of SARS-CoV-2 variants by an inhalable bispecific single-domain antibody
Cheng Li, Wuqiang Zhan, Zhenlin Yang, et al.
Cell (2022) Vol. 185, Iss. 8, pp. 1389-1401.e18
Open Access | Times Cited: 134
Safety, immunogenicity and antibody persistence of a bivalent Beta-containing booster vaccine against COVID-19: a phase 2/3 trial
Spyros Chalkias, Frank Eder, Brandon Essink, et al.
Nature Medicine (2022) Vol. 28, Iss. 11, pp. 2388-2397
Open Access | Times Cited: 126
Booster of mRNA-1273 Strengthens SARS-CoV-2 Omicron Neutralization
Nicole A. Doria‐Rose, Xiaoying Shen, Stephen D. Schmidt, et al.
medRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 123
Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern
Wenwei Li, Yaozong Chen, Jérémie Prévost, et al.
Cell Reports (2021) Vol. 38, Iss. 2, pp. 110210-110210
Open Access | Times Cited: 122
Antibody-mediated neutralization of SARS-CoV-2
Henning Gruell, Kanika Vanshylla, Timm Weber, et al.
Immunity (2022) Vol. 55, Iss. 6, pp. 925-944
Open Access | Times Cited: 117
COVID-19 in dialysis: clinical impact, immune response, prevention, and treatment
Khalil El Karoui, An S. De Vriese
Kidney International (2022) Vol. 101, Iss. 5, pp. 883-894
Open Access | Times Cited: 116
A broadly cross-reactive antibody neutralizes and protects against sarbecovirus challenge in mice
David R. Martinez, Alexandra Schäfer, S. Gobeil, et al.
Science Translational Medicine (2021) Vol. 14, Iss. 629
Open Access | Times Cited: 115
Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants
Anshumali Mittal, Arun Khattri, Vikash Verma
PLoS Pathogens (2022) Vol. 18, Iss. 2, pp. e1010260-e1010260
Open Access | Times Cited: 115
Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape
Zhennan Zhao, Jingya Zhou, Mingxiong Tian, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 114
Omicron variant Spike-specific antibody binding and Fc activity are preserved in recipients of mRNA or inactivated COVID-19 vaccines
Yannic C. Bartsch, Xin Tong, Jaewon Kang, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 642
Open Access | Times Cited: 113
Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants
Cong Sun, Chu Xie, Guo‐Long Bu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 113
Antibodies elicited by SARS-CoV-2 infection or mRNA vaccines have reduced neutralizing activity against Beta and Omicron pseudoviruses
Benjamín L. Sievers, Saborni Chakraborty, Yong Xue, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 634
Open Access | Times Cited: 107
Stopping pandemics before they start: Lessons learned from SARS-CoV-2
A.M. Edwards, Ralph S. Baric, Erica Ollmann Saphire, et al.
Science (2022) Vol. 375, Iss. 6585, pp. 1133-1139
Open Access | Times Cited: 82
Atlas of currently available human neutralizing antibodies against SARS-CoV-2 and escape by Omicron sub-variants BA.1/BA.1.1/BA.2/BA.3
Min Huang, Lili Wu, Anqi Zheng, et al.
Immunity (2022) Vol. 55, Iss. 8, pp. 1501-1514.e3
Open Access | Times Cited: 80
Deep mutational learning predicts ACE2 binding and antibody escape to combinatorial mutations in the SARS-CoV-2 receptor-binding domain
Joseph M. Taft, Cédric R. Weber, Beichen Gao, et al.
Cell (2022) Vol. 185, Iss. 21, pp. 4008-4022.e14
Open Access | Times Cited: 79
Insights on the mutational landscape of the SARS-CoV-2 Omicron variant receptor-binding domain
Nathaniel L. Miller, Thomas A. Clark, Rahul Raman, et al.
Cell Reports Medicine (2022) Vol. 3, Iss. 2, pp. 100527-100527
Open Access | Times Cited: 67
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