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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 enhanced infectivity and immune evasion of SARS-CoV-2 variants
Yongfei Cai, Jun Zhang, Tianshu Xiao, et al.
Science (2021) Vol. 373, Iss. 6555, pp. 642-648
Open Access | Times Cited: 236

Showing 1-25 of 236 citing articles:

The origins of SARS-CoV-2: A critical review
Edward C. Holmes, Stephen A. Goldstein, Angela L. Rasmussen, et al.
Cell (2021) Vol. 184, Iss. 19, pp. 4848-4856
Open Access | Times Cited: 445
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
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
Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant
Jun Zhang, Tianshu Xiao, Yongfei Cai, et al.
Science (2021) Vol. 374, Iss. 6573, pp. 1353-1360
Open Access | Times Cited: 289
Structures of the Omicron spike trimer with ACE2 and an anti-Omicron antibody
Wanchao Yin, Youwei Xu, Peiyu Xu, et al.
Science (2022) Vol. 375, Iss. 6584, pp. 1048-1053
Open Access | Times Cited: 269
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: 187
Molecular basis of receptor binding and antibody neutralization of Omicron
Hong Qin, Wenyu Han, Jiawei Li, et al.
Nature (2022) Vol. 604, Iss. 7906, pp. 546-552
Open Access | Times Cited: 187
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
Proteolytic activation of SARS‐CoV‐2 spike protein
Makoto Takeda
Microbiology and Immunology (2021) Vol. 66, Iss. 1, pp. 15-23
Open Access | Times Cited: 162
Daily longitudinal sampling of SARS-CoV-2 infection reveals substantial heterogeneity in infectiousness
Ruian Ke, Pamela P. Martinez, Rebecca L. Smith, et al.
Nature Microbiology (2022) Vol. 7, Iss. 5, pp. 640-652
Open Access | Times Cited: 158
Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function
Tzu‐Jing Yang, Pei‐Yu Yu, Yuan‐Chih Chang, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 9, pp. 731-739
Open Access | Times Cited: 156
Structural basis for SARS-CoV-2 Delta variant recognition of ACE2 receptor and broadly neutralizing antibodies
Yifan Wang, Caixuan Liu, Chao Zhang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 155
SARS-CoV-2-specific antibody and T-cell responses 1 year after infection in people recovered from COVID-19: a longitudinal cohort study
Li Guo, Geng Wang, Yeming Wang, et al.
The Lancet Microbe (2022) Vol. 3, Iss. 5, pp. e348-e356
Open Access | Times Cited: 148
Structural and functional impact by SARS-CoV-2 Omicron spike mutations
Jun Zhang, Yongfei Cai, Christy L. Lavine, et al.
Cell Reports (2022) Vol. 39, Iss. 4, pp. 110729-110729
Open Access | Times Cited: 138
Emerging SARS-CoV-2 Variants of Concern (VOCs): An Impending Global Crisis
Angel Yun-Kuan Thye, Jodi Woan‐Fei Law, Priyia Pusparajah, et al.
Biomedicines (2021) Vol. 9, Iss. 10, pp. 1303-1303
Open Access | Times Cited: 120
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
Gang Ye, Bin Liu, Fang Li
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 117
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
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
Neutralizing activity of Sputnik V vaccine sera against SARS-CoV-2 variants
Satoshi Ikegame, Mohammed Nure Alam Siddiquey, Chuan-Tien Hung, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 110
Mutations of SARS-CoV-2 spike protein: Implications on immune evasion and vaccine-induced immunity
Hylemariam Mihiretie Mengist, Arnaud John Kombe Kombe, Daniel Mekonnen, et al.
Seminars in Immunology (2021) Vol. 55, pp. 101533-101533
Open Access | Times Cited: 105
Structural and biochemical rationale for enhanced spike protein fitness in delta and kappa SARS-CoV-2 variants
James W. Saville, Dhiraj Mannar, Xing Zhu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 96
γδ T cells: origin and fate, subsets, diseases and immunotherapy
Yi Hu, Qinglin Hu, Yongsheng Li, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 76
SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy
Ziwei Yang, Yang Han, Shilei Ding, et al.
mBio (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 70
Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein
Valeria Calvaresi, Antoni G. Wrobel, Joanna Toporowska, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 43
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