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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:

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: 118

Showing 1-25 of 118 citing articles:

Neutralization of SARS-CoV-2 Omicron sub-lineages BA.1, BA.1.1, and BA.2
John P. Evans, Cong Zeng, Panke Qu, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 8, pp. 1093-1102.e3
Open Access | Times Cited: 134
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: 123
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: 118
Spike and nsp6 are key determinants of SARS-CoV-2 Omicron BA.1 attenuation
Da‐Yuan Chen, Chue Vin Chin, Devin Kenney, et al.
Nature (2023) Vol. 615, Iss. 7950, pp. 143-150
Open Access | Times Cited: 102
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: 94
Delta variant (B.1.617.2) of SARS-CoV-2: Mutations, impact, challenges and possible solutions
Manish Dhawan, Abhilasha Sharma, Priyanka Choudhary, et al.
Human Vaccines & Immunotherapeutics (2022) Vol. 18, Iss. 5
Open Access | Times Cited: 93
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: 47
SARS-CoV-2 spike opening dynamics and energetics reveal the individual roles of glycans and their collective impact
Yui Tik Pang, Atanu Acharya, Diane L. Lynch, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 60
Structural Basis for Human Receptor Recognition by SARS-CoV-2 Omicron Variant BA.1
Qibin Geng, Ke Shi, Gang Ye, et al.
Journal of Virology (2022) Vol. 96, Iss. 8
Open Access | Times Cited: 58
Omicron Spike Protein Has a Positive Electrostatic Surface That Promotes ACE2 Recognition and Antibody Escape
Hin Hark Gan, John Zinno, Fabio Piano, et al.
Frontiers in Virology (2022) Vol. 2
Open Access | Times Cited: 54
Structural basis for mouse receptor recognition by SARS-CoV-2 omicron variant
Wei Zhang, Ke Shi, Qibin Geng, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 44
Open Access | Times Cited: 43
SARS-CoV-2 spike N-terminal domain modulates TMPRSS2-dependent viral entry and fusogenicity
Bo Meng, Rawlings Datir, Jinwook Choi, et al.
Cell Reports (2022) Vol. 40, Iss. 7, pp. 111220-111220
Open Access | Times Cited: 41
Evolution of the SARS-CoV-2 Omicron spike
Ruth Parsons, Priyamvada Acharya
Cell Reports (2023) Vol. 42, Iss. 12, pp. 113444-113444
Open Access | Times Cited: 35
In Silico Discovery of Small Molecule Modulators Targeting the Achilles’ Heel of SARS-CoV-2 Spike Protein
Qing Wang, Fanhao Meng, Yuting Xie, et al.
ACS Central Science (2023) Vol. 9, Iss. 2, pp. 252-265
Open Access | Times Cited: 33
Markov State Models and Perturbation-Based Approaches Reveal Distinct Dynamic Signatures and Hidden Allosteric Pockets in the Emerging SARS-Cov-2 Spike Omicron Variant Complexes with the Host Receptor: The Interplay of Dynamics and Convergent Evolution Modulates Allostery and Functional Mechanisms
Sian Xiao, Mohammed Alshahrani, Grace Gupta, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 16, pp. 5272-5296
Open Access | Times Cited: 31
A large expert-curated cryo-EM image dataset for machine learning protein particle picking
Ashwin Dhakal, Rajan Gyawali, Liguo Wang, et al.
Scientific Data (2023) Vol. 10, Iss. 1
Open Access | Times Cited: 26
Single-molecule imaging reveals allosteric stimulation of SARS-CoV-2 spike receptor binding domain by host sialic acid
Marco A. Díaz-Salinas, Aastha Jain, Natasha D. Durham, et al.
Science Advances (2024) Vol. 10, Iss. 29
Open Access | Times Cited: 9
Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level
Rong Zhu, Daniel Canena, Mateusz Sikora, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 33
Intrinsic furin-mediated cleavability of the spike S1/S2 site from SARS-CoV-2 variant B.1.1.529 (Omicron)
Bailey Lubinski, Javier A. Jaimes, Gary R. Whittaker
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 30
Balancing Functional Tradeoffs between Protein Stability and ACE2 Binding in the SARS-CoV-2 Omicron BA.2, BA.2.75 and XBB Lineages: Dynamics-Based Network Models Reveal Epistatic Effects Modulating Compensatory Dynamic and Energetic Changes
Gennady M. Verkhivker, Mohammed Alshahrani, Grace Gupta
Viruses (2023) Vol. 15, Iss. 5, pp. 1143-1143
Open Access | Times Cited: 22
Mechanism and evolution of human ACE2 binding by SARS-CoV-2 spike
Antoni G. Wrobel
Current Opinion in Structural Biology (2023) Vol. 81, pp. 102619-102619
Open Access | Times Cited: 21
Advances in SARS-CoV-2 receptor-binding domain-based COVID-19 vaccines
Xiao‐Qing Guan, Yang Yang, Lanying Du
Expert Review of Vaccines (2023) Vol. 22, Iss. 1, pp. 422-439
Open Access | Times Cited: 20
Nanoparticle Spikes Enhance Cellular Uptake via Regulating Myosin IIA Recruitment
Lulu Huang, Xiuhai Mao, Jie Li, et al.
ACS Nano (2023) Vol. 17, Iss. 10, pp. 9155-9166
Closed Access | Times Cited: 19
Therapeutic nanobodies against SARS-CoV-2 and other pathogenic human coronaviruses
Yang Yang, Fang Li, Lanying Du
Journal of Nanobiotechnology (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 9
Role of spike in the pathogenic and antigenic behavior of SARS-CoV-2 BA.1 Omicron
Da‐Yuan Chen, Devin Kenney, Chue Vin Chin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 24
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