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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:

Assessing Antigen Structural Integrity through Glycosylation Analysis of the SARS-CoV-2 Viral Spike
Juliane Brun, Snežana Vasiljević, Bevin Gangadharan, et al.
ACS Central Science (2021) Vol. 7, Iss. 4, pp. 586-593
Open Access | Times Cited: 81

Showing 1-25 of 81 citing articles:

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: 348
The glycosylation in SARS-CoV-2 and its receptor ACE2
Yanqiu Gong, Suideng Qin, Lunzhi Dai, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 174
Fine-tuning the spike: role of the nature and topology of the glycan shield in the structure and dynamics of the SARS-CoV-2 S
Aoife M. Harbison, Carl A. Fogarty, Toan K. Phung, et al.
Chemical Science (2021) Vol. 13, Iss. 2, pp. 386-395
Open Access | Times Cited: 83
Glycosylation of SARS-CoV-2: structural and functional insights
Asif Shajahan, Lauren E. Pepi, Daniel S. Rouhani, et al.
Analytical and Bioanalytical Chemistry (2021) Vol. 413, Iss. 29, pp. 7179-7193
Open Access | Times Cited: 77
Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Top-Down Mass Spectrometry
David S. Roberts, Morgan Mann, Jake A. Melby, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 31, pp. 12014-12024
Open Access | Times Cited: 63
Identification of lectin receptors for conserved SARS‐CoV‐2 glycosylation sites
David Hoffmann, Stefan Mereiter, Yoo Jin Oh, et al.
The EMBO Journal (2021) Vol. 40, Iss. 19
Open Access | Times Cited: 62
Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation
Joel D. Allen, Himanshi Chawla, Firdaus Samsudin, et al.
Biochemistry (2021) Vol. 60, Iss. 27, pp. 2153-2169
Open Access | Times Cited: 60
Variations within the Glycan Shield of SARS-CoV-2 Impact Viral Spike Dynamics
Maddy L. Newby, Carl A. Fogarty, Joel D. Allen, et al.
Journal of Molecular Biology (2022) Vol. 435, Iss. 4, pp. 167928-167928
Open Access | Times Cited: 45
Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concern
Asif Shajahan, Lauren E. Pepi, Bhoj Kumar, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 41
Principles of SARS-CoV-2 glycosylation
Himanshi Chawla, Elisa Fadda, Max Crispin
Current Opinion in Structural Biology (2022) Vol. 75, pp. 102402-102402
Open Access | Times Cited: 39
Plant glycoengineering for designing next-generation vaccines and therapeutic proteins
Richard Strasser
Biotechnology Advances (2023) Vol. 67, pp. 108197-108197
Open Access | Times Cited: 24
Immune Epitopes of SARS-CoV-2 Spike Protein and Considerations for Universal Vaccine Development
Nicholas Magazine, Tianyi Zhang, Anang D. Bungwon, et al.
ImmunoHorizons (2024) Vol. 8, Iss. 3, pp. 214-226
Open Access | Times Cited: 10
The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
Joel D. Allen, Dylan P. Ivory, Ge Song, et al.
Cell Reports (2023) Vol. 42, Iss. 4, pp. 112307-112307
Open Access | Times Cited: 22
Restoring Protein Glycosylation with GlycoShape
Callum M. Ives, Ojas Singh, Silvia D’Andrea, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 21
Quantitative profiling of N-glycosylation of SARS-CoV-2 spike protein variants
Yongjing Xie, Michael Butler
Glycobiology (2023) Vol. 33, Iss. 3, pp. 188-202
Open Access | Times Cited: 18
Restoring protein glycosylation with GlycoShape
Callum M. Ives, Ojas Singh, Silvia D’Andrea, et al.
Nature Methods (2024) Vol. 21, Iss. 11, pp. 2117-2127
Open Access | Times Cited: 8
Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein
Shijian Zhang, Eden P. Go, Haitao Ding, et al.
Journal of Virology (2021) Vol. 96, Iss. 3
Open Access | Times Cited: 34
Role for N -glycans and calnexin-calreticulin chaperones in SARS-CoV-2 Spike maturation and viral infectivity
Qi Yang, Anju Kelkar, Anirudh Sriram, et al.
Science Advances (2022) Vol. 8, Iss. 38
Open Access | Times Cited: 27
Stabilized recombinant SARS-CoV-2 spike antigen enhances vaccine immunogenicity and protective capacity
Christian Meyer zu Natrup, Alina Tscherne, Christine Dahlke, et al.
Journal of Clinical Investigation (2022) Vol. 132, Iss. 24
Open Access | Times Cited: 27
Site‐specific glycosylation of SARS‐CoV‐2: Big challenges in mass spectrometry analysis
Diana Campos, Michael Girgis, Miloslav Šanda
PROTEOMICS (2022) Vol. 22, Iss. 15-16
Open Access | Times Cited: 23
Distinct core glycan and O-glycoform utilization of SARS-CoV-2 Omicron variant Spike protein RBD revealed by top-down mass spectrometry
David S. Roberts, Morgan Mann, Brad H. Li, et al.
Chemical Science (2022) Vol. 13, Iss. 36, pp. 10944-10949
Open Access | Times Cited: 23
Analysis of the N-glycosylation profiles of the spike proteins from the Alpha, Beta, Gamma, and Delta variants of SARS-CoV-2
Dongxia Wang, Jakub Baudys, Sarah H. Osman, et al.
Analytical and Bioanalytical Chemistry (2023) Vol. 415, Iss. 19, pp. 4779-4793
Open Access | Times Cited: 14
Multi-omics for COVID-19: driving development of therapeutics and vaccines
Mengyu Guo, Muya Xiong, Jinying Peng, et al.
National Science Review (2023) Vol. 10, Iss. 9
Open Access | Times Cited: 12
Influence of glycosylation on the immunogenicity and antigenicity of viral immunogens
Maddy L. Newby, Joel D. Allen, Max Crispin
Biotechnology Advances (2023) Vol. 70, pp. 108283-108283
Open Access | Times Cited: 12
Strategies for Proteome-Wide Quantification of Glycosylation Macro- and Micro-Heterogeneity
Pan Fang, Yanlong Ji, Thomas Oellerich, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 3, pp. 1609-1609
Open Access | Times Cited: 18
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