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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:

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

Showing 1-25 of 39 citing articles:

Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries
Yu-Xi Tsai, Ning-En Chang, Klaus Reuter, et al.
Cell (2024) Vol. 187, Iss. 5, pp. 1296-1311.e26
Open Access | Times Cited: 19
Architects of infection: A structural overview of SARS-related coronavirus spike glycoproteins
Francesca R. Hills, Jemma L. Geoghegan, Mihnea Bostina
Virology (2025), pp. 110383-110383
Open Access | Times Cited: 1
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: 44
Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective
Subhomoi Borkotoky, Debajit Dey, Zaved Hazarika
Molecular Biology Reports (2022) Vol. 50, Iss. 3, pp. 2713-2721
Open Access | Times Cited: 36
In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM
Cheng-Yu Huang, Piotr Drączkowski, Yong-Sheng Wang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 31
Coronavirus accessory protein ORF3 biology and its contribution to viral behavior and pathogenesis
Fusheng Si, Shuai Song, Ruisong Yu, et al.
iScience (2023) Vol. 26, Iss. 4, pp. 106280-106280
Open Access | Times Cited: 17
COVID and nervous system: Mechanisms and consequences
Federica Monaco, Marco Cascella
Elsevier eBooks (2025), pp. 413-435
Closed Access
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
Spike N354 glycosylation augments SARS-CoV-2 fitness for human adaptation through multiple mechanisms
Pan Liu, Can Yue, Bo Meng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Role of N343 glycosylation on the SARS-CoV-2 S RBD structure and co-receptor binding across variants of concern
Callum M. Ives, Linh Nguyen, Carl A. Fogarty, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 4
Evolving spike-proteinN-glycosylation in SARS-CoV-2 variants
Sabyasachi Baboo, Jolene K. Diedrich, Jonathan L. Torres, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 11
Uncovering the Role of N-Glycan Occupancy on the Cooperative Assembly of Spike and Angiotensin Converting Enzyme 2 Complexes: Insights from Glycoengineering and Native Mass Spectrometry
Tarick J. El‐Baba, Corinne A. Lutomski, Sean A. Burnap, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 14, pp. 8021-8032
Open Access | Times Cited: 9
Interaction of SARS-CoV-2 with host cells and antibodies: experiment and simulation
Hung Van Nguyen, Hoang Linh Nguyen, Pham Dang Lan, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 18, pp. 6497-6553
Closed Access | Times Cited: 9
In-depth characterization of protein N-glycosylation for a COVID-19 variant-design vaccine spike protein
Jiangming Huang, Shouzeng Hou, Jiao An, et al.
Analytical and Bioanalytical Chemistry (2023) Vol. 415, Iss. 8, pp. 1455-1464
Open Access | Times Cited: 8
Variations in O-Glycosylation Patterns Influence Viral Pathogenicity, Infectivity, and Transmissibility in SARS-CoV-2 Variants
Sherifdeen Onigbinde, Cristian D. Gutierrez Reyes, Mojibola Fowowe, et al.
Biomolecules (2023) Vol. 13, Iss. 10, pp. 1467-1467
Open Access | Times Cited: 8
Many Roles of Carbohydrates: A Computational Spotlight on the Coronavirus S Protein Binding
Suman Maity, Atanu Acharya
ACS Applied Bio Materials (2023) Vol. 7, Iss. 2, pp. 646-656
Open Access | Times Cited: 7
SP-A binding to the SARS-CoV-2 spike protein using hybrid quantum and classical in silico modeling and molecular pruning by Quantum Approximate Optimization Algorithm (QAOA) Based MaxCut with ZDOCK
Sona Aramyan, Kirk McGregor, Samarth Sandeep, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 11
The role ofN-glycosylation in spike antigenicity for the SARS-CoV-2 Gamma variant
Cassandra L. Pegg, Naphak Modhiran, Rhys Parry, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
Impact of glycosylation on viral vaccines
Antonio Lembo, Antonio Molinaro, Cristina De Castro, et al.
Carbohydrate Polymers (2024) Vol. 342, pp. 122402-122402
Closed Access | Times Cited: 1
Up, up, down, down: the structural biology of the SARS-CoV-2 spike protein and how it cheats the immune system
Sabrina Stäb, Nicholas M. Pearce, Dale E. Tronrud, et al.
Crystallography Reviews (2024), pp. 1-44
Open Access | Times Cited: 1
Structural Evolution of Delta (B.1.617.2) and Omicron (BA.1) Spike Glycoproteins
Ingrid G. Prandi, Carla Mavian, Emanuela Giombini, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 15, pp. 8680-8680
Open Access | Times Cited: 8
The Spike Mutants Website: A Worldwide Used Resource against SARS-CoV-2
Isabella Romeo, Ingrid G. Prandi, Emanuela Giombini, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 21, pp. 13082-13082
Open Access | Times Cited: 8
The role of N-glycosylation in spike antigenicity for the SARS-CoV-2 gamma variant
Cassandra L. Pegg, Naphak Modhiran, Rhys Parry, et al.
Glycobiology (2023) Vol. 34, Iss. 2
Open Access | Times Cited: 4
Sialic Acid and Fucose Residues on the SARS-CoV-2 Receptor-Binding Domain Modulate IgG Antibody Reactivity
Ebba Samuelsson, Ekaterina Mirgorodskaya, Kristina Nyström, et al.
ACS Infectious Diseases (2022) Vol. 8, Iss. 9, pp. 1883-1893
Open Access | Times Cited: 7
Conventional Understanding of SARS‐CoV‐2 Mpro and Common Strategies for Developing Its Inhibitors
Kun Zhou, Daquan Chen
ChemBioChem (2023) Vol. 24, Iss. 22
Closed Access | Times Cited: 3
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