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:

SARS-CoV-2 evolved variants optimize binding to cellular glycocalyx
Sang Hoon Kim, Fiona L. Kearns, Mia A. Rosenfeld, et al.
Cell Reports Physical Science (2023) Vol. 4, Iss. 4, pp. 101346-101346
Open Access | Times Cited: 41

Showing 1-25 of 41 citing articles:

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

Quantifying Fluorescence Lifetime Responsiveness of Environment-Sensitive Probes for Membrane Fluidity Measurements
Franziska Ragaller, Ellen Sjule, Yagmur Balim Urem, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 9, pp. 2154-2167
Open Access | Times Cited: 13

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

SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition
Qianyi E. Zhang, Jared Lindenberger, Ruth Parsons, et al.
Molecular Cell (2024) Vol. 84, Iss. 14, pp. 2747-2764.e7
Open Access | Times Cited: 9

Changes in total charge on spike protein of SARS-CoV-2 in emerging lineages
Anže Božič, Rudolf Podgornik
Bioinformatics Advances (2024) Vol. 4, Iss. 1
Open Access | Times Cited: 8

Variant-specific interactions at the plasma membrane: Heparan sulfate’s impact on SARS-CoV-2 binding kinetics
Dario Valter Conca, Fouzia Bano, Julius von Wirén, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5

Protecting the endothelial glycocalyx in COVID-19
Emira Adam Tay, Vimmal Vijayakumar, Raika Francesca Morales, et al.
PLoS Pathogens (2024) Vol. 20, Iss. 5, pp. e1012203-e1012203
Open Access | Times Cited: 5

Variant-Specific Interactions at the Plasma Membrane: Heparan Sulfate’s Impact on SARS-CoV-2 Binding Kinetics
Dario Valter Conca, Fouzia Bano, Małgorzata Graul, et al.
Analytical Chemistry (2025)
Open Access

Allosteric modulation by the fatty acid site in the glycosylated SARS-CoV-2 spike
A. Sofia F. Oliveira, Fiona L. Kearns, Mia A. Rosenfeld, et al.
(2025)
Open Access

A Reflection on the Use of Molecular Simulation to Respond to SARS-CoV-2 Pandemic Threats
Lorenzo Casalino, Carlos A. Ramos‐Guzmán, Rommie E. Amaro, et al.
The Journal of Physical Chemistry Letters (2025), pp. 3249-3263
Open Access

Balancing stability and function: impact of the surface charge of SARS-CoV-2 Omicron spike protein
Daniel Lauster, Rainer Haag, Matthias Ballauff, et al.
npj Viruses (2025) Vol. 3, Iss. 1
Open Access

Heparan sulfate proteoglycans remodel SARS-CoV-2 spike conformation to allow integrin interaction and infection of endothelial cells
Antonella Bugatti, Alberto Zani, Marta Bardelli, et al.
Frontiers in Cellular and Infection Microbiology (2025) Vol. 15
Open Access

Allosteric modulation by the fatty acid site in the glycosylated SARS-CoV-2 spike
A. Sofia F. Oliveira, Fiona L. Kearns, Mia A. Rosenfeld, et al.
eLife (2025) Vol. 13
Open Access

Synergistic Binding of SARS-CoV-2 to ACE2 and Gangliosides in Native Lipid Membranes
Manorama Dey, Anurag Sharma, Garvita Dhanawat, et al.
ACS Infectious Diseases (2024) Vol. 10, Iss. 3, pp. 907-916
Closed Access | Times Cited: 3

Oligomerization-driven avidity correlates with SARS-CoV-2 cellular binding and inhibition
Roi Asor, Anna Olerinyova, Sean A. Burnap, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 40
Open Access | Times Cited: 3

The accomplices: Heparan sulfates and N-glycans foster SARS-CoV-2 spike:ACE2 receptor binding and virus priming
Giulia Paiardi, Matheus Ferraz, Marco Rusnati, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 43
Open Access | Times Cited: 3

SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition
Qianyi E. Zhang, Jared Lindenberger, Ruth Parsons, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

Electrostatic Interaction between SARS-CoV-2 and Charged Surfaces: Spike Protein Evolution Changed the Game
Marc Domingo, Horacio V. Guzman, Matej Kanduč, et al.
Journal of Chemical Information and Modeling (2024) Vol. 65, Iss. 1, pp. 240-251
Open Access | Times Cited: 2

Evolution of SARS-CoV-2 spike trimers towards optimized heparan sulfate cross-linking and inter-chain mobility
Jurij Froese, Marco Mandalari, Monica Civera, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2

Docking and Molecular Dynamics Simulations Clarify Binding Sites for Interactions of Novel Marine Sulfated Glycans with SARS-CoV-2 Spike Glycoprotein
Priyanka Samanta, Sushil Kumar Mishra, Vitor H. Pomin, et al.
Molecules (2023) Vol. 28, Iss. 17, pp. 6413-6413
Open Access | Times Cited: 5

The accomplices: Heparan sulfates and N-glycans foster SARS-CoV-2 spike:ACE2 receptor binding and virus priming
Giulia Paiardi, Matheus Ferraz, Marco Rusnati, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Allosteric modulation by the fatty acid site in the glycosylated SARS-CoV-2 spike
A. Sofia F. Oliveira, Fiona L. Kearns, Mia A. Rosenfeld, et al.
(2024)
Open Access | Times Cited: 1

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