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:

Spike-heparan sulfate interactions in SARS-CoV-2 infection
Fiona L. Kearns, Daniel R. Sandoval, Lorenzo Casalino, et al.
Current Opinion in Structural Biology (2022) Vol. 76, pp. 102439-102439
Open Access | Times Cited: 69

Showing 1-25 of 69 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: 20

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: 39

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: 32

The Alterations and Roles of Glycosaminoglycans in Human Diseases
Qingchi Wang, Lianli Chi
Polymers (2022) Vol. 14, Iss. 22, pp. 5014-5014
Open Access | Times Cited: 35

Global impact of proteoglycan science on human diseases
Christopher Xie, Liliana Schaefer, Renato V. Iozzo
iScience (2023) Vol. 26, Iss. 11, pp. 108095-108095
Open Access | Times Cited: 16

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: 6

Host heparan sulfate promotes ACE2 super-cluster assembly and enhances SARS-CoV-2-associated syncytium formation
Qi Zhang, Weichun Tang, Eduardo Stancanelli, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 14

Blood-brain barrier function in response to SARS-CoV-2 and its spike protein
Łukasz Suprewicz, Krzysztof Fiedoruk, Agata Czarnowska, et al.
Neurologia i Neurochirurgia Polska (2023) Vol. 57, Iss. 1, pp. 14-25
Open Access | Times Cited: 13

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

Therapeutic development targeting host heparan sulfate proteoglycan in SARS-CoV-2 infection
Qi Zhang, Ivan Pavlinov, Yihong Ye, et al.
Frontiers in Medicine (2024) Vol. 11
Open Access | Times Cited: 5

The relationship between SARS-CoV-2 infection and type 1 diabetes mellitus
Cyril Debuysschere, Magloire Pandoua Nekoua, Enagnon Kazali Alidjinou, et al.
Nature Reviews Endocrinology (2024) Vol. 20, Iss. 10, pp. 588-599
Closed Access | Times Cited: 5

Preclinical and Clinical Investigations of Potential Drugs and Vaccines for COVID-19 Therapy: A Comprehensive Review With Recent Update
Md. Easin Mia, Mithu Howlader, Farzana Akter, et al.
Clinical Pathology (2024) Vol. 17
Open Access | Times Cited: 5

SARS-CoV-2 infectivity can be modulated through bacterial grooming of the glycocalyx
Cameron Martino, Benjamin P. Kellman, Daniel R. Sandoval, et al.
mBio (2025)
Open Access

Synthetic heparan sulfate mimics based on chitosan derivatives show broad-spectrum antiviral activity
Julia Revuelta, Luciana Rusu, Clara Francés‐Gómez, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access

Nanoparticles and Glycosaminoglycans: Progress and Applications for Cancer Therapy
Pietro Milesi, Annamaria Naggi, Francesca Baldelli Bombelli, et al.
Proteoglycan Research (2025) Vol. 3, Iss. 1
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

Heparin, Heparan Sulphate and Sepsis: Potential New Options for Treatment
John Hogwood, Elaine Gray, Barbara Mulloy
Pharmaceuticals (2023) Vol. 16, Iss. 2, pp. 271-271
Open Access | Times Cited: 12

COVID-19 Biogenesis and Intracellular Transport
Alexander A. Mirоnоv, M.A. Savin, Galina V. Beznoussenko
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 5, pp. 4523-4523
Open Access | Times Cited: 12

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

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

The Virus Entry Pathway Determines Sensitivity to the Antiviral Peptide TAT-I24
Eva Kicker, Antonio Kouros, Kurt Zatloukal, et al.
Viruses (2025) Vol. 17, Iss. 4, pp. 458-458
Open Access

Well-Defined Heparin Mimetics Can Inhibit Binding of the Trimeric Spike of SARS-CoV-2 in a Length-Dependent Manner
Lifeng Sun, Pradeep Chopra, Ilhan Tomris, et al.
JACS Au (2023) Vol. 3, Iss. 4, pp. 1185-1195
Open Access | Times Cited: 9

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