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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:

Proteolytic Activation of SARS-CoV-2 Spike at the S1/S2 Boundary: Potential Role of Proteases beyond Furin
Tiffany Tang, Javier A. Jaimes, Miya K. Bidon, et al.
ACS Infectious Diseases (2021) Vol. 7, Iss. 2, pp. 264-272
Open Access | Times Cited: 148

Showing 1-25 of 148 citing articles:

TMPRSS2 expression dictates the entry route used by SARS‐CoV‐2 to infect host cells
Jana Koch, Zina M. Uckeley, Patricio Doldan, et al.
The EMBO Journal (2021) Vol. 40, Iss. 16
Open Access | Times Cited: 292
Functional evaluation of the P681H mutation on the proteolytic activation of the SARS-CoV-2 variant B.1.1.7 (Alpha) spike
Bailey Lubinski, Maureen Hoch Vieira Fernandes, Laura E. Frazier, et al.
iScience (2021) Vol. 25, Iss. 1, pp. 103589-103589
Open Access | Times Cited: 194
Cellular host factors for SARS-CoV-2 infection
Jim Baggen, Els Vanstreels, Sander Jansen, et al.
Nature Microbiology (2021) Vol. 6, Iss. 10, pp. 1219-1232
Open Access | Times Cited: 185
A TMPRSS2 inhibitor acts as a pan-SARS-CoV-2 prophylactic and therapeutic
Tirosh Shapira, I. Abrrey Monreal, Sébastien P. Dion, et al.
Nature (2022) Vol. 605, Iss. 7909, pp. 340-348
Open Access | Times Cited: 177
Mutations in SARS-CoV-2 variants of concern link to increased spike cleavage and virus transmission
Alba Escalera, Ana S. González-Reiche, Sadaf Aslam, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 3, pp. 373-387.e7
Open Access | Times Cited: 176
Proteolytic activation of SARS‐CoV‐2 spike protein
Makoto Takeda
Microbiology and Immunology (2021) Vol. 66, Iss. 1, pp. 15-23
Open Access | Times Cited: 171
Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation
Bryan J. Fraser, Serap Beldar, Almagul Seitova, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 9, pp. 963-971
Open Access | Times Cited: 160
Cell entry by SARS-CoV-2
Ruchao Peng, Lian-Ao Wu, Qingling Wang, et al.
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 10, pp. 848-860
Open Access | Times Cited: 149
SARS-CoV-2 and the Host Cell: A Tale of Interactions
Massimo Pizzato, Chiara Baraldi, Giulia Boscato Sopetto, et al.
Frontiers in Virology (2022) Vol. 1
Open Access | Times Cited: 72
SARS-CoV-2 spike and its adaptable furin cleavage site
Gary R. Whittaker
The Lancet Microbe (2021) Vol. 2, Iss. 10, pp. e488-e489
Open Access | Times Cited: 81
Functional evaluation of the P681H mutation on the proteolytic activation the SARS-CoV-2 variant B.1.1.7 (Alpha) spike
Bailey Lubinski, Maureen Hoch Vieira Fernandes, Laura E. Frazier, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 68
Coronavirus entry: how we arrived at SARS-CoV-2
Gary R. Whittaker, Susan Daniel, Jean K. Millet
Current Opinion in Virology (2021) Vol. 47, pp. 113-120
Open Access | Times Cited: 65
The Transmembrane Protease TMPRSS2 as a Therapeutic Target for COVID-19 Treatment
Lukas Wettstein, Frank Kirchhoff, Jan Münch
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 3, pp. 1351-1351
Open Access | Times Cited: 57
Coagulation factors directly cleave SARS-CoV-2 spike and enhance viral entry
Edward R. Kastenhuber, Marisa Mercadante, Benjamin E. Nilsson-Payant, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 55
Structural conservation among variants of the SARS-CoV-2 spike postfusion bundle
Kailu Yang, Chuchu Wang, K. Ian White, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 16
Open Access | Times Cited: 44
Spread of Gamma (P.1) Sub-Lineages Carrying Spike Mutations Close to the Furin Cleavage Site and Deletions in the N-Terminal Domain Drives Ongoing Transmission of SARS-CoV-2 in Amazonas, Brazil
Felipe Gomes Naveca, Valdinete Alves do Nascimento, Victor Costa de Souza, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 1
Open Access | Times Cited: 42
SARS-CoV-2 Spike Furin Cleavage Site and S2′ Basic Residues Modulate the Entry Process in a Host Cell-Dependent Manner
Muriel Lavie, Jean Dubuisson, Sandrine Belouzard
Journal of Virology (2022) Vol. 96, Iss. 13
Open Access | Times Cited: 39
Cholesterol and COVID-19—therapeutic opportunities at the host/virus interface during cell entry
Thomas Grewal, Mai Khanh Linh Nguyen, Christa Buechler
Life Science Alliance (2024) Vol. 7, Iss. 5, pp. e202302453-e202302453
Open Access | Times Cited: 9
Discovering natural products as potential inhibitors of SARS-CoV-2 spike proteins
Muhammad Alqaaf, Ahmad Kamal Nasution, Mohammad Bozlul Karim, et al.
Scientific Reports (2025) Vol. 15, Iss. 1
Open Access | Times Cited: 1
Targeting the viral‐entry facilitators of SARS‐CoV‐2 as a therapeutic strategy in COVID‐19
Shibi Muralidar, Gayathri Gopal, Senthil Visaga Ambi
Journal of Medical Virology (2021) Vol. 93, Iss. 9, pp. 5260-5276
Open Access | Times Cited: 41
SARS-CoV-2 Infects Human ACE2-Negative Endothelial Cells through an αvβ3 Integrin-Mediated Endocytosis Even in the Presence of Vaccine-Elicited Neutralizing Antibodies
Antonella Bugatti, Federica Filippini, Marta Bardelli, et al.
Viruses (2022) Vol. 14, Iss. 4, pp. 705-705
Open Access | Times Cited: 31
Membrane attachment and fusion of HIV-1, influenza A, and SARS-CoV-2: resolving the mechanisms with biophysical methods
Geetanjali Negi, Anurag Sharma, Manorama Dey, et al.
Biophysical Reviews (2022) Vol. 14, Iss. 5, pp. 1109-1140
Open Access | Times Cited: 29
COVID-19 Therapeutic Potential of Natural Products
Zhaoxuan Low, Rafidah Lani, Vunjia Tiong, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 11, pp. 9589-9589
Open Access | Times Cited: 19
AlphaFold2 Reveals Structural Patterns of Seasonal Haplotype Diversification in SARS-CoV-2 Spike Protein Variants
Muhammad Asif Ali, Gustavo Caetano‐Anollés
Biology (2024) Vol. 13, Iss. 3, pp. 134-134
Open Access | Times Cited: 6
Targeting furin, a cellular proprotein convertase, for COVID-19 prevention and therapeutics
Xia Jiang, Dabing Li, Mazaher Maghsoudloo, et al.
Drug Discovery Today (2024) Vol. 29, Iss. 7, pp. 104026-104026
Closed Access | Times Cited: 6
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