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 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: 82

Showing 1-25 of 82 citing articles:

Two Years into the COVID-19 Pandemic: Lessons Learned
Severino Jefferson Ribeiro da Silva, Jéssica Catarine Frutuoso do Nascimento, Renata Pessôa Germano Mendes, et al.
ACS Infectious Diseases (2022) Vol. 8, Iss. 9, pp. 1758-1814
Open Access | Times Cited: 111

The Emergence of the Spike Furin Cleavage Site in SARS-CoV-2
Yujia A. Chan, Shing H. Zhan
Molecular Biology and Evolution (2021) Vol. 39, Iss. 1
Open Access | Times Cited: 60

Could SARS-CoV-2 Have Bacteriophage Behavior or Induce the Activity of Other Bacteriophages?
Carlo Brogna, Barbara Brogna, Domenico Rocco Bisaccia, et al.
Vaccines (2022) Vol. 10, Iss. 5, pp. 708-708
Open Access | Times Cited: 47

Spike Protein Cleavage-Activation in the Context of the SARS-CoV-2 P681R Mutation: an Analysis from Its First Appearance in Lineage A.23.1 Identified in Uganda
Bailey Lubinski, Laura E. Frazier, My V. T. Phan, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 4
Open Access | Times Cited: 43

Use of a risk assessment tool to determine the origin of severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2)
Xin Chen, Fatema Kalyar, Abrar Ahmad Chughtai, et al.
Risk Analysis (2024) Vol. 44, Iss. 8, pp. 1896-1906
Open Access | Times Cited: 13

Roles of the polybasic furin cleavage site of spike protein in SARS‐CoV‐2 replication, pathogenesis, and host immune responses and vaccination
Md. Golzar Hossain, Yan‐Dong Tang, Sharmin Akter, et al.
Journal of Medical Virology (2021) Vol. 94, Iss. 5, pp. 1815-1820
Closed Access | Times Cited: 49

Dual Inhibitors of Main Protease (MPro) and Cathepsin L as Potent Antivirals against SARS-CoV2
Santanu Mondal, Yongzhi Chen, G.J. Lockbaum, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 46, pp. 21035-21045
Open Access | Times Cited: 37

Molecular Virology of SARS-CoV-2 and Related Coronaviruses
Yu-An Kung, Kuo-Ming Lee, Huan-Jung Chiang, et al.
Microbiology and Molecular Biology Reviews (2022) Vol. 86, Iss. 2
Open Access | Times Cited: 34

Electrostatic Features for the Receptor Binding Domain of SARS-COV-2 Wildtype and Its Variants. Compass to the Severity of the Future Variants with the Charge-Rule
Fernando Luís Barroso da Silva, Carolina Corrêa Giron, Aatto Laaksonen
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 36, pp. 6835-6852
Open Access | Times Cited: 32

Intrinsic furin-mediated cleavability of the spike S1/S2 site from SARS-CoV-2 variant B.1.1.529 (Omicron)
Bailey Lubinski, Javier A. Jaimes, Gary R. Whittaker
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 30

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

O-Linked Sialoglycans Modulate the Proteolysis of SARS-CoV-2 Spike and Likely Contribute to the Mutational Trajectory in Variants of Concern
Edgar González-Rodríguez, Mia Zol-Hanlon, Ganka Bineva‐Todd, et al.
ACS Central Science (2023) Vol. 9, Iss. 3, pp. 393-404
Open Access | Times Cited: 22

IL-9 aggravates SARS-CoV-2 infection and exacerbates associated airway inflammation
Srikanth Sadhu, Rajdeep Dalal, Jyotsna Dandotiya, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 20

Could a Lower Toll-like Receptor (TLR) and NF-κB Activation Due to a Changed Charge Distribution in the Spike Protein Be the Reason for the Lower Pathogenicity of Omicron?
Ralf Kircheis, Oliver Planz
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 11, pp. 5966-5966
Open Access | Times Cited: 20

Neuropilin-1 Facilitates Pseudorabies Virus Replication and Viral Glycoprotein B Promotes Its Degradation in a Furin-Dependent Manner
Meng Chen, Menghang Wang, Xue-Gang Shen, et al.
Journal of Virology (2022) Vol. 96, Iss. 20
Open Access | Times Cited: 19

SARS-CoV-2 spike variants differ in their allosteric responses to linoleic acid
A. Sofia F. Oliveira, Deborah K. Shoemark, Andrew D. Davidson, et al.
Journal of Molecular Cell Biology (2023) Vol. 15, Iss. 3
Open Access | Times Cited: 12

The SARS-CoV-2 furin cleavage site: natural selection or smoking gun?
Bailey Lubinski, Gary R. Whittaker
The Lancet Microbe (2023) Vol. 4, Iss. 8, pp. e570-e570
Open Access | Times Cited: 12

A detailed examination of Coronavirus disease 2019 (COVID-19): covering past and future perspectives
Sabina Yasmin, Mohammad Yousuf Ansari
Microbial Pathogenesis (2025), pp. 107398-107398
Closed 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

Role of furin in the severity of COVID-19 infection via effects on miR-20b and miR-106a
Ismail Sami Mahmoud, Amr E. Ahmed, Olfat Shaker
Molecular Biology Reports (2025) Vol. 52, Iss. 1
Closed 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

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