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:

Understanding Mutations in Human SARS-CoV-2 Spike Glycoprotein: A Systematic Review & Meta-Analysis
Reetesh Kumar, Yogesh Srivastava, Pandiyan Muthuramalingam, et al.
Viruses (2023) Vol. 15, Iss. 4, pp. 856-856
Open Access | Times Cited: 28

Showing 1-25 of 28 citing articles:

Immunomodulatory approaches in managing lung inflammation in COVID‐19: A double‐edge sword
Geetika Verma, Manish Dhawan, AbdulRahman A. Saied, et al.
Immunity Inflammation and Disease (2023) Vol. 11, Iss. 9
Open Access | Times Cited: 18

A comprehensive analysis of SARS-CoV-2 missense mutations indicates that all possible amino acid replacements in the viral proteins occurred within the first two-and-a-half years of the pandemic
Nicole Balasco, Gianluca Damaggio, Luciana Esposito, et al.
International Journal of Biological Macromolecules (2024) Vol. 266, pp. 131054-131054
Open Access | Times Cited: 5

Origin, evolution, and spread of SARS-CoV-2
Jonas Michel Wolf, Lucas Wolf, Paul C. Wolf, et al.
Elsevier eBooks (2025), pp. 5-19
Closed Access

Decoding SARS-CoV-2 variants: Mutations, viral stability, and breakthroughs in vaccines and therapies
Zainularifeen Abduljaleel
Biophysical Chemistry (2025) Vol. 320-321, pp. 107413-107413
Closed Access

The wind of change: Gibbs energy of binding and infectivity evolution of Omicron BA.2.86 Pirola, EG.5.1, XBB.1.16 Arcturus, CH.1.1 and BN.1 variants of SARS-CoV-2
Marko Popovic, Gavrilo Šekularac, Marta Popović
Microbial Risk Analysis (2024) Vol. 26, pp. 100290-100290
Closed Access | Times Cited: 4

Advancements in SARS-CoV-2 detection: Navigating the molecular landscape and diagnostic technologies
Nuha Almulla, Raya Soltane, Ahlam Alasiri, et al.
Heliyon (2024) Vol. 10, Iss. 9, pp. e29909-e29909
Open Access | Times Cited: 3

Structural understanding of SARS-CoV-2 virus entry to host cells
Kim Le, Shrute Kannappan, Truc Kim, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 9

COVID-19: A threat to the respiratory system
Ghulam Rasool, Waqas Khan, Arif Khan, et al.
International Journal of Immunopathology and Pharmacology (2024) Vol. 38
Open Access | Times Cited: 2

Genomic surveillance of SARS-CoV-2 in Russia: insights from the VGARus platform
Ivan A. Kotov, M.R. Agletdinov, German V. Roev, et al.
Journal of microbiology epidemiology immunobiology (2024) Vol. 101, Iss. 4, pp. 435-447
Open Access | Times Cited: 1

Taking stock of the mutations in human SARS-CoV-2 spike proteins: From early days to nearly the end of COVID-19 pandemic
Lalitha Guruprasad, Gatta K. R. S. Naresh, Ganesh Boggarapu
Current Research in Structural Biology (2023) Vol. 6, pp. 100107-100107
Open Access | Times Cited: 3

Simple virus-free mouse models of COVID-19 pathologies and oral therapeutic intervention
Huabin Zhu, Anuj K. Sharma, Karina Aguilar, et al.
iScience (2024) Vol. 27, Iss. 3, pp. 109191-109191
Open Access

Whole-genome sequencing of some Ukrainian isolates of SARS-COV-2 virus and analysis of its genetic variability
S. A. Nychyk, Mykola Mandygra, Maksym Bezymennyi, et al.
Agricultural science and practice (2024) Vol. 10, Iss. 3, pp. 3-15
Open Access



Agricultural science and practice (2024) Vol. 10, Iss. 3
Open Access

Critical Point Mutations in the RBD of SARS-COV-2 Involved in Binding to ACE2
Milad Tolouie, Safar Farajnia, Davoud Farajzadeh, et al.
Molecular Genetics Microbiology and Virology (2024) Vol. 39, Iss. 1, pp. 86-94
Closed Access

Using a static magnetic field to attenuate the severity in COVID-19-invaded lungs
Hsuan-Yu Lai, Kuo-Cheng Fan, Yen-Hua Lee, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access

Protein stability models fail to capture epistatic interactions of double point mutations
Henry Dieckhaus, Brian Kuhlman
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Protein mimics of fusion core from SARS-CoV-1 can inhibit SARS-CoV-2 entry
Yancheng Zhan, Moxuan Li, Rui Gong
Biochemical and Biophysical Research Communications (2024) Vol. 736, pp. 150857-150857
Closed Access

Unmasking the Global Journey: Investigation of SARS-CoV-2 Variants of Interest Across Various Regions Through Whole-Genome and Phylogenetic Analysis
Yocyny Surendran, Parameswaran Vityashri, Nazwin Shahirah Binti Juhari, et al.
Jundishapur Journal of Microbiology (2024) Vol. 17, Iss. 9
Open Access

Protein stability models fail to capture epistatic interactions of double point mutations
Henry Dieckhaus, Brian Kuhlman
Protein Science (2024) Vol. 34, Iss. 1
Open Access

Marine Origin vs. Synthesized Compounds: In Silico Screening for a Potential Drug Against SARS-CoV-2
Amar Osmanović, Mirsada Salihović, Elma Veljović, et al.
Scientia Pharmaceutica (2024) Vol. 93, Iss. 1, pp. 2-2
Open Access

In silico identification of five binding sites on the SARS-CoV-2 spike protein and selection of seven ligands for such sites
Denilson F. Oliveira
Journal of Biomolecular Structure and Dynamics (2023), pp. 1-19
Closed Access | Times Cited: 1

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