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.

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Showing 1-25 of 38 citing articles:

The P681H Mutation in the Spike Glycoprotein of the Alpha Variant of SARS-CoV-2 Escapes IFITM Restriction and Is Necessary for Type I Interferon Resistance
María José Lista, Helena Winstone, Harry Wilson, et al.
Journal of Virology (2022) Vol. 96, Iss. 23
Open Access | Times Cited: 49

Altered host protease determinants for SARS-CoV-2 Omicron
Jasper Fuk‐Woo Chan, Xiner Huang, Bingjie Hu, et al.
Science Advances (2023) Vol. 9, Iss. 3
Open Access | Times Cited: 32

iNGNN-DTI: prediction of drug–target interaction with interpretable nested graph neural network and pretrained molecule models
Yan Sun, Yan Yi Li, Carson K. Leung, et al.
Bioinformatics (2024) Vol. 40, Iss. 3
Open Access | Times Cited: 9

New insights into the function and pathophysiology of the ectodomain sheddase A Disintegrin And Metalloproteinase 10 (ADAM10)
David P. Rosenbaum, Paul Säftig
FEBS Journal (2023) Vol. 291, Iss. 13, pp. 2733-2766
Open Access | Times Cited: 22

Initial immune response after exposure to Mycobacterium tuberculosis or to SARS-COV-2: similarities and differences
Alessandra Aiello, Saeid Najafi Fard, Delia Goletti
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 22

Neutrophil proteases are protective against SARS-CoV-2 by degrading the spike protein and dampening virus-mediated inflammation
Nathan Gf Leborgne, Christelle Devisme, Nedim Kozarac, et al.
JCI Insight (2024) Vol. 9, Iss. 7
Open Access | Times Cited: 6

Identification and differential usage of a host metalloproteinase entry pathway by SARS-CoV-2 Delta and Omicron
Mehdi Benlarbi, Geneviève Laroche, Corby Fink, et al.
iScience (2022) Vol. 25, Iss. 11, pp. 105316-105316
Open Access | Times Cited: 27

S Protein, ACE2 and Host Cell Proteases in SARS-CoV-2 Cell Entry and Infectivity; Is Soluble ACE2 a Two Blade Sword? A Narrative Review
Reza Nejat, Maziar Fayaz Torshizi, David J. Najafi
Vaccines (2023) Vol. 11, Iss. 2, pp. 204-204
Open Access | Times Cited: 16

SARS-CoV-2 Spike-Mediated Entry and Its Regulation by Host Innate Immunity
Yu Shi, Huina Hu, Qiangyun Ai, et al.
Viruses (2023) Vol. 15, Iss. 3, pp. 639-639
Open Access | Times Cited: 9

The role of influenza-A virus and coronavirus viral glycoprotein cleavage in host adaptation
Miriam Ruth Heindl, Eva Böttcher‐Friebertshäuser
Current Opinion in Virology (2023) Vol. 58, pp. 101303-101303
Open Access | Times Cited: 8

Omicsynin B4 potently blocks coronavirus infection by inhibiting host proteases cathepsin L and TMPRSS2
Yihua Li, Kun Wang, Hongmin Sun, et al.
Antiviral Research (2023) Vol. 214, pp. 105606-105606
Open Access | Times Cited: 8

Assessing the Potential Contribution of in Silico Studies in Discovering Drug Candidates that Interact with Various SARS-CoV-2 Receptors
Aganze Gloire-Aimé Mushebenge, Samuel Chima Ugbaja, Nonkululeko Avril Mbatha, et al.
(2023)
Open Access | Times Cited: 8

The Spike-Stabilizing D614G Mutation Interacts with S1/S2 Cleavage Site Mutations To Promote the Infectious Potential of SARS-CoV-2 Variants
Stacy Gellenoncourt, Nell Saunders, Rémy Robinot, et al.
Journal of Virology (2022) Vol. 96, Iss. 19
Open Access | Times Cited: 14

Control of SARS-CoV-2 infection by MT1-MMP-mediated shedding of ACE2
Xuanming Guo, Jianli Cao, Jian‐Piao Cai, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 14

SARS‐CoV‐2, periodontal pathogens, and host factors: The trinity of oral post‐acute sequelae of COVID‐19
Joel Schwartz, Kristelle J. Capistrano, Joseph L. Gluck, et al.
Reviews in Medical Virology (2024) Vol. 34, Iss. 3
Open Access | Times Cited: 2

Host Cell Proteases Involved in Human Respiratory Viral Infections and Their Inhibitors: A Review
Bailey Lubinski, Gary R. Whittaker
Viruses (2024) Vol. 16, Iss. 6, pp. 984-984
Open Access | Times Cited: 2

Metalloprotease-Dependent S2′-Activation Promotes Cell–Cell Fusion and Syncytiation of SARS-CoV-2
James V. Harte, Samantha L. Wakerlin, Andrew J. Lindsay, et al.
Viruses (2022) Vol. 14, Iss. 10, pp. 2094-2094
Open Access | Times Cited: 9

In Silico and In Vitro Evaluation of Some Amidine Derivatives as Hit Compounds towards Development of Inhibitors against Coronavirus Diseases
Ahmed H.E. Hassan, Selwan M. El‐Sayed, Mizuki Yamamoto, et al.
Viruses (2023) Vol. 15, Iss. 5, pp. 1171-1171
Open Access | Times Cited: 5

The basis of complications in the context of SARS-CoV-2 infection: Pathological activation of ADAM17
Shenghai Jiang, Hao Yang, Zhong‐Ming Sun, et al.
Biochemical and Biophysical Research Communications (2023) Vol. 679, pp. 37-46
Closed Access | Times Cited: 4

A disintegrin and metalloproteinase domain 9 facilitates SARS-CoV-2 entry into cells with low ACE2 expression
Ivonne Melano, Wei‐Chung Cheng, Li-Lan Kuo, et al.
Microbiology Spectrum (2023) Vol. 11, Iss. 5
Open Access | Times Cited: 4

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