A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells

A novel coronavirus from patients with pneumonia in China, 2019

Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244

A pneumonia outbreak associated with a new coronavirus of probable bat origin

Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969

SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897

Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein

Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586

A novel coronavirus outbreak of global health concern

Wang, C., Horby, P. W., Hayden, F. G., & Gao, G. F. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30185-9 · Cited by 7,700

The EMBL-EBI search and sequence analysis tools APIs in 2019

Madeira, F., Park, Y. M., Lee, J., Buso, N., Gur, T., Madhusoodanan, N., Basutkar, P., Tivey, A. R. N., Potter, S. C., Finn, R. D., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz268 · Cited by 4,167

Identifying SARS-CoV-2-related coronaviruses in Malayan pangolins

Lam, T. T., Jia, N., Zhang, Y.-W., Shum, M. H.-H., Jiang, J.-F., Zhu, H., Tong, Y., Shi, Y., Ni, X.-B., Liao, Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2169-0 · Cited by 1,877

Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor

Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778

YASARA View—molecular graphics for all devices—from smartphones to workstations

Krieger, E., & Vriend, G. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu426 · Cited by 1,573

Membrane remodeling by SARS-CoV-2 – double-enveloped viral replication

Mohan, J., & Wollert, T. (2021) · Faculty Reviews · doi:10.12703/r/10-17 · Cited by 27

Molecular-Level Anatomy of SARS-CoV-2 for the Battle against the COVID-19 Pandemic

Komiyama, M. (2021) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20210030 · Cited by 27

SARS-CoV-2 cell entry and targeted antiviral development

Chen, Z., Du, R., Achi, J. G., Rong, L., & Cui, Q. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.05.007 · Cited by 27

VirusViz: comparative analysis and effective visualization of viral nucleotide and amino acid variants

Bernasconi, A., Gulino, A., Alfonsi, T., Canakoglu, A., Pinoli, P., Sandionigi, A., & Ceri, S. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab478 · Cited by 27

Studying SARS-CoV-2 with Fluorescence Microscopy

Putlyaeva, L. V., & Lukyanov, K. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126558 · Cited by 27

Identification of a High-Frequency Intrahost SARS-CoV-2 Spike Variant with Enhanced Cytopathic and Fusogenic Effects

Rocheleau, L., Laroche, G., Fu, K., Stewart, C. M., Mohamud, A. O., Côté, M., Giguère, P. M., Langlois, M., & Pelchat, M. (2021) · mBio · doi:10.1128/mbio.00788-21 · Cited by 29

High diversity in Delta variant across countries revealed by genome‐wide analysis of SARS‐CoV‐2 beyond the Spike protein

Suratekar, R., Ghosh, P., Niesen, M. J. M., Donadio, G., Anand, P., Soundararajan, V., & Venkatakrishnan, A. (2022) · Molecular Systems Biology · doi:10.15252/msb.202110673 · Cited by 28

Potential Immunogenic Activity of Computationally Designed mRNA- and Peptide-Based Prophylactic Vaccines against MERS, SARS-CoV, and SARS-CoV-2: A Reverse Vaccinology Approach

Khan, T., Khan, A., Ansari, J. K., Najmi, M. H., Wei, D., Muhammad, K., & Waheed, Y. (2022) · Molecules · doi:10.3390/molecules27072375 · Cited by 27

Homogeneous surrogate virus neutralization assay to rapidly assess neutralization activity of anti-SARS-CoV-2 antibodies

Kim, S. J., Yao, Z., Marsh, M., Eckert, D. M., Kay, M. S., Lyakisheva, A., Pasic, M. D., Bansal, A., Birnboim, C., Jha, P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31300-9 · Cited by 28

A Bispecific Antibody Targeting RBD and S2 Potently Neutralizes SARS-CoV-2 Omicron and Other Variants of Concern

Yuan, M., Chen, X., Zhu, Y., Dong, X., Liu, Y., Qian, Z., Ye, L., & Liu, P. (2022) · Journal of Virology · doi:10.1128/jvi.00775-22 · Cited by 27

LRRC15 inhibits SARS-CoV-2 cellular entry in trans

Song, J., Chow, R. D.-W., Peña-Hernández, M. A., Zhang, L., Loeb, S. A., So, E. Y., Liang, O. D., Ren, P., Chen, S., Wilen, C. B., et al. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001805 · Cited by 29

Control of SARS-CoV-2 infection by MT1-MMP-mediated shedding of ACE2

Guo, X., Cao, J., Cai, J.-P., Wu, J., Huang, J., Asthana, P., Wong, S. K. K., Ye, Z.-W., Gurung, S., Zhang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35590-x · Cited by 25

No Small Matter: A Perspective on Nanotechnology-Enabled Solutions to Fight COVID-19

Jones, G. W., Monopoli, M. P., Campagnolo, L., Pietroiusti, A., Tran, L., & Fadeel, B. (2020) · Nanomedicine · doi:10.2217/nnm-2020-0286 · Cited by 28

Man-Specific, GalNAc/T/Tn-Specific and Neu5Ac-Specific Seaweed Lectins as Glycan Probes for the SARS-CoV-2 (COVID-19) Coronavirus

Barre, A., Damme, E. J. M. V., Simplicien, M., Benoist, H., & Rougé, P. (2020) · Marine Drugs · doi:10.3390/md18110543 · Cited by 27

Understanding Viral Infection Mechanisms and Patient Symptoms for the Development of COVID-19 Therapeutics

Choi, H. M., Moon, S. Y., Yang, H.-I., & Kim, K. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041737 · Cited by 28

The Mechanisms and Animal Models of SARS-CoV-2 Infection

Jia, W., Wang, J., Sun, B., Zhou, J., Shi, Y., & Zhou, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.578825 · Cited by 27

Effect of clinical isolate or cleavage site mutations in the SARS-CoV-2 spike protein on protein stability, cleavage, and cell–cell fusion

Barrett, C. T., Neal, H. E., Edmonds, K. L., Moncman, C. L., Thompson, R., Branttie, J. M., Boggs, K. B., Wu, C., Leung, D. W., & Dutch, R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100902 · Cited by 28

Proteases and variants: context matters for SARS-CoV-2 entry assays

Stevens, C. S., Oguntuyo, K. Y., & Lee, B. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.07.004 · Cited by 28

Anti-SARS-CoV-1 and −2 nanobody engineering towards avidity-inspired therapeutics

Obeng, E. M., Dzuvor, C. K. O., & Danquah, M. K. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101350 · Cited by 27

SARS-CoV-2 Infection and Pancreatic β Cell Failure

Mine, K., Nagafuchi, S., Mori, H., Takahashi, H., & Anzai, K. (2021) · Biology · doi:10.3390/biology11010022 · Cited by 26

From Immunogen to COVID-19 vaccines: Prospects for the post-pandemic era

Miao, G., Chen, Z., Cao, H., Wu, W., Chu, X., Liu, H., Zhang, L., Zhu, H., Cai, H., Lu, X., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114208 · Cited by 27

Convergent Evolution Dynamics of SARS-CoV-2 and HIV Surface Envelope Glycoproteins Driven by Host Cell Surface Receptors and Lipid Rafts: Lessons for the Future

Fantini, J., Chahinian, H., & Yahi, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031923 · Cited by 26

Systematic Exploration of SARS-CoV-2 Adaptation to Vero E6, Vero E6/TMPRSS2, and Calu-3 Cells

Aiewsakun, P., Phumiphanjarphak, W., Ludowyke, N., Purwono, P. B., Manopwisedjaroen, S., Srisaowakarn, C., Ekronarongchai, S., Suksatu, A., Yuvaniyama, J., & Thitithanyanont, A. (2023) · Genome Biology and Evolution · doi:10.1093/gbe/evad035 · Cited by 26

The effects of amino acid substitution of spike protein and genomic recombination on the evolution of SARS-CoV-2

Fang, L., Xu, J., Zhao, Y., Fan, J., Shen, J., Liu, W., & Cao, G. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1228128 · Cited by 26

SARS-CoV-2 Production in a Scalable High Cell Density Bioreactor

Offersgaard, A., Hernandez, C. R. D., Pihl, A. F., Costa, R., Venkatesan, N., Lin, X., Pham, L. V., Feng, S., Fahnøe, U., Scheel, T. K. H., et al. (2021) · Vaccines · doi:10.3390/vaccines9070706 · Cited by 26

Microbial arginine deiminase: A multifaceted green catalyst in biomedical sciences

Kawatra, A., Dhankhar, R., & Gulati, P. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.12.015 · Cited by 26

Association of COVID-19 transmission with high levels of ambient pollutants: Initiation and impact of the inflammatory response on cardiopulmonary disease

Lai, A., Chang, M. L., O'Donnell, R. P., Zhou, C., Sumner, J. A., & Hsiai, T. K. (2021) · Science of The Total Environment · doi:10.1016/j.scitotenv.2021.146464 · Cited by 25

Attenuation of SARS-CoV-2 infection by losartan in human kidney organoids

Rahmani, W., Chung, H., Sinha, S., Bui-Marinos, M. P., Arora, R., Jaffer, A., Corcoran, J. A., Biernaskie, J., & Chun, J. (2022) · iScience · doi:10.1016/j.isci.2022.103818 · Cited by 25

Annexin-V positive extracellular vesicles level is increased in severe COVID-19 disease

Jacob, V., Lambour, A., Swinyard, B., Zerbib, Y., Diouf, M., Soudet, S., Brochot, É., Six, I., Maizel, J., Slama, M., et al. (2023) · Frontiers in Medicine · doi:10.3389/fmed.2023.1186122 · Cited by 25

Unveiling the structural spectrum of SARS-CoV-2 fusion by in situ cryo-ET

Akıl, C., Xu, J., Shen, J., & Zhang, P. (2025) · Nature Communications · doi:10.1038/s41467-025-60406-z · Cited by 25

Is Spironolactone the Preferred Renin–Angiotensin–Aldosterone Inhibitor for Protection Against COVID-19?

Wilcox, C. S., & Pitt, B. (2020) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000960 · Cited by 25

Targeting host cell proteases as a potential treatment strategy to limit the spread of SARS‐CoV‐2 in the respiratory tract

El‐Shimy, I. A., Mohamed, M. M. A., Hasan, S. S., & Hadi, M. A. (2020) · Pharmacology Research & Perspectives · doi:10.1002/prp2.698 · Cited by 25

The Furin-S2′ Site in Avian Coronavirus Plays a Key Role in Central Nervous System Damage Progression

Cheng, J., Zhao, Y., Hu, Y., Zhao, J., Xue, J., & Zhang, G. (2021) · Journal of Virology · doi:10.1128/jvi.02447-20 · Cited by 25

Key Considerations for the Development of Safe and Effective SARS‐CoV‐2 Subunit Vaccine: A Peptide‐Based Vaccine Alternative

Shalash, A. O., Hussein, W. M., Skwarczyński, M., & Tóth, I. (2021) · Advanced Science · doi:10.1002/advs.202100985 · Cited by 25

Hindrance of the Proteolytic Activity of Neutrophil-Derived Serine Proteases by Serine Protease Inhibitors as a Management of Cardiovascular Diseases and Chronic Inflammation

Burster, T., Mustafa, Z., Myrzakhmetova, D., Zhanapiya, A., & Zimecki, M. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.784003 · Cited by 29

Endothelial Dysfunction in SARS-CoV-2 Infection

Nappi, F., & Singh, S. (2022) · Biomedicines · doi:10.3390/biomedicines10030654 · Cited by 26

COVID-19 and One-Carbon Metabolism

Perła‐Kaján, J., & Jakubowski, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084181 · Cited by 26

SARS-CoV-2 Delta Spike Protein Enhances the Viral Fusogenicity and Inflammatory Cytokine Production

Ao, Z., Ouyang, M. J., Olukitibi, T. A., & Yao, X. (2021) · iScience · doi:10.1016/j.isci.2022.104759 · Cited by 27

FASN inhibitor TVB-3166 prevents S-acylation of the spike protein of human coronaviruses

Mekhail, K., Lee, M., Sugiyama, M. G., Astori, A., St‐Germain, J. R., Latreille, E., Khosraviani, N., Wei, K., Li, Z., Rini, J. M., et al. (2022) · Journal of Lipid Research · doi:10.1016/j.jlr.2022.100256 · Cited by 26

Exploring the pH dependence of the SARS‐CoV ‐2 complete fusion domain and the role of its unique structural features

Birtles, D., Oh, A. E., & Lee, J. (2022) · Protein Science · doi:10.1002/pro.4390 · Cited by 26

Cytokine Storm and Neuropathological Alterations in Patients with Neurological Manifestations of COVID-19

Tsagkaris, C., Bilal, M., Aktar, İ., Aboufandi, Y., Taş, A., Aborode, A. T., Suvvari, T. K., Ahmad, S., Shkodina, A. D., Phadke, R., et al. (2022) · Current Alzheimer Research · doi:10.2174/1567205019666220908084559 · Cited by 27

Molecular Epidemiology of SARS-CoV-2: The Dominant Role of Arginine in Mutations and Infectivity

Ridgway, H. F., Ntallis, C., Chasapis, C. T., Kelaidonis, K., Matsoukas, M., Plotas, P., Apostolopoulos, V., Moore, G. J., Tsiodras, S., Paraskevis, D. N., et al. (2023) · Viruses · doi:10.3390/v15020309 · Cited by 25

Lessons Learnt from COVID-19: Computational Strategies for Facing Present and Future Pandemics

Pavan, M., & Moro, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054401 · Cited by 25

Design and characterization of novel SARS-CoV-2 fusion inhibitors with N-terminally extended HR2 peptides

Hu, Y., Zhu, Y., Yu, Y., Liu, N., Ju, X., Ding, Q., & He, Y. (2023) · Antiviral Research · doi:10.1016/j.antiviral.2023.105571 · Cited by 25

Roles of host proteases in the entry of SARS-CoV-2

Zabiegala, A., Kim, Y., & Chang, K. (2023) · Animal Diseases · doi:10.1186/s44149-023-00075-x · Cited by 25

Neutralizing Monoclonal Anti-SARS-CoV-2 Antibodies Isolated from Immunized Rabbits Define Novel Vulnerable Spike-Protein Epitope

Makdasi, E., Levy, Y., Alcalay, R., Noy-Porat, T., Zahavy, E., Mechaly, A., Epstein, E., Peretz, E., Cohen, H., Bar‐On, L., et al. (2021) · Viruses · doi:10.3390/v13040566 · Cited by 25

ELV-N32 and RvD6 isomer decrease pro-inflammatory cytokines, senescence programming, ACE2 and SARS-CoV-2-spike protein RBD binding in injured cornea

Pham, T. L., He, J., Kakazu, A. H., Calandria, J. M., Do, K. V., Nshimiyimana, R., Lam, T. F., Petasis, N. A., Bazán, H. E. P., & Bazan, N. G. (2021) · Scientific Reports · doi:10.1038/s41598-021-92293-x · Cited by 25

Interaction of Severe Acute Respiratory Syndrome Coronavirus 2 and Diabetes

Shao, S., Yang, Q., Pan, R., Yu, X., & Chen, Y. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.731974 · Cited by 27

A single dose of recombinant VSV-ΔG-spike vaccine provides protection against SARS-CoV-2 challengePreprint

Yahalom-Ronen, Y., Tamir, H., Melamed, S., Politi, B., Shifman, O., Achdout, H., Vitner, E. B., Israeli, O., Milrot, E., Stein, D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.18.160655 · Cited by 25

Involvement of Spike Protein, Furin, and ACE2 in SARS-CoV-2-Related Cardiovascular Complications

Ming, Y., & Qiang, L. (2020) · SN Comprehensive Clinical Medicine · doi:10.1007/s42399-020-00400-2 · Cited by 24

The Challenges of Vaccine Development against Betacoronaviruses: Antibody Dependent Enhancement and Sendai Virus as a Possible Vaccine Vector

Zaichuk, T. A., Nechipurenko, Y. D., Adzhubey, A. A., Оникиенко, С. Б., Черешнев, В. А., Zainutdinov, S. S., Kochneva, G. V., Sv, N., & Matveeva, O. V. (2020) · Molecular Biology · doi:10.1134/s0026893320060151 · Cited by 25

Importation of SARS‐CoV‐2 Variant B.1.1.7 in Pakistan

Umair, M., Ikram, A., Salman, M., Alam, M. M., Badar, N., Rehman, Z., Tamim, S., Khurshid, A., Ahad, A., Ahmad, H., et al. (2021) · Journal of Medical Virology · doi:10.1002/jmv.26869 · Cited by 24

What makes (hydroxy)chloroquine ineffective against COVID-19: insights from cell biology

Altulea, D., Maassen, S., Baranov, M. V., & van den Bogaart, G. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab016 · Cited by 24

SARS-CoV-2—Morphology, Transmission and Diagnosis during Pandemic, Review with Element of Meta-Analysis

Grudlewska‐Buda, K., Wiktorczyk-Kapischke, N., Wałecka-Zacharska, E., Kwiecińska-Piróg, J., Buszko, K., Leis, K., Juszczuk, K., Gospodarek-Komkowska, E., & Skowron, K. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10091962 · Cited by 27

Elevated Neopterin Levels Predict Fatal Outcome in SARS-CoV-2-Infected Patients

Chauvin, M., Larsen, M., Quirant‐Sánchez, B., Quentric, P., Dorgham, K., Royer, L., Vallet, H., Guihot, A., Combadière, B., Combadière, C., et al. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.709893 · Cited by 24

Going viral in the islet: mediators of SARS-CoV-2 entry beyond ACE2

Rangu, R., Wander, P. L., Barrow, B. M., & Zraika, S. (2022) · Journal of Molecular Endocrinology · doi:10.1530/jme-21-0282 · Cited by 26

SARS-CoV-2 infects human cardiomyocytes promoted by inflammation and oxidative stress

Tangos, M., Budde, H., Kolijn, D., Sieme, M., Zhazykbayeva, S., Lódi, M., Herwig, M., Gömöri, K., Hassoun, R., Robinson, E. L., et al. (2022) · International Journal of Cardiology · doi:10.1016/j.ijcard.2022.05.055 · Cited by 26

The diverse role of heparan sulfate and other GAGs in SARS-CoV-2 infections and therapeutics

Eilts, F., Bauer, S., Fraser, K., Dordick, J. S., Wolff, M. W., Linhardt, R. J., & Zhang, F. (2022) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2022.120167 · Cited by 24

Targeting SARS-CoV-2 and host cell receptor interactions

Lim, S. P. (2022) · Antiviral Research · doi:10.1016/j.antiviral.2022.105514 · Cited by 25

Molecular Dynamics Reveals Complex Compensatory Effects of Ionic Strength on the Severe Acute Respiratory Syndrome Coronavirus 2 Spike/Human Angiotensin-Converting Enzyme 2 Interaction

de Souza, A. S., Rivera, J. D., Almeida, V. M., Ge, P., de Souza, R. F., Farah, C. S., Ulrich, H., Marana, S. R., Salinas, R. K., & Guzzo, C. R. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c02602 · Cited by 24

Obesity-Related Inflammation and Endothelial Dysfunction in COVID-19: Impact on Disease Severity

Lorenzo, A. D., Estato, V., Castro-Faria-Neto, H. C., & Tibiriçá, E. V. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s282710 · Cited by 24

A potent synthetic nanobody targets RBD and protects mice from SARS-CoV-2 infectionPreprint

Li, T., Cai, H., Yao, H., Zhou, B., Zhang, N., Gong, Y., Zhao, Y., Shen, Q., Qin, W., Hutter, C. A. J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.09.143438 · Cited by 26

Peptide Antidotes to SARS-CoV-2 (COVID-19)Preprint

Watson, A., Ferreira, L. M. R., Hwang, P. K., Xu, J., & Stroud, R. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.06.238915 · Cited by 24

Phenotypic evolution of SARS-CoV-2 spike during the COVID-19 pandemic

Furnon, W., Cowton, V. M., Lorenzo, G. D., Orton, R. J., Herder, V., Cantoni, D. M., Ilia, G., Mendonça, D. C., Kerr, K., Allan, J., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-024-01878-5 · Cited by 23

Receptors and host factors: key players in human metapneumovirus infection

Dong, Y., Xie, Z., & Xu, L. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1557880 · Cited by 23

A perspective on potential target proteins of COVID-19: Comparison with SARS-CoV for designing new small molecules

Kumar, D., Chauhan, G., Kalra, S., Kumar, B., & Gill, M. S. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104326 · Cited by 23

Is There a Link between Bisphenol A (BPA), a Key Endocrine Disruptor, and the Risk for SARS-CoV-2 Infection and Severe COVID-19?

Zahra, A., Sisu, C., Silva, E. A., Greca, S.-C. D. A., Randeva, H. S., Chatha, K. K., Kyrou, I., & Karteris, E. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9103296 · Cited by 23

The PRRA Insert at the S1/S2 Site Modulates Cellular Tropism of SARS-CoV-2 and ACE2 Usage by the Closely Related Bat RaTG13

Liu, S., Selvaraj, P., Lien, C. Z., Nuñez, I. A., Wu, W. W., Chou, C., & Wang, T. T. (2021) · Journal of Virology · doi:10.1128/jvi.01751-20 · Cited by 24

Dysregulation of the Renin-Angiotensin-Aldosterone System (RAA) in Patients Infected with SARS-CoV-2-Possible Clinical Consequences

Dettlaff‐Pokora, A., & Świerczyński, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094503 · Cited by 23

Looking for pathways related to COVID-19: confirmation of pathogenic mechanisms by SARS-CoV-2–host interactome

Messina, F., Giombini, E., Montaldo, C., Sharma, A., Piacentini, M., Zoccoli, A., Sékaly, R., Locatelli, F., Zumla, A. I., Maeurer, M. J., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03881-8 · Cited by 23

Molecular Mechanisms of the Medicines for COVID-19

Komiyama, M. (2022) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20220179 · Cited by 23

Receptors and Cofactors That Contribute to SARS-CoV-2 Entry: Can Skin Be an Alternative Route of Entry?

Barthe, M., Hertereau, L., Lamghari, N., Osman‐Ponchet, H., & Braud, V. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076253 · Cited by 28

An ACAT inhibitor suppresses SARS-CoV-2 replication and boosts antiviral T cell activity

Wing, P. A. C., Schmidt, N. M., Peters, R., Erdmann, M., Brown, R. L., Wang, H., Swadling, L., COVIDsortium Investigators, Newman, J., Thakur, N., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011323 · Cited by 23

Microfluidic Organ-Chips and Stem Cell Models in the Fight Against COVID-19

Satta, S., Rockwood, S. J., Wang, K., Wang, S., Mozneb, M., Arzt, M., Hsiai, T. K., & Sharma, A. (2023) · Circulation Research · doi:10.1161/circresaha.122.321877 · Cited by 23

SARS-CoV-2 and the DNA damage response

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Development of SARS-CoV-2 entry antivirals

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