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

Genomics-guided identification of potential modulators of SARS-CoV-2 entry proteases, TMPRSS2 and Cathepsins B/L

Prasad, K., Alomar, S. Y., Almuqri, E. A., Rudayni, H. A., & Kumar, V. (2021) · PLoS ONE · doi:10.1371/journal.pone.0256141 · Cited by 17

Smoking Is Correlated With the Prognosis of Coronavirus Disease 2019 (COVID-19) Patients: An Observational Study

Peng, F., Lei, S., Zhang, Q., Zhong, Y., & Wu, S. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.634842 · Cited by 18

Role of Serine Proteases and Host Cell Receptors Involved in Proteolytic Activation, Entry of SARS-CoV-2 and Its Current Therapeutic Options

Dessie, G., & Malik, T. (2021) · Infection and Drug Resistance · doi:10.2147/idr.s308176 · Cited by 18

Progression and Trends in Virus from Influenza A to COVID-19: An Overview of Recent Studies

Daemi, H. B., Kulyar, M. F., He, X., Li, C., Karimpour, M., Sun, X., Zou, Z., & Jin, M. (2021) · Viruses · doi:10.3390/v13061145 · Cited by 17

Understanding the role of nACE2 in neurogenic hypertension among COVID-19 patients

Kulkarni, P. G., Sakharkar, A. J., & Banerjee, T. (2021) · Hypertension Research · doi:10.1038/s41440-021-00800-4 · Cited by 17

Discovery of diminazene as a dual inhibitor of SARS-CoV-2 human host proteases TMPRSS2 and furin using cell-based assays

Xu, Y.-M., Inácio, M. C., Liu, M. X., & Gunatilaka, A. A. L. (2022) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2022.100023 · Cited by 17

Pathogenicity of SARS‐CoV‐2 Omicron

Chu, H., & Yuen, K. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.880 · Cited by 17

VE607 stabilizes SARS-CoV-2 Spike in the “RBD-up” conformation and inhibits viral entry

Ding, S., Ullah, I., Gong, S. Y., Grover, J. R., Mohammadi, M., Chen, Y., Vézina, D., Beaudoin-Bussières, G., Verma, V. T., Goyette, G., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104528 · Cited by 18

A zebrafish model for COVID-19 recapitulates olfactory and cardiovascular pathophysiologies caused by SARS-CoV-2Preprint

Kraus, A., Casadei, E., Huertas, M., Ye, C., Bradfute, S. B., Boudinot, P., Levraud, J., & Salinas, I. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.06.368191 · Cited by 17

Review of the mechanisms of SARS-CoV-2 evolution and transmissionPreprint

Chen, J., Wang, R., & Wei, G. (2021) · PubMed · doi:10.48550/arxiv.2109.08148 · Cited by 17

S:D614G and S:H655Y are Gateway Mutations that Act Epistatically to Promote SARS-CoV-2 Variant FitnessPreprint

Yurkovetskiy, L., Egri, S. B., Kurhade, C., Díaz-Salinas, M. A., Jaimes, J. A., Nyalile, T., Xie, X., Choudhary, M. C., Dauphin, A., Li, J. Z., et al. (2023) · SSRN Electronic Journal · doi:10.1101/2023.03.30.535005 · Cited by 18

Understanding Severe Acute Respiratory Syndrome Coronavirus 2 Replication to Design Efficient Drug Combination Therapies

Ortega, J. T., Zambrano, J. L., Jastrzębska, B., Liprandi, F., Rangel, H. R., & Pujol, F. H. (2020) · Intervirology · doi:10.1159/000512141 · Cited by 16

Role of Q675H Mutation in Improving SARS-CoV-2 Spike Interaction with the Furin Binding Pocket

Bertelli, A., D’Ursi, P., Campisi, G., Messali, S., Milanesi, M., Giovanetti, M., Ciccozzi, M., Caccuri, F., & Caruso, A. (2021) · Viruses · doi:10.3390/v13122511 · Cited by 16

There is nothing exempt from the peril of mutation – The Omicron spike

Behl, T., Kaur, I., Sehgal, A., Singh, S., Sharma, N., Anwer, M. K., Makeen, H. A., Albratty, M., Alhazmi, H. A., Bhatia, S., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112756 · Cited by 16

Multiple SARS-CoV-2 Variants Exhibit Variable Target Cell Infectivity and Ability to Evade Antibody Neutralization

Tang, H., Gao, L., Wu, Z., Meng, F., Zhao, X., Shao, Y., Hou, G., Du, X., & Qin, F. X.-F. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.836232 · Cited by 16

In Silico and In Vitro Studies of Alchemilla viridiflora Rothm—Polyphenols’ Potential for Inhibition of SARS-CoV-2 Internalization

Suručić, R. V., Radović, J., Kundaković, T., Lazović, B., Travar, M., Suručić, L. T., & Škrbić, R. (2022) · Molecules · doi:10.3390/molecules27165174 · Cited by 17

SARS-COV-2/COVID-19: scenario, epidemiology, adaptive mutations, and environmental factors

Asghar, A., Imran, H. M., Bano, N., Maalik, S., Mushtaq, S., Hussain, A., Varjani, S., Aleya, L., Iqbal, H. M. N., & Bilal, M. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-022-22333-0 · Cited by 16

Silver nanoparticles with excellent biocompatibility block pseudotyped SARS-CoV-2 in the presence of lung surfactant

Gupta, G. S., Hamawandi, B., Sheward, D. J., Murrell, B., Hanke, L., McInerney, G. M., Blosi, M., Costa, A. L., Toprak, M. S., & Fadeel, B. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1083232 · Cited by 17

SKI-1/S1P Facilitates SARS-CoV-2 Spike Induced Cell-to-Cell Fusion via Activation of SREBP-2 and Metalloproteases, Whereas PCSK9 Enhances the Degradation of ACE2

Essalmani, R., Andréo, U., Evagelidis, A., Dévéhat, M. L., Ramos, O. H. P., Fruchart‐Gaillard, C., Susan‐Resiga, D., Cohen, É. A., & Seidah, N. G. (2023) · Viruses · doi:10.3390/v15020360 · Cited by 17

The role of influenza-A virus and coronavirus viral glycoprotein cleavage in host adaptation

Heindl, M. R., & Böttcher‐Friebertshäuser, E. (2023) · Current Opinion in Virology · doi:10.1016/j.coviro.2023.101303 · Cited by 16

Molecular mechanisms of human coronavirus NL63 infection and replication

Castillo, G., Mora-Díaz, J. C., Breuer, M., Singh, P., Nelli, R. K., & Gimenez-Lirola, L. G. (2023) · Virus Research · doi:10.1016/j.virusres.2023.199078 · Cited by 18

Omicsynin B4 potently blocks coronavirus infection by inhibiting host proteases cathepsin L and TMPRSS2

Li, Y., Wang, K., Sun, H., Wu, S., Wang, H., Shi, Y., Li, X., Yan, H., Yang, G. H., Wu, M., et al. (2023) · Antiviral Research · doi:10.1016/j.antiviral.2023.105606 · Cited by 18

The impact of S2 mutations on Omicron SARS-CoV-2 cell surface expression and fusogenicity

Escalera, A., Laporte, M., Turner, S., Karakus, U., Gonzalez-Reiche, A. S., van de Guchte, A., Farrugia, K., Khalil, Z., van Bakel, H., Smith, D. J., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2297553 · Cited by 16

Neutrophil proteases are protective against SARS-CoV-2 by degrading the spike protein and dampening virus-mediated inflammation

Leborgne, N. G. F., Devisme, C., Kozarac, N., Veiga, I. B., Ebert, N., Godel, A., Grau‐Roma, L., Scherer, M., Plattet, P., Thiel, V., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.174133 · Cited by 17

Targeting ATP2B1 impairs PI3K/Akt/FOXO signaling and reduces SARS-COV-2 infection and replication

Antonellis, P. D., Ferrucci, V., Miceli, M., Bibbò, F., Asadzadeh, F., Gorini, F., Mattivi, A., Boccia, A. S., Russo, R., Andolfo, I., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00164-z · Cited by 16

Smoking and vaping alter genes related to mechanisms of SARS-CoV-2 susceptibility and severity: a systematic review and meta-analysis

Bowsher, R., Marczylo, T. H., Gooch, K. E., Bailey, A., Wright, M., & Marczylo, E. L. (2024) · European Respiratory Journal · doi:10.1183/13993003.00133-2024 · Cited by 16

Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants

Ke, Z., Peacock, T. P., Brown, J. C., Sheppard, C., Croll, T. I., Kotecha, A., Goldhill, D. H., Barclay, W., & Briggs, J. A. G. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00303-1 · Cited by 16

Analysis of Structures of SARS-CoV-2 Papain-like Protease Bound with Ligands Unveils Structural Features for Inhibiting the Enzyme

Varghese, A., Liu, J., Liu, B., Guo, W., Dong, F., Patterson, T. A., & Hong, H. (2025) · Molecules · doi:10.3390/molecules30030491 · Cited by 16

Comparative host–pathogen protein–protein interaction analysis of recent coronavirus outbreaks and important host targets identification

Khan, A. A., & Khan, Z. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbaa207 · Cited by 16

Interfering with Host Proteases in SARS-CoV-2 Entry as a Promising Therapeutic Strategy

Müller, P., Maus, H., Hammerschmidt, S. J., Knaff, P. M., Mailänder, V., Schirmeister, T., & Kersten, C. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210526111318 · Cited by 17

Evolutionary insights into the furin cleavage sites of SARS-CoV-2 variants from humans and animals

Nagy, A., Basiouni, S., Parvin, R., Hafez, H. M., & Shehata, A. A. (2021) · Archives of Virology · doi:10.1007/s00705-021-05166-z · Cited by 16

Know your enemy and know yourself – the case of SARS-CoV-2 host factors

Lee, W. S., Yousefi, M., Yan, B., Yong, C. L., & Ooi, Y. S. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.08.007 · Cited by 16

Kallikreins emerge as new regulators of viral infections

Pampalakis, G., Zingkou, E., Panagiotidis, C. Α., & Sotiropoulou, G. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03922-7 · Cited by 16

A vesicular stomatitis virus-based prime-boost vaccination strategy induces potent and protective neutralizing antibodies against SARS-CoV-2

Kim, G. N., Choi, J.-A., Wu, K., Saeedian, N., Yang, E., Park, H., Woo, S., Lim, G., Kim, S.-G., Eo, S.-K., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010092 · Cited by 17

Molecular Simulations suggest Vitamins, Retinoids and Steroids as Ligands of the Free Fatty Acid Pocket of the SARS‐CoV‐2 Spike Protein**

Shoemark, D. K., Colenso, C. K., Toelzer, C., Gupta, K., Sessions, R. B., Davidson, A. D., Berger, I., Schaffitzel, C., SPENCER, J. M., & Mulholland, A. J. (2021) · Angewandte Chemie · doi:10.1002/ange.202015639 · Cited by 16

The Increased Amyloidogenicity of Spike RBD and pH-Dependent Binding to ACE2 May Contribute to the Transmissibility and Pathogenic Properties of SARS-CoV-2 Omicron as Suggested by In Silico Study

Aksenova, A. Y., Likhachev, I. V., Grishin, S. Y., & Galzitskaya, O. V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113502 · Cited by 16

Cryo-EM reveals binding of linoleic acid to SARS-CoV-2 spike glycoprotein, suggesting an antiviral treatment strategy

Toelzer, C., Gupta, K., Berger, I., & Schaffitzel, C. (2023) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798323000049 · Cited by 16

Chemical Evolution of Rhinovirus Identifies Capsid-Destabilizing Mutations Driving Low-pH-Independent Genome Uncoating

Murer, L., Petkidis, A., Vallet, T., Vignuzzi, M., & Greber, U. F. (2021) · Journal of Virology · doi:10.1128/jvi.01060-21 · Cited by 17

SARS-CoV-2 and SARS-CoV spike-mediated cell-cell fusion differ in the requirements for receptor expression and proteolytic activationPreprint

Hörnich, B. F., Großkopf, A. K., Schlagowski, S., Tenbusch, M., Kleine‐Weber, H., Neipel, F., Stahl-Hennig, C., & Hahn, A. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.25.221135 · Cited by 16

Structural proteins of human coronaviruses: what makes them different?

Minigulov, N., Boranbayev, K., Bekbossynova, A., Gadilgereyeva, B., & Filchakova, O. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1458383 · Cited by 18

ACE2 expression is related to the interferon response in airway epithelial cells but is that functional for SARS-CoV-2 entry?

Scagnolari, C., Bitossi, C., Viscido, A., Frasca, F., Oliveto, G., Scordio, M., Petrarca, L., Mancino, E., Nenna, R., Riva, E., et al. (2021) · Cytokine · doi:10.1016/j.cyto.2021.155430 · Cited by 15

Natural products provide a new perspective for anti-complement treatment of severe COVID-19: a review

Fan, Y., Wang, Y., Yu, S., Chang, J. B. P., Yan, Y., Wang, Y., & Bian, Y. (2021) · Chinese Medicine · doi:10.1186/s13020-021-00478-3 · Cited by 15

Mind the feline coronavirus: Comparison with SARS-CoV-2

Gao, Y.-Y., Liang, X.-Y., Wang, Q., Zhang, S., Zhao, H., Wang, K., Hu, G., Liu, W. J., & Feng-shan, G. (2022) · Gene · doi:10.1016/j.gene.2022.146443 · Cited by 15

Heterogeneous expression of ACE2, TMPRSS2, and FURIN at single-cell resolution in advanced non-small cell lung cancer

Liu, Z., Xiaohua, G., Li, Z., Shan, S., Wu, F., & Ren, T. (2022) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-022-04253-1 · Cited by 15

Druggable targets and therapeutic development for COVID-19

Duan, X., Lacko, L. A., & Chen, S. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.963701 · Cited by 15

An Experimental Framework for Developing Point-of-Need Biosensors: Connecting Bio-Layer Interferometry and Electrochemical Impedance Spectroscopy

Ullah, S. F., Moreira, G. A. M., Datta, S., McLamore, E. S., & Vanegas, D. C. (2022) · Biosensors · doi:10.3390/bios12110938 · Cited by 15

Differences in syncytia formation by SARS-CoV-2 variants modify host chromatin accessibility and cellular senescence via TP53

Lee, J. D., Menasché, B. L., Mavrikaki, M., Uyemura, M. M., Hong, S. M., Kozlova, N. V., Wei, J., Alfajaro, M. M., Filler, R. B., Müller, A. M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113478 · Cited by 17

Overview of the SARS-CoV-2 nucleocapsid protein

Eltayeb, A., Al-Sarraj, F. M., Alharbi, M. G., Albiheyri, R. S., Mattar, E. H., Zeid, I. M. A., Bouback, T. A., Bamagoos, A. A., Johny, B. O. A., Uversky, V. N., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129523 · Cited by 16

Nanobody engineering for SARS-CoV-2 neutralization and detection

Hannula, L., Kuivanen, S. H., Lasham, J., Kant, R., Kareinen, L., Bogacheva, M. S., Strandin, T. M., Sironen, T. A., Hepojoki, J., Sharma, V., et al. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.04199-22 · Cited by 15

Progress in SARS-CoV-2, diagnostic and clinical treatment of COVID-19

Li, Y., Lu, S.-M., Wang, J.-L., Yao, H., & Liang, L. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e33179 · Cited by 15

The virus that shook the world: questions and answers about SARS-CoV-2 and COVID-19

Alexandrova, R., Beykov, P., Vassilev, D. I., Jukič, M., & Podlipnik, Č. (2020) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2020.1847683 · Cited by 16

Potential Simultaneous Inhibitors of Angiotensin-Converting Enzyme 2 and Transmembrane Protease, Serine 2

Wu, C., Lin, Y., Yang, Y., Shu, L., Cheng, Y.-C., & Liu, H. T. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.584158 · Cited by 15

Micronutrients and phytochemicals against COVID-19: Mechanism and molecular targets

Bellik, Y., Bachir‐bey, M., Fatmi, W., Kouidri, M., Souagui, Y., & Selles, S. M. A. (2020) · Annals of Phytomedicine An International Journal · doi:10.21276/ap.2020.9.2.3 · Cited by 15

Association between circulating furin levels, obesity and pro‐inflammatory markers in children

Swärd, P., Rosengren, B. E., Jehpsson, L., & Karlsson, M. K. (2021) · Acta Paediatrica · doi:10.1111/apa.15774 · Cited by 15

Host proviral and antiviral factors for SARS-CoV-2

Lv, L., & Zhang, L. (2021) · Virus Genes · doi:10.1007/s11262-021-01869-2 · Cited by 16

Prediction of the Effects of Variants and Differential Expression of Key Host Genes ACE2 , TMPRSS2 , and FURIN in SARS-CoV-2 Pathogenesis: An In Silico Approach

Hossain, M. S., Tonmoy, M. I. Q., Fariha, A., Islam, M. S., Roy, A. S., Islam, M. N., Kar, K., Alam, M. R., & Rahaman, M. M. (2021) · Bioinformatics and Biology Insights · doi:10.1177/11779322211054684 · Cited by 15

Supporting Cells of the Human Olfactory Epithelium Co-Express the Lipid Scramblase TMEM16F and ACE2 and May Cause Smell Loss by SARS-CoV-2 Spike-Induced Syncytia

Hernandez, A., Gonzalez‐Velandia, K. Y., Rangaswamy, U., Guarneri, G., Boscolo‐Rizzo, P., Tofanelli, M., Gardenal, N., Sanges, R., Dibattista, M., Tirelli, G., et al. (2022) · Cellular Physiology and Biochemistry · doi:10.33594/000000531 · Cited by 17

The spike glycoprotein of highly pathogenic human coronaviruses: structural insights for understanding infection, evolution and inhibition

Qiao, S., Zhang, S., Ge, J., & Wang, X. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13454 · Cited by 16

SARS-CoV-2 infects an in vitro model of the human developing pancreas through endocytosis

Szlachcic, W. J., Dąbrowska, A., Milewska, A., Ziojla, N., Błaszczyk, K., Barreto-Durán, E., Sanak, M., Surmiak, M., Owczarek, K., Grzanka, D., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104594 · Cited by 16

Development of a Biosensor Based on Angiotensin‐Converting Enzyme II for Severe Acute Respiratory Syndrome Coronavirus 2 Detection in Human Saliva

Moreira, G. A. M., Casso-Hartmann, L., Datta, S., Dean, D. M. D., McLamore, E. S., & Vanegas, D. C. (2022) · Frontiers in Sensors · doi:10.3389/fsens.2022.917380 · Cited by 15

Human interaction targets of SARS-CoV-2 spike protein: A systematic review

Faraji, S. N., Raee, M. J., Hashemi, S. M. A., Daryabor, G., Tabrizi, R., Dashti, F. S., Behboudi, E., Heidarnejad, K., Nowrouzi‐Sohrabi, P., & Hatam, G. (2022) · European Journal of Inflammation · doi:10.1177/1721727x221095382 · Cited by 16

Host Cell Proteases Mediating SARS-CoV-2 Entry: An Overview

Oubahmane, M., Hdoufane, I., Bjij, I., Lahcen, N. A., Villemin, D., Daoud, R., Allali, A. E., & Cherqaoui, D. (2022) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026622666220726122339 · Cited by 15

The field of protein function prediction as viewed by different domain scientists

Ramola, R., Friedberg, I., & Predrag Radivojac, A. (2022) · Bioinformatics Advances · doi:10.1093/bioadv/vbac057 · Cited by 15

Targeted screening of genetic associations with COVID-19 susceptibility and severity

Li, P., Ke, Y., Shen, W., Shi, S., Wang, Y., Lin, K., Guo, X., Wang, C., Zhang, Y., & Zhao, Z. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1073880 · Cited by 15

SARS-CoV-2 infection induces persistent adipose tissue damage in aged golden Syrian hamsters

Bogard, G., Barthelemy, J., Hantute-Ghesquier, A., Sencio, V., Rodrigues, P. B., Séron, K., Robil, C., Flourens, A., Pinet, F., Eberlé, D., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05574-w · Cited by 16

A non-transmissible live attenuated SARS-CoV-2 vaccine

Adler, J. M., Vidal, R. M., Voß, A., Kunder, S., Nascimento, M., Abdelgawad, A., Langner, C., Vladimirova, D., Osterrieder, N., Gruber, A. D., et al. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2023.05.004 · Cited by 16

Antibody-mediated spike activation promotes cell-cell transmission of SARS-CoV-2

Yu, S., Zheng, X., Zhou, Y. R., Gao, Y., Zhou, B., Zhao, Y., Li, T., Li, Y., Mou, J., Cui, X., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011789 · Cited by 15

Screening for inhibitory effects of crude drugs on furin-like enzymatic activities

Kiba, Y., Oyama, R., Misawa, S., Tanikawa, T., Kitamura, M., & Suzuki, R. (2021) · Journal of Natural Medicines · doi:10.1007/s11418-021-01519-9 · Cited by 15

In vitro characterization of the furin inhibitor MI-1851: Albumin binding, interaction with cytochrome P450 enzymes and cytotoxicity

Pászti-Gere, E., Szentkirályi-Tóth, A., Szabó, P. T., Steinmetzer, T., Fliszár-Nyúl, E., & Poór, M. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113124 · Cited by 16

SARS-CoV-2 infection studies in lung organoids identify TSPAN8 as novel mediatorPreprint

Hysenaj, L., Little, S., Kulhanek, K. R., Gbenedio, O. M., Rodriguez, L., Shen, A. S., Lone, J., Lupin-Jimenez, L. C., Bonser, L. R., Serwas, N. K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.01.446640 · Cited by 15

SARS-CoV-2 variants of concern have acquired mutations associated with an increased spike cleavagePreprint

Escalera, A., Gonzalez-Reiche, A. S., Aslam, S., Mena, I., Pearl, R. L., Laporte, M., Fossati, A., Rathnasinghe, R., Alshammary, H., van de Guchte, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.05.455290 · Cited by 15

Identification of Atovaquone, Ouabain and Mebendazole as FDA Approved Drugs Tar-geting SARS-CoV-2 (Version 4)Preprint

Farag, A., Wang, P., Boys, I. N., Eitson, J. L., Ohlson, M. B., Fan, W., McDougal, M. B., Ahmed, M., Schoggins, J. W., & Sadek, H. A. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12003930 · Cited by 15

MCMV-based vaccine vectors expressing full-length viral proteins provide long-term humoral immune protection upon a single-shot vaccination

Kim, Y., Zheng, X., Eschke, K., Chaudhry, M. Z., Bertoglio, F., Tomić, A., Krmpotić, A., Hoffmann, M., Bar-On, Y., Boehme, J., et al. (2022) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00814-5 · Cited by 14

The Importance of Glycosylation in COVID-19 Infection

Pribić, T., Lauc, G., & Trbojević‐Akmačić, I. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-70115-4_12 · Cited by 15

Characterization of SARS-CoV-2 Variants N501Y.V1 and N501Y.V2 Spike on Viral Infectivity

Tang, H., Gao, L., Wu, Z., Meng, F., Zhao, X., Shao, Y., Shi, X., Qiao, S., An, J., Du, X., et al. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.720357 · Cited by 15

FDA approved drugs with antiviral activity against SARS-CoV-2: From structure-based repurposing to host-specific mechanisms

Ahmed, M. S., Farag, A., Boys, I. N., Wang, P., Menendez-Montes, I., Nguyen, N. U. N., Eitson, J. L., Ohlson, M. B., Fan, W., McDougal, M. B., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114614 · Cited by 14

Single-molecule FRET for virology: 20 years of insight into protein structure and dynamics

Groves, D. C., Hepp, C., Kapanidis, A. N., & Robb, N. C. (2023) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583523000021 · Cited by 15

Antiviral effect and safety of nafamostat mesilate in patients with mild early-onset COVID-19: An exploratory multicentre randomized controlled clinical trial

Okugawa, S., Ikeda, M., Kashiwabara, K., Moritoyo, T., Kohsaka, T., Shimizu, T., Hagiya, H., Hasegawa, K., Otsuka, F., Miwa, A., et al. (2023) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2023.106922 · Cited by 14

Variations in O-Glycosylation Patterns Influence Viral Pathogenicity, Infectivity, and Transmissibility in SARS-CoV-2 Variants

Onigbinde, S. B., Reyes, C. D. G., Fowowe, M., Daramola, O. E., Atashi, M., Bennett, A. I., & Mechref, Y. S. (2023) · Biomolecules · doi:10.3390/biom13101467 · Cited by 14

Mechanisms of SARS-CoV-2 Inactivation Using UVC Laser Radiation

Devitt, G., Johnson, P., Hanrahan, N., Lane, S. I. R., Vidalle, M. C., Sheth, B., Allen, J. D., Humbert, M. V., Spalluto, C. M., Hervé, R., et al. (2023) · ACS Photonics · doi:10.1021/acsphotonics.3c00828 · Cited by 14

Natural products as a source of Coronavirus entry inhibitors

Szabó, D., Crowe, A. P., Mamotte, C. D. S., & Strappe, P. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1353971 · Cited by 14

Nanomolar anti-SARS-CoV-2 Omicron activity of the host-directed TMPRSS2 inhibitor N-0385 and synergistic action with direct-acting antivirals

Pérez‐Vargas, J., Lemieux, G., Thompson, C. A. H., Désilets, A., Ennis, S., Gao, G., Gordon, D. G., Schulz, A. L., Niikura, M., Nabi, I. R., et al. (2024) · Antiviral Research · doi:10.1016/j.antiviral.2024.105869 · Cited by 14

Establishment of replication-competent vesicular stomatitis virus recapitulating SADS-CoV entry

Zhu, Z., Han, Y., Gong, M., Sun, B., Zhang, R., & Ding, Q. (2024) · Journal of Virology · doi:10.1128/jvi.01957-23 · Cited by 14

Subsequent Waves of Convergent Evolution in SARS-CoV-2 Genes and Proteins

Focosi, D., Spezia, P. G., & Maggi, F. (2024) · Vaccines · doi:10.3390/vaccines12080887 · Cited by 14

SARS-CoV-2 spike fusion peptide trans interaction with phosphatidylserine lipid triggers membrane fusion for viral entry

Singh, P., Pahari, P., Mukherjee, S., Karmakar, S., Hoffmann, M., Mandal, T., & Das, D. K. (2024) · mBio · doi:10.1128/mbio.01077-24 · Cited by 17

Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy

Zhang, Q., Rosa, R. S. L., Ray, A., Durlet, K., Dorrazehi, G. M., Bernardi, R. C., & Alsteens, D. (2025) · Nature Communications · doi:10.1038/s41467-024-55358-9 · Cited by 14

Does COVID-19 Vaccination Warrant the Classical Principle “ofelein i mi vlaptin”?

Doulberis, M., Papaefthymiou, A., Kotronis, G., Gialamprinou, D., Soteriades, E. S., Kyriakopoulos, A. M., Chatzimichael, E., Kafafyllidou, K., Liatsos, C. N., Chatzistefanou, I., et al. (2021) · Medicina · doi:10.3390/medicina57030253 · Cited by 14

Profiling COVID-19 Genetic Research: A Data-Driven Study Utilizing Intelligent Bibliometrics

Wu, M., Zhang, Y., Grosser, M., Tipper, S., Venter, D. J., Lin, H., & Jie Lu, B. (2021) · Frontiers in Research Metrics and Analytics · doi:10.3389/frma.2021.683212 · Cited by 14

Network-Based Identification and Experimental Validation of Drug Candidates Toward SARS-CoV-2 via Targeting Virus–Host Interactome

Fang, J., Wu, Q., Ye, F., Cai, C., Xu, L., Gu, Y., Wang, Q., Liu, A., Tan, W., & Du, G. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.728960 · Cited by 14

Therapeutically effective covalent spike protein inhibitors in treatment of SARS-CoV-2

Choudhary, V., Gupta, A., Sharma, R., & Parmar, H. S. (2021) · Journal of Proteins and Proteomics · doi:10.1007/s42485-021-00074-x · Cited by 15

Microsecond simulations and CD spectroscopy reveals the intrinsically disordered nature of SARS-CoV-2 spike-C-terminal cytoplasmic tail (residues 1242–1273) in isolation

Kumar, P., Bhardwaj, T., Garg, N., & Giri, R. (2021) · Virology · doi:10.1016/j.virol.2021.11.005 · Cited by 14

Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein

Arora, P., Sidarovich, A., Graichen, L., Hörnich, B. F., Hahn, A. S., Hoffmann, M., & Pöhlmann, S. (2022) · PLoS ONE · doi:10.1371/journal.pone.0265453 · Cited by 14

Investigations on SARS-CoV-2 Susceptibility of Domestic and Wild Animals Using Primary Cell Culture Models Derived from the Upper and Lower Respiratory Tract

Färber, I., Krüger, J., Rocha, C., Armando, F., von Köckritz‐Blickwede, M., Pöhlmann, S., Braun, A. C., Baumgärtner, W., Runft, S., & Krüger, N. (2022) · Viruses · doi:10.3390/v14040828 · Cited by 14

The consequences of viral infection on host DNA damage response: a focus on SARS-CoVs

Mekawy, A. S., Alaswad, Z., Ibrahim, A. A., Mohamed, A. A., AlOkda, A., & Elserafy, M. (2022) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-022-00388-3 · Cited by 15

Comprehensive overview of COVID-19-related respiratory failure: focus on cellular interactions

Rarani, F. Z., Rarani, M. Z., Hamblin, M. R., Rashidi, B., Hashemian, S. M. R., & Mirzaei, H. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00363-3 · Cited by 15

Implications of the novel mutations in the SARS-CoV-2 genome for transmission, disease severity and the vaccine development

Akkız, H. (2021) · Journal of Translational Science · doi:10.15761/jts.1000424 · Cited by 14

Reactive Centre Loop Mutagenesis of SerpinB3 to Target TMPRSS2 and Furin: Inhibition of SARS-CoV-2 Cell Entry and Replication

Singh, S., O’Reilly, S. R., Gewaid, H. E., Bowie, A., Gautier, V., & Worrall, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012522 · Cited by 14

Applications of nanobodies in the prevention, detection, and treatment of the evolving SARS-CoV-2

Wang, W., Hu, Y., Li, B., Wang, H., & Shen, J. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115401 · Cited by 14

SARS-CoV-2 pandemics: An update of CRISPR in diagnosis and host–virus interaction studies

Tang, W., Tran, A.-T., Wang, L., & Horng, J. (2023) · Biomedical Journal · doi:10.1016/j.bj.2023.02.007 · Cited by 18

Polyvalent Nano-Lectin Potently Neutralizes SARS-CoV-2 by Targeting Glycans on the Viral Spike Protein

Budhadev, D., Hooper, J., Rocha, C., Nehlmeier, I., Kempf, A. M., Hoffmann, M., Krüger, N., Zhou, D., Pöhlmann, S., & Guo, Y. (2023) · JACS Au · doi:10.1021/jacsau.3c00163 · Cited by 15

Furin cleavage of SARS-CoV-2 Spike promotes but is not essential for infection and cell-cell fusion

Papa, G., Mallery, D. L., Albecka, A., Welch, L. G., Cattin‐Ortolá, J., Lupták, J., Paul, D., McMahon, H. T., Goodfellow, I., Carter, A. P., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009246 · Cited by 321

The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets

Peacock, T. P., Goldhill, D. H., Zhou, J., Baillon, L., Frise, R., Swann, O. C., Kugathasan, R., Penn, R., Brown, J. C., Sanchez-David, R. Y., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00908-w · Cited by 802

The furin cleavage site of SARS-CoV-2 spike protein is a key determinant for transmission due to enhanced replication in airway cellsPreprint

Peacock, T. P., Goldhill, D. H., Zhou, J., Baillon, L., Frise, R., Swann, O. C., Kugathasan, R., Penn, R., Brown, J. C., Sanchez-David, R. Y., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.30.318311 · Cited by 88

Why All the Fury over Furin?

Osman, E. E. A., Rehemtulla, A., & Neamati, N. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00518 · Cited by 54

A robust reporting system for measurement of SARS-CoV-2 spike fusion efficiency

Huang, C., Yang, Y., Yang, P., Wang, F., Li, X., Song, X., Wang, Y., Yu, C., Wang, X., & Wang, S. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01037-4 · Cited by 6