Cell entry mechanisms of SARS-CoV-2

Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China

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Clinical course and risk factors for mortality of adult inpatients with COVID-19 in Wuhan, China: a retrospective cohort study

Zhou, F., Yu, T., Du, R., Fan, G., Liu, Y., Liu, Z., Xiang, J., Wang, Y., Song, B., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30566-3 · Cited by 27,263

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

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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

Early transmission dynamics in Wuhan, China, of novel coronavirus-infected pneumonia

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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

Virological assessment of hospitalized patients with COVID-2019

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Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus

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Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus

Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F. (2020) · Journal of Virology · doi:10.1128/jvi.00127-20 · Cited by 4,341

Short-Chain Fatty Acids in the Microbiota–Gut–Brain Axis: Role in Neurodegenerative Disorders and Viral Infections

Majumdar, A., Venkatesh, I. P. S., & Basu, A. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00803 · Cited by 86

In Vitro and In Vivo Models for Studying SARS-CoV-2, the Etiological Agent Responsible for COVID-19 Pandemic

Rosa, R. B., Dantas, W. M., do Nascimento, J. C. F., da Silva, M. V., de Oliveira, R. N., & Pena, L. (2021) · Viruses · doi:10.3390/v13030379 · Cited by 89

Membrane Nanoparticles Derived from ACE2-Rich Cells Block SARS-CoV-2 Infection

Wang, C., Wang, S., Chen, Y., Zhao, J., Han, S., Zhao, G., Kang, J., Liu, Y., Wang, L., Wang, X., et al. (2021) · ACS Nano · doi:10.1021/acsnano.0c06836 · Cited by 84

Immunological Aspects of SARS-CoV-2 Infection and the Putative Beneficial Role of Vitamin-D

Peng, M.-Y., Liu, W.-C., Zheng, J.-Q., Lu, C., Hou, Y., Zheng, C., Song, J.-Y., Lu, K., & Chao, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105251 · Cited by 86

Recent advances in SARS-CoV-2 Spike protein and RBD mutations comparison between new variants Alpha (B.1.1.7, United Kingdom), Beta (B.1.351, South Africa), Gamma (P.1, Brazil) and Delta (B.1.617.2, India)

Sanches, P. R. D. S., Charlie‐Silva, I., Braz, H. L. B., Bittar, C., Calmon, M. F., Rahal, P., & Cilli, E. M. (2021) · Journal of Virus Eradication · doi:10.1016/j.jve.2021.100054 · Cited by 88

A Systematic Review on COVID-19 Vaccine Strategies, Their Effectiveness, and Issues

Khandker, S. S., Godman, B., Jawad, M. I., Meghla, B. A., Tisha, T. A., Khondoker, M. U., Haq, M. A., Charan, J., Talukder, A. A., Azmuda, N., et al. (2021) · Vaccines · doi:10.3390/vaccines9121387 · Cited by 88

Deletion of the SARS-CoV-2 Spike Cytoplasmic Tail Increases Infectivity in Pseudovirus Neutralization Assays

Yu, J., Li, Z., He, X., Gebre, M. S., Bondzie, E. A., Wan, H., Jacob-Dolan, C., Martinez, D. R., Nkolola, J. P., Baric, R. S., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00044-21 · Cited by 85

Potential antiviral activity of isorhamnetin against SARS‐CoV ‐2 spike pseudotyped virus in vitro

Zhan, Y., Ta, W., Tang, W., Hua, R., Wang, J., Wang, C., & Lu, W. Z. (2021) · Drug Development Research · doi:10.1002/ddr.21815 · Cited by 85

Potential Therapeutic Targets and Vaccine Development for SARS-CoV-2/COVID-19 Pandemic Management: A Review on the Recent Update

Anand, U., Jakhmola, S., Indari, O., Jha, H. C., Chen, Z., Tripathi, V. S., & de la Lastra, J. M. P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.658519 · Cited by 84

Host-pathogen interaction in COVID-19: Pathogenesis, potential therapeutics and vaccination strategies

Varghese, P. M., Tsolaki, A. G., Yasmin, H., Shastri, A., Ferluga, J., Vatish, M., Madan, T., & Kishore, U. (2020) · Immunobiology · doi:10.1016/j.imbio.2020.152008 · Cited by 83

Repurposing the Ebola and Marburg Virus Inhibitors Tilorone, Quinacrine, and Pyronaridine: In Vitro Activity against SARS-CoV‑2 and Potential Mechanisms

Puhl, A. C., Fritch, E. J., Lane, T. R., Tse, L. V., Yount, B. L., Sacramento, C. Q., Rodrigues, N. F., Tavella, T. A., Costa, F. T. M., Weston, S. M., et al. (2021) · ACS Omega · doi:10.1021/acsomega.0c05996 · Cited by 82

Neutralizing Antibodies in COVID-19 Patients and Vaccine Recipients after Two Doses of BNT162b2

Favresse, J., Gillot, C., Chiaro, L. D., Eucher, C., Elsen, M., Eeckhoudt, S. V., David, C., Morimont, L., Dogné, J., & Douxfils, J. (2021) · Viruses · doi:10.3390/v13071364 · Cited by 85

Targeting the Heme-Heme Oxygenase System to Prevent Severe Complications Following COVID-19 Infections

Wagener, F. A. D. T. G., Pickkers, P., Peterson, S. J., Immenschuh, S., & Abraham, N. G. (2020) · Antioxidants · doi:10.3390/antiox9060540 · Cited by 81

Priming of SARS-CoV-2 S protein by several membrane-bound serine proteinases could explain enhanced viral infectivity and systemic COVID-19 infection

Fuentes‐Prior, P. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.015980 · Cited by 84

Heparan Sulfate Proteoglycans in Viral Infection and Treatment: A Special Focus on SARS-CoV-2

Pasquale, V. D., Quiccione, M. S., Tafuri, S., Avallone, L., & Pavone, L. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126574 · Cited by 85

Inflammation in COVID-19: from pathogenesis to treatment.

Wong, R. S.-Y. (2021) · PubMed · Cited by 81

Immunogenic and reactogenic efficacy of Covaxin and Covishield: a comparative review

Das, S., Kar, S. S., Samanta, S., Banerjee, J., Giri, B., & Dash, S. K. (2022) · Immunologic Research · doi:10.1007/s12026-022-09265-0 · Cited by 82

The triumvirate: why hypertension, obesity, and diabetes are risk factors for adverse effects in patients with COVID-19

Shah, H., Khan, M. S. H., Dhurandhar, N. V., & Hegde, V. (2021) · Acta Diabetologica · doi:10.1007/s00592-020-01636-z · Cited by 80

Berberine and Obatoclax Inhibit SARS-Cov-2 Replication in Primary Human Nasal Epithelial Cells In Vitro

Varghese, F. S., van Woudenbergh, E., Overheul, G. J., Eleveld, M. J., Kurver, L., van Heerbeek, N., van Laarhoven, A., Miesen, P., den Hartog, G., de Jonge, M. I., et al. (2021) · Viruses · doi:10.3390/v13020282 · Cited by 80

Marine sulfated polysaccharides as potential antiviral drug candidates to treat Corona Virus disease (COVID-19)

Andrew, M., & Jayaraman, G. (2021) · Carbohydrate Research · doi:10.1016/j.carres.2021.108326 · Cited by 80

A high-throughput screen for TMPRSS2 expression identifies FDA-approved compounds that can limit SARS-CoV-2 entry

Chen, Y., Lear, T., Evankovich, J. W., Larsen, M. B., Lin, B., Alfaras, I., Kennerdell, J. R., Salminen, L., Camarco, D. P., Lockwood, K. C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24156-y · Cited by 82

Advances in the design and development of SARS-CoV-2 vaccines

Peng, X., Cheng, J., Gong, H., Yuan, M.-D., Zhao, X., Li, Z., & Wei, D. (2021) · Military Medical Research · doi:10.1186/s40779-021-00360-1 · Cited by 84

Comprehensive Review on Current Interventions, Diagnostics, and Nanotechnology Perspectives against SARS-CoV-2

Chauhan, D. S., Prasad, R., Srivastava, R., Jaggi, M., Chauhan, S. C., & Yallapu, M. M. (2020) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.0c00323 · Cited by 81

Inflammatory Response Leads to Neuronal Death in Human Post-Mortem Cerebral Cortex in Patients with COVID-19

Boroujeni, M. E., Simani, L., Bluyssen, H. A. R., Samadikhah, H. R., Benisi, S. Z., Hassani, S., Dilmaghani, N. A., Fathi, M., Vakili, K. G., Mahmoudiasl, G., et al. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00111 · Cited by 81

SARS-CoV-2 Disrupts Proximal Elements in the JAK-STAT Pathway

Chen, D. W., Khan, N., Close, B. J., Goel, R. K., Blum, B. C., Tavares, A. H., Kenney, D., Conway, H. L., Ewoldt, J. K., Chitalia, V. C., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00862-21 · Cited by 81

A ferritin-based COVID-19 nanoparticle vaccine that elicits robust, durable, broad-spectrum neutralizing antisera in non-human primates

Weidenbacher, P. A. B., Sanyal, M., Friedland, N., Tang, S., Arunachalam, P. S., Hu, M., Kumru, O. S., Morris, M. K., Fontenot, J. A., Shirreff, L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37417-9 · Cited by 81

Inhaled drug delivery: Past, present, and future

Yue, L., Zhang, X., Zhao, C., Chen, R., Chen, X. S., & Rao, L. (2023) · Nano Today · doi:10.1016/j.nantod.2023.101942 · Cited by 84

The SARS-CoV-2 variants associated with infections in India, B.1.617, show enhanced spike cleavage by furinPreprint

Peacock, T. P., Sheppard, C., Brown, J. C., Goonawardane, N., Zhou, J., Whiteley, M., de Silva, T. I., & Barclay, W. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.28.446163 · Cited by 83

Cardiovascular Complications Associated with COVID-19 and Potential Therapeutic Strategies

Samidurai, A., & Das, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186790 · Cited by 82

ACE2 and Furin Expressions in Oral Epithelial Cells Possibly Facilitate COVID-19 Infection via Respiratory and Fecal–Oral Routes

Zhong, M., Lin, B., Pathak, J. L., Gao, H., Young, A. J., Wang, X., Liu, C., Wu, K., Liu, M., Chen, J.-M., et al. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.580796 · Cited by 83

The development of Nanosota-1 as anti-SARS-CoV-2 nanobody drug candidates

Ye, G., Gallant, J. P., Massey, C., Shi, K., Tai, W., Zheng, J., Odle, A. E., Vickers, M. A., Shang, J., Wan, Y., et al. (2021) · eLife · doi:10.7554/elife.64815 · Cited by 78

SARS-CoV-2 Infection: New Molecular, Phylogenetic, and Pathogenetic Insights. Efficacy of Current Vaccines and the Potential Risk of Variants

Rotondo, J. C., Martini, F., Maritati, M., Mazziotta, C., Mauro, G. D., Lanzillotti, C., Barp, N., Gallerani, A., Tognon, M. G., & Contini, C. (2021) · Viruses · doi:10.3390/v13091687 · Cited by 81

Novel virus-like nanoparticle vaccine effectively protects animal model from SARS-CoV-2 infection

Geng, Q., Tai, W., Baxter, V. K., Shi, J., Wan, Y., Zhang, X., Montgomery, S. A., Taft-Benz, S., Anderson, E. J., Knight, A. C., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009897 · Cited by 78

Genetic susceptibility of COVID-19: a systematic review of current evidence

SeyedAlinaghi, S., Mehrtak, M., MohsseniPour, M., Mirzapour, P., Barzegary, A., Habibi, P., Badie, B. M., Afsahi, A. M., Karimi, A., Heydari, M., et al. (2021) · European journal of medical research · doi:10.1186/s40001-021-00516-8 · Cited by 78

Cardiomyocytes recruit monocytes upon SARS-CoV-2 infection by secreting CCL2

Yang, L., Nilsson-Payant, B. E., Han, Y., Jaffré, F., Zhu, J., Wang, P., Zhang, T., Redmond, D., Houghton, S., Møller, R., et al. (2021) · Stem Cell Reports · doi:10.1016/j.stemcr.2021.07.012 · Cited by 77

Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles

Koppisetti, R. K., Fulcher, Y. G., & Doren, S. R. V. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05435 · Cited by 81

The Transmembrane Protease TMPRSS2 as a Therapeutic Target for COVID-19 Treatment

Wettstein, L., Kirchhoff, F., & Münch, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031351 · Cited by 80

SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy

Yang, Z., Han, Y., Ding, S., Shi, W., Zhou, T., Finzi, A., Kwong, P. D., Mothes, W., & Lu, M. (2022) · mBio · doi:10.1128/mbio.03227-21 · Cited by 78

Severe COVID-19 Lung Infection in Older People and Periodontitis

Aquino-Martínez, R., & Vigueras, S. H. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10020279 · Cited by 79

ACE2 expression is elevated in airway epithelial cells from older and male healthy individuals but reduced in asthma

Wark, P. A. B., Pathinayake, P. S., Kaiko, G. E., Nichol, K., Ali, A., Chen, L., Sutanto, E. N., Garratt, L. W., Sohal, S. S., Lu, W., et al. (2021) · Respirology · doi:10.1111/resp.14003 · Cited by 76

Evidence For and Against Direct Kidney Infection by SARS-CoV-2 in Patients with COVID-19

Hassler, L., Reyes, F., Sparks, M. A., Welling, P. A., & BATLLE, D. C. (2021) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.04560421 · Cited by 76

Discovery of Cyclic Peptide Ligands to the SARS-CoV-2 Spike Protein Using mRNA Display

Norman, A. R., Franck, C., Christie, M., Hawkins, P. M. E., Patel, K., Ashhurst, A. S., Aggarwal, A., Low, J. K. K., Siddiquee, R., Ashley, C. L., et al. (2021) · ACS Central Science · doi:10.1021/acscentsci.0c01708 · Cited by 76

Neurotropism of SARS-CoV-2 and neurological diseases of the central nervous system in COVID-19 patients

Veleri, S. (2021) · Experimental Brain Research · doi:10.1007/s00221-021-06244-z · Cited by 77

Epigenetic regulation of ACE2, the receptor of the SARS-CoV-2 virus1

Beacon, T. H., Delcuve, G. P., & Davie, J. (2020) · Genome · doi:10.1139/gen-2020-0124 · Cited by 76

Lead SARS-CoV-2 Candidate Vaccines: Expectations from Phase III Trials and Recommendations Post-Vaccine Approval

Tumban, E. (2020) · Viruses · doi:10.3390/v13010054 · Cited by 76

Discovery of potential small molecular SARS-CoV-2 entry blockers targeting the spike protein

Wang, L., Wu, Y. L., Yao, S., Ge, H., Zhu, Y., Chen, K., Chen, W., Zhang, Y., Zhu, W. J., Wang, H., et al. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00735-z · Cited by 77

Identification of lectin receptors for conserved SARS‐CoV‐2 glycosylation sites

Hoffmann, D., Mereiter, S., Oh, Y. J., Monteil, V., Elder, E., Zhu, R., Canena, D., Hain, L., Laurent, E., Grünwald‐Gruber, C., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108375 · Cited by 77

Pulmonary fibrosis from molecular mechanisms to therapeutic interventions: lessons from post-COVID-19 patients

Giacomelli, C., Piccarducci, R., Marchetti, L., Romei, C., & Martini, C. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114812 · Cited by 77

Role of genomics in combating COVID-19 pandemic

Saravanan, K. A., Panigrahi, M., Kumar, H., Rajawat, D., Nayak, S. S., Bhushan, B., & Dutt, T. (2022) · Gene · doi:10.1016/j.gene.2022.146387 · Cited by 81

Induced dysregulation of ACE2 by SARS-CoV-2 plays a key role in COVID-19 severity

Mehrabadi, M. E., Hemmati, R., Tashakor, A., Homaei, A. A., Yousefzadeh, M., Hemati, K., & Hosseinkhani, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111363 · Cited by 75

Multidisciplinary Approaches Identify Compounds that Bind to Human ACE2 or SARS-CoV-2 Spike Protein as Candidates to Block SARS-CoV-2–ACE2 Receptor Interactions

Day, C. J., Bailly, B., Guillon, P., Dirr, L., Jen, F. E. ‐., Spillings, B. L., Mak, J., von Itzstein, M., Haselhorst, T., & Jennings, M. P. (2021) · mBio · doi:10.1128/mbio.03681-20 · Cited by 75

Aerosolized Nanoliposomal Carrier of Remdesivir: An Effective Alternative for COVID-19 Treatment In Vitro

Vartak, R., Patil, S. M., Saraswat, A. L., Patki, M., Kunda, N. K., & Patel, K. R. (2021) · Nanomedicine · doi:10.2217/nnm-2020-0475 · Cited by 74

Evolution of the SARS-CoV-2 Omicron spike

Parsons, R., & Acharya, P. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113444 · Cited by 79

In Silico Identification of Potential Natural Product Inhibitors of Human Proteases Key to SARS-CoV-2 Infection

Vivek-Ananth, R. P., Rana, A., Rajan, N., Biswal, H. S., & Samal, A. (2020) · Molecules · doi:10.3390/molecules25173822 · Cited by 74

Screening and druggability analysis of some plant metabolites against SARS-CoV-2: An integrative computational approach

Azim, K. F., Ahmed, S. R., Banik, A., Khan, M. M. R., Deb, A., & Somana, S. R. (2020) · Informatics in Medicine Unlocked · doi:10.1016/j.imu.2020.100367 · Cited by 75

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

Zune, A. L. D., Olwal, C. O., Beyeme, T. S., & Paemka, L. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01448 · Cited by 73

Transcription Factor Nrf2 as a Potential Therapeutic Target for Prevention of Cytokine Storm in COVID-19 Patients

Zinovkin, R. A., & Grebenchikov, O. A. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920070111 · Cited by 73

Potential Detrimental Role of Soluble ACE2 in Severe COVID-19 Comorbid Patients

Rahman, M., Hasan, M., & Ahmed, A. (2020) · Reviews in Medical Virology · doi:10.1002/rmv.2213 · Cited by 72

Quantifying Absolute Neutralization Titers against SARS-CoV-2 by a Standardized Virus Neutralization Assay Allows for Cross-Cohort Comparisons of COVID-19 Sera

Oguntuyo, K. Y., Stevens, C. S., Hung, C.-T., Ikegame, S., Acklin, J. A., Kowdle, S., Carmichael, J. C., Chiu, H.-P., Azarm, K. D., Haas, G. D., et al. (2021) · mBio · doi:10.1128/mbio.02492-20 · Cited by 73

Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants

Li, T., Xue, W., Zheng, Q., Song, S., Yang, C., Xiong, H., Zhang, S., Hong, M., Zhang, Y., Yu, H. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25997-3 · Cited by 72

ACE2, COVID-19 Infection, Inflammation, and Coagulopathy: Missing Pieces in the Puzzle

Abassi, Z. A., Higazi, A. A., Kinaneh, S., Armaly, Z., Skorecki, K. L., & Heyman, S. N. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.574753 · Cited by 72

An ACE2 Microbody Containing a Single Immunoglobulin Fc Domain Is a Potent Inhibitor of SARS-CoV-2

Tada, T., Fan, C., Chen, J., Kaur, R., Stapleford, K. A., Gristick, H. B., Dcosta, B. M., Wilen, C. B., Nimigean, C. M., & Landau, N. R. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108528 · Cited by 72

Graphene Sheets with Defined Dual Functionalities for the Strong SARS‐CoV‐2 Interactions

Donskyi, I. S., Nie, C., Ludwig, K., Trimpert, J., Ahmed, R., Quaas, E., Achazi, K., Radnik, J., Adeli, M., Haag, R., et al. (2021) · Small · doi:10.1002/smll.202007091 · Cited by 74

Tracing the origins of SARS-COV-2 in coronavirus phylogenies: a review

Sallard, E., Halloy, J., Casañe, D., Decroly, É., & van Helden, J. (2021) · Environmental Chemistry Letters · doi:10.1007/s10311-020-01151-1 · Cited by 79

Therapeutic activity of an inhaled potent SARS-CoV-2 neutralizing human monoclonal antibody in hamsters

Piepenbrink, M. S., Park, J., Oladunni, F. S., Deshpande, A. A., Basu, M., Sarkar, S., Loos, A., Woo, J. C., Lovalenti, P. M., Sloan, D. D., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100218 · Cited by 73

The envelope protein of SARS‐CoV‐2 increases intra‐Golgi pH and forms a cation channel that is regulated by pH

Cabrera-García, D., Bekdash, R., Abbott, G. W., Yazawa, M., & Harrison, N. L. (2021) · The Journal of Physiology · doi:10.1113/jp281037 · Cited by 78

Insights on SARS-CoV-2 Molecular Interactions With the Renin-Angiotensin System

Costa, L. B., Perez, L. G., Palmeira, V. A., Cordeiro, T. M. E., Ribeiro, V. T., Lanza, K., & Silva, A. C. S. E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.559841 · Cited by 71

Experimental and in silico evidence suggests vaccines are unlikely to be affected by D614G mutation in SARS-CoV-2 spike protein

McAuley, A. J., Kuiper, M. J., Durr, P. A., Bruce, M. P., Barr, J. A., Todd, S., Au, G. G., Blasdell, K. R., Tachedjian, M., Lowther, S., et al. (2020) · npj Vaccines · doi:10.1038/s41541-020-00246-8 · Cited by 70

Molecular Basis of SARS-CoV‑2 Infection and Rational Design of Potential Antiviral Agents: Modeling and Simulation Approaches

Francés‐Monerris, A., Hognon, C., Miclot, T., García‐Iriepa, C., Iriepa, I., Terenzi, A., Grandemange, S., Barone, G., Marazzi, M., & Monari, A. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00779 · Cited by 72

Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?

Kurpe, S., Grishin, S. Y., Surin, A. K., Panfilov, A. V., Slizen, M. V., Chowdhury, S. D., & Galzitskaya, O. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249552 · Cited by 70

Host Serine Proteases: A Potential Targeted Therapy for COVID-19 and Influenza

Saadat, Y. R., Khatibi, S. M. H., Vahed, S. Z., & Ardalan, M. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.725528 · Cited by 76

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Li, X., Yuan, H., Li, X., & Wang, H. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28212 · Cited by 76

Virtual screening and molecular dynamics simulations provide insight into repurposing drugs against SARS-CoV-2 variants Spike protein/ACE2 interface

Pirolli, D., Righino, B., Camponeschi, C., Ria, F., Sante, G. D., & Rosa, M. C. D. (2023) · Scientific Reports · doi:10.1038/s41598-023-28716-8 · Cited by 74

Bioactivity, bioavailability, and gut microbiota transformations of dietary phenolic compounds: implications for COVID-19

Augusti, P. R., Conterato, G. M. M., Denardin, C. C., Prazeres, I. D., Serra, T., Bronze, M. R., & Emanuelli, T. (2021) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2021.108787 · Cited by 72

Design of an epitope-based peptide vaccine against the SARS-CoV-2: a vaccine-informatics approach

Alam, A., Khan, A., Imam, N., Siddiqui, M. F., Waseem, M., Malik, M. Z., & Ishrat, R. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbaa340 · Cited by 68

Why Is COVID-19 More Severe in Patients With Diabetes? The Role of Angiotensin-Converting Enzyme 2, Endothelial Dysfunction and the Immunoinflammatory System

Roberts, J., Pritchard, A. L., Treweeke, A. T., Rossi, A. G., Brace, N., Cahill, P. A., MacRury, S. M., Wei, J., & Megson, I. L. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.629933 · Cited by 68

Neuropilin-1 assists SARS-CoV-2 infection by stimulating the separation of Spike protein S1 and S2

Li, Z., & Buck, M. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.05.026 · Cited by 72

Acute SARS-CoV-2 infection is associated with an increased abundance of bacterial pathogens, including Pseudomonas aeruginosa in the nose

Rhoades, N. S., Pinski, A. N., Monsibais, A. N., Jankeel, A., Doratt, B. M., Cinco, I. R., Ibraim, I. C., & Messaoudi, I. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109637 · Cited by 73

The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein

Dokainish, H. M., Re, S., Mori, T., Kobayashi, C., Jung, J., & Sugita, Y. (2022) · eLife · doi:10.7554/elife.75720 · Cited by 70

Safety, Tolerability, and Pharmacokinetics of the Novel Antiviral Agent Ensitrelvir Fumaric Acid, a SARS-CoV-2 3CL Protease Inhibitor, in Healthy Adults

Shimizu, R., Sonoyama, T., Fukuhara, T., Kuwata, A., Matsuo, Y., & Kubota, R. (2022) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00632-22 · Cited by 68

Coronavirus entry: how we arrived at SARS-CoV-2

Whittaker, G. R., Daniel, S., & Millet, J. K. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.02.006 · Cited by 67

A proof of concept for neutralizing antibody-guided vaccine design against SARS-CoV-2

Zhang, L., Cao, L., Gao, X., Zheng, B., Deng, Y., Li, J., Feng, R., Bian, Q., Guo, X., Wang, N., et al. (2021) · National Science Review · doi:10.1093/nsr/nwab053 · Cited by 69

Tagged extracellular vesicles with the RBD of the viral spike protein for delivery of antiviral agents against SARS-COV-2 infection

Fu, Y., & Xiong, S. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.05.049 · Cited by 67

Dynamics of SARS-CoV-2 Spike Proteins in Cell Entry: Control Elements in the Amino-Terminal Domains

Qing, E., Kicmal, T., Kumar, B., Hawkins, G. M., Timm, E. C., Perlman, S. M., & Gallagher, T. (2021) · mBio · doi:10.1128/mbio.01590-21 · Cited by 70

Coronavirus Infection and Cholesterol Metabolism

Dai, J., Wang, H., Liao, Y., Tan, L., Sun, Y., Song, C., Liu, W., Qiu, X., & Ding, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.791267 · Cited by 68

Covid-19 a triggering factor of autoimmune and multi-inflammatory diseases

Sher, E. K., Ćosović, A., Džidić-Krivić, A., Farhat, E. K., Pinjić, E., & Sher, F. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121531 · Cited by 67

In silico investigation of spice molecules as potent inhibitor of SARS-CoV-2

Rout, J., Swain, B. C., & Tripathy, U. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1819879 · Cited by 66

Free SARS-CoV-2 Spike Protein S1 Particles May Play a Role in the Pathogenesis of COVID-19 Infection

Letarov, A. V., Babenko, V. V., & Kulikov, E. E. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297921030032 · Cited by 66

Potential Role of Antioxidant and Anti-Inflammatory Therapies to Prevent Severe SARS-Cov-2 Complications

Pasini, A. M. F., Stranieri, C., Cominacini, L., & Mozzini, C. (2021) · Antioxidants · doi:10.3390/antiox10020272 · Cited by 68

Molecular optimization, docking, and dynamic simulation profiling of selective aromatic phytochemical ligands in blocking the SARS-CoV-2 S protein attachment to ACE2 receptor: an in silico approach of targeted drug designing

Dey, D., Paul, P. K., Azad, S. A., Mazid, M. F. A., Khan, A. M., Sharif, M. A., & Rahman, M. H. (2021) · Journal of Advanced Veterinary and Animal Research · doi:10.5455/javar.2021.h481 · Cited by 66

Perspectives on RNA Vaccine Candidates for COVID-19

Borah, P., Deb, P. K., Al‐Shar’i, N. A., Dahabiyeh, L. A., Venugopala, K. N., Singh, V., Shinu, P., Hussain, S., Deka, S., Chandrasekaran, B., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.635245 · Cited by 67

Landscape of epitopes targeted by T cells in 852 individuals recovered from COVID-19: Meta-analysis, immunoprevalence, and web platform

Quadeer, A. A., Ahmed, S. F., & McKay, M. R. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100312 · Cited by 71

Targeting genomic SARS-CoV-2 RNA with siRNAs allows efficient inhibition of viral replication and spread

Ambike, S. S., Cheng, C., Feuerherd, M., Velkov, S., Baldassi, D., Afridi, S. Q., Porras-Gonzalez, D., Wei, X. C., Hagen, P., Kneidinger, N., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1248 · Cited by 73

Advances in the development of therapeutic strategies against COVID-19 and perspectives in the drug design for emerging SARS-CoV-2 variants

Yin, J., Li, C., Ye, C., Ruan, Z., Liang, Y., Li, Y., Wu, J., & Luo, Z. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.01.026 · Cited by 66

Antiviral cyclic peptides targeting the main protease of SARS-CoV-2

Johansen‐Leete, J., Ullrich, S., Fry, S. E., Frkic, R. L., Bedding, M. J., Aggarwal, A., Ashhurst, A. S., Ekanayake, K. B., Mahawaththa, M. C., Sasi, V. M., et al. (2022) · Chemical Science · doi:10.1039/d1sc06750h · Cited by 67

Nanotechnology‐facilitated vaccine development during the coronavirus disease 2019 (COVID‐19) pandemic

Wang, Z., Cui, K., Costabel, U., & Zhang, X. (2022) · Exploration · doi:10.1002/exp.20210082 · Cited by 68

Extracellular vesicles mediate antibody-resistant transmission of SARS-CoV-2

Xia, B., Pan, X., Luo, R., Shen, X., Li, S., Wang, Y., Zuo, X., Wu, Y. L., Guo, Y., Xiao, G., et al. (2023) · Cell Discovery · doi:10.1038/s41421-022-00510-2 · Cited by 67

Immunoinflammatory, Thrombohaemostatic, and Cardiovascular Mechanisms in COVID-19

Gencer, S., Lacy, M., Atzler, D., van der Vorst, E. P. C., Döring, Y., & Weber, C. (2020) · Thrombosis and Haemostasis · doi:10.1055/s-0040-1718735 · Cited by 66

Elucidation of interactions regulating conformational stability and dynamics of SARS-CoV-2 S-protein

Mori, T., Jung, J., Kobayashi, C., Dokainish, H., Re, S., & Sugita, Y. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.01.012 · Cited by 68

Diverse Effects of Exosomes on COVID-19: A Perspective of Progress From Transmission to Therapeutic Developments

Gurunathan, S., Kang, M.-H., & Kim, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.716407 · Cited by 67

Molecular mechanisms of COVID-19

Li, F. (2022) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273322096759

Mechanisms of SARS-CoV-2 entry into cells

Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,022

The structural basis of accelerated host cell entry by SARS‐CoV‐2†

Seyran, M., Takayama, K., Uversky, V. N., Lundstrom, K. H., Palù, G., Sherchan, S. P., Attrish, D., Rezaei, N., Aljabali, A. A. A., Ghosh, S., et al. (2020) · FEBS Journal · doi:10.1111/febs.15651 · Cited by 161

SARS-CoV-2, Early Entry Events

CHAMBERS, J. K., Yu, J., Valdés, J. J., & Arulanandam, B. P. (2020) · Journal of Pathogens · doi:10.1155/2020/9238696 · Cited by 32

A Transmembrane Serine Protease Is Linked to the Severe Acute Respiratory Syndrome Coronavirus Receptor and Activates Virus Entry

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