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

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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

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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

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

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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

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SARS-CoV-2 tropism, entry, replication, and propagation: Considerations for drug discovery and development

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Endothelium Infection and Dysregulation by SARS-CoV-2: Evidence and Caveats in COVID-19

Bernard, I., Limonta, D., Mahal, L. K., & Hobman, T. C. (2020) · Viruses · doi:10.3390/v13010029 · Cited by 187

The in vitro antiviral activity of lactoferrin against common human coronaviruses and SARS-CoV-2 is mediated by targeting the heparan sulfate co-receptor

Hu, Y., Meng, X., Zhang, F., Xiang, Y., & Wang, J. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.1888660 · Cited by 183

Proteolytic activation of SARS‐CoV‐2 spike protein

Takeda, M. (2021) · Microbiology and Immunology · doi:10.1111/1348-0421.12945 · Cited by 194

Distinctive Roles of Furin and TMPRSS2 in SARS-CoV-2 Infectivity

Essalmani, R., Jain, J., Susan‐Resiga, D., Andréo, U., Evagelidis, A., Derbali, R. M., Huynh, D. N., Dallaire, F., Laporte, M., Delpal, A., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00128-22 · Cited by 194

SARS-CoV-2 drives NLRP3 inflammasome activation in human microglia through spike protein

Albornoz, E. A., Amarilla, A. A., Modhiran, N., Parker, S. E., Li, X. X., Wijesundara, D. K., Aguado, J., Zamora, A. C. P., McMillan, C. L. D., Liang, B., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01831-0 · Cited by 191

Two-Component Spike Nanoparticle Vaccine Protects Macaques from SARS-CoV-2 Infection

Brouwer, P. J. M., Brinkkemper, M., Maisonnasse, P., Dereuddre‐Bosquet, N., Grobben, M., Claireaux, M. A. F., de Gast, M., Marlin, R., Chesnais, V., Diry, S., et al. (2020) · Cell · doi:10.1016/j.cell.2021.01.035 · Cited by 188

COVID-19 and Respiratory System Disorders

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SARS-CoV-2 Cell Entry Factors ACE2 and TMPRSS2 Are Expressed in the Microvasculature and Ducts of Human Pancreas but Are Not Enriched in β Cells

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Peptide and peptide-based inhibitors of SARS-CoV-2 entry

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SARS-CoV-2 variants with mutations at the S1/S2 cleavage site are generated in vitro during propagation in TMPRSS2-deficient cells

Sasaki, M., Uemura, K., Sato, A., Toba, S., Sanaki, T., Maenaka, K., Hall, W. W., Orba, Y., & Sawa, H. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009233 · Cited by 183

Discovery of Di- and Trihaloacetamides as Covalent SARS-CoV-2 Main Protease Inhibitors with High Target Specificity

Ma, C., Xia, Z., Sacco, M. D., Hu, Y., Townsend, J. A., Meng, X., Choza, J. I., Tan, H., Jang, J., Gongora, M. V., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c08060 · Cited by 177

Recent Advancement in mRNA Vaccine Development and Applications

Fayez, N. A., Nassar, M. S., Alshehri, A. A., Alnefaie, M. K., Almughem, F. A., Alshehri, B. Y., Alawad, A. O., & Tawfik, E. A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15071972 · Cited by 187

A Comprehensive Review of Viral Characteristics, Transmission, Pathophysiology, Immune Response, and Management of SARS-CoV-2 and COVID-19 as a Basis for Controlling the Pandemic

Triggle, C. R., Bansal, D., Ding, H., Islam, M. M., Farag, E., Hadi, H. A., & Sultan, A. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.631139 · Cited by 187

Hypertension and related diseases in the era of COVID-19: a report from the Japanese Society of Hypertension Task Force on COVID-19

Shibata, S., Arima, H., Asayama, K., Hoshide, S., Ichihara, A., Ishimitsu, T., Kario, K., Kishi, T., Mogi, M., Nishiyama, A., et al. (2020) · Hypertension Research · doi:10.1038/s41440-020-0515-0 · Cited by 181

SARS-CoV-2 spike variants exhibit differential infectivity and neutralization resistance to convalescent or post-vaccination sera

Kuzmina, A., Khalaila, Y., Voloshin, O., Keren‐Naus, A., Cohen, L. B., Raviv, Y., Shemer‐Avni, Y., Rosenberg, E., & Taube, R. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.008 · Cited by 177

Novel Systemic Inflammation Markers to Predict COVID-19 Prognosis

Karimi, A., Shobeiri, P., Kulasinghe, A., & Rezaei, N. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.741061 · Cited by 171

Immunology of COVID‐19: Mechanisms, clinical outcome, diagnostics, and perspectives—A report of the European Academy of Allergy and Clinical Immunology (EAACI)

Sokołowska, M., Łukasik, Z. M., Agache, I. O., Akdiş, C. A., Akdiş, D., Akdiş, M., Barcik, W., Brough, H. A., Eiwegger, T., Eljaszewicz, A., et al. (2020) · Allergy · doi:10.1111/all.14462 · Cited by 170

Antiviral Activity Exerted by Natural Products against Human Viruses

Musarra‐Pizzo, M., Pennisi, R., Amor, I. B., Mandalari, G., & Sciortino, M. T. (2021) · Viruses · doi:10.3390/v13050828 · Cited by 170

mRNA-based SARS-CoV-2 vaccine candidate CVnCoV induces high levels of virus-neutralising antibodies and mediates protection in rodents

Rauch, S., Roth, N., Schwendt, K., Fotin-Mleczek, M., Mueller, S. O., & Petsch, B. (2021) · npj Vaccines · doi:10.1038/s41541-021-00311-w · Cited by 165

Broad and Differential Animal Angiotensin-Converting Enzyme 2 Receptor Usage by SARS-CoV-2

Zhao, X., Chen, D., Szabla, R., Zheng, M., Li, G., Du, P., Zheng, S., Li, X., Song, C., Li, R., et al. (2020) · Journal of Virology · doi:10.1128/jvi.00940-20 · Cited by 165

Antiviral Activity of Reagents in Mouth Rinses against SARS-CoV-2

Carrouel, F., Gonçalves, L. S., Conte, M. P., Campus, G., Fisher, J., Fraticelli, L., Gadea-Deschamps, É., Ottolenghi, L., & Bourgeois, D. M. (2020) · Journal of Dental Research · doi:10.1177/0022034520967933 · Cited by 163

Acute and chronic neurological disorders in COVID-19: potential mechanisms of disease

Balcom, E. F., Nath, A., & Power, C. (2021) · Brain · doi:10.1093/brain/awab302 · Cited by 163

Neuropilin‑1 as a new potential SARS‑CoV‑2 infection mediator implicated in the neurologic features and central nervous system involvement of COVID‑19

Davies, J., Randeva, H. S., Chatha, K. K., Hall, M., Spandidos, D. A., Karteris, E., & Kyrou, I. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11510 · Cited by 160

The sequence at Spike S1/S2 site enables cleavage by furin and phospho-regulation in SARS-CoV2 but not in SARS-CoV1 or MERS-CoV

Örd, M., Faustova, I., & Loog, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-74101-0 · Cited by 159

COVID-19-Associated Neurological Disorders: The Potential Route of CNS Invasion and Blood-Brain Barrier Relevance

Achar, A., & Ghosh, C. (2020) · Cells · doi:10.3390/cells9112360 · Cited by 160

Could SARS-CoV-2 Spike Protein Be Responsible for Long-COVID Syndrome?

Theoharides, T. C. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02696-0 · Cited by 156

The spike protein of SARS-CoV-2 induces endothelial inflammation through integrin α5β1 and NF-κB signaling

Robles, J. P., Zamora, M., Adán‐Castro, E., Siqueiros‐Márquez, L., de la Escalera, G. M., & Clapp, C. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101695 · Cited by 156

TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry

Baggen, J., Jacquemyn, M., Persoons, L., Vanstreels, E., Pye, V. E., Wrobel, A. G., Calvaresi, V., Martin, S. R., Roustan, C., Cronin, N., et al. (2023) · Cell · doi:10.1016/j.cell.2023.06.005 · Cited by 159

Convalescent-Phase Sera and Vaccine-Elicited Antibodies Largely Maintain Neutralizing Titer against Global SARS-CoV-2 Variant Spikes

Tada, T., Dcosta, B. M., Samanovic, M. I., Herati, R. S., Cornelius, A. R., Zhou, H., Vaill, A., Kazmierski, W., Mulligan, M. J., & Landau, N. R. (2021) · mBio · doi:10.1128/mbio.00696-21 · Cited by 155

Glycopeptide Antibiotic Teicoplanin Inhibits Cell Entry of SARS-CoV-2 by Suppressing the Proteolytic Activity of Cathepsin L

Yu, F., Pan, T. S., Huang, F., Ying, R., Liu, J., Fan, H., Zhang, J., Liu, W., Lin, Y., Yuan, Y., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.884034 · Cited by 152

SARS-CoV-2 entry into human airway organoids is serine protease-mediated and facilitated by the multibasic cleavage site

Mykytyn, A. Z., Breugem, T. I., Riesebosch, S., Schipper, D., van den Doel, P. B., Rottier, R. J., Lamers, M. M., & Haagmans, B. L. (2021) · eLife · doi:10.7554/elife.64508 · Cited by 153

Targeting the Main Protease of SARS‐CoV‐2: From the Establishment of High Throughput Screening to the Design of Tailored Inhibitors

Breidenbach, J., Lemke, C., Pillaiyar, T., Schäkel, L., Hamwi, G. A., Diett, M., Gedschold, R., Geiger, N., Lopez, V., Mirza, S., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202016961 · Cited by 149

Prospect of SARS-CoV-2 spike protein: Potential role in vaccine and therapeutic development

Samrat, S. K., Tharappel, A. M., Li, Z., & Li, H. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198141 · Cited by 148

Can SARS-CoV-2 Virus Use Multiple Receptors to Enter Host Cells?

Gadanec, L. K., McSweeney, K. R., Qaradakhi, T., Ali, B. A., Zulli, A., & Apostolopoulos, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22030992 · Cited by 147

COVID-19 and risk of neurodegenerative disorders: A Mendelian randomization study

Li, C., Liu, J., Lin, J., & Shang, H. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02052-3 · Cited by 150

Small-Molecule Inhibitors of the Coronavirus Spike: ACE2 Protein–Protein Interaction as Blockers of Viral Attachment and Entry for SARS-CoV-2

Bojadzic, D., Alcazar, O., Chen, J., Chuang, S.-T., Capcha, J. M. C., Shehadeh, L. A., & Buchwald, P. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00070 · Cited by 147

Obesity and COVID-19: Molecular Mechanisms Linking Both Pandemics

Ritter, A., Kreis, N., Louwen, F., & Yuan, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165793 · Cited by 145

Structural and functional impact by SARS-CoV-2 Omicron spike mutations

Zhang, J., Cai, Y., Lavine, C. L., Peng, H., Zhu, H., Anand, K., Tong, P., Gautam, A. K., Mayer, M. L., Rits‐Volloch, S., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110729 · Cited by 145

Host and viral determinants for efficient SARS-CoV-2 infection of the human lung

Chu, H., Hu, B., Huang, X., Chai, Y., Zhou, D., Wang, Y., Shuai, H., Yang, D., Hou, Y., Zhang, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20457-w · Cited by 141

Cytokine storm in COVID-19: from viral infection to immune responses, diagnosis and therapy

Jiang, Y.-Z., Rubin, L., Peng, T., Liu, L., Xing, X., Lazarovici, P., & Zheng, W. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59272 · Cited by 144

Virus-Mediated Cell-Cell Fusion

Leroy, H., Han, M., Woottum, M., Bracq, L., Bouchet, J., Xie, M., & Bénichou, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249644 · Cited by 149

Two Years into the COVID-19 Pandemic: Lessons Learned

da Silva, S. J. R., do Nascimento, J. C. F., Mendes, R. P. G., Guarines, K. M., da Silva, C. T. A., da Silva, P. G., de Magalhães, J. J. F., Vigar, J. R. J., Silva‐Júnior, A., Kohl, A., et al. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00204 · Cited by 155

Efforts at COVID-19 Vaccine Development: Challenges and Successes

Haque, A., & Pant, A. B. (2020) · Vaccines · doi:10.3390/vaccines8040739 · Cited by 141

Angiotensin-converting enzyme 2 (ACE2): SARS-CoV-2 receptor and RAS modulator

Bian, J., & Li, Z. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.006 · Cited by 148

The SARS-Coronavirus Infection Cycle: A Survey of Viral Membrane Proteins, Their Functional Interactions and Pathogenesis

Wong, N. A., & Saier, M. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031308 · Cited by 144

D614G mutation of SARS-CoV-2 spike protein enhances viral infectivityPreprint

Hu, J., He, C., Gao, Q., Zhang, G., Cao, X., Long, Q., Deng, H., Huang, L., Chen, J., Wang, K., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.20.161323 · Cited by 140

SARS-CoV-2 growth, furin-cleavage-site adaptation and neutralization using serum from acutely infected hospitalized COVID-19 patients

Klimstra, W. B., Tilston-Lunel, N. L., Nambulli, S., Boslett, J., McMillen, C. M., Gilliland, T., Dunn, M. D., Sun, C., Wheeler, S. E., Wells, A., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001481 · Cited by 137

Multiple Neuroinvasive Pathways in COVID-19

Bougakov, D., Podell, K., & Goldberg, E. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02152-5 · Cited by 142

Camostat mesylate against SARS‐CoV‐2 and COVID‐19—Rationale, dosing and safety

Breining, P., Frølund, A. L., Højen, J. F., Gunst, J. D., Stærke, N. B., Sædder, E. A., Cases, M., Little, P. S., Nielsen, L. P., Søgaard, O. S., et al. (2020) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13533 · Cited by 141

Furin cleavage of the SARS-CoV-2 spike is modulated by O -glycosylation

Zhang, L., Mann, M. D., Syed, Z. A., Reynolds, H. M., Tian, E., Samara, N. L., Zeldin, D. C., Tabak, L. A., & Hagen, K. G. T. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109905118 · Cited by 139

COVID-19 Diagnosis: A Comprehensive Review of the RT-qPCR Method for Detection of SARS-CoV-2

Dutta, D., Naiyer, S., Mansuri, S., Soni, N., Singh, V., Bhat, K. H., Singh, N., Arora, G., & Mansuri, M. S. (2022) · Diagnostics · doi:10.3390/diagnostics12061503 · Cited by 151

A Wearable Tele-Health System towards Monitoring COVID-19 and Chronic Diseases

Jiang, W., Majumder, S., Kumar, S., Subramaniam, S., Li, X., Khedri, R., Mondal, T. K., Abolghasemian, M., Satia, I., & Deen, M. J. (2021) · IEEE Reviews in Biomedical Engineering · doi:10.1109/rbme.2021.3069815 · Cited by 140

ACE2: the molecular doorway to SARS-CoV-2

Medina-Enríquez, M. M., López‐León, S., Carlos-Escalante, J. A., Torres, Z. A., Cuapio, A., & Wegman-Ostrosky, T. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00519-8 · Cited by 136

Antigen Presentation of mRNA-Based and Virus-Vectored SARS-CoV-2 Vaccines

Rijkers, G. T., Weterings, N., Obregón‐Henao, A., Dutt, T., Dutt, T. S., van Overveld, F. J., & Henao-Tamayo, M. I. (2021) · Vaccines · doi:10.3390/vaccines9080848 · Cited by 139

SPR Based Biosensing Chip for COVID-19 Diagnosis—A Review

Pandey, P. S., Raghuwanshi, S. K., Shadab, A., Ansari, M. T. I., Tiwari, U. K., & Kumar, S. (2022) · IEEE Sensors Journal · doi:10.1109/jsen.2022.3181423 · Cited by 137

SARS-CoV-2 infection risk assessment in the endometrium: viral infection-related gene expression across the menstrual cycle

Henarejos-Castillo, I., Sebastián-León, P., Devesa-Peiró, A., Pellicer, A., & Díaz-Gimeno, P. (2020) · Fertility and Sterility · doi:10.1016/j.fertnstert.2020.06.026 · Cited by 134

Systematic analysis of SARS-CoV-2 infection of an ACE2-negative human airway cell

Puray‐Chavez, M., LaPak, K. M., Schrank, T. P., Elliott, J. L., Bhatt, D. P., Agajanian, M. J., Jasuja, R., Lawson, D. Q., Davis, K., Rothlauf, P. W., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109364 · Cited by 139

Establishment of a well-characterized SARS-CoV-2 lentiviral pseudovirus neutralization assay using 293T cells with stable expression of ACE2 and TMPRSS2

Neerukonda, S. N., Vassell, R. A., Herrup, R., Liu, S., Wang, T. T., Takeda, K., Yang, Y., Lin, T.-L., Wang, W., & Weiss, C. D. (2021) · PLoS ONE · doi:10.1371/journal.pone.0248348 · Cited by 133

A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells

Mellott, D. M., Tseng, C.-T. K., Drelich, A. K., Fajtová, P., Chenna, B., Kostomiris, D. H., Hsu, J. C., Zhu, J., Taylor, Z. W., Kocurek, K. I., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.0c00875 · Cited by 131

Molecular diversity of coronavirus host cell entry receptors

Millet, J. K., Jaimes, J. A., & Whittaker, G. R. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa057 · Cited by 137

COVID-19 and Cancer Comorbidity: Therapeutic Opportunities and Challenges

Pathania, A. S., Prathipati, P., Abdul, B. A., Chava, S. P., Katta, S. S., Gupta, S. C., Gangula, P. R., Pandey, M. K., Durden, D. L., Byrareddy, S. N., et al. (2020) · Theranostics · doi:10.7150/thno.51471 · Cited by 131

Recent advances in nanomaterials based biosensors for point of care (PoC) diagnosis of Covid-19 – A minireview

Annasamy, G., Kumar, N. A., & Anand, S. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2021.116205 · Cited by 131

Endocytosis of abiotic nanomaterials and nanobiovectors: Inhibition of membrane trafficking

Makvandi, P., Chen, M., Sartorius, R., Zarrabi, A., Ashrafizadeh, M., Moghaddam, F. D., Ma, J., Mattoli, V., & Tay, F. R. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101279 · Cited by 131

Phosphatidylserine receptors enhance SARS-CoV-2 infection

Bohan, D., Ert, H. A. V., Ruggio, N., Rogers, K. J., Badreddine, M., Aguilar-Briseño, J. A., Elliff, J. M., Chávez, R. A. R., Gao, B., Stokowy, T., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009743 · Cited by 132

Beneficial Properties of Bromelain

Hikisz, P., & Bernasinska-Slomczewska, J. (2021) · Nutrients · doi:10.3390/nu13124313 · Cited by 142

Curcumin, a traditional spice component, can hold the promise against COVID-19?

Soni, V. K., Mehta, A., Ratre, Y. K., Tiwari, A. K., Amit, A., Singh, R. P., Sonkar, S. C., Chaturvedi, N., Shukla, D., & Vishvakarma, N. K. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173551 · Cited by 128

AT-527, a Double Prodrug of a Guanosine Nucleotide Analog, Is a Potent Inhibitor of SARS-CoV-2 In Vitro and a Promising Oral Antiviral for Treatment of COVID-19

Good, S. S., Westover, J. B., Jung, K., Zhou, X.-J., Moussa, A. M., Colla, P. L., Collu, G., Canard, B., & Sommadossi, J. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02479-20 · Cited by 128

Unique and complementary suppression of cGAS-STING and RNA sensing- triggered innate immune responses by SARS-CoV-2 proteins

Rui, Y., Su, J., Shen, S., Hu, Y., Huang, D., Zheng, W., Lou, M., Shi, Y., Wang, M., Chen, S., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00515-5 · Cited by 137

Perspectives on SARS-CoV-2 Main Protease Inhibitors

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The SARS-CoV-2 Cytopathic Effect Is Blocked by Lysosome Alkalizing Small Molecules

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