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

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

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Cell entry mechanisms of SARS-CoV-2

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Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses

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Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV

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Structure, Function, and Evolution of Coronavirus Spike Proteins

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Identification of a new human coronavirus

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The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade

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Characterization and Complete Genome Sequence of a Novel Coronavirus, Coronavirus HKU1, from Patients with Pneumonia

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Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells

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Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites

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Another Decade, Another Coronavirus

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Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry

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TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes

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Coronavirus membrane fusion mechanism offers a potential target for antiviral development

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De novo design of picomolar SARS-CoV-2 miniprotein inhibitors

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Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis

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

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Broad host range of SARS-CoV-2 predicted by comparative and structural analysis of ACE2 in vertebrates

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Cultivation of a Novel Type of Common-cold Virus in Organ Cultures

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Identification of Required Host Factors for SARS-CoV-2 Infection in Human Cells

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Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry

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Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer

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SARS-CoV-2 infects cells after viral entry via clathrin-mediated endocytosis

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Dissecting virus entry via endocytosis

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Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop

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Toll-Like Receptor 3 Signaling via TRIF Contributes to a Protective Innate Immune Response to Severe Acute Respiratory Syndrome Coronavirus Infection

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Coronavirus Cell Entry Occurs through the Endo-/Lysosomal Pathway in a Proteolysis-Dependent Manner

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TMPRSS2 Activates the Human Coronavirus 229E for Cathepsin-Independent Host Cell Entry and Is Expressed in Viral Target Cells in the Respiratory Epithelium

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Ready, Set, Fuse! The Coronavirus Spike Protein and Acquisition of Fusion Competence

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Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection

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Characterization of a Highly Conserved Domain within the Severe Acute Respiratory Syndrome Coronavirus Spike Protein S2 Domain with Characteristics of a Viral Fusion Peptide

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The Anticoagulant Nafamostat Potently Inhibits SARS-CoV-2 S Protein-Mediated Fusion in a Cell Fusion Assay System and Viral Infection In Vitro in a Cell-Type-Dependent Manner

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LY6E impairs coronavirus fusion and confers immune control of viral disease

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Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2

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MyD88 Is Required for Protection from Lethal Infection with a Mouse-Adapted SARS-CoV

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Entry of Human Coronavirus NL63 into the Cell

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Interferon induction of IFITM proteins promotes infection by human coronavirus OC43

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The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner

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Cleavage of the SARS Coronavirus Spike Glycoprotein by Airway Proteases Enhances Virus Entry into Human Bronchial Epithelial Cells In Vitro

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Proteolytic Activation of SARS-CoV-2 Spike at the S1/S2 Boundary: Potential Role of Proteases beyond Furin

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Molecular diversity of coronavirus host cell entry receptors

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Identification of Residues Controlling Restriction versus Enhancing Activities of IFITM Proteins on Entry of Human Coronaviruses

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ATP1A1-Mediated Src Signaling Inhibits Coronavirus Entry into Host Cells

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Ca 2+ Ions Promote Fusion of Middle East Respiratory Syndrome Coronavirus with Host Cells and Increase Infectivity

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

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Tetraspanins: Architects of Viral Entry and Exit Platforms

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Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain

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Early events of SARS coronavirus infection in vero cells

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

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Ca2+-dependent mechanism of membrane insertion and destabilization by the SARS-CoV-2 fusion peptide

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Ezrin Interacts with the SARS Coronavirus Spike Protein and Restrains Infection at the Entry Stage

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Evaluating MERS-CoV Entry Pathways

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Highly potent anti-SARS-CoV-2 multivalent DARPin therapeutic candidatesPreprint

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USP11 mediates repair of DNA–protein cross-links by deubiquitinating SPRTN metalloprotease

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Antiviral drugs targeting endosomal membrane proteins inhibit distant animal and human pathogenic viruses

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IgG1 conformational behavior: elucidation of the N-glycosylation role via molecular dynamics

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HCoV-229E spike protein fusion activation by trypsin-like serine proteases is mediated by proteolytic processing in the S2′ region

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Structures and functions of coronavirus replication–transcription complexes and their relevance for SARS-CoV-2 drug design

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Cellular host factors for SARS-CoV-2 infection

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Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe

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Functional evaluation of the P681H mutation on the proteolytic activation of the SARS-CoV-2 variant B.1.1.7 (Alpha) spike

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Viral Membrane Fusion: A Dance Between Proteins and Lipids

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Inhibitors of L-Type Calcium Channels Show Therapeutic Potential for Treating SARS-CoV-2 Infections by Preventing Virus Entry and Spread

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SARS-CoV-2 spike and its adaptable furin cleavage site

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The Emergence of the Spike Furin Cleavage Site in SARS-CoV-2

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A systematic review of Vaccine Breakthrough Infections by SARS-CoV-2 Delta Variant

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Drug Combinations as a First Line of Defense against Coronaviruses and Other Emerging Viruses

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Binding of SARS-CoV-2 Fusion Peptide to Host Endosome and Plasma Membrane

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SARS-CoV-2 spike N-terminal domain modulates TMPRSS2-dependent viral entry and fusogenicity

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Spike Protein Cleavage-Activation Mediated by the SARS-CoV-2 P681R Mutation: A Case-Study From Its First Appearance in Variant of Interest (VOI) A.23.1 Identified in UgandaPreprint

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SARS-CoV-2 Spike Furin Cleavage Site and S2′ Basic Residues Modulate the Entry Process in a Host Cell-Dependent Manner

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Spike Protein Cleavage-Activation in the Context of the SARS-CoV-2 P681R Mutation: an Analysis from Its First Appearance in Lineage A.23.1 Identified in Uganda

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Natural and Recombinant SARS-CoV-2 Isolates Rapidly Evolve In Vitro to Higher Infectivity through More Efficient Binding to Heparan Sulfate and Reduced S1/S2 Cleavage

Shiliaev, N., Lukash, T., Palchevska, O., Crossman, D. K., Green, T. J., Crowley, M. R., Frolova, E. I., & Frolov, I. V. (2021) · Journal of Virology · doi:10.1128/jvi.01357-21 · Cited by 40 · see citing works

Monoclonal antibody targeting the conserved region of the SARS-CoV-2 spike protein to overcome viral variants

Wu, W.-L., Chiang, C.-Y., Lai, S.-C., Yu, C.-Y., Huang, Y., Liao, H., Liao, C., Chen, H., & Liu, S. (2022) · JCI Insight · doi:10.1172/jci.insight.157597 · Cited by 41 · see citing works

A weak COPI binding motif in the cytoplasmic tail of SARS‐CoV‐2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization

Jennings, B. C., Kornfeld, S. A., & Doray, B. (2021) · FEBS Letters · doi:10.1002/1873-3468.14109 · Cited by 31 · see citing works

Merging microfluidics with luminescence immunoassays for urgent point-of-care diagnostics of COVID-19

Yuan, H., Chen, P., Wan, C., Li, Y., & Liu, B. (2022) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2022.116814 · Cited by 33 · see citing works

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 26 · see citing works

Precision nutrition to reset virus-induced human metabolic reprogramming and dysregulation (HMRD) in long-COVID

Naidu, A. S., Wang, C., Rao, P., Mancini, F., Clemens, R., Wirakartakusumah, A., Chiu, H., Yen, C., Porretta, S., Mathai, I., et al. (2024) · npj Science of Food · doi:10.1038/s41538-024-00261-2 · Cited by 30 · see citing works

Isothermal amplification and fluorescent detection of SARS-CoV-2 and SARS-CoV-2 variant virus in nasopharyngeal swabs

Jones, L. P., Bakre, A. A., Naikare, H. K., Kolhe, R. B., Sánchez, S., Mosley, Y. C., & Tripp, R. A. (2021) · PLoS ONE · doi:10.1371/journal.pone.0257563 · Cited by 20 · see citing works

Infection of Human Cells by SARS-CoV-2 and Molecular Overview of Gastrointestinal, Neurological, and Hepatic Problems in COVID-19 Patients

Rahban, M., Stanek, A., Hooshmand, A., Khamineh, Y., Ahi, S., Kazim, S. N., Ahmad, F., Muronetz, V. I., Abousenna, M. S., Zolghadri, S., et al. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10214802 · Cited by 20 · see citing works

Acquisition of Furin Cleavage Site and Further SARS-CoV-2 Evolution Change the Mechanisms of Viral Entry, Infection Spread, and Cell Signaling

Frolova, E. I., Palchevska, O., Lukash, T., Domínguez, F. D. B. P., Britt, W. J., & Frolov, I. V. (2022) · Journal of Virology · doi:10.1128/jvi.00753-22 · Cited by 18 · see citing works

Predicted pH-dependent stability of SARS-CoV-2 spike protein trimer from interfacial acidic groups

Lobo, V. R., & Warwicker, J. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.08.049 · Cited by 18 · see citing works

Structural Dynamics and Molecular Evolution of the SARS-CoV-2 Spike Protein

Wolf, K., Kwan, J. C., & Kamil, J. P. (2022) · mBio · doi:10.1128/mbio.02030-21 · Cited by 18 · see citing works

The Physical Basis for pH Sensitivity in Biomolecular Structure and Function, With Application to the Spike Protein of SARS-CoV-2

Warwicker, J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.834011 · Cited by 17 · see citing works

Recent insights into the structure and function of coronavirus ribonucleases

Frazier, M. N., Riccio, A. A., Wilson, I. M., Copeland, W. C., & Stanley, R. E. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13414 · Cited by 16 · see citing works

Proviral role of human respiratory epithelial cell‐derived small extracellular vesicles in SARS‐CoV‐2 infection

Berry, F., Morin‐Dewaele, M., Majidipur, A., Jamet, T., Bartier, S., Ignjatovic, E., Toniutti, D., Lopes, J. G., Soyeux, P., Maillé, P., et al. (2022) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12269 · Cited by 18 · see citing works

Interaction of SARS-CoV-2 with host cells and antibodies: experiment and simulation

Nguyen, H. V., Nguyen, H. L., Lan, P. D., Thai, N. Q., Sikora, M., & Li, M. S. (2023) · Chemical Society Reviews · doi:10.1039/d1cs01170g · Cited by 14 · see citing works

The Role of SARS-CoV-2 Nucleocapsid Protein in Host Inflammation

Cao, Y., Wang, Y., Huang, D.-G., & Tan, Y. (2025) · Viruses · doi:10.3390/v17081046 · Cited by 12 · see citing works

Different Binding Modes of SARS-CoV-1 and SARS-CoV-2 Fusion Peptides to Cell Membranes: The Influence of Peptide Helix Length

Shen, H., Wu, Z., & Chen, L. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c01295 · Cited by 12 · see citing works

Effect of Disulfide Bridge on the Binding of SARS-CoV-2 Fusion Peptide to Cell Membrane: A Coarse-Grained Study

Shen, H., & Wu, Z. (2022) · ACS Omega · doi:10.1021/acsomega.2c05079 · Cited by 11 · see citing works

Knockout of angiotensin converting enzyme-2 receptor leads to morphological aberrations in rodent olfactory centers and dysfunctions associated with sense of smell

Mahajan, S., Sen, D., Sunil, A., Srikanth, P., Marathe, S. D., Shaw, K., Sahare, M., Galande, S., & Abraham, N. M. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1180868 · Cited by 11 · see citing works

SARS-CoV-2 Protein S Fusion Peptide Is Capable of Wrapping Negatively-Charged Phospholipids

Villalaı́n, J. (2023) · Membranes · doi:10.3390/membranes13030344 · Cited by 9 · see citing works

Rapid and Scalable Production of Functional SARS-CoV-2 Virus-like Particles (VLPs) by a Stable HEK293 Cell Pool

Puarattana-aroonkorn, S., Tharakaraman, K., Suriyawipada, D., Ruchirawat, M., Fuangthong, M., Sasisekharan, R., & Artpradit, C. (2024) · Vaccines · doi:10.3390/vaccines12060561 · Cited by 8 · see citing works

Inactivation of viruses related to foodborne infections using cold plasma technology

Thirumdas, R. (2022) · Journal of Food Safety · doi:10.1111/jfs.12988 · Cited by 8 · see citing works

Interactions of SARS-CoV-2 and MERS-CoV fusion peptides measured using single-molecule force methods

Qiu, C., Whittaker, G. R., Gellman, S. H., Daniel, S., & Abbott, N. L. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.01.016 · Cited by 8 · see citing works

Regulating the microenvironment with nanomaterials: Potential strategies to ameliorate COVID-19

Liu, Z., Han, Z., Jin, X., An, J., Kim, J., Chen, W., Kim, J. S., Zheng, J., & Deng, J. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.02.010 · Cited by 6 · see citing works

Heptad stereotypy, S/Q layering, and remote origin of the SARS-CoV-2 fusion core

Marchetti, C., Vaglietti, S., Rizzo, F., Nardo, G. D., Colnaghi, L., Ghirardi, M., & Fiumara, F. (2021) · Virus Evolution · doi:10.1093/ve/veab097 · Cited by 6 · see citing works

Neurotropic SARS-CoV-2: Causalities and Realities

Pardasani, M., & Abraham, N. M. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.108573 · Cited by 5 · see citing works

Therapeutic Potentials of Black Seeds (Nigella sativa) in the Management of COVID-19 -A Review of Clinical and In-silico Studies

Balasubramanian, R., Maideen, N. M. P., Gobinath, M., Rafiullah, M., & Muthusamy, S. (2022) · Anti-Infective Agents · doi:10.2174/2211352520666220802150156 · Cited by 6 · see citing works

A Comparison of Conserved Features in the Human Coronavirus Family Shows That Studies of Viruses Less Pathogenic than SARS-CoV-2, Such as HCoV-OC43, Are Good Model Systems for Elucidating Basic Mechanisms of Infection and Replication in Standard Laboratories

Heffner, A. L., & Rouault, T. A. (2025) · Viruses · doi:10.3390/v17020256 · Cited by 5 · see citing works

Cryo-EM structure of ACE2-SIT1 in complex with tiagabine

Bröer, A., Hu, Z., Kukułowicz, J., Yadav, A., Zhang, T., Dai, L., Bajda, M., Yan, R., & Bröer, S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107687 · Cited by 5 · see citing works

Effect of Double Mutation (L452R and E484Q) in RBD of Spike Protein on its Interaction with ACE2 Receptor Protein

Das, C., Hazarika, P., Deb, A., et al. (2022) · Biointerface Research in Applied Chemistry · doi:10.33263/briac131.097 · Cited by 5 · see citing works

Genome-wide bioinformatics analysis of human protease capacity for proteolytic cleavage of the SARS-CoV-2 spike glycoprotein

Matveev, E. V., Ponomarev, G. V., & Kazanov, M. D. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.03530-23 · Cited by 4 · see citing works

The critical role of aromatic residues in the binding of the SARS-CoV-2 fusion peptide to phospholipid bilayer membranes

Shen, H., Chen, L., & Yang, H. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp03045a · Cited by 4 · see citing works

Formulation Development of a COVID-19 Recombinant Spike Protein-Based Vaccine

Xiao, E., Mirabel, C., Clénet, D., Zhu, S., James, A., Ettorre, L., Williams, T., Szeto, J., Rahman, N., & Ausar, S. F. (2024) · Vaccines · doi:10.3390/vaccines12080830 · Cited by 3 · see citing works

Systems medicine framework for repurposable drug combinations for COVID-19 comorbidities

Saranya, S. V., Thamanna, L., & Chellapandi, P. (2024) · Medicine in Omics · doi:10.1016/j.meomic.2024.100038 · Cited by 3 · see citing works

Endotheliitis, Shunts, and Ventilation–Perfusion Mismatch in Coronavirus Disease 2019: A Literature Review of Disease Mechanisms

González-Ruiz, F. J., Lazcano‐Díaz, E. A., Baeza-Herrera, L. A., Villalobos-Pedroza, M., Aleman, E. T., Zuñiga-Salcedo, M. G., Cruz-Rodríguez, C., López-Polanco, A., Torres-Pulido, A., de Cossío, A. S.-G., et al. (2022) · Annals of Medicine and Surgery · doi:10.1016/j.amsu.2022.103820 · Cited by 3 · see citing works

Interaction mechanism of cold atmospheric plasmas and fusion peptides of spike protein in SARS-CoV-2 revealed by reactive molecular dynamics simulation

Chen, Y., Chai, Z., & Zhang, Y. T. (2024) · Physics of Plasmas · doi:10.1063/5.0216072 · Cited by 2 · see citing works

Binding of SARS-CoV-2 fusion peptide to host membranesPreprint

Schaefer, S. L., Jung, H., & Hummer, G. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.10.443474 · Cited by 2 · see citing works

Exploring coronavirus cell entry with functional viromics

Jefferson, V. A., Endlich-Frazier, A., & Letko, M. C. (2026) · Journal of Virology · doi:10.1128/jvi.01728-25 · Cited by 1 · see citing works

Structural proteins in the mechanisms of betacoronavirus virion assembly

Zaloilo, I., Zaloilo, О., Rud, Y., & Buchatskyi, L. (2022) · The Ukrainian Biochemical Journal · doi:10.15407/ubj94.04.005 · Cited by 1 · see citing works

Relationship between monomer packing, receptor binding domain pocket status, and pH, in the spike trimer of SARS-CoV-2 variantsPreprint

Warwicker, J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.14.472554 · Cited by 1 · see citing works

Characterization of Hydrophobic Interactions of SARS-CoV-2 and MERS-CoV Spike Protein Fusion Peptides Using Single Molecule Force MeasurementsPreprint

Qiu, C., Whittaker, G. R., Gellman, S. H., Daniel, S., & Abbott, N. L. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.05.483104 · Cited by 1 · see citing works

Genome-wide Bioinformatics Analysis of Human Protease Specificity Identified Potential Cathepsin L Cleavage Site at K790 Position of the SARS-CoV-2 Spike GlycoproteinPreprint

Matveev, E. V., Ponomarev, G. V., & Kazanov, M. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.19.553950

Correlation between IL-17, TGF-β and PTPN-22 Levels and Covid-19 Severity in Patients with and without Autoimmune Diseases

Elaskalany, F. E. Z., Hassan, M. M., Agban, M. N., & Elkhawaga, A. A. (2024) · The Egyptian Journal of Medical Microbiology · doi:10.21608/ejmm.2024.338126

A Bioinformatics Method for Identification of Human Proteases Active against Viral Envelope Glycoproteins: A Case Study on the SARS-CoV-2 Spike Protein

Matveev, E. V., Ponomarev, G. V., & Kazanov, M. D. (2024) · Molecular Biology · doi:10.1134/s0026893324020122

A bioinformatics method for identification of human proteases active against viral envelope glycoproteins: a case study on the SARS-CoV-2 spike protein

Matveev, E. V., Ponomarev, G. V., & Kazanov, M. D. (2024) · Molecular Biology · doi:10.31857/s0026898424010176

Teicoplanin attenuates RNA virus infection in vitroPreprint

Españo, E., Kim, J., Park, S. O., Padasas, B. T., Kim, S., Son, J.-H., Oh, J., Woo, E.-E., Lee, Y.-R., Hwang, S. Y., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.29.615295

CAML Model for Computational Biology

Chaudhuri, P. P., Dutta, A., Choudhury, S. P., Chowdhury, D. R., & Hazari, R. (2025) · Springer eBooks · doi:10.1007/978-981-96-1501-8_5

pH-induced structural changes in SARS-CoV-2 spike variantsPreprint

Oliveira, A. S., Tulli, L., Kearns, F. L., Casalino, L., Rosenfeld, M. A., Berger, I., Schaffitzel, C., Davidson, A. D., Haddrell, A., Reid, J. P., et al. (2025) · bioRxiv · doi:10.1101/2025.11.17.688702 · Cited by 1 · see citing works

In Silico Exploration of Potential Inhibitors Targeting SARS ‐ CoV ‐2 Non‐Structural Protein 15 (Nsp15): A Comprehensive Overview of Current Research

Yazdani, B., Sirous, H., Farzam, F., Ansarizadeh, S., Taheri, M. K., Pourmohammad‐Hosseini, G., Masjedi, M. N.-K., Daneshipour, K., Shakeri, D., Houshangi, M., et al. (2025) · Chemical Biology & Drug Design · doi:10.1111/cbdd.70218

A spike-binding protein as a versatile tool to detect and inhibit transmissible gastroenteritis virus

Khan, M., Lejal, N., Boursin, F., Jacquelin, J., Bigault, L., Minard, P., Valerio‐Lepiniec, M., Urvoas, A., Blanchard, Y., Contrant, M., et al. (2026) · Virology · doi:10.1016/j.virol.2026.110887

Mécanismes d’entrée de SARS-CoV-2 : relation hôte-virus au site de primo-infection et repositionnement thérapeutique

Morin‐Dewaele, M. (2023) · doi:10.70675/3332ee05z67cez489cza3e8zb3843eed7d42

Low-pH-induced conformational changes in the spike protein promote porcine deltacoronavirus infection by enhancing viral binding efficiency to the porcine aminopeptidase receptor

Yu, R., Zhang, L., Zhou, P., Zhang, Z., Bai, Y., Wang, D., Liu, Y., Wang, X., Du, G., Yuan, L., et al. (2026) · Journal of Virology · doi:10.1128/jvi.01168-26

Mechanisms of SARS-CoV-2 entry into cells

Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,082 · see citing works

Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies

Santamaria-Castro, I., Leiva-Rebollo, R., Marín‐Wong, S., Jiménez-Guardeño, J. M., & Ortega‐Prieto, A. M. (2025) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00260-24 · Cited by 6 · see citing works

SARS-CoV-2突变背景下的病毒入侵机制研究进展与干预策略

Wang, G., Bai, Y., Wang, Z., & Xu, Y. (2022) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2022-0457

Cell entry by SARS-CoV-2

Peng, R., Wu, L.-A., Wang, Q., Qi, J., & Gao, G. F. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.06.001 · Cited by 164 · see citing works

Ready, Set, Fuse! The Coronavirus Spike Protein and Acquisition of Fusion Competence

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