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

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

Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30183-5 · Cited by 48,884

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

Isolation of a Novel Coronavirus from a Man with Pneumonia in Saudi Arabia

Zaki, A. M., van Boheemen, S., Bestebroer, T. M., Osterhaus, A. D. M. E., & Fouchier, R. A. M. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1211721 · Cited by 5,677

Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis

Hamming, I., Timens, W., Bulthuis, M., Lely, A., Navis, G., & van Goor, H. (2004) · The Journal of Pathology · doi:10.1002/path.1570 · Cited by 5,676

Identification of a novel coronavirus in patients with severe acute respiratory syndrome

Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574

A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome

Tg, K., Erdman, D. D., Cs, G., Zaki, Peret, T. C. T., Emery, S. L., Tong, S., Urbani, C., Comer, J. A., Lim, W., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030781 · Cited by 4,353

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

Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109

Inactivation of Pseudovirus Expressing the D614G Spike Protein Mutation using Nitric Oxide‐Plasma Activated Water

Patel, P., Kaushik, N., Acharya, T. R., Lenka, S. S., Ghosh, S., Wahab, R., Verma, S. K., Choi, E. H., & Kaushik, N. K. (2024) · Advanced Science · doi:10.1002/advs.202411515 · Cited by 5

Dimethoxycurcumin Acidifies Endolysosomes and Inhibits SARS-CoV-2 Entry

Khan, N., Afghah, Z., Baral, A., Geiger, J. D., & Chen, X. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.923018 · Cited by 5

The COVID-19 Cell Signalling Problem: Spike, RAGE, PKC, p38, NFκB & IL-6 Hyper-Expression and the Human Ezrin Peptide, VIP, PKA-CREB Solution

Holms, R. (2022) · Immuno · doi:10.3390/immuno2020017 · Cited by 5

A Clathrin light chain A reporter mouse for in vivo imaging of endocytosis

Grimm, E., van der Hoeven, F., Sardella, D., Willig, K. I., Engel, U., Veits, N., Engel, R. R., Cavalcanti‐Adam, E. A., Bestvater, F., Bordoni, L., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0273660 · Cited by 5

Insights into COVID-19: Perspectives on Drug Remedies and Host Cell Responses

Awad, A. M., Hansen, K., Rio, D. D., Flores, D., Barghash, R. F., Kakkola, L., Julkunen, I., & Awad, K. (2023) · Biomolecules · doi:10.3390/biom13101452 · Cited by 5

Porcine deltacoronavirus enters ST cells by clathrin-mediated endocytosis and does not require Rab5, Rab7, or Rab11

Li, S., Xiao, D., Zhang, L., Chen, R., Song, D., Wen, Y., Wu, R. J., Zhao, Q., Du, S., Yan, Q., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02553-23 · Cited by 5

Rapid macropinocytic transfer of α-synuclein to lysosomesPreprint

Bayati, A., Banks, E., Han, C., Luo, W., Reintsch, W., Zorca, C. E., Shlaifer, I., del Cid‐Pellitero, E., Vanderperre, B., McBride, H. M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.06.475207 · Cited by 5

In silico and bioassay-guided identification of potential anti-SARS-CoV-2 tentative candidate compounds from Andrographis paniculata extract

Kerdsiri, J., Hengphasatporn, K., Pitaksuteepong, T., Nuengchamnong, N., Suroengrit, A., Chupinidsakulwong, P., Shigeta, Y., Bhattarakosol, P., Boonyasuppayakorn, S., & Waranuch, N. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.11.050 · Cited by 5

Proteomic Profiling of Human Peripheral Blood Cell Targets of IgG Induced by SARS-CoV-2: Insights into Vaccine Safety

Machado, N. R., do Nascimento, L. A., Fagundes, B. O., Borges, J. V. D. S., Sgnotto, F. D. R., Bergamasco, I. S., Fernandes, J. R., Pinto, T. N. C., Pietrobon, A. J., Benard, G., et al. (2025) · Vaccines · doi:10.3390/vaccines13070694 · Cited by 4

Altered hACE2 binding affinity and S1/S2 cleavage efficiency of SARS-CoV-2 spike protein mutants affect viral cell entry

Wang, K., Pan, Y., Wang, D., Yuan, Y., Li, M., Chen, Y., Bi, L., & Zhang, X. (2023) · Virologica Sinica · doi:10.1016/j.virs.2023.06.005 · Cited by 4

An In Silico Design of Peptides Targeting the S1/S2 Cleavage Site of the SARS-CoV-2 Spike Protein

Ho, C. M., Nazarie, W. F. W. M., & Lee, C. (2023) · Viruses · doi:10.3390/v15091930 · Cited by 4

Design, synthesis and biological evaluation of novel 1,2,4a,5-tetrahydro-4H-benzo[b][1,4]oxazino[4,3-d][1,4]oxazine-based AAK1 inhibitors with anti-viral property against SARS-CoV-2

Mao, N., Xu, Y., Che, H., Yao, X., Gao, Y., Wang, C., Deng, H., Hui, Z., Zhang, H., & Ye, X. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116232 · Cited by 4

Current development of severe acute respiratory syndrome coronavirus 2 neutralizing antibodies (Review)

Zhang, T., Yang, D., Tang, L., & Hu, Y. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13272 · Cited by 5

SLC38A9 regulates SARS-CoV-2 viral entry

Datta, G., Rezagholizadeh, N., Hasler, W. A., Khan, N., & Chen, X. (2024) · iScience · doi:10.1016/j.isci.2024.110387 · Cited by 5

Taming the storm: potential anti-inflammatory compounds targeting SARS-CoV-2 MPro

Anton, D. B., de Lima, J. C., Dahmer, B. R., Camini, A. M., Goettert, M. I., & Timmers, L. F. S. M. (2024) · Inflammopharmacology · doi:10.1007/s10787-024-01525-9 · Cited by 4

Drug Repurposing for COVID-19 by Constructing a Comorbidity Network with Central Nervous System Disorders

Qian, J., Yang, B., Wang, S., Yuan, S., Zhu, W., Zhou, Z., Zhang, Y., & Hu, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168917 · Cited by 5

Placenta a potential gateway of prenatal SARS-CoV-2 infection: A review

Indra, S., Chalak, K., Das, P., & Mukhopadhyay, A. (2024) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/j.ejogrb.2024.10.027 · Cited by 4

Cellular sialoglycans are differentially required for endosomal and cell-surface entry of SARS-CoV-2 in lung cell lines

Siwak, K. C., LeBlanc, E. V., Scott, H. M., Kim, Y., Pellizzari-Delano, I. E., Ball, A. M., Temperton, N. J., Capicciotti, C. J., & Colpitts, C. C. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012365 · Cited by 5

Deltacoronavirus HKU11, HKU13, PDCoV (HKU15) and HKU17 spike pseudoviruses enter avian DF-1 cells via clathrin-mediated endocytosis in a Rab5-, Rab7- and pH-dependent manner

Liang, Q., Ji, C., Wang, B., Chen, W., Cong, F., Huang, Y., & Huang, Y. (2025) · Veterinary Research · doi:10.1186/s13567-024-01442-3 · Cited by 4

Structural basis and mode of action for two broadly neutralizing nanobodies targeting the highly conserved spike stem-helix of sarbecoviruses including SARS-CoV-2 and its variants

Guo, L., Chen, Z., Lin, S., Yang, F., Yang, J., Wang, L., Zhang, X., Yuan, X., He, B., Cao, Y., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013034 · Cited by 4

Epigenetic Targets and Pathways Linked to SARS-CoV-2 Infection and Pathology

Rabaan, A. A., Aljeldah, M. M., Shammari, B. R. A., Alsubki, R. A., Alotaibi, J., Alhashem, Y. N., Alali, N. A., Sulaiman, T., Alsalem, Z. H., Bajunaid, H. A., et al. (2023) · Microorganisms · doi:10.3390/microorganisms11020341 · Cited by 4

ACE2 Receptor: A Potential Pharmacological Target in COVID-19

Zhu, Y., Zhang, S., Wang, Z., Wang, Z., & Zhu, S. (2023) · Current Protein and Peptide Science · doi:10.2174/1389203724666230816092518 · Cited by 4

Oral Epithelial Cells Expressing Low or Undetectable Levels of Human Angiotensin-Converting Enzyme 2 Are Susceptible to SARS-CoV-2 Virus Infection In Vitro

Ebraham, L., Xu, C., Wang, A. R., Hernandez, C., Siclari, N., Rajah, D., Walter, L., Marras, S. A. E., Tyagi, S., Fine, D. H., et al. (2023) · Pathogens · doi:10.3390/pathogens12060843 · Cited by 4

Distinct Molecular Mechanisms Characterizing Pathogenesis of SARS-CoV-2

Lee, S. J., Kim, Y., & Ahn, D. (2022) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2206.06064 · Cited by 4

Modulation of Tau Tubulin Kinases ((TTBK1 and TTBK2) Impacts CiliogenesisPreprint

Potjewyd, F., Gonzalez, A. M., Chaikuad, A., Howell, S., Dunn, A. S., Beltran, A. A., Smith, J. L., Drewry, D. H., Beltrán, A. S., & Axtman, A. D. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4114954 · Cited by 4

Infection-Simulator, Immunostimulatory and Immunomodulatory Effects of Interferons I and III in Biological Systems: A New Era in Vaccinology and Therapeutics Possible?Preprint

Carp, T.-N., Metoudi, M., & Ojha, V. (2024) · Preprints.org · doi:10.20944/preprints202212.0155.v6 · Cited by 4

Drug repurposing for respiratory infections

Israr, J., Alam, S., & Kumar, A. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.03.033 · Cited by 3

Interaction of SARS-CoV-2 Spike protein with ACE2 induces cortical actin modulation, including dephosphorylation of ERM proteins and reduction of cortical stiffness

Ly, T. K., Tachibana, K., Yamamoto, N., Ando, K., Isoda, T., & Kihara, T. (2024) · Human Cell · doi:10.1007/s13577-024-01142-2 · Cited by 3

The biomechanical phenomena observed in the cell invasion pathway of porcine epidemic diarrhea virus: a review

Zou, H., Wang, Y., Luo, G., & Huang, S. (2025) · Archives of Virology · doi:10.1007/s00705-025-06326-1 · Cited by 3

ACE2-independent entry factors for SARS-CoV-2 infection and immune activation

Sun, Y., Wong, L.-Y. R., & Chang, T. L.-Y. (2025) · mBio · doi:10.1128/mbio.01897-24 · Cited by 3

Molecular mechanism of cholesterol-dependent membrane fusion in SARS-CoV-2 entry

Li, W., Wu, M., Feng, S., Su, J., Niu, Q., Lin, W., Fan, J., Cui, L., Xiang, Y., Li, H., et al. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02573-z · Cited by 3

A mechanical-thermodynamic model for understanding endocytosis of COVID-19 virus SARS-CoV-2

Mahata, P., Vennamneni, L., & Chattopadhyay, S. (2022) · Proceedings of the Institution of Mechanical Engineers Part C Journal of Mechanical Engineering Science · doi:10.1177/09544062221098538 · Cited by 3

Endocytosis inhibitors block SARS-CoV-2 pseudoparticle infection of mink lung epithelium

Song, A., Phandthong, R., & Talbot, P. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1258975 · Cited by 2

In silico evidence that substitution of glycine for valine (p.G8V) in a common variant of TMPRSS2 isoform 1 increases accessibility to an endocytic signal: implication for SARS-CoV-2 entry into host cells and susceptibility to COVID-19.

Calcagnile, M., Damiano, F., Lobreglio, G., Siculella, L., Bozzetti, M., Forgez, P., Malgoyre, A., Libert, N., Bucci, C., Alifano, M., et al. (2024) · Biochimie · doi:10.1016/j.biochi.2024.05.004 · Cited by 3

Dexamethasone disrupts intracellular pH homeostasis to delay coronavirus infectious bronchitis virus cell entry via sodium hydrogen exchanger 3 activation

Dai, J., Feng, Y., Long, H., Liao, Y., Tan, L., Sun, Y., Song, C., Qiu, X., & Ding, C. (2025) · Journal of Virology · doi:10.1128/jvi.01894-24 · Cited by 3

Inhibition of the Clathrin Terminal Domain—Amphiphysin Protein–Protein Interaction. Probing the Pitstop 2 Aromatic Moiety

Prichard, K. L., Robertson, M. J., Chau, N., Xue, J., Neuenschwander, M., Fink, U., Horatscheck, A., Nazaré, M., Robinson, P. J., Haucke, V., et al. (2025) · ChemMedChem · doi:10.1002/cmdc.202500321 · Cited by 3

Evolution of the SARS-CoV-2 spike protein in utilizing host transmembrane serine proteases

Milewska, A., Cofas‐Vargas, L. F., Poma, A. B., & Pyrć, K. (2025) · iScience · doi:10.1016/j.isci.2025.113318 · Cited by 5

Zebrafish as a model for SARS-CoV-2 infection, pathogenesis, transmission, and drug screening

Ravindran, C., & Mukherjee, S. (2025) · Virology · doi:10.1016/j.virol.2025.110662 · Cited by 3

The localization and function of the moonlighting protein Clathrin during oocyte maturation

Camia, B., Longo, M., Bergonzi, A., Dezza, I., Biggiogera, M., Redi, C. A., Casasco, A., & Monti, M. (2024) · Developmental Biology · doi:10.1016/j.ydbio.2024.09.001 · Cited by 3

The Proton‐Activated Chloride Channel Inhibits SARS‐CoV‐2 Spike Protein‐Mediated Viral Entry Through the Endosomal Pathway

Koylass, N., Sachithanandham, J., Osei‐Owusu, J., Chen, K. H., Cheng, Y., Pekosz, A. S., & Qiu, Z. (2025) · Journal of Cellular Physiology · doi:10.1002/jcp.70063 · Cited by 3

Inhibitory effect of [6]-shogaol against 3CLpro activity and SARS-CoV-2 infection

Tanikawa, T., Hayashi, T., Kiba, Y., Kamauchi, H., Someya, Y., & Kitamura, M. (2025) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-025-05094-4 · Cited by 3

Transcriptome Analysis of Lungs in a Mouse Model of Severe COVID-19

Cohen-Gihon, I., Israeli, O., Tidhar, A., Sapoznikov, A., Evgy, Y., Stein, D., Aftalion, M., Gur, D., Orr, I., Zvi, A., et al. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.848465 · Cited by 3

Tissue‐ and cell‐expression of druggable host proteins provide insights into repurposing drugs for COVID ‐19

Li, J., Xue, Y., Wang, X., Smith, L. S., He, B., Liu, S., & Zhu, H. (2022) · Clinical and Translational Science · doi:10.1111/cts.13400 · Cited by 3

Antiparasitic Drugs against SARS-CoV-2: A Comprehensive Literature Survey

Alvarez, E. C., Dolci, M., Perego, F., Signorini, L., Parapini, S., D’Alessandro, S., Denti, L., Basilico, N., Taramelli, D., Ferrante, P., et al. (2022) · Microorganisms · doi:10.3390/microorganisms10071284 · Cited by 4

Pharmacological perturbation of intracellular dynamics as a SARS-CoV-2 antiviral strategyPreprint

Bakhache, W., Partiot, E., Lučanský, V., Bare, Y., Bonaventure, B., Goujon, C., Boriès, C., Deffieu, M. S., & Gaudin, R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.10.459410 · Cited by 3

Host kinase CSNK2 is a target for inhibition of pathogenic β-coronaviruses including SARS-CoV-2Preprint

Yang, X., Dickmander, R. J., Bayati, A., Taft-Benz, S., Smith, J. L., Wells, C. I., Madden, E. A., Brown, J. W., Lenarcic, E. M., Yount, B. L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.03.474779 · Cited by 3

ARF6 is a host factor for SARS-CoV-2 infection in vitroPreprint

Mirabelli, C., Sherman, E. J., Cunha, J. B., Wotring, J. W., Saghir, J. E., Harder, J. L., Kretzler, M., Sexton, J. Z., Emmer, B. T., & Wobus, C. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.09.495482 · Cited by 3

Calpeptin is a potent cathepsin inhibitor and drug candidate for SARS-CoV-2 infectionsPreprint

Reinke, P. Y. A., de Souza, E. E., Günther, S., Falke, S., Lieske, J., Ewert, W., Loboda, J., Herrmann, A., Mashhour, A. R., Karničar, K., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2450926/v1 · Cited by 3

Nanotechnology-Driven Strategy Against SARS-CoV-2: Pluronic F127-Based Nanomicelles with or Without Atazanavir Reduce Viral Replication in Calu-3 Cells

Ricci‐Júnior, E., Rosa, A. D. S., do Nascimento, T., Santos‐Oliveira, R., da Silva, M. A. N., Barreto-Vieira, D. F., Batista, L. T., da Conceição, G. B., Quintão, T. A. N., Ferreira, V. N. S., et al. (2025) · Viruses · doi:10.3390/v17040518 · Cited by 3

Combined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosis

Maestro, A., Zaccai, N. R., Gonzalez-Martinez, J. F., Sánchez-Puga, P., Tajuelo, J., Rubio, M. A., Santamaría, A., Carrascosa-Tejedor, J., Pereira, D., Marín-Montesinos, I., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08597-5 · Cited by 3

SARS-CoV-2 spike triggers TLR7-dependent endolysosome dysfunction and senescence in human astrocytes

Hasler, W. A., McKay, E., Datta, G., Johnson, S., Rezagholizadeh, N., & Chen, X. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03586-1 · Cited by 2

A novel host-targeted inhibitor of clathrin-mediated endocytosis limits spring viremia of carp virus infection

Liu, L., Zhou, Y., Wang, H., Hu, Y., & Chen, J. K. (2026) · mBio · doi:10.1128/mbio.00453-26 · Cited by 2

The Essential Role of Sorting Nexin 5 in Virus-Induced Autophagy

Li, D.-Y., Wen, J.-H., Liang, S., & Tang, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.947384 · Cited by 2

CLN7/MFSD8 may be an important factor for SARS-CoV-2 cell entry

Heinl, E.-S., Lorenz, S., Schmidt, B., Laqtom, N. N., Mazzulli, J. R., Francelle, L., Yu, T. W., Greenberg, B. M., Storch, S., Tegtmeier, I., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105082 · Cited by 3

Maternal Fever and Reduced Fetal Movement as Predictive Risk Factors for Adverse Neonatal Outcome in Cases of Congenital SARS-CoV-2 Infection: A Meta-Analysis of Individual Participant Data from Case Reports and Case Series

Bernad, E. S., Duică, F., Antoniadis, P., Moza, A., Lungeanu, D., Craina, M. L., Bernad, B.-C., Maghet, E., Vasilache, I.-A., Maghiari, A. L., et al. (2023) · Viruses · doi:10.3390/v15071615 · Cited by 2

Bridging the Gap: Can COVID-19 Research Help Combat African Swine Fever?

Pakotiprapha, D., Kuhaudomlarp, S., Tinikul, R., & Chanarat, S. (2023) · Viruses · doi:10.3390/v15091925 · Cited by 3

The cross-talk study between immune system and SARS-CoV-2

Alamer, E. (2023) · Journal Of Advanced Pharmacy Education And Research · doi:10.51847/8u5axm8acl · Cited by 2

Sequestration of membrane cholesterol by cholesterol-binding proteins inhibits SARS-CoV-2 entry into Vero E6 cells

Kulma, M., Šakanović, A., Zavec, A. B., Caserman, S., Omersa, N., Šolinc, G., Orehek, S., Hafner‐Bratkovič, I., Kuhar, U., Slavec, B., et al. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.149954 · Cited by 2

Inhibition of endocytic uptake of severe acute respiratory syndrome coronavirus 2 and endo-lysosomal acidification by diphenoxylate

Shin, J. S., Jang, Y., Kim, D., Jung, E., Lee, M. K., Kim, B., Ahn, S., Shin, Y., Jang, S. S., Yun, C. S., et al. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00341-24 · Cited by 2

Cortactin: A major cellular target of viral, protozoal, and fungal pathogens

Sharafutdinov, I., Friedrich, B., Rottner, K., Backert, S., & Tegtmeyer, N. (2024) · Molecular Microbiology · doi:10.1111/mmi.15284 · Cited by 2

Bacterial Membrane Vesicles as a Novel Vaccine Platform against SARS-CoV-2

Çolak, Ç. Y. (2024) · Current Microbiology · doi:10.1007/s00284-024-03846-y · Cited by 2

Kinetic Landscape of Single Virus-like Particles Highlights the Efficacy of SARS-CoV-2 Internalization

Atemin, A., Ivanova, A., Peppel, W., Stamatov, R., Gallegos, R., Durden, H., Uzunova, S., Vershinin, M. D., Saffarian, S., & Stoynov, S. (2024) · Viruses · doi:10.3390/v16081341 · Cited by 2

RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis

Qin, W., Kong, N., Xie, S., Liu, H., Yang, X., Wang, Y., Cao, X., Liu, Y., Wang, J., Sun, H., et al. (2025) · Journal of Virology · doi:10.1128/jvi.01760-24 · Cited by 4

SARS-CoV-2 infection of human cortical cells is influenced by the interaction between aneuploidy and biological sex: insights from a Down syndrome in vitro model

Lioudyno, M., Sevrioukov, E. A., Olivarria, G. M., Hitchcock, L., Javonillo, D. I., Campos, S. M., Rivera, I., Wright, S. T., Head, E., Fortea, J., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02895-2 · Cited by 3

SARS-CoV-2 infection enhancement by amphotericin B: implications for disease management

Nguyen, D. V., Laidlaw, S. M., Dong, X., Wand, M. E., Horton, A., Sutton, M., Tree, J. A., Milligan, R., Erdmann, M., Matthews, D. A., et al. (2025) · Journal of Virology · doi:10.1128/jvi.00519-25 · Cited by 2

SARS-CoV-2 pseudoparticles preferentially infect ectoderm in human embryonic tissues

Song, A., & Talbot, P. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1733662 · Cited by 1

Targeting Natural Plant Metabolites for Hunting SARS-CoV-2 Omicron BA.1 Variant Inhibitors: Extraction, Molecular Docking, Molecular Dynamics, and Physicochemical Properties Study

Hassan, H. A., Hassan, A. R., Mohamed, E. A. R., Al-Khdhairawi, A. A. Q., Taha, H. E., El-Tantawy, H. M., Abdel-Rahman, I. A. M., Raslan, A. E., Allemailem, K. S., Almatroudi, A., et al. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44100342 · Cited by 2

Cellular and Molecular Mechanisms of Pathogenic and Protective Immune Responses to SARS-CoV-2 and Implications of COVID-19 Vaccines

Akbar, S. M. F., Mahtab, M. A., & Khan, S. (2023) · Vaccines · doi:10.3390/vaccines11030615 · Cited by 2

Macropinocytosis and SARS-CoV-2 cell entry

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Yadav, M., Dhakla, P., Rawat, R., Dahiya, M., & Kumar, A. (2023) · Springer eBooks · doi:10.1007/978-981-19-5399-6_24 · Cited by 1

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Karim, M., Saul, S., Ghita, L., Sahoo, M. K., Ye, C., Bhalla, N., Jin, J., Park, J., Martínez-Gualda, B., East, M. P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.18.484178 · Cited by 1

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Inoue, Y., Tanaka, N., Tanaka, Y., Inoue, S., Morita, K., Zhuang, M., Hattori, T., & Sugamura, K. (2007) · Journal of Virology · doi:10.1128/jvi.00253-07 · Cited by 369

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Wang, H., Yang, P., Liu, K., Guo, F., Zhang, Y., Zhang, G., & Jiang, C. (2008) · Cell Research · doi:10.1038/cr.2008.15 · Cited by 700

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