The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses
Open accessPublished version of a preprint
Abstract
Over the past 20 years, several coronaviruses have crossed the species barrier into humans, causing outbreaks of severe, and often fatal, respiratory illness. Since SARS-CoV was first identified in animal markets, global viromics projects have discovered thousands of coronavirus sequences in diverse animals and geographic regions. Unfortunately, there are few tools available to functionally test these viruses for their ability to infect humans, which has severely hampered efforts to predict the next zoonotic viral outbreak. Here, we developed an approach to rapidly screen lineage B betacoronaviruses, such as SARS-CoV and the recent SARS-CoV-2, for receptor usage and their ability to infect cell types from different species. We show that host protease processing during viral entry is a significant barrier for several lineage B viruses and that bypassing this barrier allows several lineage B viruses to enter human cells through an unknown receptor. We also demonstrate how different lineage B viruses can recombine to gain entry into human cells, and confirm that human ACE2 is the receptor for the recently emerging SARS-CoV-2.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The S protein mediates binding of coronaviruses to angiotensin converting enzyme 2 (ACE2) on the surface of various cell types including epithelial cells of the pulmonary alveolus (4–6).”
From An Alphavirus -derived replicon RNA vaccine induces SARS-CoV-2 neutralizing antibody and T cell responses in mice and nonhuman primates (2020) · cites this paper as [5]
Experimental — accuracy not yet measuredIn the citing paper
“it directly interacts with the cellular receptor angiotensin converting enzyme 2 (ACE2) which mediates host cell entry”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Letko et al., 2020
In the citing paper
“SARS-CoV-2 is a single-stranded RNA β-coronavirus and a member of the subgenus Sarbecovirus (beta-CoV lineage B).”
From Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection (2020) · cites this paper as Letko et al., 2020
In the citing paper
“It is the seventh member of the Coronaviridae known to infect humans so far, two of which, SARS-CoV and MERS-CoV, caused global health threats previously (Guarner, 2020; Letko et al., 2020).”
From Oral Microbiome and SARS-CoV-2: Beware of Lung Co-infection (2020) · cites this paper as Letko et al., 2020
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
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
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740
Bats Are Natural Reservoirs of SARS-Like Coronaviruses
Li, W., Shi, Z., Yu, M., Ren, W., Smith, C. S., Epstein, J. H., Wang, H., Crameri, G. S., Hú, Z., Zhang, H., et al. (2005) · Science · doi:10.1126/science.1118391 · Cited by 2,571
Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
Raj, V. S., Mou, H., Smits, S. L., Dekkers, D. H. W., Müller, M. A., Dijkman, R., Muth, D., Demmers, J. A. A., Zaki, A., Fouchier, R. A. M., et al. (2013) · Nature · doi:10.1038/nature12005 · Cited by 2,061
Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
Li, F., Li, W., Farzan, M., & Harrison, S. C. (2005) · Science · doi:10.1126/science.1116480 · Cited by 2,035
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778
Severe acute respiratory syndrome coronavirus-like virus in Chinese horseshoe bats
Lau, S. K. P., Woo, P. C. Y., Li, K. S. M., Huang, Y. P., Tsoi, H., Wong, B. H. L., Wong, S. S. Y., Leung, S.-Y., Chan, K., & Yuen, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506735102 · Cited by 1,561
Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,076
Cited by
Sorted by citations
Items 701–800 of 1,005
Potential of SARS-CoV-2 to Cause CNS Infection: Biologic Fundamental and Clinical Experience
Huang, J., Zheng, M., Tang, X., Chen, Y., Tong, A., & Zhou, L. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.00659 · Cited by 50
SARS-CoV-2 Molecular Network Structure
Dı́az, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00870 · Cited by 49
On the road to ending the COVID-19 pandemic: Are we there yet?
Case, J. B., Winkler, E. S., Errico, J. M., & Diamond, M. (2021) · Virology · doi:10.1016/j.virol.2021.02.003 · Cited by 47
Mandolesi, M., Sheward, D. J., Hanke, L., Ma, J., Pushparaj, P., Vidakovics, L. P., Kim, C., Ádori, M., Lenart, K., Loré, K., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100252 · Cited by 46
Huang, L., Yuen, T. T., Ye, Z., Liu, S., Zhang, G., Chu, H., & Yue, J. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00584-6 · Cited by 50
Immunopathology and Immunopathogenesis of COVID-19, what we know and what we should learn
Shahgolzari, M., Yavari, A., Arjeini, Y., Miri, S. M., Darabi, A., Nejad, A. S. M., & Keshavarz, M. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101417 · Cited by 50
Crowley, A. R., Natarajan, H., Hederman, A. P., Bobak, C. A., Weiner, J. A., Wieland-Alter, W., Lee, J., Bloch, E. M., Tobian, A. A. R., Redd, A. D., et al. (2022) · eLife · doi:10.7554/elife.75228 · Cited by 51
Host–Pathogen Interactions Influencing Zoonotic Spillover Potential and Transmission in Humans
Escudero-Pérez, B., Lalande, A., Mathieu, C., & Lawrence, P. (2023) · Viruses · doi:10.3390/v15030599 · Cited by 56
Diagnostics and analysis of SARS-CoV-2: current status, recent advances, challenges and perspectives
Dong, T., Wang, M., Liu, J., Ma, P., Pang, S., Liu, W., & Liu, A. (2023) · Chemical Science · doi:10.1039/d2sc06665c · Cited by 50
Mosaic sarbecovirus nanoparticles elicit cross-reactive responses in pre-vaccinated animals
Cohen, A. A., Keeffe, J. R., Schiepers, A., Dross, S., Greaney, A. J., Rorick, A. V., Gao, H., Gnanapragasam, P. N. P., Fan, C., West, A. P., et al. (2024) · Cell · doi:10.1016/j.cell.2024.07.052 · Cited by 51
Ghaffari, S., Roshanravan, N., Tutunchi, H., Ostadrahimi, A., Pouraghaei, M., & Kafil, B. (2020) · Archives of Medical Research · doi:10.1016/j.arcmed.2020.04.006 · Cited by 50
Petushkova, A. I., & Zamyatnin, A. A. (2020) · Pharmaceuticals · doi:10.3390/ph13100277 · Cited by 50
Huang, S., & Wang, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063060 · Cited by 50
Ellis, D., Brunette, N., Crawford, K. H. D., Walls, A. C., Pham, M. N., Chen, C., Herpoldt, K., Fiala, B., Murphy, M., Pettie, D., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.710263 · Cited by 45
Raoufi, M., Khalili, S., Mansouri, M., Mahdavi, A., & Khalili, N. (2020) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2020.108286 · Cited by 49
Addressing the worldwide shortages of face masks
Ji, D., Li, F., Li, X., & Ramakrishna, S. (2020) · BMC Materials · doi:10.1186/s42833-020-00015-w · Cited by 49
Aghayan, H. R., Salimian, F., Abedini, A., Ghazi, S. F., Yunesian, M., Alavi-Moghadam, S., Makarem, J., Majidzadeh‐A, K., Hatamkhani, A., Moghri, M., et al. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02953-6 · Cited by 49
Human coronavirus HKU1 recognition of the TMPRSS2 host receptor
McCallum, M., Park, Y., Stewart, C., Sprouse, K. R., Addetia, A., Brown, J. T., Tortorici, M. A., Gibson, C. A., Wong, E., Ieven, M. M., et al. (2024) · Cell · doi:10.1016/j.cell.2024.06.006 · Cited by 51
Vashi, Y., Jagrit, V., & Kumar, S. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104382 · Cited by 48
Luo, Z., Ang, M. J. Y., Chan, S. Y., Yi, Z., Goh, Y. Y., Yan, S., Tao, J., Liu, K., Li, X., Zhang, H., et al. (2020) · Research · doi:10.34133/2020/6925296 · Cited by 51
Beyond Infection: Integrating Competence into Reservoir Host Prediction
Becker, D. J., Seifert, S. N., & Carlson, C. J. (2020) · Trends in Ecology & Evolution · doi:10.1016/j.tree.2020.08.014 · Cited by 49
Hsieh, W., Lin, C., Lin, T., Lin, C., Chang, H., Tsai, C.-H., Wu, H., & Lin, C. (2021) · Diagnostics · doi:10.3390/diagnostics11101760 · Cited by 49
Insight into the role of clathrin‐mediated endocytosis inhibitors in SARS‐CoV‐2 infection
Alkafaas, S. S., Abdallah, A. M., Ghosh, S. B., Loutfy, S. A., Elkafas, S. S., Fattah, N. F. A., & Hessien, M. (2022) · Reviews in Medical Virology · doi:10.1002/rmv.2403 · Cited by 53
Drug Repurposing Screens Reveal FDA Approved Drugs Active Against SARS-CoV-2Preprint
Dittmar, M., Lee, J. S., Whig, K., Segrist, E., Li, M., Jurado, K. A., Samby, K., Ramage, H. R., Schultz, D., & Cherry, S. R. (2020) · SSRN Electronic Journal · doi:10.1101/2020.06.19.161042 · Cited by 49
Gyebi, G. A., Adegunloye, A. P., Ibrahim, I. M., Ogunyemi, O. M., Afolabi, S. O., & Ogunro, O. B. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1835726 · Cited by 49
The Current Status of Drug Repositioning and Vaccine Developments for the COVID-19 Pandemic
Won, J., & Lee, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249775 · Cited by 49
Shagufta, & Ahmad, I. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113157 · Cited by 47
Bonora, B. M., Avogaro, A., & Fadini, G. P. (2021) · Journal of Endocrinological Investigation · doi:10.1007/s40618-021-01515-6 · Cited by 48
Knyazev, E. N., Nersisyan, S. A., & Tonevitsky, A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636966 · Cited by 47
Kar, S., Devnath, P., Emran, T. B., Tallei, T. E., Mitra, S., & Dhama, K. (2022) · Immunity Inflammation and Disease · doi:10.1002/iid3.604 · Cited by 42
Mechanisms of COVID-19 pathogenesis in diabetes
Narasimhulu, C. A., & Singla, D. K. (2022) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00204.2022 · Cited by 50
SARS-CoV-2 Omicron BA.1 and BA.2 are attenuated in rhesus macaques as compared to Delta
van Doremalen, N., Singh, M., Saturday, T. A., Yinda, C. K., Pérez-Pérez, L., Bohler, F., Weishampel, Z. A., Lewis, M. C., Schulz, J. E., Williamson, B. N., et al. (2022) · Science Advances · doi:10.1126/sciadv.ade1860 · Cited by 47
Self-citationThe SARS-CoV-2 spike protein binds and modulates estrogen receptors
Solís, Ó., Beccari, A. R., Iaconis, D., Talarico, C., Ruiz-Bedoya, C. A., Nwachukwu, J. C., Cimini, A., Castelli, V., Bertini, R., Montopoli, M., et al. (2022) · Science Advances · doi:10.1126/sciadv.add4150 · Cited by 56
What are the current anti-COVID-19 drugs? From traditional to smart molecular mechanisms
Aboul‐Fotouh, S., Mahmoud, A. N., Elnahas, E. M., Habib, M. Z., & Abdelraouf, S. M. (2023) · Virology Journal · doi:10.1186/s12985-023-02210-z · Cited by 54
da Silva, P. G., Mesquita, J. R., Nascimento, M. D. S. J., & Ferreira, V. A. M. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.141483 · Cited by 53
Li, N., Zhao, L., & Zhan, X. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30055 · Cited by 48
Nano-Biomimetic Drug Delivery Vehicles: Potential Approaches for COVID-19 Treatment
Witika, B. A., Makoni, P. A., Mweetwa, L. L., Ntemi, P. V., Chikukwa, M. T. R., Matafwali, S. K., Mwila, C., Mudenda, S., Katandula, J., & Walker, R. B. (2020) · Molecules · doi:10.3390/molecules25245952 · Cited by 49
Srivastava, N., Garg, P., Srivastava, P., & Seth, P. K. (2021) · PeerJ · doi:10.7717/peerj.11171 · Cited by 47
Suleman, M., Yousafi, Q., Ali, J., Ali, S. S., Hussain, Z., Ali, S., Waseem, M., Iqbal, A., Ahmad, S., Khan, A., et al. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104936 · Cited by 49
Benlarbi, M., Laroche, G., Fink, C., Fu, K., Mulloy, R. P., Phan, A., Ariana, A., Stewart, C. M., Prévost, J., Beaudoin-Bussières, G., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105316 · Cited by 51
mRNA vaccine CVnCoV protects non-human primates from SARS-CoV-2 challenge infection
Rauch, S., Gooch, K., Hall, Y., Salguero, F. J., Dennis, M. J., Gleeson, F. V., Harris, D., Ho, C., Humphries, H. E., Longet, S., et al. (2020) · doi:10.1101/2020.12.23.424138 · Cited by 48
Braz, H. L. B., Silveira, J. A. D. M., Marinho, A. D., de Moraes, M. E. A., de Moraes, M. O., Monteiro, H. S. A., & Jorge, R. J. B. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.106119 · Cited by 50
Genetic and Pathogenic Characterization of SARS-CoV-2: A Review
Bahrami, A., & Ferns, G. A. (2020) · Future Virology · doi:10.2217/fvl-2020-0129 · Cited by 49
Variations in Orf3a protein of SARS-CoV-2 alter its structure and function
Azad, G. K., & Khan, P. K. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.100933 · Cited by 47
Upadhyay, V., Lucas, A., Panja, S., Miyauchi, R., & Mallela, K. M. G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101208 · Cited by 44
A review: Antibody-dependent enhancement in COVID-19: The not so friendly side of antibodies
Sánchez‐Zuno, G. A., Matuz-Flores, M. G., González-Estévez, G., Nicoletti, F., Turrubiates‐Hernández, F. J., Mangano, K., & Muñóz-Valle, J. F. (2021) · International Journal of Immunopathology and Pharmacology · doi:10.1177/20587384211050199 · Cited by 48
Long COVID, neuropsychiatric disorders, psychotropics, present and future
Tang, S. W., Leonard, B. E., & Helmeste, D. M. (2022) · Acta Neuropsychiatrica · doi:10.1017/neu.2022.6 · Cited by 45
Israeli, M., Finkel, Y., Yahalom-Ronen, Y., Paran, N., Chitlaru, T., Israeli, O., Cohen-Gihon, I., Aftalion, M., Falach, R., Rotem, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29896-z · Cited by 46
Li, H., Zhao, C., Zhang, Y., Yuan, F., Zhang, Q., Shi, X., Zhang, L., Qin, C., & Zheng, A. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1830715 · Cited by 44
Roadmap to the Bioanalytical Testing of COVID-19: From Sample Collection to Disease Surveillance
Hosseini, A., Pandey, R., Osman, E., Victorious, A. P., Li, F., Didar, T. F., & Soleymani, L. (2020) · ACS Sensors · doi:10.1021/acssensors.0c01377 · Cited by 50
Reinhold, A., Tzankov, A., Matter, M. S., Mihic‐Probst, D., Scholl, H. P. N., & Meyer, P. (2021) · Ophthalmic Research · doi:10.1159/000514573 · Cited by 47
Multiplex Biosensing for Simultaneous Detection of Mutations in SARS-CoV-2
Xi, H., Jiang, H., Juhas, M., & Zhang, Y. (2021) · ACS Omega · doi:10.1021/acsomega.1c04024 · Cited by 48
The SARS‐CoV‐2 Spike Glycoprotein Directly Binds Exogeneous Sialic Acids: A NMR View
Unione, L., Moure, M. J., Lenza, M. P., Oyenarte, I., Ereño‐Orbea, J., Ardá, A., & Jiménez‐Barbero, J. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202201432 · Cited by 49
Tioni, M. F., Jordan, R., Pena, A. S., Garg, A., Wu, D., Phan, S. I., Weiss, C. M., Cheng, X., Greenhouse, J. J., Orekov, T., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00509-6 · Cited by 45
Ricke, D. O., & Malone, R. W. (2020) · SSRN Electronic Journal · doi:10.20944/preprints202003.0138.v1 · Cited by 48
A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike GlycoproteinPreprint
Joyce, M. G., Sankhala, R. S., Chen, W., Choe, M., Bai, H., Hajduczki, A., Yan, L., Sterling, S. L., Peterson, C. E., Green, E. C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.15.992883 · Cited by 43
Advanced drug delivery systems can assist in targeting coronavirus disease (COVID-19): A hypothesis
Mehta, M., Prasher, P., Sharma, M., Shastri, M. D., Khurana, N., Vyas, M., Dureja, H., Gupta, G., Anand, K., Satija, S., et al. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.110254 · Cited by 47
Xiong, S., Zhang, L., Qadir, A. S., Richner, J. M., Class, J., Rehman, J., & Malik, A. B. (2021) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.121.316925 · Cited by 48
Balachandran, H., Phetsouphanh, C., Agapiou, D., Adhikari, A., Rodrigo, C., Hammoud, M., Shrestha, L. B., Keoshkerian, E., Gupta, M., Turville, S. G., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110345 · Cited by 45
Dromedary camel nanobodies broadly neutralize SARS-CoV-2 variants
Hong, J., Kwon, H. J., Cachau, R., Chen, C. Z., Butay, K. J., Duan, Z., Li, D., Ren, H., Liang, T., Zhu, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201433119 · Cited by 47
Applications of carbon nanotube biosensors: Sensing the future
Ranjbari, S., Bolourinezhad, M., Kesharwani, P., Rezayi, M., & Sahebkar, A. (2024) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2024.105747 · Cited by 46
Utility of Proteomics in Emerging and Re-Emerging Infectious Diseases Caused by RNA Viruses
Sperk, M., van Domselaar, R., Murillo, J. R., Mikaeloff, F., Vinhas, B. S., Saccon, E., Sönnerborg, A. B., Singh, K. D., Gupta, S., Végvári, Á., et al. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00380 · Cited by 47
SARS-CoV-2 Antigens Expressed in Plants Detect Antibody Responses in COVID-19 Patients
Makatsa, M. S., Tincho, M. B., Wendoh, J. M., Ismail, S. D., Nesamari, R., Pêra, F. F. P. G., Beer, S., David, A., Jugwanth, S., Gededzha, M. P., et al. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.589940 · Cited by 49
Danilenko, V., Devyatkin, A., Marsova, M., Shibilova, M., Ilyasov, R. A., & Shmyrev, V. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s333887 · Cited by 54
Structure and Mutations of SARS-CoV-2 Spike Protein: A Focused Overview
Mehra, R., & Kepp, K. P. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00433 · Cited by 45
A monoclonal antibody that neutralizes SARS-CoV-2 variants, SARS-CoV, and other sarbecoviruses
Wang, P., Casner, R. G., Nair, M. S., Yu, J., Guo, Y., Wang, M., Chan, J. F., Cerutti, G., Iketani, S., Liu, L., et al. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.2011623 · Cited by 43
Mutational analysis of structural proteins of SARS-CoV-2
Jakhmola, S., Indari, O., Kashyap, D., Varshney, N., Das, A., Manivannan, E., & Jha, H. C. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e06572 · Cited by 48
The Development of SARS-CoV-2 Variants: The Gene Makes the Disease
Pérez-Gómez, R. (2021) · Journal of Developmental Biology · doi:10.3390/jdb9040058 · Cited by 47
Engineering ACE2 decoy receptors to combat viral escapability
Arimori, T., Ikemura, N., Okamoto, T., Takagi, J., Standley, D. M., & Hoshino, A. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.06.011 · Cited by 44
Shi, G., Li, T., Lai, K. K., Johnson, R. F., Yewdell, J. W., & Compton, A. A. (2024) · Nature Communications · doi:10.1038/s41467-024-45075-8 · Cited by 49
Gupta, A., & Gupta, G. S. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04107-3 · Cited by 45
Casagrande, M. K., Fitzek, A., Spitzer, M. S., Püschel, K., Glatzel, M., Krasemann, S., Aepfelbacher, M., Nörz, D. S., Lütgehetmann, M., Pfefferle, S., et al. (2021) · British Journal of Ophthalmology · doi:10.1136/bjophthalmol-2020-318618 · Cited by 43
Verma, D., Church, T. M., & Swaminathan, S. (2021) · Journal of Virology · doi:10.1128/jvi.00192-21 · Cited by 46
Application of machine learning for the diagnosis of COVID-19
Podder, P., Bharati, S., Mondal, M. R. H., & Köse, U. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-824536-1.00008-3 · Cited by 45
Jung, J., Zahmanova, G., Minkov, I. N., & Lomonossoff, G. P. (2022) · Plant Biotechnology Journal · doi:10.1111/pbi.13813 · Cited by 49
Yu, M., Zhu, Y., Li, Y., Chen, Z., Li, Z., Wang, J., Li, Z., Zhang, F., & Ding, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.884433 · Cited by 45
Expanded ACE2 dependencies of diverse SARS-like coronavirus receptor binding domains
Roelle, S. M., Shukla, N., Pham, A. T., Bruchez, A. M., & Matreyek, K. A. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001738 · Cited by 40
Luo, J., Zhu, X., Jian, J., Chen, X., & Yin, K. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa176 · Cited by 45
Burra, P., Soto-Díaz, K., Chalen, I., Gonzalez-Ricon, R., Istanto, D. D., & Caetano-Anollés, G. (2021) · Evolutionary bioinformatics online · doi:10.1177/1176934321989695 · Cited by 43
Kantarcıoğlu, B., Iqbal, O., Walenga, J. M., Lewis, B., Lewis, J., Carter, C. A., Singh, M., Lievano, F. A., Tafur, A. J., Ramacciotti, E., et al. (2021) · Clinical and Applied Thrombosis/Hemostasis · doi:10.1177/10760296211021498 · Cited by 45
Vieira, C. C., Nery, L., Martins, L. D. B. U., Jabour, L. G. P. P., Dias, R. F., & Silva, A. C. S. E. (2020) · Current Drug Targets · doi:10.2174/1389450121666201020154033 · Cited by 46
Jafarzadeh, A., Nemati, M., Saha, B., Bansode, Y. D., & Jafarzadeh, S. (2020) · Viral Immunology · doi:10.1089/vim.2020.0076 · Cited by 57
Overview of Targets and Potential Drugs of SARS-CoV-2 According to the Viral Replication
Zhang, Y., & Tang, L. V. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00526 · Cited by 50
Brierley, L., & Fowler, A. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009149 · Cited by 44
Studying SARS-CoV-2 infectivity and therapeutic responses with complex organoids
Chen, K. G., Park, K., & Spence, J. R. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00721-x · Cited by 45
Longitudinal Systemic and Mucosal Immune Responses to SARS-CoV-2 Infection
Wright, P. F., Prevost-Reilly, A., Natarajan, H., Brickley, E. B., Connor, R. I., Wieland‐Alter, W., Miele, A. S., Weiner, J. A., Nerenz, R. D., & Ackerman, M. E. (2022) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiac065 · Cited by 44
Zhavoronkov, A. A., Zagribelnyy, B. A., Zhebrak, A., Aladinskiy, V., Terentiev, V. A., Vanhaelen, Q., Bezrukov, D. S., Polykovskiy, D. A., Shayakhmetov, R., Filimonov, A., et al. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12301457.v1 · Cited by 44
Valyaeva, A. A., Zharikova, A. A., Kasianov, A. S., Vassetzky, Y. S., & Sheval, E. V. (2020) · Scientific Reports · doi:10.1038/s41598-020-74598-5 · Cited by 46
D’Errico, S., Zanon, M., Montanaro, M., Radaelli, D., Sessa, F., Mizio, G. D., Montana, A., Corrao, S., Salerno, M., & Pomara, C. (2020) · Microorganisms · doi:10.3390/microorganisms8111642 · Cited by 42
Gut Dysbiosis during COVID-19 and Potential Effect of Probiotics
Hung, Y., Lee, C., Lee, J., Tsai, P.-J., & Ko, W. (2021) · Microorganisms · doi:10.3390/microorganisms9081605 · Cited by 45
Impact of COVID 19 on erectile function
Adeyemi, D. H., Odetayo, A. F., Hamed, M. A., & Akhigbe, R. E. (2022) · The Aging Male · doi:10.1080/13685538.2022.2104833 · Cited by 45
Thapaliya, K., Marshall‐Gradisnik, S., Barth, M., Eaton-Fitch, N., & Barnden, L. R. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1125208 · Cited by 50
Clark, J. J., Hoxie, I., Adelsberg, D. C., Sapse, I. A., Andreata‐Santos, R., Yong, J. S., Amanat, F., Tcheou, J., Raskin, A. J., Singh, G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114922 · Cited by 43
Review of COVID‐19 and male genital tract
Hesari, F. S., Hosseinzadeh, S. S., & Sardroud, M. A. A. M. (2020) · Andrologia · doi:10.1111/and.13914 · Cited by 43
DPP-4 inhibition and COVID-19: From initial concerns to recent expectations
Scheen, A. J. (2020) · Diabetes & Metabolism · doi:10.1016/j.diabet.2020.11.005 · Cited by 43
Application of lung microphysiological systems to COVID-19 modeling and drug discovery: a review
Sun, A., Hoffman, T., Luu, B. Q., Ashammakhi, N. A., & Li, S. (2021) · Bio-Design and Manufacturing · doi:10.1007/s42242-021-00136-5 · Cited by 42
Wu, D., Kolesnikov, A. V., Yin, R. M., Guest, J. D., Gowthaman, R., Shmelev, A., Serdyuk, Y. V., Dianov, D. V., Efimov, G. A., Pierce, B. G., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27669-8 · Cited by 45
Cong, Y., Feng, Y., Ni, H., Zhi, F., Miao, Y., Fang, B., Zhang, L., & Zhang, J. Z. H. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00241 · Cited by 40
Xu, J., Huang, C., Fan, G., Liu, Z., Shang, L., Zhou, F., Wang, Y., Yu, J., Yang, L., Xie, K., et al. (2020) · Frontiers of Medicine · doi:10.1007/s11684-020-0800-y · Cited by 42
Riley, T. P., Chou, H., Hu, R., Bzymek, K. P., Correia, A. R., Partin, A. C., Li, D., Gong, D., Wang, Z., Yu, X., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.660198 · Cited by 43
Metadata
- Authors
- Letko, M., Marzi, A., & Munster, V.
- Affiliations
- National Institutes of Health (US)
- National Institute of Allergy and Infectious Diseases (US)
- Corresponding author
- Letko, Michael
- Munster, Vincent
- Venue
- Nature Microbiology
- Published
- 2020-02-24
- Volume
- 5
- Issue
- 4
- Pages
- 562-569
- ISSN
- 2058-5276 (ISSN-L)
- PMC
- PMC7095430
- OpenAlex
- W3008394341
- Cited by
- 3,109
- References
- 38
- Citations by year
- 2026: 47 · 2025: 122 · 2024: 198 · 2023: 287 · 2022: 571 · 2021: 874 · 2020: 1002
- FWCI
- 89.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Microbiology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Chinese Center for Disease Control and Prevention
- Chinese Academy of Medical Sciences
- Peking Union Medical College
- National Institute of Allergy and Infectious Diseases
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Zoonotic diseases and public health
- Keywords
- SARS-CoV-2, SARS-CoV, cell entry, ACE2 receptor, zoonotic transmission, viral recombination, cross-species infection
- MeSH terms
- Protein Domains, Betacoronavirus, Receptors, Coronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Cell Line, Humans, Peptidyl-Dipeptidase A, Mutation, Pneumonia, Viral, Receptors, Virus, Recombinant Fusion Proteins, Trypsin, Coronavirus Infections, Dipeptidyl Peptidase 4, CD13 Antigens, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Pandemics, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
