Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

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 · see citing works

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works

<i>Coot</i> : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works

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 · see citing works

Epidemiological and clinical characteristics of 99 cases of 2019 novel Coronavirus pneumonia in Wuhan, China: a descriptive study.

Chen, N., Zhou, M., Dong, X., Qu, J., Gong, F., Han, Y., Qiu, Y., Wang, J., Liu, Y., Wei, Y., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30211-7 · Cited by 21,415 · see citing works

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 · see citing works

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

Li, Q., Guan, X., Wu, P., Wang, X., Zhou, L., Tong, Y., Ren, R., Leung, K. S. M., Lau, E. H. Y., Wong, J. Y., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001316 · Cited by 16,575 · see citing works

Comparative Protein Modelling by Satisfaction of Spatial Restraints

Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977 · see citing works

Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding

Lu, R., Zhao, X., Li, J., Niu, P., Yang, B., Wu, H., Wang, W., Song, H., Huang, B., Zhu, N., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30251-8 · Cited by 11,907 · see citing works

A new coronavirus associated with human respiratory disease in China

Wu, F., Zhao, S., Yu, B., Chen, Y.-M., Wang, W., Song, Z.-G., Hu, Y., Tao, Z.-W., Tian, J.-H., Pei, Y.-Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2008-3 · Cited by 11,688 · see citing works

cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination

Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works

A familial cluster of pneumonia associated with the 2019 novel coronavirus indicating person-to-person transmission: a study of a family cluster

Chan, J., Yuan, S.-F., Kok, K.-H., To, K., Chu, H., Yang, J., Xing, F., Liu, J.-L., Yip, C., Poon, R., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30154-9 · Cited by 8,450 · see citing works

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 · see citing works

<i>PHENIX</i> : building new software for automated crystallographic structure determination

Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361 · see citing works

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

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

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 · see citing works

ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps

Croll, T. (2018) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798318002425 · Cited by 1,934 · see citing works

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

Coutard, B., Valle, C., de Lamballerie, X. N., Canard, B., Seidah, N. G., & Decroly, É. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104742 · Cited by 1,685 · see citing works

The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex

Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489 · see citing works

Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody

Tian, X., Li, C., Huang, A., Xia, S., Lu, S., Shi, Z., Lu, L., Jiang, S., Yang, Z., Wu, Y., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1729069 · Cited by 1,239 · see citing works

Evidence that TMPRSS2 Activates the Severe Acute Respiratory Syndrome Coronavirus Spike Protein for Membrane Fusion and Reduces Viral Control by the Humoral Immune Response

Glowacka, I., Bertram, S., Müller, M. A., Allen, P. W., Soilleux, E. J., Pfefferle, S., Steffen, I., Tsegaye, T. S., He, Y., Gnirß, K., et al. (2011) · Journal of Virology · doi:10.1128/jvi.02232-10 · Cited by 1,109 · see citing works

Collaboration gets the most out of software

Morin, A., Eisenbraun, B., Key, J., Sanschagrin, P. C., Timony, M. A., Ottaviano, M., & Piotr Sliz, A. (2013) · eLife · doi:10.7554/elife.01456 · Cited by 1,095 · see citing works

Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen

Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073 · see citing works

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

Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,073 · see citing works

Real-time cryo–EM data pre-processing with Warp

Tegunov, D., & Cramer, P. (2018) · Nature Methods · doi:10.1038/s41592-019-0580-y · Cited by 923 · see citing works

cisTEM, user-friendly software for single-particle image processing

Grant, T. S., Rohou, A. L., & Grigorieff, N. (2018) · eLife · doi:10.7554/elife.35383 · Cited by 879 · see citing works

Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2

Song, W., Gui, M., Wang, X., & Xiang, Y. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007236 · Cited by 842 · see citing works

Pre-fusion structure of a human coronavirus spike protein

Kirchdoerfer, R. N., Cottrell, C. A., Wang, N., Pallesen, J., Yassine, H. M., Turner, H. L., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2016) · Nature · doi:10.1038/nature17200 · Cited by 765 · see citing works

Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains

Yuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., et al. (2017) · Nature Communications · doi:10.1038/ncomms15092 · Cited by 761 · see citing works

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582 · see citing works

Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding

Gui, M., Song, W., Zhou, H., Xu, J., Chen, S., Xiang, Y., & Wang, X. (2016) · Cell Research · doi:10.1038/cr.2016.152 · Cited by 577 · see citing works

Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion

Walls, A. C., Tortorici, M. A., Snijder, J., Xiong, X., Bosch, B., Rey, F. A., & Veesler, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708727114 · Cited by 539 · see citing works

Structure of the Hemagglutinin Precursor Cleavage Site, a Determinant of Influenza Pathogenicity and the Origin of the Labile Conformation

Chen, J., Lee, K. H., Steinhauer, D. A., Stevens, D. J., Skehel, J. J., & Wiley, D. C. (1998) · Cell · doi:10.1016/s0092-8674(00)81771-7 · Cited by 476 · see citing works

Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis

Kirchdoerfer, R. N., Wang, N., Pallesen, J., Wrapp, D., Turner, H. L., Cottrell, C. A., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2018) · Scientific Reports · doi:10.1038/s41598-018-34171-7 · Cited by 466 · see citing works

Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

Walls, A. C., Tortorici, M. A., Frenz, B., Snijder, J., Li, W., Rey, F. A., DiMaio, F., Bosch, B., & Veesler, D. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3293 · Cited by 415 · see citing works

Leginon: an automated system for acquisition of images from vitreous ice specimens.

Carragher, B., Kisseberth, N., Kriegman, D., Milligan, R., Potter, C., Pulokas, J., & Reilein, A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4314 · Cited by 334 · see citing works

Cathepsin L Functionally Cleaves the Severe Acute Respiratory Syndrome Coronavirus Class I Fusion Protein Upstream of Rather than Adjacent to the Fusion Peptide

Bosch, B., Bartelink, W., & Rottier, P. J. M. (2008) · Journal of Virology · doi:10.1128/jvi.00415-08 · Cited by 315 · see citing works

Structure of Severe Acute Respiratory Syndrome Coronavirus Receptor-binding Domain Complexed with Neutralizing Antibody

Prabakaran, P., Gan, J., Feng, Y., Zhu, Z., Choudhry, V., Xiao, X., Ji, X., & Dimitrov, D. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600697200 · Cited by 232 · see citing works

Structural Basis of Neutralization by a Human Anti-severe Acute Respiratory Syndrome Spike Protein Antibody, 80R

Hwang, W. C., Lin, Y., Santelli, E., Sui, J., Jaroszewski, L., Stec, B., Farzan, M., Marasco, W. A., & Liddington, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603275200 · Cited by 203 · see citing works

Automatic local resolution-based sharpening of cryo-EM maps

Ramírez-Aportela, E., Vilas, J. L., Glukhova, A., Melero, R., Conesa, P., Martínez, M., Maluenda, D., Mota, J., Jiménez, A., Vargas, J., et al. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz671 · Cited by 130 · see citing works

The 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation

Wrapp, D., & McLellan, J. S. (2019) · Journal of Virology · doi:10.1128/jvi.00923-19 · Cited by 104 · see citing works

Publisher Correction: Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis

Kirchdoerfer, R. N., Wang, N., Pallesen, J., Wrapp, D., Turner, H. L., Cottrell, C. A., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2018) · Scientific Reports · doi:10.1038/s41598-018-36918-8 · Cited by 98 · see citing works

Safety and Efficacy of the BNT162b2 mRNA Covid-19 Vaccine

Polack, F. P., Thomas, S. J., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Perez, J. L., Pérez Marc, G., Moreira, E. D., Zerbini, C., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2034577 · Cited by 14,592 · see citing works

UCSF ChimeraX : Structure visualization for researchers, educators, and developers

Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,327 · see citing works

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

Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586 · see citing works

Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983 · see citing works

Multidisciplinary research priorities for the COVID-19 pandemic: a call for action for mental health science

Holmes, E. A., O'Connor, R. C., Perry, V. H., Tracey, I., Wessely, S., Arseneault, L., Ballard, C., Christensen, H., Cohen Silver, R., Everall, I., et al. (2020) · The Lancet Psychiatry · doi:10.1016/s2215-0366(20)30168-1 · Cited by 5,715 · see citing works

Characteristics of SARS-CoV-2 and COVID-19

Hu, B., Guo, H., Zhou, P., & Shi, Z.-L. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00459-7 · Cited by 5,291 · see citing works

The proximal origin of SARS-CoV-2

Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C., & Garry, R. F. (2020) · Nature Medicine · doi:10.1038/s41591-020-0820-9 · Cited by 5,081 · see citing works

Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q. (2020) · Science · doi:10.1126/science.abb2762 · Cited by 4,950 · see citing works

The trinity of COVID-19: immunity, inflammation and intervention

Tay, M. Z., Poh, C. M., Rénia, L., MacAry, P. A., & Ng, L. F. P. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-0311-8 · Cited by 4,360 · see citing works

Association of cardiac injury with mortality in hospitalized patients with COVID-19 in Wuhan, China

Shi, S., Qin, M., Shen, B., Cai, Y., Liu, T., Yang, F., Gong, W., Liu, X., Liang, J., Zhao, Q., et al. (2020) · JAMA Cardiology · doi:10.1001/jamacardio.2020.0950 · Cited by 4,349 · see citing works

Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus

Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281 · see citing works

Epidemiology of COVID-19 Among Children in China

Dong, Y., Mo, X., Hu, Y., Qi, X., Jiang, F., Jiang, Z., & Tong, S. (2020) · PEDIATRICS · doi:10.1542/peds.2020-0702 · Cited by 4,130 · see citing works

Structural basis of receptor recognition by SARS-CoV-2

Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · see citing works

An mRNA Vaccine against SARS-CoV-2 — Preliminary Report

Jackson, L. A., Anderson, E. J., Rouphael, N. G., Roberts, P. C., Makhene, M., Coler, R. N., McCullough, M. P., Chappell, J. D., Denison, M. R., Stevens, L. J., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2022483 · Cited by 3,237 · see citing works

Extrapulmonary manifestations of COVID-19

Gupta, A., Madhavan, M. V., Sehgal, K., Nair, N., Mahajan, S., Sehrawat, T. S., Bikdeli, B., Ahluwalia, N., Ausiello, J. C., Wan, E. Y., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0968-3 · Cited by 3,185 · see citing works

Cell entry mechanisms of SARS-CoV-2

Shang, J., Wan, Y., Luo, C., Ye, G., Geng, Q., Auerbach, A., & Li, F. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003138117 · Cited by 3,142 · see citing works

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

Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.045 · Cited by 2,892 · see citing works

Immunological memory to SARS-CoV-2 assessed for up to 8 months after infection.

Dan, J. M., Mateus, J., Kato, Y., Hastie, K. M., Yu, E. D., Faliti, C. E., Grifoni, A., Ramirez, S. I., Haupt, S., Frazier, A., et al. (2021) · Science · doi:10.1126/science.abf4063 · Cited by 2,656 · see citing works

RNA-Based COVID-19 Vaccine BNT162b2 Selected for a Pivotal Efficacy Study

Walsh, E. E., Frenck, R., Falsey, A. R., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Neuzil, K., Mulligan, M. J., Bailey, R., et al. (2020) · doi:10.1101/2020.08.17.20176651 · Cited by 2,615 · see citing works

Transmission routes of 2019-nCoV and controls in dental practice

Peng, X., Xu, X., Li, Y., Cheng, L., Zhou, X., & Ren, B. (2020) · International Journal of Oral Science · doi:10.1038/s41368-020-0075-9 · Cited by 2,436 · see citing works

Systematic review of COVID‐19 in children shows milder cases and a better prognosis than adults

Ludvigsson, J. F. (2020) · Acta Paediatrica · doi:10.1111/apa.15270 · Cited by 2,313 · see citing works

SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues

Ziegler, C. G. K., Allon, S. J., Nyquist, S. K., Mbano, I. M., Miao, V. N., Tzouanas, C. N., Cao, Y., Yousif, A. S., Bals, J., Hauser, B. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.035 · Cited by 2,284 · see citing works

Evidence of the COVID-19 virus targeting the CNS: tissue distribution, host-virus interaction, and proposed neurotropic mechanisms

Baig, A. M., Khaleeq, A., Ali, U., & Syeda, H. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00122 · Cited by 2,207 · see citing works

Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19

Huang, Y., Yang, C., Xu, X.-F., Xü, W., & Liu, S. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0485-4 · Cited by 2,207 · see citing works

Inhibition of SARS-CoV-2 Infections in Engineered Human Tissues Using Clinical-Grade Soluble Human ACE2

Monteil, V., Kwon, H., Prado, P., Hagelkrüys, A., Wimmer, R. A., Stahl, M., Leopoldi, A., Garreta, E., Hurtado del Pozo, C., Prosper, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.004 · Cited by 2,122 · see citing works

Renin-angiotensin-aldosterone system inhibitors in patients with Covid-19

Vaduganathan, M., Vardeny, O., Michel, T., McMurray, J. J. V., Pfeffer, M. A., & Solomon, S. D. (2020) · New England Journal of Medicine · doi:10.1056/nejmsr2005760 · Cited by 2,101 · see citing works

SARS-CoV-2 vaccines in development

Krammer, F. (2020) · Nature · doi:10.1038/s41586-020-2798-3 · Cited by 2,098 · see citing works

Nervous system involvement after infection with COVID-19 and other coronaviruses

Wu, Y., Xu, X., Chen, Z., Duan, J., Hashimoto, K., Yang, L., Liu, C., & Yang, C. (2020) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2020.03.031 · Cited by 2,046 · see citing works

Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding

Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956 · see citing works

Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity

Cantuti-Castelvetri, L., Ojha, R., Pedro, L. D., Djannatian, M., Franz, J., Kuivanen, S., van der Meer, F., Kallio, K., Kaya, T., Anastasina, M., et al. (2020) · Science · doi:10.1126/science.abd2985 · Cited by 1,925 · see citing works

Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody

Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885 · see citing works

Angiotensin-Converting Enzyme 2: SARS-CoV-2 Receptor and Regulator of the Renin-Angiotensin System: Celebrating the 20th Anniversary of the Discovery of ACE2

Gheblawi, M., Wang, K., Viveiros, A., Nguyen, Q., Zhong, J.-C., Turner, A. J., Raizada, M. K., Grant, M. B., & Oudit, G. Y. (2020) · Circulation Research · doi:10.1161/circresaha.120.317015 · Cited by 1,882 · see citing works

Adaptive immunity to SARS-CoV-2 and COVID-19

Sette, A., & Crotty, S. (2021) · Cell · doi:10.1016/j.cell.2021.01.007 · Cited by 1,860 · see citing works

A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells

Hoffmann, M., Kleine-Weber, H., & Pöhlmann, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.022 · Cited by 1,852 · see citing works

Rapid Detection of COVID-19 Causative Virus (SARS-CoV-2) in Human Nasopharyngeal Swab Specimens Using Field-Effect Transistor-Based Biosensor

Seo, G., Lee, G., Kim, M. J., Baek, S.-H., Choi, M., Ku, K. B., Lee, C., Jun, S., Park, D., Kim, H. G., et al. (2020) · ACS Nano · doi:10.1021/acsnano.0c02823 · Cited by 1,838 · see citing works

A serological assay to detect SARS-CoV-2 seroconversion in humans

Amanat, F., Stadlbauer, D., Strohmeier, S., Nguyen, T. H. O., Chromikova, V., McMahon, M., Jiang, K., Arunkumar, G. A., Jurczyszak, D., Polanco, J., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0913-5 · Cited by 1,769 · see citing works

Diagnosing COVID-19: The Disease and Tools for Detection

Udugama, B. N., Kadhiresan, P., Kozlowski, H. N., Malekjahani, A., Osborne, M., Li, V. Y. C., Chen, H., Mubareka, S., Gubbay, J. B., & Chan, W. C. W. (2020) · ACS Nano · doi:10.1021/acsnano.0c02624 · Cited by 1,763 · see citing works

Human neutralizing antibodies elicited by SARS-CoV-2 infection

Ju, B., Zhang, Q., Ge, J., Wang, R., Sun, J., Ge, X., Yu, J., Shan, S., Zhou, B., Song, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2380-z · Cited by 1,667 · see citing works

Safety and Efficacy of the BNT162b2 mRNA Covid-19 Vaccine through 6 Months

Thomas, S. J., Moreira, E. D., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Perez, J. L., Pérez Marc, G., Polack, F. P., Zerbini, C., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2110345 · Cited by 1,640 · see citing works

High Contagiousness and Rapid Spread of Severe Acute Respiratory Syndrome Coronavirus 2

Sanche, S., Lin, Y. T., Xu, C., Romero-Severson, E., Hengartner, N., & Ke, R. (2020) · Emerging Infectious Diseases · doi:10.3201/eid2607.200282 · Cited by 1,619 · see citing works

SARS-CoV-2 mRNA Vaccine Design Enabled by Prototype Pathogen Preparedness

Corbett, K. S., Edwards, D. K., Leist, S. R., Abiona, O. M., Boyoglu-Barnum, S., Gillespie, R. A., Himansu, S., Schäfer, A., Ziwawo, C. T., DiPiazza, A. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2622-0 · Cited by 1,615 · see citing works

Global epidemiology, health burden and effective interventions for elevated blood pressure and hypertension

Zhou, B., Perel, P., Mensah, G. A., & Ezzati, M. (2021) · Nature Reviews Cardiology · doi:10.1038/s41569-021-00559-8 · Cited by 1,612 · see citing works

Virology, Epidemiology, Pathogenesis, and Control of COVID-19

Jin, Y., Yang, H., Ji, W., Wu, W., Chen, S., Zhang, W., & Duan, G. (2020) · Viruses · doi:10.3390/v12040372 · Cited by 1,604 · see citing works

SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599 · see citing works

On the origin and continuing evolution of SARS-CoV-2

Tang, X., Wu, C., Li, X., Song, Y., Yao, X., Wu, X., Duan, Y., Zhang, H., Wang, Y., Qian, Z., et al. (2020) · National Science Review · doi:10.1093/nsr/nwaa036 · Cited by 1,592 · see citing works

CD147-spike protein is a novel route for SARS-CoV-2 infection to host cells

Wang, K., Chen, W., Zhang, Z., Deng, Y., Lian, J., Du, P. F., Wei, D., Yang, Z., Sun, X., Gong, L., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00426-x · Cited by 1,592 · see citing works

Network-based drug repurposing for novel coronavirus 2019-nCoV/SARS-CoV-2

Zhou, Y., Hou, Y., Shen, J., Huang, Y., Martin, W., & Cheng, F. (2020) · Cell Discovery · doi:10.1038/s41421-020-0153-3 · Cited by 1,588 · see citing works

RCSB Protein Data Bank: powerful new tools for exploring 3D structures of biological macromolecules for basic and applied research and education in fundamental biology, biomedicine, biotechnology, bioengineering and energy sciences

Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581 · see citing works

SARS-CoV-2 productively infects human gut enterocytes

Lamers, M. M., Beumer, J., van der Vaart, J., Knoops, K., Puschhof, J., Breugem, T. I., Ravelli, R. B. G., Paul van Schayck, J., Mykytyn, A. Z., Duimel, H. Q., et al. (2020) · Science · doi:10.1126/science.abc1669 · Cited by 1,573 · see citing works

The COVID-19 pandemic

Ciotti, M., Ciccozzi, M., Terrinoni, A., Jiang, W.-C., Wang, C.-B., & Bernardini, S. (2020) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2020.1783198 · Cited by 1,567 · see citing works

mRNA-lipid nanoparticle COVID-19 vaccines: structure and stability

Schoenmaker, L., Witzigmann, D., Kulkarni, J. A., Verbeke, R., Kersten, G., Jiskoot, W., & Crommelin, D. J. A. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.120586 · Cited by 1,566 · see citing works

Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction

Punjani, A., Zhang, H., & Fleet, D. J. (2020) · Nature Methods · doi:10.1038/s41592-020-00990-8 · Cited by 1,559 · see citing works

mRNA vaccines for infectious diseases: principles, delivery and clinical translation

Chaudhary, N., Weissman, D., & Whitehead, K. A. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00283-5 · Cited by 1,555 · see citing works

Unique epidemiological and clinical features of the emerging 2019 novel coronavirus pneumonia (COVID‐19) implicate special control measures

Wang, Y., Wang, Y., Chen, Y., & Qin, Q. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25748 · Cited by 1,521 · see citing works

Considerable escape of SARS-CoV-2 Omicron to antibody neutralization

Planas, D., Saunders, N., Maes, P., Guivel-Benhassine, F., Planchais, C., Buchrieser, J., Bolland, W.-H., Porrot, F., Staropoli, I., Lemoine, F., et al. (2022) · Nature · doi:10.1038/s41586-021-04389-z · Cited by 1,514 · see citing works

Site-specific glycan analysis of the SARS-CoV-2 spike

Watanabe, Y., Allen, J. D., Wrapp, D., McLellan, J. S., & Crispin, M. (2020) · Science · doi:10.1126/science.abb9983 · Cited by 1,507 · see citing works

SARS-CoV-2 Reverse Genetics Reveals a Variable Infection Gradient in the Respiratory Tract

Hou, Y. J., Okuda, K., Edwards, C. E., Martinez, D. R., Asakura, T., Dinnon, K. H., Kato, T., Lee, R. E., Yount, B. L., Mascenik, T. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.042 · Cited by 1,488 · see citing works

COVID-19 and the cardiovascular system: implications for risk assessment, diagnosis, and treatment options

Guzik, T. J., MOHIDDIN, S. A., Dimarco, A. D., Patel, V., Savvatis, K., Marelli‐Berg, F. M., Madhur, M. S., Tomaszewski, M., Maffia, P., D’Acquisto, F., et al. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa106 · Cited by 1,451 · see citing works

The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity

Li, Q., Wu, J., Nie, J., Zhang, L., Hao, H., Liu, S., Zhao, C., Zhang, Q., Liu, H., Nie, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.012 · Cited by 1,420 · see citing works

A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., So, R. T. Y., Lv, H., Mok, C. K. P., & Wilson, I. A. (2020) · Science · doi:10.1126/science.abb7269 · Cited by 1,405 · see citing works

Diabetes is a risk factor for the progression and prognosis of <scp>COVID</scp>‐19

Guo, W., Li, M., Dong, Y., Zhou, H., Zhang, Z., Tian, C., Qin, R., Wang, H., Shen, Y., Du, K., et al. (2020) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.3319 · Cited by 1,404 · see citing works

COVID-19 and cardiovascular disease: from basic mechanisms to clinical perspectives

Nishiga, M., Wang, D. W., Han, Y., Lewis, D. B., & Wu, J. C. (2020) · Nature Reviews Cardiology · doi:10.1038/s41569-020-0413-9 · Cited by 1,400 · see citing works

Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology

Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395 · see citing works

SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity

Zhang, L., Jackson, C. B., Mou, H., Ojha, A., Peng, H., Quinlan, B. D., Rangarajan, E. S., Pan, A., Vanderheiden, A., Suthar, M. S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19808-4 · Cited by 1,387 · see citing works

A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2

Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385 · see citing works

Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike

Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349 · see citing works

Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion

Xia, S., Liu, M., Wang, C., Xu, W., Lan, Q., Feng, S., Qi, F., Bao, L., Du, L., Liu, S., et al. (2020) · Cell Research · doi:10.1038/s41422-020-0305-x · Cited by 1,340 · see citing works

Research and Development on Therapeutic Agents and Vaccines for COVID-19 and Related Human Coronavirus Diseases

Liu, C., Zhou, Q. A., Li, Y., Garner, L. V., Watkins, S. P., Carter, L. J., Smoot, J., Gregg, A. C., Daniels, A. D., Jervey, S. R., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00272 · Cited by 1,304 · see citing works

Structure-based design of prefusion-stabilized SARS-CoV-2 spikes

Hsieh, C.-L., Goldsmith, J. A., Schaub, J. M., DiVenere, A. M., Kuo, H.-C., Javanmardi, K., Le, K. C., Wrapp, D., Lee, A. G., Liu, Y., et al. (2020) · Science · doi:10.1126/science.abd0826 · Cited by 1,303 · see citing works

Neuropilin-1 is a host factor for SARS-CoV-2 infection

Daly, J. L., Simonetti, B., Klein, K., Chen, K.-E., Williamson, M. K., Antón-Plágaro, C., Shoemark, D. K., Simón-Gracia, L., Bauer, M., Hollandi, R., et al. (2020) · Science · doi:10.1126/science.abd3072 · Cited by 1,251 · see citing works

Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model

Rogers, T. F., Zhao, F., Huang, D., Beutler, N., Burns, A., He, W.-T., Limbo, O., Smith, C., Song, G., Woehl, J., et al. (2020) · Science · doi:10.1126/science.abc7520 · Cited by 1,230 · see citing works

Broad and strong memory CD4+ and CD8+ T cells induced by SARS-CoV-2 in UK convalescent individuals following COVID-19

Peng, Y., Mentzer, A. J., Liu, G., Yao, X., Yin, Z., Dong, D., Dejnirattisai, W., Rostron, T., Supasa, P., Liu, C., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0782-6 · Cited by 1,179 · see citing works

Distinct conformational states of SARS-CoV-2 spike protein

Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221 · see citing works

Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir

Yin, W., Mao, C., Luan, X., Shen, D.-D., Shen, Q., Su, H., Wang, X., Zhou, F., Zhao, W., Gao, M., et al. (2020) · Science · doi:10.1126/science.abc1560 · Cited by 1,219 · see citing works

Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail

Hansen, J., Baum, A., Pascal, K. E., Russo, V., Giordano, S., Wloga, E., Fulton, B. O., Yan, Y., Koon, K., Patel, K., et al. (2020) · Science · doi:10.1126/science.abd0827 · Cited by 1,210 · see citing works

Review of the 2019 novel coronavirus (SARS-CoV-2) based on current evidence

Wang, L., Wang, Y., Ye, D., & Liu, Q. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105948 · Cited by 1,200 · see citing works

Robust neutralizing antibodies to SARS-CoV-2 infection persist for months

Wajnberg, A., Amanat, F., Firpo, A., Altman, D. R., Bailey, M. J., Mansour, M., McMahon, M., Meade, P., Mendu, D. R., Muellers, K., et al. (2020) · Science · doi:10.1126/science.abd7728 · Cited by 1,195 · see citing works

Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells

Cao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.025 · Cited by 1,188 · see citing works

Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies

Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Cell Host &amp; Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178 · see citing works

Mechanisms of SARS-CoV-2 Transmission and Pathogenesis

Harrison, A. G., Lin, T., & Wang, P. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.10.004 · Cited by 1,177 · see citing works

Role of angiotensin-converting enzyme 2 (ACE2) in COVID-19

Ni, W., Yang, X., Yang, D., Bao, J., Li, R., Xiao, Y., Hou, C., Wang, H., Liu, J., Yang, D., et al. (2020) · Critical Care · doi:10.1186/s13054-020-03120-0 · Cited by 1,175 · see citing works

Coronavirus disease 2019 (COVID-19): current status and future perspectives

Li, H., Liu, S., Yu, X.-H., Tang, S., & Tang, C. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105951 · Cited by 1,174 · see citing works

SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2

Clausen, T. M., Sandoval, D. R., Spliid, C. B., Pihl, J., Perrett, H. R., Painter, C. D., Narayanan, A., Majowicz, S. A., Kwong, E. M., McVicar, R. N., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.033 · Cited by 1,162 · see citing works

Phase 1–2 Trial of a SARS-CoV-2 Recombinant Spike Protein Nanoparticle Vaccine

Keech, C., Albert, G., Cho, I., Robertson, A., Reed, P., Neal, S., Plested, J. S., Zhu, M., Cloney-Clark, S., Zhou, H., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2026920 · Cited by 1,156 · see citing works

Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability

Brouwer, P. J. M., Caniels, T. G., van der Straten, K., Snitselaar, J. L., Aldon, Y., Bangaru, S., Torres, J. L., Okba, N. M. A., Claireaux, M., Kerster, G., et al. (2020) · Science · doi:10.1126/science.abc5902 · Cited by 1,140 · see citing works

Immune correlates analysis of the mRNA-1273 COVID-19 vaccine efficacy clinical trial

Gilbert, P. B., Montefiori, D. C., McDermott, A. B., Fong, Y., Benkeser, D., Deng, W., Zhou, H., Houchens, C. R., Martins, K., Jayashankar, L., et al. (2022) · Science · doi:10.1126/science.abm3425 · Cited by 1,137 · see citing works

SARS-CoV-2 Vaccines: Status Report

Amanat, F., & Krammer, F. (2020) · Immunity · doi:10.1016/j.immuni.2020.03.007 · Cited by 1,120 · see citing works

Angiotensin‐converting enzyme 2 ( ACE2 ), SARS‐CoV ‐2 and the pathophysiology of coronavirus disease 2019 ( COVID ‐19)

Bourgonje, A. R., Abdulle, A. E., Timens, W., Hillebrands, J., Navis, G. J., Gordijn, S. J., Bolling, M. C., Dijkstra, G. D. H., Voors, A. A., Osterhaus, A. D. M. E., et al. (2020) · The Journal of Pathology · doi:10.1002/path.5471 · Cited by 1,119 · see citing works

Insights into SARS-CoV-2 genome, structure, evolution, pathogenesis and therapies: Structural genomics approach

Naqvi, A. A. T., Fatima, K., Mohammad, T., Fatima, U., Singh, I. K., Singh, A. K., Atif, S. M., Hariprasad, G., Hasan, G. M., & Hassan, M. I. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165878 · Cited by 1,118 · see citing works

Preliminary Identification of Potential Vaccine Targets for the COVID-19 Coronavirus (SARS-CoV-2) Based on SARS-CoV Immunological Studies

Ahmed, S. F., Quadeer, A. A., & McKay, M. R. (2020) · Viruses · doi:10.3390/v12030254 · Cited by 1,116 · see citing works

A human monoclonal antibody blocking SARS-CoV-2 infection

Wang, C., Li, W., Drabek, D., Okba, N. M. A., van Haperen, R., Osterhaus, A. D. M. E., van Kuppeveld, F. J. M., Haagmans, B. L., Grosveld, F. G., & Bosch, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16256-y · Cited by 1,115 · see citing works

Structures and distributions of SARS-CoV-2 spike proteins on intact virions

Ke, Z., Otón, J., Qu, K., Cortese, M., Žíla, V., McKeane, L., Nakane, T., Zivanov, J., Neufeldt, C. J., Cerikan, B., et al. (2020) · Nature · doi:10.1038/s41586-020-2665-2 · Cited by 1,114 · see citing works

Understanding of COVID‐19 based on current evidence

Sun, P., Lu, X., Xu, C., Sun, W., & Pan, B. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25722 · Cited by 1,107 · see citing works

SARS-CoV-2 receptor ACE2 and TMPRSS2 are primarily expressed in bronchial transient secretory cells

Lukassen, S., Chua, R. L., Trefzer, T. B., Kahn, N. C., Schneider, M. A., Muley, T., Winter, H., Meister, M. A., Veith, C., Boots, A. W., et al. (2020) · The EMBO Journal · doi:10.15252/embj.20105114 · Cited by 1,082 · see citing works

The deadly coronaviruses: The 2003 SARS pandemic and the 2020 novel coronavirus epidemic in China

Yang, Y., Peng, F., Wang, R., Guan, K., Jiang, T., Xu, G., Sun, J., & Chang, C. C.-C. (2020) · Journal of Autoimmunity · doi:10.1016/j.jaut.2020.102434 · Cited by 1,073 · see citing works

Evaluation of the mRNA-1273 Vaccine against SARS-CoV-2 in Nonhuman Primates

Corbett, K. S., Flynn, B., Foulds, K. E., Francica, J. R., Boyoglu-Barnum, S., Werner, A. P., Flach, B., O’Connell, S., Bock, K. W., Minai, M., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2024671 · Cited by 1,066 · see citing works

Molecular Architecture of the SARS-CoV-2 Virus

Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060 · see citing works

Dual-Functional Plasmonic Photothermal Biosensors for Highly Accurate Severe Acute Respiratory Syndrome Coronavirus 2 Detection

Qiu, G., Gai, Z., Tao, Y., Schmitt, J., Kullak-Ublick, G. A., & Wang, J. (2020) · ACS Nano · doi:10.1021/acsnano.0c02439 · Cited by 1,050 · see citing works

Potently neutralizing and protective human antibodies against SARS-CoV-2

Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041 · see citing works

Structure of the nCoV trimeric spike

Vinson, V. J. (2020) · Science · doi:10.1126/science.367.6483.1207-c · Cited by 2 · see citing works

Characterization of the SARS-CoV-2 Spike in an Early Prefusion ConformationPreprint

Li, T., Zheng, Q., Yu, H. J., Wu, D., Xue, W., Zhang, Y., Huang, X., Zhou, L., Zhang, Z., Zha, Z., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.16.994152 · Cited by 15 · see citing works

Important Structural Insights of the 2019-NCoV Spike Protein

Hossain, M. M. (2022) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2022.47.007551

Potent binding of 2019 novel coronavirus spike protein by a SARS coronavirus-specific human monoclonal antibody

Tian, X., Li, C., Huang, A., Xia, S., Lu, S., Shi, Z., Lu, L., Jiang, S., Yang, Z., Wu, Y., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1729069 · Cited by 1,239 · see citing works

Structural basis for the recognition of the 2019-nCoV by human ACE2Preprint

Yan, R., Zhang, Y., Guo, Y., Xia, L., & Zhou, Q. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.19.956946 · Cited by 134 · see citing works