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

The neighbor-joining method: a new method for reconstructing phylogenetic trees.

Saitou, N., & Nei, M. (1987) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040454 · Cited by 59,962 · see citing works

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

CONFIDENCE LIMITS ON PHYLOGENIES: AN APPROACH USING THE BOOTSTRAP

Felsenstein, J. (1985) · Evolution · doi:10.1111/j.1558-5646.1985.tb00420.x · Cited by 44,735 · see citing works

MEGA7: Molecular Evolutionary Genetics Analysis Version 7.0 for Bigger Datasets

Kumar, S., Stecher, G., & Tamura, K. (2016) · Molecular Biology and Evolution · doi:10.1093/molbev/msw054 · Cited by 43,923 · see citing works

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 · see citing works

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · 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

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

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

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 · 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

MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and coronavirus disease-2019 (COVID-19): The epidemic and the challenges

Lai, C.-C., Shih, T.-P., Ko, W.-C., Tang, H.-J., & Hsueh, P.-R. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.105924 · Cited by 6,068 · 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

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

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 · see citing works

Prospects for inferring very large phylogenies by using the neighbor-joining method

Tamura, K., Nei, M., & Kumar, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404206101 · Cited by 5,588 · see citing works

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446 · 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

New tools for automated high-resolution cryo-EM structure determination in RELION-3

Zivanov, J., Nakane, T., Forsberg, B., Kimanius, D., Hagen, W., Lindahl, E., & Scheres, S. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,377 · see citing works

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 4,345 · 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

A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus–induced lung injury

Kuba, K., Imai, Y., Rao, S., Gao, H., Guo, F., Guan, B., Huan, Y., Yang, P., Zhang, Y., Deng, W., et al. (2005) · Nature Medicine · doi:10.1038/nm1267 · Cited by 3,445 · see citing works

Gctf: Real-time CTF determination and correction

Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · 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

Multiple Sequence Alignment Using ClustalW and ClustalX

Thompson, J., Gibson, T. J., & Higgins, D. G. (2002) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0203s00 · Cited by 2,989 · 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

Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy

Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416 · 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

Rapid similarity searches of nucleic acid and protein data banks.

Wilbur, W. J., & Lipman, D. J. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.3.726 · Cited by 1,546 · 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

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

IgBLAST: an immunoglobulin variable domain sequence analysis tool

Ye, J., Ma, N., Madden, T., & Ostell, J. M. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt382 · Cited by 1,161 · 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

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

High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy

Chen, S., McMullan, G., Faruqi, A. R., Murshudov, G. N., Short, J. M., Scheres, S. H. W., & Henderson, R. A. (2013) · Ultramicroscopy · doi:10.1016/j.ultramic.2013.06.004 · Cited by 1,005 · see citing works

A noncompeting pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2

Wu, Y., Wang, F., Shen, C., Peng, W., Li, D., Zhao, C., Li, Z., Li, S., Bi, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc2241 · Cited by 955 · see citing works

Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2

Kimanius, D., Forsberg, B. O., Scheres, S. H. W., & Lindahl, E. R. (2016) · eLife · doi:10.7554/elife.18722 · Cited by 903 · see citing works

A Bayesian View on Cryo-EM Structure Determination

Scheres, S. H. W. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.11.010 · Cited by 875 · see citing works

Change-O: a toolkit for analyzing large-scale B cell immunoglobulin repertoire sequencing data

Gupta, N. T., Heiden, J. A. V., Uduman, M., Gadala-Maria, D., Yaari, G., & Kleinstein, S. H. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btv359 · Cited by 869 · see citing works

Flexible Fitting of Atomic Structures into Electron Microscopy Maps Using Molecular Dynamics

Trabuco, L. G., Villa, E., Mitra, K., Frank, J., & Schulten, K. J. (2008) · Structure · doi:10.1016/j.str.2008.03.005 · Cited by 866 · 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

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

Grant, T. S., & Grigorieff, N. (2015) · eLife · doi:10.7554/elife.06980 · Cited by 840 · see citing works

Coronavirus Spike Proteins in Viral Entry and Pathogenesis

Gallagher, T. M., & Buchmeier, M. J. (2001) · Virology · doi:10.1006/viro.2000.0757 · Cited by 658 · see citing works

Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies

Wrapp, D., De Vlieger, D., Corbett, K. S., Torres, G. M., Wang, N., Van Breedam, W., Roose, K., van Schie, L., Hoffmann, M., Pöhlmann, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.031 · Cited by 610 · see citing works

Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond

Lu, G., Wang, Q., & Gao, G. F. (2015) · Trends in Microbiology · doi:10.1016/j.tim.2015.06.003 · Cited by 606 · see citing works

CDR3 length in antigen-specific immune receptors.

Rock, E. P., Sibbald, P. R., Davis, M. M., & Chien, Y. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.179.1.323 · Cited by 500 · see citing works

Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen

Smith, K., Garman, L., Wrammert, J., Zheng, N., Capra, J. D., Ahmed, R., & Wilson, P. C. (2009) · Nature Protocols · doi:10.1038/nprot.2009.3 · Cited by 471 · see citing works

Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research

Simmons, G., Zmora, P., Gierer, S., Heurich, A., & Pöhlmann, S. (2013) · Antiviral Research · doi:10.1016/j.antiviral.2013.09.028 · Cited by 413 · see citing works

IMGT/V-QUEST: IMGT Standardized Analysis of the Immunoglobulin (IG) and T Cell Receptor (TR) Nucleotide SequencesPreprint

Giudicelli, V., Brochet, X., & Lefranc, M. (2011) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot5633 · Cited by 380 · see citing works

Human monoclonal antibodies block the binding of SARS-CoV-2 spike protein to angiotensin converting enzyme 2 receptor

Chen, X., Li, R., Pan, Z., Qian, C., Yang, Y., You, R., Zhao, J., Liu, P., Gao, L., Li, Z., et al. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0426-7 · Cited by 325 · see citing works

Automated acquisition of cryo-electron micrographs for single particle reconstruction on an FEI Tecnai electron microscope

Lei, J., & FRANK, J. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.01.002 · Cited by 301 · see citing works

Potent human neutralizing antibodies elicited by SARS-CoV-2 infectionPreprint

Ju, B., Zhang, Q., Ge, X., et al. (2020) · bioRxiv · doi:10.1101/2020.03.21.990770 · Cited by 256 · see citing works

High-throughput isolation of immunoglobulin genes from single human B cells and expression as monoclonal antibodies

Liao, H., Levesque, M. C., Nagel, A., Dixon, A., Zhang, R., Walter, E. B., Parks, R., Whitesides, J. F., Marshall, D. J., Hwang, K., et al. (2009) · Journal of Virological Methods · doi:10.1016/j.jviromet.2009.02.014 · Cited by 255 · see citing works

What’s new in the renin-angiotensin system?

Kuhn, J. H., Li, W., Choe, H., & Farzan, M. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4242-5 · Cited by 250 · see citing works

Importance of Neutralizing Monoclonal Antibodies Targeting Multiple Antigenic Sites on the Middle East Respiratory Syndrome Coronavirus Spike Glycoprotein To Avoid Neutralization Escape

Wang, L., Shi, W., Chappell, J. D., Joyce, M. G., Zhang, Y., Kanekiyo, M., Becker, M. M., van Doremalen, N., Fischer, R., Wang, N., et al. (2018) · Journal of Virology · doi:10.1128/jvi.02002-17 · Cited by 169 · see citing works

Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus

Krempl, C. D., Schultze, B., Laude, H., & Herrler, G. (1997) · Journal of Virology · doi:10.1128/jvi.71.4.3285-3287.1997 · Cited by 166 · see citing works

The Secret Life of ACE2 as a Receptor for the SARS Virus

Dimitrov, D. S. (2003) · Cell · doi:10.1016/s0092-8674(03)00976-0 · Cited by 145 · see citing works

Structural definition of a neutralization epitope on the N-terminal domain of MERS-CoV spike glycoprotein

Zhou, H., Chen, Y., Zhang, S., Niu, P., Qin, K., Jia, W., Huang, B., Zhang, S., Lan, J., Zhang, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10897-4 · Cited by 142 · see citing works

Structural and Functional Analysis of the Surface Protein of Human Coronavirus OC43

Künkel, F., & Herrler, G. (1993) · Virology · doi:10.1006/viro.1993.1360 · Cited by 119 · see citing works

Antibodies and vaccines against Middle East respiratory syndrome coronavirus

Xu, J., Jia, W., Wang, P., Zhang, S., Shi, X., Wang, X., & Zhang, L. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1624482 · Cited by 85 · see citing works

Large‐scale analysis of somatic hypermutations in antibodies reveals which structural regions, positions and amino acids are modified to improve affinity

Burkovitz, A., Sela‐Culang, I., & Ofran, Y. (2013) · FEBS Journal · doi:10.1111/febs.12597 · Cited by 48 · see citing works

An LASV GPC pseudotyped virus based reporter system enables evaluation of vaccines in mice under non-BSL-4 conditions

Li, Q., Liu, Q., Huang, W., Wu, J., Nie, J., Wang, M., Zhao, C., Zhang, L., & Wang, Y. (2017) · Vaccine · doi:10.1016/j.vaccine.2017.07.101 · Cited by 23 · see citing works

Copper tolerance in a population of Silene vulgaris ssp. maritima (A. & D. Love) at Dolfrwynog Bog near Dolgellau, North Wales

Price, C. G., & Abrahams, P. W. (1994) · Environmental Geochemistry and Health · doi:10.1007/bf00149590 · Cited by 7 · see citing works

SARS-CoV-2 variants, spike mutations and immune escape

Harvey, W. T., Carabelli, A. M., Jackson, B., Gupta, R. K., Thomson, E. C., Harrison, E. M., Ludden, C., Reeve, R., Rambaut, A., COVID-19 Genomics UK (COG-UK) Consortium, et al. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00573-0 · Cited by 3,528 · see citing works

Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7

Wang, P., Nair, M. S., Liu, L., Iketani, S., Luo, Y., Guo, Y., Wang, M., Yu, J., Zhang, B., Kwong, P. D., et al. (2021) · Nature · doi:10.1038/s41586-021-03398-2 · Cited by 2,312 · see citing works

Detection of a SARS-CoV-2 variant of concern in South Africa

Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510 · 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

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

Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants

Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308 · 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

Immunogenicity and safety of a recombinant adenovirus type-5-vectored COVID-19 vaccine in healthy adults aged 18 years or older: a randomised, double-blind, placebo-controlled, phase 2 trial

Zhu, F.-C., Guan, X.-H., Li, Y.-H., Huang, J.-Y., Jiang, T., Hou, L.-H., Li, J.-X., Yang, B.-F., Wang, L., Wang, W.-J., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)31605-6 · Cited by 1,225 · see citing works

Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition

Greaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host &amp; Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016 · see citing works

Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera

Zhou, D., Dejnirattisai, W., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.037 · Cited by 992 · see citing works

SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma

Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147 · 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

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901 · see citing works

The biological and clinical significance of emerging SARS-CoV-2 variants

Tao, K., Tzou, P. L., Nouhin, J., Gupta, R. K., de Oliveira, T., Kosakovsky Pond, S. L., Fera, D., & Shafer, R. W. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-021-00408-x · Cited by 1,009 · see citing works

SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses

Dejnirattisai, W., Huo, J., Zhou, D., Zahradník, J., Supasa, P., Liu, C., Duyvesteyn, H. M. E., Ginn, H. M., Mentzer, A. J., Tuekprakhon, A., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.046 · Cited by 930 · see citing works

Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies

Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795 · see citing works

SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development

Wang, M.-Y., Zhao, R., Gao, L.-J., Gao, X.-F., Wang, D.-P., & Cao, J.-M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.587269 · Cited by 874 · see citing works

Preexisting and de novo humoral immunity to SARS-CoV-2 in humans

Ng, K. W., Faulkner, N., Cornish, G. H., Rosa, A., Harvey, R., Hussain, S., Ulferts, R., Earl, C., Wrobel, A. G., Benton, D. J., et al. (2020) · Science · doi:10.1126/science.abe1107 · Cited by 886 · see citing works

BNT162b vaccines protect rhesus macaques from SARS-CoV-2

Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03275-y · Cited by 694 · see citing works

Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum

Liu, C., Ginn, H. M., Dejnirattisai, W., Supasa, P., Wang, B., Tuekprakhon, A., Nutalai, R., Zhou, D., Mentzer, A. J., Zhao, Y., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.020 · Cited by 669 · see citing works

SARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies

Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R., Walls, A. C., Kemp S, S. A., Bassi, J., Pinto, D., Fregni, C. S., et al. (2021) · doi:10.1101/2021.01.19.21249840 · Cited by 729 · see citing works

Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies

Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R. P., Walls, A. C., Kemp, S. A., Bassi, J., Pinto, D., Silacci-Fregni, C., et al. (2021) · Nature · doi:10.1038/s41586-021-03412-7 · Cited by 728 · see citing works

Structural basis of a shared antibody response to SARS-CoV-2

Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589 · see citing works

SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex

Mannar, D., Saville, J. W., Zhu, X., Srivastava, S. S., Berezuk, A. M., Tuttle, K. S., Marquez, A. C., Sekirov, I., & Subramaniam, S. (2022) · Science · doi:10.1126/science.abn7760 · Cited by 630 · see citing works

mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection

Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · Science · doi:10.1126/science.abg9175 · Cited by 557 · see citing works

Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite

Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host &amp; Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519 · see citing works

Enhanced SARS-CoV-2 neutralization by dimeric IgA

Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Viant, C., Gaebler, C., Cipolla, M., Hoffmann, H.-H., Oliveira, T. Y., Oren, D. A., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abf1555 · Cited by 475 · see citing works

Recurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape

McCarthy, K. R., Rennick, L. J., Nambulli, S., Robinson-McCarthy, L. R., Bain, W. G., Haidar, G., & Duprex, W. P. (2021) · Science · doi:10.1126/science.abf6950 · Cited by 535 · see citing works

SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern

McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412 · see citing works

Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera

Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.033 · Cited by 460 · see citing works

Spread of a SARS-CoV-2 variant through Europe in the summer of 2020

Hodcroft, E. B., Zuber, M., Nadeau, S., Vaughan, T. G., Crawford, K. H. D., Althaus, C. L., Reichmuth, M. L., Bowen, J. E., Walls, A. C., Corti, D., et al. (2021) · Nature · doi:10.1038/s41586-021-03677-y · Cited by 425 · see citing works

The antigenic anatomy of SARS-CoV-2 receptor binding domain

Dejnirattisai, W., Zhou, D., Ginn, H. M., Duyvesteyn, H. M. E., Supasa, P., Case, J. B., Zhao, Y., Walter, T. S., Mentzer, A. J., Liu, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.032 · Cited by 371 · see citing works

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants

Yuan, M., Huang, D., Lee, C.-C. D., Wu, N. C., Jackson, A. M., Zhu, X., Liu, H., Peng, L., van Gils, M. J., Sanders, R. W., et al. (2021) · doi:10.1101/2021.02.16.430500 · Cited by 364 · see citing works

A Therapeutic Non-self-reactive SARS-CoV-2 Antibody Protects from Lung Pathology in a COVID-19 Hamster Model

Kreye, J., Reincke, S. M., Kornau, H.-C., Sánchez-Sendin, E., Corman, V. M., Liu, H., Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.049 · Cited by 347 · see citing works

A thermostable, closed SARS-CoV-2 spike protein trimer

Xiong, X., Qu, K., Ciazynska, K. A., Hosmillo, M., Carter, A. P., Ebrahimi, S., Ke, Z., Scheres, S. H. W., Bergamaschi, L., Grice, G. L., et al. (2020) · Nature Structural &amp; Molecular Biology · doi:10.1038/s41594-020-0478-5 · Cited by 313 · see citing works

SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma

Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166

Quantification of SARS-CoV-2 neutralizing antibody by wild-type plaque reduction neutralization, microneutralization and pseudotyped virus neutralization assays

Bewley, K. R., Coombes, N. S., Gagnon, L., McInroy, L., Baker, N., Shaik, I., St-Jean, J. R., St-Amant, N., Buttigieg, K. R., Humphries, H. E., et al. (2021) · Nature Protocols · doi:10.1038/s41596-021-00536-y · Cited by 293 · see citing works

SARS-CoV-2 escape <i>in vitro</i> from a highly neutralizing COVID-19 convalescent plasma

Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451

SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2

Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.005 · Cited by 273 · see citing works

Engineered ACE2 receptor traps potently neutralize SARS-CoV-2

Glasgow, A., Glasgow, J., Limonta, D., Solomon, P., Lui, I., Zhang, Y., Nix, M. A., Rettko, N. J., Zha, S., Yamin, R., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016093117 · Cited by 251 · see citing works

A human coronavirus evolves antigenically to escape antibody immunity

Eguia, R., Crawford, K. H. D., Stevens-Ayers, T., Kelnhofer-Millevolte, L., Greninger, A. L., Englund, J. A., Boeckh, M. J., & Bloom, J. D. (2020) · doi:10.1101/2020.12.17.423313 · Cited by 258 · see citing works

Antibodies elicited by mRNA-1273 vaccination bind more broadly to the receptor binding domain than do those from SARS-CoV-2 infection

Greaney, A. J., Loes, A. N., Gentles, L. E., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9915 · Cited by 244 · see citing works

Analysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability to use ACE2 receptors from additional species

Wang, R., Zhang, Q., Ge, J., Ren, W., Zhang, R., Lan, J., Ju, B., Su, B., Yu, F., Chen, P., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.06.003 · Cited by 240 · see citing works

Two-step strategy for the identification of SARS-CoV-2 variant of concern 202012/01 and other variants with spike deletion H69–V70, France, August to December 2020

Bal, A., Destras, G., Gaymard, A., Stefic, K., Marlet, J., Eymieux, S., Regue, H., Semanas, Q., d’Aubarede, C., Billaud, G., et al. (2021) · Eurosurveillance · doi:10.2807/1560-7917.es.2021.26.3.2100008 · Cited by 212 · see citing works

Recurrent emergence and transmission of a SARS-CoV-2 spike deletion H69/V70

Kemp, S. A., Meng, B., Ferriera, I. A., Datir, R., Harvey, W. T., Papa, G., Lytras, S., Collier, D. A., Mohamed, A., Gallo, G., et al. (2020) · doi:10.1101/2020.12.14.422555 · Cited by 252 · see citing works

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

Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · doi:10.1101/2020.12.31.425021 · Cited by 1,178 · see citing works

Comparison of the immunogenicity of <scp>BNT162b2</scp> and <scp>CoronaVac COVID</scp> ‐19 vaccines in Hong Kong

Mok, C. K. P., Cohen, C. A., Cheng, S. M. S., Chen, C., Kwok, K., Yiu, K., Chan, T., Bull, M., Ling, K. C., Dai, Z., et al. (2022) · Respirology · doi:10.1111/resp.14191 · Cited by 162 · see citing works

Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization

Shan, S., Luo, S., Yang, Z., Hong, J., Su, Y., Ding, F., Fu, L., Li, C., Chen, P., Ma, J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2122954119 · Cited by 157 · see citing works

A prefusion SARS-CoV-2 spike RNA vaccine is highly immunogenic and prevents lung infection in non-human primates

Vogel, A. B., Kanevsky, I., Che, Y., Swanson, K. A., Muik, A., Vormehr, M., Kranz, L. M., Walzer, K. C., Hein, S., Güler, A., et al. (2020) · doi:10.1101/2020.09.08.280818 · Cited by 126 · see citing works

N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2

McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · doi:10.1101/2021.01.14.426475 · Cited by 901 · see citing works

Partial resistance of SARS-CoV-2 Delta variants to vaccine-elicited antibodies and convalescent sera

Tada, T., Zhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., & Landau, N. R. (2021) · iScience · doi:10.1016/j.isci.2021.103341 · Cited by 101 · see citing works

A single mRNA immunization boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection

Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · doi:10.1101/2021.02.05.21251182 · Cited by 559 · see citing works

Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain

Tan, T. J. C., Yuan, M., Kuzelka, K., Padron, G. C., Beal, J. R., Chen, X., Wang, Y., Rivera-Cardona, J., Zhu, X., Stadtmueller, B. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24123-7 · Cited by 75 · see citing works

Tackling COVID-19 with neutralizing monoclonal antibodies

Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.07.027 · Cited by 78 · see citing works

E484K as an innovative phylogenetic event for viral evolution: Genomic analysis of the E484K spike mutation in SARS-CoV-2 lineages from Brazil

Ferrareze, P. A. G., Franceschi, V. B., Mayer, A. D. M., Caldana, G. D., Zimerman, R. A., & Thompson, C. E. (2021) · Infection, Genetics and Evolution · doi:10.1016/j.meegid.2021.104941 · Cited by 82 · see citing works

Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein

Suryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · doi:10.1101/2021.01.19.427324 · Cited by 361 · see citing works

The Spike Proteins of SARS-CoV-2 B.1.617 and B.1.618 Variants Identified in India Provide Partial Resistance to Vaccine-elicited and Therapeutic Monoclonal Antibodies

Tada, T., Zhou, H., Dcosta, B. M., Samanovic, M. I., Mulligan, M. J., & Landau, N. R. (2021) · doi:10.1101/2021.05.14.444076 · Cited by 101 · see citing works

The N-terminal domain of spike glycoprotein mediates SARS-CoV-2 infection by associating with L-SIGN and DC-SIGN

Soh, W. T., Liu, Y., Nakayama, E. E., Ono, C., Torii, S., Nakagami, H., Matsuura, Y., Shioda, T., & Arase, H. (2020) · doi:10.1101/2020.11.05.369264 · Cited by 61 · see citing works

Development of potency, breadth and resilience to viral escape mutations in SARS-CoV-2 neutralizing antibodies

Muecksch, F., Weisblum, Y., Barnes, C. O., Schmidt, F., Schaefer-Babajew, D., Lorenzi, J. C. C., Flyak, A. I., DeLaitsch, A. T., Huey-Tubman, K. E., Hou, S., et al. (2021) · doi:10.1101/2021.03.07.434227 · Cited by 39 · see citing works

Impact of the B.1.1.7 variant on neutralizing monoclonal antibodies recognizing diverse epitopes on SARS-CoV-2 Spike

Graham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galao, R. P., Lista, M. J., et al. (2021) · doi:10.1101/2021.02.03.429355 · Cited by 27 · see citing works

A Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants

Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.766821 · Cited by 21 · 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

Structural Analysis of Spike Protein Mutations in the SARS-CoV-2 P.3 Variant

Bascos, N. A. D., Mirano-Bascos, D., & Saloma, C. P. (2021) · doi:10.1101/2021.03.06.434059 · Cited by 11 · see citing works

Author response for "Conformational variability of loops in the SARS‐CoV ‐2 spike protein"

Wong, S. W. K., & Liu, Z. (2021) · doi:10.1002/prot.26266/v2/response1

Retraction Note: Presence of viral spike protein and vaccinal spike protein in the blood serum of patients with long-COVID syndrome.

Dhuli, K., Medori, M. C., Micheletti, C., et al. (2024) · PubMed · doi:10.26355/eurrev_202403_35774

Review for "Conformational variability of loops in the SARS‐CoV ‐2 spike protein"

(2021) · doi:10.1002/prot.26266/v2/review1

Faculty Opinions recommendation of Toward a pan-SARS-CoV-2 vaccine targeting conserved epitopes on spike and non-spike proteins for potent, broad and durable immune responses.

Dey, A. (2023) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.742617398.793598514