The DOI matches its Crossref record; 106 of the 109 references it cites were found in a registry or an index.
Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
Open accessPublished version of a preprint
Abstract
and RBD epitopes on SARS-CoV-2 spike. Moreover, a 3.4 Å cryo-electron microscopy (cryo-EM) structure of a neutralizing monoclonal Fab-spike complex revealed an epitope that blocks ACE2 receptor binding. Modeling based on these structures suggested different potentials for inter-spike crosslinking by IgGs on viruses, and characterized IgGs would not be affected by identified SARS-CoV-2 spike mutations. Overall, our studies structurally define a recurrent anti-SARS-CoV-2 antibody class derived from VH3-53/VH3-66 and similarity to a SARS-CoV VH3-30 antibody, providing criteria for evaluating vaccine-elicited antibodies.
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?
In the citing paper
“Moreover, the plasma neutralizing activity, and the relative numbers of RBD-specific memory B cells were equivalent to individuals who recovered from natural infection7,8.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“As expected, plasma neutralizing activity was directly correlated to anti-S and -RBD binding titers in ELISAs7,8 (Fig. 1c, d, and Extended Data Fig. 2a–d).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“A475V is resistant to class 1 antibodies (structurally defined as described29); E484K and Q493R are resistant to class 2 antibodies7,8,12,13,29,30,32,33; while R346S, N439K, and N440K are resistant to class 3 antibodies7,8,12,13,29,33.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“In addition, antibodies that share the same combination of IGHV and IGLV genes in vaccinees comprised 39% of all the clonal sequences (Extended Data Fig. 4b) and 59% when combined with naturally infected individuals7,8 (Fig. 2f), and some of these antibodies were nearly identical (Extended Data Table 3 and 4).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“Class 1 and 2 antibodies are among the most potent and also the most abundant antibodies7,8,21,22,25,39.”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“Consistent with the plasma neutralization results, the geometric mean neutralization half-maximal inhibitory concentration of the Pfizer-BioNTech and Moderna vaccinee antibodies were not significantly different from each other or to antibody collections obtained from naturally infected individuals 1.3 or 6.2 months after infection (Fig. 3a and 7,8).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“In anti-RBD ELISAs the mean half-maximal effective concentration (EC50) was higher than that observed in infected individuals after 6.2 months but not significantly different from antibodies obtained 1.3 months after infection (Extended Data Fig. 6a, and Table 5 and 7,8).”
From mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants (2021) · cites this paper as [8]
In the citing paper
“Numerous neutralizing anti-RBD monoclonal antibodies (mAbs) have been characterized, the most potent of which block the RBD-ACE2 interaction (16, 17, 22–24, 32–37).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [32]
In the citing paper
“Antibodies binding to the RBD can potently block attachment of the virus to ACE2 and thereby neutralize the virus”
From SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2 (2021) · cites this paper as Barnes et al., 2020
In the citing paper
“Their engagement with the RBD is dictated by CDR-H1 and CDR-H2, while the CDR-H3 is characteristically short and makes rather few interactions”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Barnes et al., 2020
In the citing paper
“A number of public antibody responses have been reported for SARS-CoV-2, principal among these being VH3–53/VH3–66 and VH1–58 (VH3–30 is also found, but the antibodies are not potent neutralizers) (Yuan et al., 2020; Barnes et al., 2020; Dejnirattisai et al., 2021).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Barnes 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
MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability
Katoh, K., & Standley, D. M. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst010 · Cited by 46,209
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 45,882
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : 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
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
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
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
Self-citationGuindon, S., Dufayard, J.-F., Lefort, V., Anisimova, M., Hordijk, W., & Gascuel, O. (2010) · Systematic Biology · doi:10.1093/sysbio/syq010 · Cited by 18,376
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576
Flagged first, then by citations
3 of the 109 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 601–700 of 803
Adhikari, N., Amin, S. A., & Jha, T. (2020) · Methods in pharmacology and toxicology · doi:10.1007/7653_2020_46 · Cited by 5
The role of chemical biology in the fight against SARS-CoV-2
Burslem, G. M. (2021) · Biochemical Journal · doi:10.1042/bcj20200514 · Cited by 4
Valgardsdottir, R., Cattaneo, I., Napolitano, G., Raglio, A., Spinelli, O., Salmoiraghi, S., Castilletti, C., Lapa, D., Capobianchi, M. R., Farina, C., et al. (2021) · Antibodies · doi:10.3390/antib10030026 · Cited by 4
Broad Spectrum Antiviral Therapy can Supersede Vaccination Strategy for Combating COVID-19 Pandemic
Chakraborty, A. K. (2021) · Medical Journal of Clinical Trials & Case Studies · doi:10.23880/mjccs-16000298 · Cited by 3
Antibodies Against Biofilms: Mechanisms and Applications
Watson, A., Maan, H., Kolodkin‐Gal, I., & Freund, N. T. (2022) · Springer series on biofilms · doi:10.1007/978-3-031-10992-8_11 · Cited by 4
SARS-CoV-2 Serological Investigation of White-Tailed Deer in Northeastern Ohio
Boley, P. A., Dennis, P. M., Faraone, J. N., Xu, J., Liu, M., Niu, X., Gibson, S., Hale, V. L., Wang, Q., Liu, S., et al. (2023) · Viruses · doi:10.3390/v15071603 · Cited by 4
Shah, M., & Woo, H. G. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1236617 · Cited by 4
Johnson, L., Bartlett, M. L., Ramirez, F., Heger, C. D., & Smith, D. R. (2023) · Journal of Immunological Methods · doi:10.1016/j.jim.2023.113586 · Cited by 4
A surrogate cell‐based SARS‐CoV‐2 spike blocking assay
Schuh, W., Baus, L., Steinmetz, T. D., Schulz, S. R., Weckwerth, L., Roth, E. A., Hauke, M., Krause, S. K., Morhart, P., Rauh, M., et al. (2021) · European Journal of Immunology · doi:10.1002/eji.202149302 · Cited by 5
Self-citationEpitope Analysis of Anti-SARS-CoV-2 Neutralizing Antibodies
Xue, J., & Tao, S. (2021) · Current Medical Science · doi:10.1007/s11596-021-2453-8 · Cited by 4
How to Deal With Vaccine Breakthrough Infection With SARS-CoV-2 Variants
Guo, Y., Jun, M., Liu, C., Chen, G., Chi, Y., Zheng, S., & Wang, H. (2022) · Frontiers in Public Health · doi:10.3389/fpubh.2022.842303 · Cited by 4
Cheng, M. H., Krieger, J., Xiang, Y., Kaynak, B., Shi, Y., Arditi, M., & Bahar, İ. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3907841 · Cited by 4
Addetia, A., Schäfer, A., Sprouse, K. R., Valdez, A., Taylor, A., Navarro, M.-J., Brown, J. T., Leaf, E. M., Miranda, M. C., Walls, A. C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.11.652904 · Cited by 4
Major classes of neutralizing antibodies evaded by the SARS-CoV-2 Omicron variant
Yuan, M., & Wilson, I. A. (2023) · Structure · doi:10.1016/j.str.2023.06.005 · Cited by 3
Mishra, S., Sharma, M., Singh, M. K., Pati, S., & Dehury, B. (2023) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.3c01443 · Cited by 3
Oyama, K., & Ueda, T. (2024) · PLoS ONE · doi:10.1371/journal.pone.0307320 · Cited by 3
Carter, J. J., Hurlburt, N. K., Scherer, E. M., Singh, S., Rodarte, J. V., Smith, R. A. J., Lewis, P., Kinzelman, R., Kieltyka, J., Cabãn, M. E., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013086 · Cited by 3
Applications of IgY in Human Medicine
Vieira-Pires, R. S., Morgan, P. M., Choraria, A., Gandhimathi, C., Michael, A., Ôchoa-Pires, T., Salimian, J., Rajan, S., & Meenatchisundaram, S. (2021) · Springer eBooks · doi:10.1007/978-3-030-72688-1_16 · Cited by 3
Molecular Insights of SARS-CoV-2 Infection and Molecular Treatments
Abdurrahman, L., Fang, X., & Zhang, Y. (2021) · Current Molecular Medicine · doi:10.2174/1566524021666211013121831 · Cited by 4
A Bacterial Cell-Based Assay To Study SARS-CoV-2 Protein-Protein Interactions
Springstein, B. L., Deighan, P., Grabe, G. J., & Hochschild, A. (2021) · mBio · doi:10.1128/mbio.02936-21 · Cited by 4
Addala, S., Vissapragada, M., Aggunna, M., Mukala, N., Lanka, M., Gampa, S., Sodasani, M., Chintalapati, J., Kamidi, A., Veeranna, R. P., et al. (2022) · Vaccines · doi:10.3390/vaccines10060841 · Cited by 3
Treatment of COVID-19 by monoclonal antibodies and the traditional Chinese medicine
Ling, Y., Dong, Y., Li, Q., Huang, D., Li, Z., & Chen, M. (2022) · Medicine in Novel Technology and Devices · doi:10.1016/j.medntd.2022.100159 · Cited by 5
Engineering recombinantly expressed lectin-based antiviral agents
Maier, I. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.990875 · Cited by 4
Raghunathan, S., Navabshan, I., Badar, B., Kim, J., & MubarakAli, D. (2022) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2022.102585 · Cited by 3
COVID-19 vaccine immunity in oncology patients
Uslu, G. H., Rakıcı, S. Y., & Yazıcı, Z. A. (2023) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.4149/bll_2023_030 · Cited by 3
Jirarojwattana, P., Shanmugaraj, B., Rattanapisit, K., & Phoolcharoen, W. (2023) · Biotechnology Reports · doi:10.1016/j.btre.2023.e00796 · Cited by 3
Lundin, S. B., Kann, H., Fulurija, A., Andersson, B., Nakka, S. S., Andersson, L., Gisslén, M., & Harandi, A. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1166924 · Cited by 3
A human antibody derived from original SARS-CoV-2 infection effectively neutralizes omicron
Li, T., Zhou, B., Dong, H., Lavillette, D., & Li, D. (2024) · Advanced Biotechnology · doi:10.1007/s44307-024-00011-1 · Cited by 3
Guerra, D., Radić, L., Brinkkemper, M., Poniman, M., van der Maas, L., Torres, J. L., Ward, A. B., Sliepen, K., Schinkel, J., Sanders, R. W., et al. (2024) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2024.2388344 · Cited by 3
The impact of high-resolution structural data on stemming the COVID-19 pandemic
Cox, R. M., & Plemper, R. K. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.05.005 · Cited by 3
Therapeutic Strategies against COVID-19 and Structural Characterization of SARS-CoV-2: A Review
Jeong, G. U., Song, H., Yoon, G. Y., Kim, D., & Kwon, Y. (2021) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pamicr2ed.2.2021.16 · Cited by 3
Gerez, G., Martinez, J., Steinbrugger, C., Bouanich, S., Dimino, J., Piegay, C., Combe, M., Berthier, F., & Daniel, S. (2022) · Biomolecules · doi:10.3390/biom12091170 · Cited by 3
Brief Overview of the Currently Available COVID-19 Vaccines
Krasilnikova, A. V. (2022) · Journal of Clinical and Health Sciences · doi:10.24191/jchs.v7i1.14658 · Cited by 2
Kelly, D. F., Jonaid, G. M., Kaylor, L., Solares, M. J., Berry, S., DiCecco, L., Dearnaley, W. J., & Casasanta, M. A. (2023) · Micromachines · doi:10.3390/mi14101869 · Cited by 3
RetractedWITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v21 · Cited by 3
A high-throughput multiplex array for antigen-specific serology with automated analysisPreprint
Rosenberg, A. F., Killian, J. T., Green, T. J., Akther, J., Hossain, M. E., Shang, Q., Qiu, S., Guang, Y., Randall, T. D., Lund, F. E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.29.534777 · Cited by 3
Lv, N., Chen, P., Dai, X., Xu, H., Li, Z., Shan, Z., Li, J., Guo, F., Chen, Y., Li, J., et al. (2025) · Advanced Science · doi:10.1002/advs.202517192 · Cited by 2
Conde, L., Oliveira, D. L., Maciel, G., Castro, F., Albuquerque, A., Rodrigues, D. A., Mello, Y., de Asis, G. M., Gabrielle, B., Ferreira, S. S., et al. (2025) · The Journal of Immunology · doi:10.1093/jimmun/vkaf305 · Cited by 2
Lefebvre, M., Chahinian, H., Yahi, N., & Fantini, J. (2026) · Biomolecules · doi:10.3390/biom16010111 · Cited by 2
Single molecule force spectroscopy for evaluating inhibitors of SARS-CoV-2 variants of concern
Zhu, R., Oh, Y. J., & Hinterdorfer, P. (2026) · European Biophysics Journal · doi:10.1007/s00249-026-01818-7 · Cited by 2
Zhang, H., Han, Z., Zou, C., Huang, Y., Sun, S., Peng, O., Ashraf, U., Xu, Q., Ge, Y., Kang, Q., et al. (2026) · iMetaOmics. · doi:10.1002/imo2.70077 · Cited by 2
Wang, L., Aliyari, S. R., Sands, N., Lee, B. Y., Yu, A., Xia, S., Jolkovsky, E. L., Zhang, S., Kim, J. T., & Cheng, G. (2026) · Immunity & Inflammation · doi:10.1007/s44466-025-00020-2 · Cited by 2
Huang, S., Wu, S., Li, F., Li, P., Sun, P., Cao, Y., Bao, H., Dong, K., Yang, J., Zhang, H., et al. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1013893 · Cited by 2
Immune response to SARS-CoV-2 variants after immunization with different vaccines in Mexico
Garay, E., Whelan, S. P. J., DuBois, R. M., O’Rourke, S. M., Salgado-Escobar, A. E., Muñoz‐Medina, J. E., Arias, C. F., & López, S. (2024) · Epidemiology and Infection · doi:10.1017/s0950268824000219 · Cited by 2
Jamal, G. A., Jahangirian, E., & Tarrahimofrad, H. (2024) · Protein and Peptide Letters · doi:10.2174/0109298665320319240809095727 · Cited by 2
Stabilizing Prefusion SARS-CoV-2 Spike by Destabilizing the Postfusion Conformation
Chakraborty, D., Singh, R., Rajmani, R. S., Kumar, S., Ringe, R. P., & Varadarajan, R. (2025) · Vaccines · doi:10.3390/vaccines13030315 · Cited by 2
Gan, M., Cao, J., Ouyang, Q., Xu, X., Wang, X., Dan, P., Yao, Y., Fu, H., Yao, X., Lin, X., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07076-z · Cited by 2
Yu, P., Yang, T., & Hsu, S. D. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.07.013 · Cited by 2
Human antibody BD-218 has broad neutralizing activity against concerning variants of SARS-CoV-2
Wang, B., Xu, H., Liang, Z., Zhao, T.-N., Zhang, X., Peng, T., Wang, Y., & Su, X. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.12.120 · Cited by 2
Fundamental aspects of the structural biology of coronaviruses
Lara-Hernández, I., Coronado-Ipiña, M. Á., Rocha-Rosas, K., & Comas‐García, M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-90248-9.00011-5 · Cited by 2
Fischer, M. F. S., Crowe, J. E., & Meiler, J. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010230 · Cited by 3
Ulinici, M., Suljič, A., Poggianella, M., Bonotto, R. M., Rus, K. R., Paraschiv, A., Bonetti, A. M., Todiraş, M., Corlăteanu, A., Groppa, S. A., et al. (2023) · Vaccines · doi:10.3390/vaccines11030637 · Cited by 2
Gutlapalli, S. D., Ganipineni, V. D. P., Danda, S., Fabián, D., Okorie, I. J., Paramsothy, J., Kailayanathan, T., Umyarova, R., Aviles, C., Garlapati, S. K. P., et al. (2023) · Cureus · doi:10.7759/cureus.36809 · Cited by 2
Ilie, O., Boloș, A., Nita, I.-B., Cojocariu, R.-O., Balmuș, I.-M., Ciobica, A., Trus, C., & Doroftei, B. (2021) · The Journal of Nervous and Mental Disease · doi:10.1097/nmd.0000000000001445 · Cited by 2
Elterman, D., Baard, J., Averbeck, M. A., HASSOUNA, M. M., Takahashi, S., Chibuzo, I. N., Sebastianelli, A., & Gacci, M. (2021) · Société Internationale d’Urologie Journal · doi:10.48083/jtru9739 · Cited by 2
The quantitative landscape of the neutralizing antibody response to SARS-CoV-2Preprint
Padmanabhan, P., Desikan, R., & Dixit, N. M. (2020) · medRxiv · doi:10.1101/2020.09.25.20201996 · Cited by 2
Wang, S.-L., Wu, D.-H., Xiong, H.-L., Wang, J., Tang, Z., Chen, Z.-H., Wang, Y.-Z., Zhang, Y.-L., Ying, D., Lin, X., et al. (2021) · bioRxiv · doi:10.1101/2021.04.10.439161 · Cited by 2
Fukuzawa, K., Kato, K., Watanabe, C., Kawashima, Y., Handa, Y., Yamamoto, A., Watanabe, K., Ohyama, T., Kamisaka, K., Takaya, D., et al. (2021) · doi:10.33774/chemrxiv-2021-njqc8 · Cited by 2
Author response: Cross-reactive antibodies after SARS-CoV-2 infection and vaccination
Grobben, M., van der Straten, K., Brouwer, P. J. M., Brinkkemper, M., Maisonnasse, P., Dereuddre‐Bosquet, N., Appelman, B., Lavell, A. A., van Vught, L. A., Burger, J. A., et al. (2021) · eLife · doi:10.7554/elife.70330.sa2 · Cited by 2
Rossotti, M. A., van Faassen, H., Tran, A., Sheff, J. G., Sandhu, J. K., Duque, D., Hewitt, M., Wen, S., Bavananthasivam, R., Beitari, S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.20.473401 · Cited by 2
WITHDRAWNPreprint
Datta, S. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v11 · Cited by 2
Yi, C., Sun, X., Lin, Y., Gu, C., Ding, L., Lu, X. P., Yang, Z. Y., Zhang, Y., Ma, L., Gu, W., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-497595/v1 · Cited by 2
Would It Be Possible to Stabilize Prefusion SARS-COV-2 Spikes with Ligands?Preprint
Coll, J. M. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13453919.v1 · Cited by 2
Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC complexes by cryoEMPreprint
Saotome, K., Dudgeon, D., Colotti, K., Moore, M. J., Jones, J. L., Zhou, Y., Rafique, A., Yancopoulos, G. D., Murphy, A. J., Lin, J. C.-Y., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.18.504455 · Cited by 2
Structural prediction of chimeric immunogens to elicit targeted antibodies against betacoronavirusesPreprint
Simpson, J., & Kasson, P. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.31.526494 · Cited by 2
Dzuvor, C. K. O., Moak, S. P., McManus, L. R., Thomas, A., Dzordzorme, A. E., Kim, T., Joseph, J., Foley, V., Gordon, I. J., Novik, L., et al. (2025) · Research Square · doi:10.1101/2025.10.01.679649 · Cited by 2
Viral immunity: Basic mechanisms and therapeutic applications—a Keystone Symposia report
Cable, J., Balachandran, S., Daley‐Bauer, L. P., Rustagi, A., Antony, F., Frere, J. J., Strampe, J., Kedzierska, K., Cannon, J. L., McGargill, M. A., et al. (2023) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14960 · Cited by 1
Assembly of Coronaviruses and CoV-Like-Particles
Cadena-López, D., Villalba-Nieto, M., Campos-Melendez, F., Rosales‐Mendoza, S., & Comas‐García, M. (2023) · Springer series in biophysics · doi:10.1007/978-3-031-36815-8_7 · Cited by 1
A bivalent form of a RBD-specific synthetic antibody effectively neutralizes SARS-CoV-2 variants
Kim, D., Kim, U., Park, I. H., Ryu, B., Yoo, Y., Cha, J. S., Yoon, G., Kim, S.-H., Oh, H., Seo, J.-Y., et al. (2023) · Antiviral Research · doi:10.1016/j.antiviral.2023.105738 · Cited by 1
In Situ Imaging of Virus-Infected Cells by Cryo-Electron Tomography: An Overview
Víjayakríshnan, S. (2023) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-40086-5_1 · Cited by 1
Progress and prospect of SARS-CoV-2 NTD-specific antibodies
Qi, G. U. I., Zhang, Z., & Ju, B. (2024) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0175 · Cited by 1
Phenomenological Modeling of Antibody Response from Vaccine Strain Composition
Ovchinnikov, V., & Karplus, M. (2025) · Antibodies · doi:10.3390/antib14010006 · Cited by 1
Lutter, L., Beal, D. M., Stanley, M., Roobol, J., Martin, S., Budge, J. D., Lee, P. E., Nemoto‐Smith, E., Brown, I. R., Warren, M. J., et al. (2026) · Nanoscale Horizons · doi:10.1039/d6nh00151c · Cited by 1
O’Connor, D., Clutterbuck, E., Gibani, M. M., Bibi, S., Sanders, K. A., Makinson, R., Kelly, D. F., & Pollard, A. J. (2025) · Nature Communications · doi:10.1038/s41467-025-61571-x · Cited by 1
Alkhofash, N. F., & Ali, B. R. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1589534 · Cited by 1
Comparative analysis of adaptive immunity to SARS-CoV-2 in infected children and adults
Nantel, S., Arnold, C. R., Bhatt, M., Galipeau, Y., Bourdin, B., Bowes, J., Zemek, R. L., Langlois, M., Quach, C., Decaluwe, H., et al. (2025) · Pediatric Research · doi:10.1038/s41390-025-04256-x · Cited by 2
Chen, C., Lovendahl, K. N., Overbaugh, J. M., & Lee, K. K. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013143 · Cited by 1
Development of an ultrahigh affinity, trimeric ACE2 biologic as a universal SARS-CoV-2 antagonist
Gonzales, J. E., Young, T., Choi, H., Park, M., Jewel, Y., Fan, C., Purohit, R., Björkman, P. J., & Williams, J. C. (2025) · Communications Biology · doi:10.1038/s42003-025-08819-w · Cited by 1
PDBe-KB Complexes: Enabling Functional Insight from Macromolecular Complexes in the PDB
Appasamy, S. D., Nair, S. S., Lawal, D. K., Pidruchna, I., Midlik, A., Leines, G. D., Balasubramaniyan, B., Afonso, M. Q. L., Fleming, J., & Velankar, S. S. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169613 · Cited by 1
Rahimnahal, S., Yousefizadeh, S., & Mohammadi, Y. S. (2026) · PLoS ONE · doi:10.1371/journal.pone.0334662 · Cited by 1
Linkage-aware inference of fitness from short-read time-series genomic data
Abdullah, S. M., Sohail, M. S., Louie, R. H. Y., Sun, Y., Barton, J. P., & McKay, M. R. (2026) · Virus Evolution · doi:10.1093/ve/veag027 · Cited by 1
Marcos-Villar, L., Perdiguero, B., Sin, L., Álvarez, E., Flores, S., Casasnovas, J. M., Pons, T., Sorzano, C. Ó. S., del Hoyo, D., Lapuhs, P., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1787877 · Cited by 1
Sawant, J., Patil, A. A., Thakar, M. R., & Kurle, S. N. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1810369 · Cited by 1
Frische, A., Gunalan, V., Krogfelt, K. A., Fomsgaard, A., & Lassaunière, R. (2023) · Vaccines · doi:10.3390/vaccines11091451 · Cited by 1
Potential use of CRISPR/Cas13 system for vaccine development against various RNA-viral infections
Mohanty, B., Mir, R. A., Priyadarshini, A., Bhat, K. A., Barati, S., Asl, E. R., Choi, J. R., & Rasmi, Y. (2024) · Future Virology · doi:10.1080/17460794.2024.2403253 · Cited by 1
Jana, I. D., Kanjo, K., Roy, S., Bhasin, M., Bhattacharya, S., Banerjee, I., Jana, S., Chatterjee, A., Chakraborty, A., Chakraborty, S. K., et al. (2025) · Journal of Virology · doi:10.1128/jvi.00051-25 · Cited by 1
Immunoinformatics Analysis of SARS-CoV-2 Isolated from Karst of Bats in Malang, Indonesia
Hadi, M. I., Prawira, A. S., Diyanah, K. C., Suprayogi, D., Keman, S., Mirasa, Y. A., & Alamudi, M. Y. (2021) · Indian Journal of Forensic Medicine & Toxicology · doi:10.37506/ijfmt.v15i2.14805 · Cited by 1
Warghane, A. J., Petkar, T., Usha Preeyaa, S., Kumari, N., & Ranjan, L. (2021) · Eurasian Journal of Medicine and Oncology · doi:10.14744/ejmo.2021.52103 · Cited by 1
Huerta-Miranda, G. A., García-García, W. I., Limón, A. M. V., & Miranda‐Hernández, M. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.2019123 · Cited by 1
Listenberger, L. L., Joiner, C. M., & Terrell, C. R. (2022) · CourseSource · doi:10.24918/cs.2022.5
Cell Entry and Unusual Replication of SARS-CoV-2
McCann, N. R., & Castellino, F. (2022) · Current Drug Targets · doi:10.2174/1389450124666221014102927 · Cited by 1
Dingens, A. S., Pratap, P. P., Malone, K. D., Hilton, S. K., Ketas, T. J., Cottrell, C. A., Overbaugh, J. M., Moore, J. P., Klasse, P. J., Ward, A. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.21.348623 · Cited by 1
Sun, J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.01.363788 · Cited by 1
MHC-II constrains the natural neutralizing antibody response to the SARS-CoV-2 spike RBM in humansPreprint
Castro, A., Ozturk, K., Zanetti, M., & Carter, H. (2020) · bioRxiv · doi:10.1101/2020.12.26.424449 · Cited by 1
Synthetic protein antigens for COVID-19 diagnosticsPreprint
Schein, C. H., Levine, C. B., McLellan, S., Negi, S. S., Braun, W. A., Dreskin, S. C., Anaya, E. S., & Schmidt, J. G. (2021) · medRxiv · doi:10.1101/2021.02.23.21251934 · Cited by 1
Novel neutralization mechanism of a human antibody with pan-coronavirus reactivityPreprint
Sun, X., Yi, C., Zhu, Y., Ding, L., Xia, S., Gu, C., Lu, X., Chen, S., Yang, Z., Zhang, Y., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-952553/v1 · Cited by 1
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv-2021-l393t-v35 · Cited by 1
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v30 · Cited by 1
WITHDRAWNPreprint
Datta, S. (2020) · ChemRxiv · doi:10.26434/chemrxiv.13102877.v15 · Cited by 1
WITHDRAWNPreprint
Datta, S. (2021) · ChemRxiv · doi:10.26434/chemrxiv-2021-l393t-v33 · Cited by 1
Metadata
- Authors
- 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., Lorenzi, J. C. C., Finkin, S., Hägglöf, T., Hurley, A., Millard, K. G., Weisblum, Y., Schmidt, F., Hatziioannou, T., Bieniasz, P. D., Caskey, M., Robbiani, D. F., Nussenzweig, M. C., & Bjorkman, P. J.
- Affiliations
- California Institute of Technology (US)
- Rockefeller University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nussenzweig, Michel C.
- ORCID
- Barnes, Christopher O.
- West, Anthony P.
- Hoffmann, Magnus A.G.
- Sharaf, Naima G.
- Hoffman, Pauline R.
- Koranda, Nicholas
- Gristick, Harry B.
- Gaebler, Christian
- Muecksch, Frauke
- Lorenzi, Julio C. Cetrulo
- Finkin, Shlomo
- Hägglöf, Thomas
- Hurley, Arlene
- Millard, Katrina G.
- Weisblum, Yiska
- Schmidt, Fabian
- Bieniasz, Paul D.
- Caskey, Marina
- Robbiani, Davide F.
- Nussenzweig, Michel C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 182
- Issue
- 4
- Pages
- 828-842.e16
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7311918
- OpenAlex
- W3036607916
- Cited by
- 795
- References
- 109
- Citations by year
- 2026: 34 · 2025: 49 · 2024: 50 · 2023: 84 · 2022: 151 · 2021: 319 · 2020: 107
- FWCI
- 21.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-nd)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- National Center for Advancing Translational Sciences (UL1 TR001866)
- Burroughs Wellcome Fund
- Howard Hughes Medical Institute
- Basic Energy Sciences (DE-AC02-76SF00515)
- National Institute of General Medical Sciences (P41GM103393, 2U19AI111825, P50 8 P50 AI150464-13, P01-AI138938-S1)
- Bill and Melinda Gates Foundation (INV-002143)
- Office of Science
- Biological and Environmental Research
- U.S. Department of Energy
- Beckman Institute, California Institute of Technology
- George Mason University
- California Institute of Technology
- National Institutes of Health
- Rockefeller University
- Icahn School of Medicine at Mount Sinai
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2 spike protein, human antibodies, neutralizing antibodies, ACE2 binding, IgG, spike protein mutations, vaccine-elicited antibodies, antibody structure
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
