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

UCSF Chimera—A visualization system for exploratory research and analysis

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Overview of the CCP 4 suite and current developments

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An interactive web-based dashboard to track COVID-19 in real time

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Inference of Macromolecular Assemblies from Crystalline State

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Computational Protein Design for COVID-19 Research and Emerging Therapeutics

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The SARS-CoV-2 neutralizing antibody response to SD1 and its evasion by BA.2.86

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Antibody Resistance of SARS-CoV-2 Omicron BA.1, BA.1.1, BA.2 and BA.3 Sub-LineagesPreprint

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Different Profiles of Antibodies and Cytokines Were Found Between Severe and Moderate COVID-19 Patients

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Endogenous Antibody Responses to SARS-CoV-2 in Patients With Mild or Moderate COVID-19 Who Received Bamlanivimab Alone or Bamlanivimab and Etesevimab Together

Zhang, L., Poorbaugh, J., Dougan, M. L., Chen, P., Gottlieb, R., Huhn, G. D., Beasley, S., Daniels, M., Trinh, T. N. V., Crisp, M., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.790469 · Cited by 25

Antibody Response of BNT162b2 and CoronaVac Platforms in Recovered Individuals Previously Infected by COVID-19 against SARS-CoV-2 Wild Type and Delta Variant

Zhang, R., Khong, K.-W., Leung, K., Liu, D., Fan, Y., Lu, L., Chan, P.-C., Chen, L., To, K. K., Chen, H., et al. (2021) · Vaccines · doi:10.3390/vaccines9121442 · Cited by 24

Coordinated evolution at amino acid sites of SARS-CoV-2 spike

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An inactivated NDV-HXP-S COVID-19 vaccine elicits a higher proportion of neutralizing antibodies in humans than mRNA vaccination

Carreño, J. M., Raskin, A. J., Singh, G., Tcheou, J., Kawabata, H., Gleason, C., Srivastava, K., Vigdorovich, V. I., Dambrauskas, N., Gupta, S. L., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo2847 · Cited by 24

Durability and breadth of neutralisation following multiple antigen exposures to SARS-CoV-2 infection and/or COVID-19 vaccination

Underwood, A. P., Sølund, C. S., Fernandez-Antunez, C., Villadsen, S. L., Mikkelsen, L. S., Fahnøe, U., Bollerup, S., Winckelmann, A. A., Schneider, U. V., Binderup, A., et al. (2023) · EBioMedicine · doi:10.1016/j.ebiom.2023.104475 · Cited by 21

Mutations in S2 subunit of SARS-CoV-2 Omicron spike strongly influence its conformation, fusogenicity, and neutralization sensitivity

Kumar, S., Delipan, R., Chakraborty, D., Kanjo, K., Singh, R., Singh, N., Siddiqui, S., Tyagi, A., Jha, V., Thakur, K. G., et al. (2023) · Journal of Virology · doi:10.1128/jvi.00922-23 · Cited by 23

SARS-CoV-2 ferritin nanoparticle vaccines elicit broad SARS coronavirus immunogenicityPreprint

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Distinct shifts in site-specific glycosylation pattern of SARS-CoV-2 spike proteins associated with arising mutations in the D614G and Alpha variants

Kuo, C., Yang, T., Chien, Y.-C., Yu, P., Hsu, S. D., & Khoo, K. (2021) · Glycobiology · doi:10.1093/glycob/cwab102 · Cited by 23

Neutralizing antibody responses over time in demographically and clinically diverse individuals recovered from SARS-CoV-2 infection in the United States and Peru: A cohort study

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ChAdOx1 nCoV-19 vaccine elicits monoclonal antibodies with cross-neutralizing activity against SARS-CoV-2 viral variants

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Single-molecule imaging reveals allosteric stimulation of SARS-CoV-2 spike receptor binding domain by host sialic acid

Díaz-Salinas, M. A., Jain, A., Durham, N. D., & Munro, J. B. (2024) · Science Advances · doi:10.1126/sciadv.adk4920 · Cited by 22

Antigenic minimalism of SARS-CoV-2 is linked to surges in COVID-19 community transmission and vaccine breakthrough infectionsPreprint

Venkatakrishnan, A., Anand, P., Lenehan, P. J., Ghosh, P., Suratekar, R., Siroha, A., Chowdhury, D. R., O’Horo, J. C., Yao, J. D. C., Pritt, B. S., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-555451/v1 · Cited by 22

Nanoscale warriors against viral invaders: a comprehensive review of Nanobodies as potential antiviral therapeutics

Verma, V., Sinha, N., & Raja, A. (2025) · mAbs · doi:10.1080/19420862.2025.2486390 · Cited by 21

N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry

Wang, D., Zhou, B., Keppel, T. R., Solano, M. I., Baudys, J., Goldstein, J. M., Finn, M. G., Fan, X., Chapman, A. P., Bundy, J. L., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-02904-w · Cited by 19

Insights into the structural peculiarities of the N-terminal and receptor binding domains of the spike protein from the SARS-CoV-2 Omicron variant

Bayani, F., Hashkavaei, N. S., Uversky, V. N., Mozaffari‐Jovin, S., & Sefidbakht, Y. (2022) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2022.105735 · Cited by 21

Heterologous SARS-CoV-2 spike protein booster elicits durable and broad antibody responses against the receptor-binding domain

Takano, T., Sato, T., Kotaki, R., Moriyama, S., Fukushi, S., Shinoda, M., Kabasawa, K., Shimada, N., Kousaka, M., Adachi, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37128-1 · Cited by 26

SARS-CoV-2 spike conformation determines plasma neutralizing activityPreprint

Bowen, J. E., Walls, A. C., Joshi, A., Sprouse, K. R., Stewart, C., Tortorici, M. A., Franko, N., Logue, J. K., Mazzitelli, I. G., Tilles, S. W., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.19.473391 · Cited by 21

Spread of endemic SARS-CoV-2 lineages in Russia before April 2021

Klink, G. V., Safina, K. R., Garushyants, S. K., Moldovan, M. A., Nabieva, E., Komissarov, A. B., Lioznov, D. A., & Bazykin, G. A. (2022) · PLoS ONE · doi:10.1371/journal.pone.0270717 · Cited by 21

Comprehensive Overview of Broadly Neutralizing Antibodies against SARS-CoV-2 Variants

Cui, L., Li, T., Xue, W., Zhang, S., Wang, H., Liu, H., Gu, Y., Xia, N., & Li, S. (2024) · Viruses · doi:10.3390/v16060900 · Cited by 18

Rapid, early, and potent Spike-directed IgG, IgM, and IgA distinguish asymptomatic from mildly symptomatic COVID-19 in Uganda, with IgG persisting for 28 months

Serwanga, J., Ankunda, V., Sembera, J., Kato, L., Oluka, G. K., Baine, C., Odoch, G., Kayiwa, J. T., Auma, B. O., Jjuuko, M., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1152522 · Cited by 20

Analysis of the N-glycosylation profiles of the spike proteins from the Alpha, Beta, Gamma, and Delta variants of SARS-CoV-2

Wang, D., Baudys, J., Osman, S. H., & Barr, J. R. (2023) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-023-04771-y · Cited by 19

A broadly reactive antibody targeting the N-terminal domain of SARS-CoV-2 spike confers Fc-mediated protection

Adams, L. J., VanBlargan, L. A., Liu, Z., Gilchuk, P., Zhao, H., Chen, R. E., Raju, S., Chong, Z., Whitener, B. M., Shrihari, S., et al. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101305 · Cited by 18

Investigation and Comparison of Specific Antibodies’ Affinity Interaction with SARS-CoV-2 Wild-Type, B.1.1.7, and B.1.351 Spike Protein by Total Internal Reflection Ellipsometry

Plikusienė, I., Mačiulis, V., Juciutė, S., Maciulevičienė, R., Balevičius, S., Ramanavičius, A., & Ramanavičienė, A. (2022) · Biosensors · doi:10.3390/bios12050351 · Cited by 19

More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells

Gaetano, S. D., Capasso, D., Delre, P., Pirone, L., Saviano, M., Pedone, E. M., & Mangiatordi, G. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126462 · Cited by 19

Protein engineering responses to the COVID-19 pandemic

Hsieh, C., & McLellan, J. S. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102385 · Cited by 17

Structural and computational design of a SARS-CoV-2 spike antigen with improved expression and immunogenicity

Williams, J. A., Biancucci, M., Lessen, L. N., Tian, S., Balsaraf, A., Chen, L., Chesterman, C. C., Maruggi, G., Vandepaer, S., Huang, Y., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg0330 · Cited by 18

Broadly neutralizing antibodies derived from the earliest COVID-19 convalescents protect mice from SARS-CoV-2 variants challenge

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Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain

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Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants

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The neutralization potency of anti-SARS-CoV-2 therapeutic human monoclonal antibodies is retained against viral variants

Makdasi, E., Zvi, A., Alcalay, R., Noy-Porat, T., Peretz, E., Mechaly, A., Levy, Y., Epstein, E., Chitlaru, T., Tennenhouse, A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109679 · Cited by 19

Structural Dynamics and Molecular Evolution of the SARS-CoV-2 Spike Protein

Wolf, K., Kwan, J. C., & Kamil, J. P. (2022) · mBio · doi:10.1128/mbio.02030-21 · Cited by 17

Conserved Neutralizing Epitopes on the N-Terminal Domain of Variant SARS-CoV-2 Spike ProteinsPreprint

Wang, Z.-J., Muecksch, F., Cho, A., Gaebler, C., Hoffmann, H., Ramos, V. A., Zong, S., Cipolla, M., Johnson, B., Schmidt, F., et al. (2022) · bioRxiv · doi:10.1101/2022.02.01.478695 · Cited by 20

From Alpha to Omicron SARS‐CoV‐2 variants: What their evolutionary signatures can tell us?

Andreata‐Santos, R., Janini, L. M., & Durães‐Carvalho, R. (2022) · Journal of Medical Virology · doi:10.1002/jmv.27555 · Cited by 17

SARS-CoV-2 spike variants differ in their allosteric responses to linoleic acid

Oliveira, A. S. F., Shoemark, D. K., Davidson, A. D., Berger, I., Schaffitzel, C., & Mulholland, A. J. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad021 · Cited by 18

Emerging variants develop total escape from potent monoclonal antibodies induced by BA.4/5 infection

Liu, C., Das, R., Dijokaite-Guraliuc, A., Zhou, D., Mentzer, A. J., Supasa, P., Selvaraj, M., Duyvesteyn, H. M. E., Ritter, T. G., Temperton, N. J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47393-3 · Cited by 17

Deep repertoire mining uncovers ultra-broad coronavirus neutralizing antibodies targeting multiple spike epitopes

Hurtado, J., Rogers, T. F., Jaffe, D. B., Adams, B. A., Bangaru, S., Garcia, E., Capozzola, T., Messmer, T., Sharma, P., Song, G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114307 · Cited by 17

Protein nanoparticle vaccines induce potent neutralizing antibody responses against MERS-CoV

Chao, C. W., Sprouse, K. R., Miranda, M. C., Catanzaro, N., Hubbard, M. L., Addetia, A., Stewart, C., Brown, J. T., Dosey, A. M., Valdez, A., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115036 · Cited by 18

Structural and energetic profiling of SARS-CoV-2 receptor binding domain antibody recognition and the impact of circulating variants

Yin, R. M., Guest, J. D., Taherzadeh, G., Gowthaman, R., Mittra, I., Quackenbush, J., & Pierce, B. G. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009380 · Cited by 18

Distinct BCR repertoires elicited by SARS-CoV-2 RBD and S vaccinations in mice

Tian, S., Ji, K., Wang, M., Wang, F., Wang, H., Huang, W., Huang, Q., & Yan, J. (2021) · Cell Discovery · doi:10.1038/s41421-021-00331-9 · Cited by 16

Optimization of Anti-SARS-CoV-2 Neutralizing Antibody Therapies: Roadmap to Improve Clinical Effectiveness and Implementation

van der Straten, K., van Gils, M. J., de Taeye, S. W., & de Bree, G. J. (2022) · Frontiers in Medical Technology · doi:10.3389/fmedt.2022.867982 · Cited by 17

Cell-based reporter assays for measurements of antibody-mediated cellular cytotoxicity and phagocytosis against SARS-CoV-2 spike protein

Hong, Y., Guo, H., Wei, M., Zhang, Y., Fang, M., Cheng, T., Li, Z., Ge, S., Yao, X., Yuan, Q., et al. (2022) · Journal of Virological Methods · doi:10.1016/j.jviromet.2022.114564 · Cited by 16

Structures of the SARS-CoV-2 spike glycoprotein and applications for novel drug development

Liu, X.-H., Cheng, T., Liu, B., Chi, J., Shu, T., & Wang, T. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.955648 · Cited by 17

Broad strategies for neutralizing SARS-CoV-2 and other human coronaviruses with monoclonal antibodies

Ling, Z., Yi, C., Sun, X., Yang, Z., & Sun, B. (2022) · Science China Life Sciences · doi:10.1007/s11427-022-2215-6 · Cited by 16

Deep mutagenesis scanning using whole trimeric SARS-CoV-2 spike highlights the importance of NTD-RBD interactions in determining spike phenotype

Kugathasan, R., Sukhova, K., Moshe, M., Kellam, P., & Barclay, W. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011545 · Cited by 16

Evolutionary trajectory of SARS-CoV-2 genome shifts during widespread vaccination and emergence of Omicron variant

Gayvert, K. M., McKay, S., Lim, W. K., Baum, A., Kyratsous, C. A., Copin, R., & Atwal, G. S. (2023) · npj Viruses · doi:10.1038/s44298-023-00007-z · Cited by 17

Bispecific antibodies targeting the N-terminal and receptor binding domains potently neutralize SARS-CoV-2 variants of concern

Rubio, A. A., Baharani, V. A., Dadonaite, B., Parada, M., Abernathy, M. E., Wang, Z., Lee, Y. E., Eso, M. R., Phung, J. L., Ramos, I., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adq5720 · Cited by 21

Mutational Hotspot in the SARS-CoV-2 Spike Protein N-Terminal Domain Conferring Immune Escape Potential

Kubik, S., Arrigo, N., Bonet, J., & Xu, Z. (2021) · Viruses · doi:10.3390/v13112114 · Cited by 16

Long Term Immune Response Produced by the SputnikV Vaccine

Martynova, E. V., Hamza, S., Garanina, E. E., Kabwe, E., Markelova, M., Shakirova, V. G., Хаертынова, И. М., Kaushal, N., Baranwal, M., Rizvanov, A. A., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011211 · Cited by 18

Omicron-specific ultra-potent SARS-CoV-2 neutralizing antibodies targeting the N1/N2 loop of Spike N-terminal domain

Niu, X., Li, Z., Wang, J., Jian, F., Yu, Y., Song, W., Yisimayi, A., Du, S., Zhang, Z., Wang, Q., et al. (2024) · Emerging Microbes & Infections · doi:10.1080/22221751.2024.2412990 · Cited by 15

Frequent use of IGHV3-30-3 in SARS-CoV-2 neutralizing antibody responses

Pushparaj, P., Nicoletto, A., Dopico, X. C., Sheward, D. J., Kim, S., Ekström, S., Murrell, B., Corcoran, M., & Hedestam, G. B. K. (2023) · Frontiers in Virology · doi:10.3389/fviro.2023.1128253 · Cited by 16

Convergence of immune escape strategies highlights plasticity of SARS-CoV-2 spike

Yu, X., Juraszek, J., Rutten, L., Bakkers, M. J. G., Blokland, S., Melchers, J. M., van den Broek, N. J. F., Verwilligen, A., Abeywickrema, P. D., Vingerhoets, J., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011308 · Cited by 16

Therapeutic antibodies and alternative formats against SARS-CoV-2

Winiger, R. R., & Perez, L. H. (2024) · Antiviral Research · doi:10.1016/j.antiviral.2024.105820 · Cited by 16

Potent neutralization of SARS-CoV-2 variants by RBD nanoparticle and prefusion-stabilized spike immunogens

Miranda, M. C., Kepl, E., Navarro, M. J., Chen, C., Johnson, M. R., Sprouse, K. R., Stewart, C., Palser, A. L., Valdez, A. S., Pettie, D., et al. (2024) · npj Vaccines · doi:10.1038/s41541-024-00982-1 · Cited by 14

Immunology of SARS-CoV-2 infections and vaccines

Schenten, D., & Bhattacharya, D. (2021) · Advances in immunology · doi:10.1016/bs.ai.2021.08.002 · Cited by 14

Neutralizing and enhancing antibodies against SARS-CoV-2

Liu, Y., & Arase, H. (2022) · Inflammation and Regeneration · doi:10.1186/s41232-022-00233-7 · Cited by 13

Interaction of SARS-CoV-2 with host cells and antibodies: experiment and simulation

Nguyen, H. V., Nguyen, H. L., Lan, P. D., Thai, N. Q., Sikora, M., & Li, M. S. (2023) · Chemical Society Reviews · doi:10.1039/d1cs01170g · Cited by 15

Antibodies utilizing VL6-57 light chains target a convergent cryptic epitope on SARS-CoV-2 spike protein and potentially drive the genesis of Omicron variants

Yan, Q., Gao, X., Liu, B., Hou, R., He, P., Ma, Y., Zhang, Y., Zhang, Y., Li, Z., Chen, Q., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51770-3 · Cited by 15

SARS-CoV-2 variants resist antibody neutralization and broaden host ACE2 usagePreprint

Wang, R., Zhang, Q., Ge, J., Ren, W., Zhang, R., Lan, J., Ju, B., Su, B., Yu, F., Chen, P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.09.434497 · Cited by 14

Structural and functional characterizations of altered infectivity and immune evasion of SARS-CoV-2 Omicron variantPreprint

Cui, Z., Liu, P., Wang, N., Wang, L., Fan, K., Zhu, Q., Wang, K., Chen, R., Feng, R., Jia, Z., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.29.474402 · Cited by 14

Optimizing a human monoclonal antibody for better neutralization of SARS-CoV-2

Wang, Q., Guo, Y., Casner, R. G., Yu, J., Nair, M. S., Ho, J., Reddem, E. R., Mellis, I. A., Wu, M., Tzang, C.-C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61472-z · Cited by 15

Impact of systemic SARS-CoV-2 vaccination on mucosal IgA responses to subsequent breakthrough infection

Marking, U. W., Bladh, O., Aguilera, K., Pongrácz, T., Havervall, S., Greilert‐Norin, N., Blom, K. G., Klingström, J., Wang, Y., Åberg, M., et al. (2025) · EBioMedicine · doi:10.1016/j.ebiom.2025.105912 · Cited by 16

Evidence of recurrent selection of mutations commonly found in SARS-CoV-2 variants of concern in viruses infecting immunocompromised patients

Goes, L. R., Siqueira, J. D., Garrido, M. M., Alves, B. M., Cicala, C., Arthos, J. A., Viola, J. P. B., & Soares, M. A. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.946549 · Cited by 12

Broad and potent neutralizing antibodies are elicited in vaccinated individuals following Delta/BA.1 breakthrough infection

Seow, J., Shalim, Z. A., Graham, C., Kimuda, S., Pillai, A., Lechmere, T., Kurshan, A., Khimji, A. M., Snell, L. B., Nebbia, G., et al. (2023) · mBio · doi:10.1128/mbio.01206-23 · Cited by 10

Characterisation of the antibody-mediated selective pressure driving intra-host evolution of SARS-CoV-2 in prolonged infection

Schöfbänker, M., Günther, T., Lorentzen, E. U., Romberg, M.-L., Hennies, M. T., Neddermeyer, R., Müller, M. M., Mellmann, A., Bojarzyn, C. R., Lenz, G., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012624 · Cited by 16

A novel competition ELISA for the rapid quantification of SARS‐CoV ‐2 neutralizing antibodies in convalescent plasma

Wouters, E., Verbrugghe, C., Devloo, R., Debruyne, I., Clippel, D. D., Heddegem, L. V., Asch, K. V., Gaver, V. V., Vanbrabant, M., Muylaert, A., et al. (2021) · Transfusion · doi:10.1111/trf.16652 · Cited by 13

Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins

Overduin, M., Kervin, T. A., & Tran, A. (2022) · iScience · doi:10.1016/j.isci.2022.104722 · Cited by 14

Network analysis uncovers the communication structure of SARS-CoV-2 spike protein identifying sites for immunogen design

Manrique, P. D., Chakraborty, S., Henderson, R. C., Edwards, R. J., Mansbach, R. A., Nguyen, K., Stalls, V., Saunders, C., Mansouri, K., Acharya, P., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105855 · Cited by 13

mRNA vaccines and hybrid immunity use different B cell germlines against Omicron BA.4 and BA.5

Andreano, E., Paciello, I., Pierleoni, G., Maccari, G., Antonelli, G., Abbiento, V., Pileri, P., Benincasa, L., Giglioli, G., Piccini, G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37422-y · Cited by 14

Antibodies to S2 domain of SARS-CoV-2 spike protein in Moderna mRNA vaccinated subjects sustain antibody-dependent NK cell-mediated cell cytotoxicity against Omicron BA.1

Balinsky, C. A., Jiang, L., Jani, V., Cheng, Y., Zhang, Z., Belinskaya, T., Qiu, Q., Long, T. K., Schilling, M. A., Jenkins, S. A., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1266829 · Cited by 15

Enhanced Surface Accessibility of SARS-CoV-2 Omicron Spike Protein Due to an Altered Glycosylation Profile

Wang, D., Zhang, Z., Baudys, J., Haynes, C. A., Osman, S. H., Zhou, B., Barr, J. R., & Gumbart, J. C. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00015 · Cited by 13

An Antigenic Space Framework for Understanding Antibody Escape of SARS-CoV-2 Variants

Miller, N. L., Clark, T., Raman, R., & Sasisekharan, R. (2021) · Viruses · doi:10.3390/v13102009 · Cited by 10

Contributions of single-particle cryoelectron microscopy toward fighting COVID-19

Rapp, M., Shapiro, L. S., & Frank, J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.10.005 · Cited by 12

A combination of potently neutralizing monoclonal antibodies isolated from an Indian convalescent donor protects against the SARS-CoV-2 Delta variant

Hingankar, N. K., Deshpande, S., Das, P., Rizvi, Z. A., Wibmer, C. K., Mashilo, P., Ansari, M. Y., Burns, A., Barman, S., Zhao, F., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010465 · Cited by 14

Association Between Human Immunodeficiency Virus Viremia and Compromised Neutralization of Severe Acute Respiratory Syndrome Coronavirus 2 Beta Variant

Hwa, S.-H., Snyman, J., Bernstein, M. P., Ganga, Y., Cele, S., Muema, D., Tan, C. W., Khan, K., Karim, F., Hanekom, W. A., et al. (2022) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiac343 · Cited by 12

Broad SARS-CoV-2 neutralization by monoclonal and bispecific antibodies derived from a Gamma-infected individual

Guerra, D., Beaumont, T., Radić, L., Kerster, G., van der Straten, K., Yuan, M., Torres, J. L., Lee, W.-H., Liu, H., Poniman, M., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108009 · Cited by 13

Antibodies that neutralize all current SARS-CoV-2 variants of concern by conformational lockingPreprint

Liu, L., Casner, R. G., Guo, Y., Wang, Q., Iketani, S., Chan, J. F., Yu, J., Dadonaite, B., Nair, M. S., Mohri, H., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.08.536123 · Cited by 12

Potent NTD-Targeting Neutralizing Antibodies against SARS-CoV-2 Selected from a Synthetic Immune System

Li, W., Wang, F., Li, Y., Yan, L., Liu, L., Zhu, W., Ma, P., Shi, X., & Yang, G. (2023) · Vaccines · doi:10.3390/vaccines11040771 · Cited by 11

Risk assessment of SARS-CoV-2 replicating and evolving in animals

Zhao, J., Kang, M., Wu, H., Sun, B., Baele, G., He, W., Lu, M., Suchard, M. A., Ji, X., He, N., et al. (2023) · Trends in Microbiology · doi:10.1016/j.tim.2023.07.002 · Cited by 12

Biology and Behavior of Severe Acute Respiratory Syndrome Coronavirus Contagion with Emphasis on Treatment Strategies, Risk Assessment, and Resilience

Baldwin, J., Noorali, S., & Vaseashta, A. (2023) · COVID · doi:10.3390/covid3090089 · Cited by 14

Heterogeneous SARS-CoV-2-Neutralizing Activities After Infection and Vaccination

Graninger, M., Camp, J. V., Aberle, S. W., Traugott, M. T., Hoepler, W., Puchhammer‐Stöckl, E., Weseslindtner, L., Zoufaly, A., Aberle, J. H., & Stiasny, K. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.888794 · Cited by 12

Antigenic mapping reveals sites of vulnerability on α-HCoV spike protein

Xiang, J., Su, J., Lan, Q., Zhao, W., Zhou, Y., Xu, Y., Niu, J., Xia, S., Qi, Q., Sidhu, S. S., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04160-8 · Cited by 11

Exploring Conformational Landscapes and Cryptic Binding Pockets in Distinct Functional States of the SARS-CoV-2 Omicron BA.1 and BA.2 Trimers: Mutation-Induced Modulation of Protein Dynamics and Network-Guided Prediction of Variant-Specific Allosteric Binding Sites

Verkhivker, G. M., Alshahrani, M., & Gupta, G. (2023) · Viruses · doi:10.3390/v15102009 · Cited by 11

The role of N-glycosylation in spike antigenicity for the SARS-CoV-2 gamma variant

Pegg, C. L., Modhiran, N., Parry, R. H., Liang, B., Amarilla, A. A., Khromykh, A. A., Burr, L. D., Young, P. R., Chappell, K. J., Schulz, B. L., et al. (2023) · Glycobiology · doi:10.1093/glycob/cwad097 · Cited by 13

An anti-SARS-CoV-2 non-neutralizing antibody with Fc-effector function defines a new NTD epitope and delays neuroinvasion and death in K18-hACE2 micePreprint

Beaudoin-Bussières, G., Chen, Y.-Z., Ullah, I., Prévost, J., Tolbert, W., Symmes, K., Ding, S.-L., Benlarbi, M., Gong, S., Tauzin, A., et al. (2021) · bioRxiv · doi:10.1101/2021.09.08.459408 · Cited by 15

Engineered ACE2 counteracts vaccine-evading SARS-CoV-2 Omicron variantPreprint

Ikemura, N., Taminishi, S., Inaba, T., Arimori, T., Motooka, D., Katoh, K., Kirita, Y., Higuchi, Y., Li, S., Suzuki, T., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.22.473804 · Cited by 11

Evolving spike-protein N -glycosylation in SARS-CoV-2 variantsPreprint

Baboo, S., Diedrich, J. K., Torres, J. L., Copps, J., Singh, B., Garrett, P. T., Ward, A. B., Paulson, J. C., & Yates, J. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.08.539897 · Cited by 10

Deep immunoglobulin repertoire sequencing depicts a comprehensive atlas of spike-specific antibody lineages shared among COVID-19 convalescents

Yan, Q., Zhang, Y., Hou, R., Pan, W., Liang, H., Gao, X., Deng, W., Huang, X., Qu, L., Tang, C., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2290841 · Cited by 9

SARS-CoV-2 neutralizing antibody specificities differ dramatically between recently infected infants and immune-imprinted individuals

Dadonaite, B., Burrell, A. R., Logue, J., Chu, H. Y., Payne, D. C., Haslam, D. B., Staat, M. A., & Bloom, J. D. (2025) · Journal of Virology · doi:10.1128/jvi.00109-25 · Cited by 10

Public antibodies: convergent signatures in human humoral immunity against pathogens

Rao, V. N., & Coelho, C. H. (2025) · mBio · doi:10.1128/mbio.02247-24 · Cited by 10

GLYCO: a tool to quantify glycan shielding of glycosylated proteins

Lee, M., Reveiz, M., Rawi, R., Kwong, P. D., & Chuang, G. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab791 · Cited by 10

On the Evolutionary Trajectory of SARS-CoV-2: Host Immunity as a Driver of Adaptation in RNA Viruses

Warger, J., & Gaudieri, S. (2022) · Viruses · doi:10.3390/v15010070 · Cited by 11

Humoral Immune Response Profile of COVID-19 Reveals Severity and Variant-Specific Epitopes: Lessons from SARS-CoV-2 Peptide Microarray

Acharjee, A., Ray, A., Salkar, A., Bihani, S., Tuckley, C., Shastri, J. S., Agrawal, S. R., Duttagupta, S. P., & Srivastava, S. (2023) · Viruses · doi:10.3390/v15010248 · Cited by 10

Cryo-EM and cryo-ET of the spike, virion, and antibody neutralization of SARS-CoV-2 and VOCs

Xu, C., Han, W., & Cong, Y. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102664 · Cited by 9

Profiling Humoral Immunity After Mixing and Matching COVID-19 Vaccines Using SARS-CoV-2 Variant Protein Microarrays

Kuo, H., Kuo, K.-C., Du, P.-X., Keskin, B. B., Su, W., Ho, T., Tsai, P.-S., Pau, C. H., Shih, H.-C., Huang, Y., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100507 · Cited by 12

Ultrapotent bispecific antibodies neutralize emerging SARS-CoV-2 variantsPreprint

Cho, H., Gonzales-Wartz, K. K., Huang, D.-L., Yuan, M., Peterson, M., Liang, J. Y., Beutler, N., Torres, J., Cong, Y., Postnikova, E., et al. (2021) · bioRxiv · doi:10.1101/2021.04.01.437942 · Cited by 10

Neutralisation resistance of SARS-CoV-2 spike-variants is primarily mediated by synergistic receptor binding domain substitutions

Pham, L. V., Underwood, A. P., Binderup, A., Fahnøe, U., Fernandez-Antunez, C., Mendez, B. L., Ryberg, L. A., Galli, A., Sølund, C. S., Weis, N. M., et al. (2024) · Emerging Microbes & Infections · doi:10.1080/22221751.2024.2412643 · Cited by 9

Neutralizing antibody 5-7 defines a distinct site of vulnerability in SARS-CoV-2 spike N-terminal domain

Cerutti, G., Guo, Y., Wang, P., Nair, M. S., Wang, M., Huang, Y., Yu, J., Liu, L., Katsamba, P. S., Bahna, F. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109928 · Cited by 63

An NTD supersite of attack

Lok, S. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.010 · Cited by 63

Conserved Neutralizing Epitopes on the N-Terminal Domain of Variant SARS-CoV-2 Spike ProteinsPreprint

Wang, Z.-J., Muecksch, F., Cho, A., Gaebler, C., Hoffmann, H., Ramos, V. A., Zong, S., Cipolla, M., Johnson, B., Schmidt, F., et al. (2022) · bioRxiv · doi:10.1101/2022.02.01.478695 · Cited by 20

Hitting SARS-CoV-2 in a new spot

Vinson, V. J. (2020) · Science · doi:10.1126/science.369.6504.639-l

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