A Potently Neutralizing Antibody Protects Mice against SARS-CoV-2 Infection

Basic local alignment search tool

Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · 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

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

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

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

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

Comprehensive Integration of Single-Cell Data

Stuart, T., Butler, A., Hoffman, P., Hafemeister, C., Papalexi, E., Mauck, W. M., Hao, Y., Stoeckius, M., Smibert, P., & Satija, R. (2019) · Cell · doi:10.1016/j.cell.2019.05.031 · Cited by 15,453 · see citing works

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

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

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

Identification of a novel coronavirus in patients with severe acute respiratory syndrome

Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574 · 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

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 · cited 3× · see citing works

Structure, Function, and Evolution of Coronavirus Spike Proteins

Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740 · see citing works

Janeway's Immunobiology

MURPHY, K. M. M., & Weaver, C. T. (2016) · W.W. Norton eBooks · doi:10.1201/9781315533247 · Cited by 2,262 · 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 · cited 1× · see citing works

Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine

Tai, W., He, L., Zhang, X., Pu, J., Voronin, D., Jiang, S., Zhou, Y., & Du, L. (2020) · Cellular & Molecular Immunology · doi:10.1038/s41423-020-0400-4 · Cited by 1,654 · see citing works

The spike protein of SARS-CoV — a target for vaccine and therapeutic development

Du, L., He, Y., Zhou, Y., Liu, S., Zheng, B.-J., & Jiang, S. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2090 · Cited by 1,649 · see citing works

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

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

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

Reconstructing lineage hierarchies of the distal lung epithelium using single-cell RNA-seq

Treutlein, B., Brownfield, D. G., Wu, A. R., Neff, N. F., Mantalas, G. L., Espinoza, F. H., Desai, T. J., Krasnow, M. A., & Quake, S. R. (2014) · Nature · doi:10.1038/nature13173 · Cited by 1,342 · see citing works

Pathogenesis and transmission of SARS-CoV-2 in golden hamsters

Sia, S. F., Yan, L.-M., Chin, A. W. H., Fung, K., Choy, K.-T., Wong, A. Y. L., Kaewpreedee, P., Perera, R. A. P. M., Poon, L. L. M., Nicholls, J. M., et al. (2020) · Nature · doi:10.1038/s41586-020-2342-5 · Cited by 1,303 · see citing works

A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2

Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286 · 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

Ensembl 2020

Yates, A. D., Achuthan, P., Akanni, W. A., Allen, J., Allen, J., Álvarez-Jarreta, J., Amode, M. R., Armean, I. M., Azov, A. G., Bennett, R., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz966 · Cited by 1,162 · 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

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

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

ACE2 Receptor Expression and Severe Acute Respiratory Syndrome Coronavirus Infection Depend on Differentiation of Human Airway Epithelia

Jia, H. P., Look, D. C., Shi, L., Hickey, M. A., Pewe, L. L., Netland, J., Farzan, M., Wohlford-Lenane, C., Perlman, S. M., & McCray, P. B. (2005) · Journal of Virology · doi:10.1128/jvi.79.23.14614-14621.2005 · Cited by 950 · 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

IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains

Lefranc, M., Pommie, C., Ruíz, M., Giudicelli, V., Foulquier, E., Truong, L., Contet, V., & Lefranc, G. (2002) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(02)00039-3 · Cited by 823 · see citing works

IMGT unique numbering for immunoglobulin and T cell receptor constant domains and Ig superfamily C-like domains

Lefranc, M., Pommie, C., Kaas, Q., Duprat, É., Bosc, N., Guiraudou, D., Jean, C., Ruíz, M., da Piedade, I., Rouard, M., et al. (2004) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2004.07.003 · Cited by 808 · see citing works

Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase

Wang, Q., Wu, J., Wang, H., Gao, Y., Liu, Q., Mu, A., Ji, W., Yan, L., Zhu, Y., Zhu, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.034 · Cited by 779 · see citing works

Evaluation of the concentration and bioactivity of adenovirus vectors for gene therapy

Mittereder, N., March, K. L., & Trapnell, B. C. (1996) · Journal of Virology · doi:10.1128/jvi.70.11.7498-7509.1996 · Cited by 778 · see citing works

Mouse Genome Database (MGD) 2019

Bult, C. J., Blake, J. A., Smith, C. L., Kadin, J. A., Richardson, J. E., the Mouse Genome Database Group, Anagnostopoulos, A., Asabor, R., Baldarelli, R. M., Beal, J. S., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1056 · Cited by 686 · see citing works

Modernizing Reference Genome Assemblies

Church, D., Schneider, V. A., Graves, T., Auger, K., Cunningham, F., Bouk, N., Chen, H.-C., Agarwala, R., McLaren, W., Ritchie, G., et al. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001091 · Cited by 563 · see citing works

IMGT/GENE-DB: a comprehensive database for human and mouse immunoglobulin and T cell receptor genes

Giudicelli, V. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki010 · Cited by 548 · see citing works

Severe Acute Respiratory Syndrome Coronavirus 2 from Patient with Coronavirus Disease, United States

Harcourt, J. L., Tamin, A., Lu, X., Kamili, S., Sakthivel, S. K., Murray, J., Queen, K. J., Tao, Y., Paden, C. R., Zhang, J., et al. (2020) · Emerging infectious diseases · doi:10.3201/eid2606.200516 · Cited by 524 · see citing works

The potential danger of suboptimal antibody responses in COVID-19

Iwasaki, A., & Yang, Y.-X. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-0321-6 · Cited by 510 · see citing works

A SARS-CoV-2 Infection Model in Mice Demonstrates Protection by Neutralizing Antibodies

Hassan, A. O., Case, J. B., Winkler, E. S., Thackray, L. B., Kafai, N. M., Bailey, A. L., McCune, B. T., Fox, J. M., Chen, R. E., Alsoussi, W. B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.011 · Cited by 477 · see citing works

pRESTO: a toolkit for processing high-throughput sequencing raw reads of lymphocyte receptor repertoires

Heiden, J. A. V., Yaari, G., Uduman, M., Stern, J. N. H., O’Connor, K. C., Hafler, D. A., Vigneault, F., & Kleinstein, S. H. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu138 · Cited by 469 · see citing works

Paul Ehrlich (1854-1915) and His Contributions to the Foundation and Birth of Translational Medicine

Valent, P., Groner, B., Schumacher, U., Superti‐Furga, G., Busslinger, M., Královics, R., Zielinski, C. C., Penninger, J. M., Kerjaschki, D., Stingl, G., et al. (2016) · Journal of Innate Immunity · doi:10.1159/000443526 · Cited by 410 · see citing works

Protective monotherapy against lethal Ebola virus infection by a potently neutralizing antibody

Corti, D., Misasi, J., Mulangu, S., Stanley, D. A., Kanekiyo, M., Wollen-Roberts, S. E., Ploquin, A., Doria‐Rose, N. A., Staupe, R. P., Bailey, M., et al. (2016) · Science · doi:10.1126/science.aad5224 · Cited by 398 · see citing works

Structural Basis of Zika Virus-Specific Antibody Protection

Zhao, H., Fernández, E., Dowd, K. A., Speer, S. D., Platt, D. J., Gorman, M. J., Govero, J., Nelson, C. A., Pierson, T. C., Diamond, M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.020 · Cited by 377 · see citing works

TLR9/MyD88 signaling is required for class switching to pathogenic IgG2a and 2b autoantibodies in SLE

Ehlers, M., Fukuyama, H., McGaha, T. L., Aderem, A. A., & Ravetch, J. V. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052438 · Cited by 338 · see citing works

Cloning and expression of murine Ig genes from single B cells

Tiller, T., Busse, C. E., & Wardemann, H. (2009) · Journal of Immunological Methods · doi:10.1016/j.jim.2009.08.009 · Cited by 277 · see citing works

Blocking Monoclonal Antibodies Specific for Mouse IFN- α / β Receptor Subunit 1 (IFNAR-1) from Mice Immunized by In Vivo Hydrodynamic Transfection

Sheehan, K. C. F., Lai, K. S., Dunn, G. P., Bruce, A. T., Diamond, M. S., Heutel, J. D., Dungo-Arthur, C., Carrero, J. A., White, J. M., Hertzog, P. J., et al. (2006) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2006.26.804 · Cited by 260 · see citing works

Evasion of antibody neutralization in emerging severe acute respiratory syndrome coronaviruses

Yang, Z., Werner, H. C., Kong, W., Leung, K., Traggiai, E., Lanzavecchia, A., & Nabel, G. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409065102 · Cited by 250 · see citing works

The Ensembl REST API: Ensembl Data for Any Language

Yates, A. D., Beal, K., Keenan, S., McLaren, W., Pignatelli, M., Ritchie, G., Ruffier, M., Taylor, K., Vullo, A., & Flicek, P. (2014) · Bioinform. · doi:10.1093/bioinformatics/btu613 · Cited by 213 · see citing works

Housekeeping and tissue-specific genes in mouse tissues

Kouadjo, K. E., Nishida, Y., Cadrin-Girard, J.-F., Yoshioka, M., & St‐Amand, J. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-127 · Cited by 205 · see citing works

Sequencing and cloning of antigen-specific antibodies from mouse memory B cells

von Boehmer, L., Liu, C., Ackerman, S. E., Gitlin, A. D., Wang, Q., Gazumyan, A., & Nussenzweig, M. C. (2016) · Nature Protocols · doi:10.1038/nprot.2016.102 · Cited by 203 · see citing works

Longitudinal Analysis of the Human B Cell Response to Ebola Virus Infection

Davis, C. W., Jackson, K., McElroy, A. K., Halfmann, P., Huang, J. Y., Chennareddy, C., Piper, A., Leung, Y., Albariño, C., Crozier, I., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.036 · Cited by 172 · see citing works

Hierarchical Clustering Can Identify B Cell Clones with High Confidence in Ig Repertoire Sequencing Data

Gupta, N. T., Adams, K., Briggs, A. W., Timberlake, S. C., Vigneault, F., & Kleinstein, S. H. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601850 · Cited by 159 · see citing works

Leveraging heterogeneity across multiple datasets increases cell-mixture deconvolution accuracy and reduces biological and technical biases

Vallania, F., Tam, A., Lofgren, S., Schaffert, S. A., Azad, T. D., Bongen, E., Haynes, W. A., Alsup, M., Alonso, M. N., Davis, M. M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07242-6 · Cited by 158 · see citing works

Coronaviren als Ursache respiratorischer Infektionen

Corman, V. M., Lienau, J., & Witzenrath, M. (2019) · Der Internist · doi:10.1007/s00108-019-00671-5 · Cited by 140 · see citing works

Monoclonal Antibodies for Emerging Infectious Diseases — Borrowing from History

Marston, H. D., Paules, C. I., & Fauci, A. S. (2018) · New England Journal of Medicine · doi:10.1056/nejmp1802256 · Cited by 125 · see citing works

The Ensembl Web Site: Mechanics of a Genome BrowserPreprint

Stalker, J. W., Gibbins, B., Meidl, P., Smith, J. A., Spooner, W., Hotz, H.-R., & Cox, A. V. (2004) · Genome Research · doi:10.1101/gr.1863004 · Cited by 122 · 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

Monoclonal Antibody Therapy for Ebola Virus Disease

Levine, M. M. (2019) · New England Journal of Medicine · doi:10.1056/nejme1915350 · Cited by 70 · see citing works

Refined protocol for generating monoclonal antibodies from single human and murine B cells

Ho, I. Y., Bunker, J. J., Erickson, S. A., Neu, K. E., Huang, M., Cortese, M., Pulendran, B., & Wilson, P. C. (2016) · Journal of Immunological Methods · doi:10.1016/j.jim.2016.09.001 · Cited by 68 · see citing works

Pathogenesis and transmission of SARS-CoV-2 virus in golden Syrian hamstersPreprint

Sia, S. F., Yan, L.-M., Chin, A. W. H., et al. (2020) · Research Square · doi:10.21203/rs.3.rs-20774/v1 · Cited by 65 · see citing works

The clinical pharmacology of therapeutic monoclonal antibodies in the treatment of malignancy; have the magic bullets arrived?

Newsome, B. W., & Ernstoff, M. S. (2008) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2008.03187.x · Cited by 63 · see citing works

SARS-CoV-2 vaccines in development

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

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 & Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178 · 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 & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016 · see citing works

Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies

Chen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881 · see citing works

De novo design of picomolar SARS-CoV-2 miniprotein inhibitors

Cao, L., Goreshnik, I., Coventry, B., Case, J. B., Miller, L., Kozodoy, L., Chen, R. E., Carter, L., Walls, A. C., Park, Y.-J., et al. (2020) · Science · doi:10.1126/science.abd9909 · Cited by 742 · see citing works

Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization

Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.01.014 · Cited by 725 · see citing works

Functional SARS-CoV-2-Specific Immune Memory Persists after Mild COVID-19

Rodda, L. B., Netland, J., Shehata, L., Pruner, K. B., Morawski, P. A., Thouvenel, C. D., Takehara, K. K., Eggenberger, J., Hemann, E. A., Waterman, H. R., et al. (2021) · Cell · doi:10.1016/j.cell.2020.11.029 · Cited by 647 · see citing works

A Single-Dose Intranasal ChAd Vaccine Protects Upper and Lower Respiratory Tracts against SARS-CoV-2

Hassan, A. O., Kafai, N. M., Dmitriev, I., Fox, J., Smith, B. K., Harvey, I. B., Chen, R. E., Winkler, E. S., Wessel, A. W., Case, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.026 · Cited by 568 · see citing works

Elicitation of Potent Neutralizing Antibody Responses by Designed Protein Nanoparticle Vaccines for SARS-CoV-2

Walls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532 · see citing works

SARS-CoV-2 infection induces long-lived bone marrow plasma cells in humans

Turner, J. S., Kim, W., Kalaidina, E., Goss, C. W., Rauseo, A. M., Schmitz, A. J., Hansen, L., Haile, A., Klebert, M. K., Pusic, I., et al. (2021) · Nature · doi:10.1038/s41586-021-03647-4 · Cited by 515 · see citing works

Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms

Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510 · see citing works

Heterogeneity of meningeal B cells reveals a lymphopoietic niche at the CNS borders

Brioschi, S., Wang, W.-L., Peng, V., Wang, M., Shchukina, I., Greenberg, Z. J., Bando, J. K., Jaeger, N., Czepielewski, R. S., Swain, A., et al. (2021) · Science · doi:10.1126/science.abf9277 · Cited by 472 · 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.2021.05.005 · Cited by 375 · see citing works

Human neutralizing antibodies against SARS-CoV-2 require intact Fc effector functions for optimal therapeutic protection

Winkler, E. S., Gilchuk, P., Yu, J., Bailey, A. L., Chen, R. E., Chong, Z., Zost, S. J., Jang, H., Huang, Y., Allen, J. D., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.026 · Cited by 366 · 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) · Cell · doi:10.1016/j.cell.2021.03.029 · Cited by 397 · see citing works

SARS-CoV-2, COVID-19 and the aging immune system

Bartleson, J. M., Radenkovic, D., Covarrubias, A. J., Furman, D., Winer, D. A., & Verdin, E. (2021) · Nature Aging · doi:10.1038/s43587-021-00114-7 · Cited by 359 · see citing works

COVID-19 mRNA vaccine induced antibody responses against three SARS-CoV-2 variants

(2021) · doi:10.1038/s41467-021-24285-4 · Cited by 272 · see citing works

A human coronavirus evolves antigenically to escape antibody immunity

(2021) · doi:10.1371/journal.ppat.1009453 · Cited by 258 · 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

SARS-CoV-2 spreads through cell-to-cell transmission

Zeng, C., Evans, J. P., King, T., Zheng, Y.-M., Oltz, E. M., Whelan, S. P. J., Saif, L. J., Peeples, M. E., & Liu, S.-L. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111400119 · Cited by 246 · see citing works

Monoclonal antibodies for COVID-19 therapy and SARS-CoV-2 detection

Hwang, Y., Lu, R., Su, S.-C., Chiang, P.-Y., Ko, S.-H., Ke, F.-Y., Liang, K.-H., Hsieh, T.-Y., & Wu, H. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-021-00784-w · Cited by 236 · see citing works

In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains

Chen, R. E., Winkler, E. S., Case, J. B., Aziati, I. D., Bricker, T. L., Joshi, A., Darling, T. L., Ying, B., Errico, J. M., Shrihari, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03720-y · Cited by 209 · see citing works

De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2

Linsky, T. W., Vergara, R., Codina, N., Nelson, J. W., Walker, M. J., Su, W., Barnes, C. O., Hsiang, T.-Y., Esser-Nobis, K., Yu, K., et al. (2020) · Science · doi:10.1126/science.abe0075 · Cited by 216 · see citing works

Antibody structure prediction using interpretable deep learning

Ruffolo, J. A., Sulam, J., & Gray, J. J. (2022) · Patterns · doi:10.1016/j.patter.2021.100406 · Cited by 216 · see citing works

Live imaging of SARS-CoV-2 infection in mice reveals that neutralizing antibodies require Fc function for optimal efficacy

Ullah, I., Prévost, J., Ladinsky, M., Stone, H., Lu, M.-L., Anand, S., Beaudoin-Bussières, G., Symmes, K., Benlarbi, M., Ding, S.-L., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.015 · Cited by 152 · see citing works

Extremely potent human monoclonal antibodies from COVID-19 convalescent patients

Andreano, E., Nicastri, E., Paciello, I., Pileri, P., Manganaro, N., Piccini, G., Manenti, A., Pantano, E., Kabanova, A., Troisi, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.035 · Cited by 200 · 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

Replication-Competent Vesicular Stomatitis Virus Vaccine Vector Protects against SARS-CoV-2-Mediated Pathogenesis in Mice

Case, J., Rothlauf, P. W., Chen, R. E., Kafai, N. M., Fox, J., Smith, B. K., Shrihari, S., McCune, B. T., Harvey, I. B., Keeler, S. P., et al. (2020) · Cell Host and Microbe · doi:10.1016/j.chom.2020.07.018 · Cited by 184 · see citing works

Structural basis for broad coronavirus neutralization

Sauer, M. M., Tortorici, M., Park, Y.-J., Walls, A., Homad, L. J., Acton, O., Bowen, J., Wang, C., Xiong, X., de van der Schueren, W. J., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00596-4 · Cited by 199 · see citing works

Neurological Manifestations of COVID-19 Feature T Cell Exhaustion and Dedifferentiated Monocytes in Cerebrospinal Fluid

Heming, M., Li, X., Räuber, S. J., Mausberg, A. K., Börsch, A., Hartlehnert, M., Singhal, A., Lu, I., Fleischer, M., Szepanowski, F., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.12.011 · Cited by 179 · see citing works

SARS-CoV-2 spike variants exhibit differential infectivity and neutralization resistance to convalescent or post-vaccination sera

Kuzmina, A., Khalaila, Y., Voloshin, O., Keren-Naus, A., Boehm-Cohen, L., Raviv, Y., Shemer-Avni, Y., Rosenberg, E., & Taube, R. (2021) · Cell Host and Microbe · doi:10.1016/j.chom.2021.03.008 · Cited by 188 · see citing works

SARS-CoV-2 Omicron boosting induces de novo B cell response in humans

Alsoussi, W. B., Malladi, S. K., Zhou, J. Q., Liu, Z., Ying, B., Kim, W., Schmitz, A. J., Lei, T., Horvath, S. C., Sturtz, A. J., et al. (2023) · Nature · doi:10.1038/s41586-023-06025-4 · Cited by 167 · see citing works

Development of a rapid Focus Reduction Neutralization Test Assay for measuring SARS-CoV-2 neutralizing antibodies

Vanderheiden, A., Edara, V., Floyd, K., Kauffman, R. C., Mantus, G., Anderson, E., Rouphael, N., Edupuganti, S., Shi, P.-Y., Menachery, V., et al. (2020) · Current Protocols in Immunology · doi:10.1002/cpim.116 · Cited by 141 · see citing works

Molecular Architecture of Early Dissemination and Massive Second Wave of the SARS-CoV-2 Virus in a Major Metropolitan Area

Long, S., Olsen, R., Christensen, P. A., Bernard, D. W., Davis, J. J., Shukla, M., Nguyen, M., Saavedra, M., Yerramilli, P., Pruitt, L., et al. (2020) · mBio · doi:10.1128/mbio.02707-20 · Cited by 121 · see citing works

Systematic analysis of SARS-CoV-2 infection of an ACE2-negative human airway cell

Puray‐Chavez, M., LaPak, K. M., Schrank, T. P., Elliott, J. L., Bhatt, D. P., Agajanian, M. J., Jasuja, R., Lawson, D. Q., Davis, K., Rothlauf, P. W., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109364 · Cited by 131 · see citing works

Landscape analysis of escape variants identifies SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization

Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., et al. (2020) · doi:10.1101/2020.11.06.372037 · Cited by 135 · see citing works

An intranasal vaccine durably protects against SARS-CoV-2 variants in mice

Hassan, A. O., Shrihari, S., Gorman, M. J., Ying, B., Yuan, D., Raju, S., Chen, R. E., Dmitriev, I. P., Kashentseva, E. A., Adams, L. J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109452 · Cited by 129 · see citing works

Multivalent designed proteins neutralize SARS-CoV-2 variants of concern and confer protection against infection in mice

Hunt, A. C., Case, J. B., Park, Y., Cao, L., Wu, K., Walls, A. C., Liu, Z., Bowen, J. E., Yeh, A. H.-W., Saini, S., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn1252 · Cited by 116 · see citing works

Animal Models for COVID-19: Hamsters, Mouse, Ferret, Mink, Tree Shrew, and Non-human Primates

Shou, S., Liu, M., Yang, Y., Kang, N., Song, Y., Tan, D., Liu, N.-N., Wang, F., Liu, J., & Xie, Y.-H. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.626553 · Cited by 112 · see citing works

COVID-19 antibodies on trial

DeFrancesco, L. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0732-8 · Cited by 116 · see citing works

Humoral immune responses and neutralizing antibodies against SARS-CoV-2; implications in pathogenesis and protective immunity

Carrillo, J., Izquierdo‐Useros, N., Ávila‐Nieto, C., Pradenas, E., Clotet, B., & Blanco, J. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.108 · Cited by 114 · see citing works

Single-cell immunology of SARS-CoV-2 infection

Tian, Y., Carpp, L. N., Miller, H. E. R., Zager, M. A., Newell, E. W., & Gottardo, R. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-01131-y · Cited by 114 · see citing works

Current status of therapeutic monoclonal antibodies against SARS-CoV-2

Kumar, S., Chandele, A., & Sharma, A. K. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009885 · Cited by 103 · see citing works

Neutralizing antibody against SARS-CoV-2 spike in COVID-19 patients, health care workers, and convalescent plasma donors

Zeng, C., Evans, J. P., Pearson, R., Qu, P., Zheng, Y.-M., Robinson, R., Hall‐Stoodley, L., Yount, J. S., Pannu, S. R., Mallampalli, R. K., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.143213 · Cited by 87 · see citing works

A potently neutralizing SARS-CoV-2 antibody inhibits variants of concern by utilizing unique binding residues in a highly conserved epitope

VanBlargan, L. A., Adams, L., Liu, Z.-M., Chen, R. E., Gilchuk, P., Raju, S., Smith, B. K., Zhao, H.-Y., Case, J., Winkler, E. S., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.016 · Cited by 95 · see citing works

Evaluation of a commercially-available surrogate virus neutralization test for severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)

Valcourt, E. J., Manguiat, K., Robinson, A., Chen, J., Dimitrova, K., Philipson, C., Lamoureux, L., McLachlan, E., Schiffman, Z., Drebot, M., et al. (2020) · Diagnostic microbiology and infectious disease · doi:10.1016/j.diagmicrobio.2020.115294 · Cited by 93 · see citing works

Imprinting of serum neutralizing antibodies by Wuhan-1 mRNA vaccines

Liang, C.-Y., Raju, S., Liu, Z., Li, Y., Arunkumar, G. A., Case, J. B., Scheaffer, S. M., Zost, S. J., Acreman, C. M., Gagné, M., et al. (2024) · Nature · doi:10.1038/s41586-024-07539-1 · Cited by 82 · see citing works

The Principles of Antibody Therapy for Infectious Diseases with Relevance for COVID-19

Casadevall, A., Pirofski, L., & Joyner, M. J. (2021) · mBio · doi:10.1128/mbio.03372-20 · Cited by 80 · 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

Challenges and developments in universal vaccine design against SARS-CoV-2 variants

Zhao, F., Zai, X., Zhang, Z., Xu, J., & Chen, W. (2022) · npj Vaccines · doi:10.1038/s41541-022-00597-4 · Cited by 81 · 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

A public vaccine-induced human antibody protects against SARS-CoV-2 and emerging variants

Schmitz, A. J., Turner, J. S., Liu, Z., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T. L., Darling, T. L., Adelsberg, D. C., Alsoussi, W. B., et al. (2021) · doi:10.1101/2021.03.24.436864 · Cited by 72 · see citing works

A vaccine-induced public antibody protects against SARS-CoV-2 and emerging variants

Schmitz, A. J., Turner, J., Liu, Z.-M., Zhou, J. Q., Aziati, I. D., Chen, R. E., Joshi, A., Bricker, T., Darling, T. L., Adelsberg, D. C., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.013 · Cited by 58 · see citing works

SARS-CoV-2 antibodies, serum inflammatory biomarkers and clinical severity of hospitalized COVID-19 patients

Gozalbo‐Rovira, R., Giménez, E., Latorre, V., Francés‐Gómez, C., Albert, E., Buesa, J., Marina, A., Blasco, M. L., Signes‐Costa, J., Rodríguez‐Díaz, J., et al. (2020) · Journal of Clinical Virology · doi:10.1016/j.jcv.2020.104611 · Cited by 70 · see citing works

Animal models for SARS-CoV-2

Lee, C.-Y., & Lowen, A. C. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.03.009 · Cited by 64 · see citing works

Coronavirus Antiviral Research Database (CoV-RDB): An Online Database Designed to Facilitate Comparisons between Candidate Anti-Coronavirus Compounds

Tzou, P. L., Tao, K., Nouhin, J., Rhee, S., Hu, B. D., Pai, S., Parkin, N. T., & Shafer, R. W. (2020) · Viruses · doi:10.3390/v12091006 · Cited by 61 · see citing works

Human Basigin (CD147) Does Not Directly Interact with SARS-CoV-2 Spike Glycoprotein

Ragotte, R. J., Pulido, D., Donnellan, F. R., Hill, M. L., Gorini, G., Davies, H. D., Brun, J., McHugh, K., King, L. D. W., Skinner, K., et al. (2021) · mSphere · doi:10.1128/msphere.00647-21 · Cited by 64 · see citing works

Immunosenescence and inflamm-ageing in COVID-19

Zinatizadeh, M. R., Zarandi, P. K., Ghiasi, M., Kooshki, H., Mohammadi, M., Amani, J., & Rezaei, N. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101818 · Cited by 62 · see citing works

Protoporphyrin IX and verteporfin potently inhibit SARS-CoV-2 infection in vitro and in a mouse model expressing human ACE2

Gu, C., Wu, Y., Guo, H., Zhu, Y., Xu, W., Wang, Y., Zhou, Y., Sun, Z., Cai, X., Li, Y., et al. (2020) · 中国科学通报：英文版 · doi:10.1016/j.scib.2020.12.005 · Cited by 60 · see citing works

Global SNP analysis of 11,183 SARS‐CoV‐2 strains reveals high genetic diversity

Yuan, F., Wang, L., Fāng, Y., & Wang, L. (2020) · Transboundary and Emerging Diseases · doi:10.1111/tbed.13931 · Cited by 57 · see citing works

Intranasal Administration of a Monoclonal Neutralizing Antibody Protects Mice against SARS-CoV-2 Infection

Halwe, S., Kupke, A., Vanshylla, K., Liberta, F., Gruell, H., Zehner, M., Rohde, C., Krähling, V., Serra, M. G., Kreer, C., et al. (2021) · Viruses · doi:10.3390/v13081498 · Cited by 53 · see citing works

Follicular T cells optimize the germinal center response to SARS-CoV-2 protein vaccination in mice

Cavazzoni, C. B., Hanson, B. L., Podestà, M. A., Bechu, E. D., Clement, R. L., Zhang, H., Daccache, J., Robles, T. R., Hett, E. C., Vora, K. A., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110399 · Cited by 56 · see citing works

Post-exposure protection of SARS-CoV-2 lethal infected K18-hACE2 transgenic mice by neutralizing human monoclonal antibody

Rosenfeld, R., Noy-Porat, T., Mechaly, A., Makdasi, E., Levy, Y., Alcalay, R., Falach, R., Aftalion, M., Epstein, E., Gur, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21239-8 · Cited by 55 · see citing works

Off-the-shelf CAR natural killer cells secreting IL-15 target spike in treating COVID-19

Lu, T., Ma, R., Dong, W.-J., Teng, K.-Y., Kollath, D. S., Li, Z.-Y., Yi, J., Bustillos, C., Ma, S.-B., Tian, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30216-8 · Cited by 47 · see citing works

Directed evolution of potent neutralizing nanobodies against SARS-CoV-2 using CDR-swapping mutagenesis

Zupancic, J. M., Desai, A. A., Schardt, J. S., Pornnoppadol, G., Makowski, E. K., Smith, M. D., Kennedy, A. A., Barbosa, M. G. D. M., Cascalho, M., Lanigan, T. M., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.05.019 · Cited by 54 · see citing works

On the road to ending the COVID-19 pandemic: Are we there yet?

Case, J., Winkler, E. S., Errico, J., & Diamond, M. S. (2021) · Virology · doi:10.1016/j.virol.2021.02.003 · Cited by 41 · see citing works

Distinct patterns of SARS-CoV-2 BA.2.87.1 and JN.1 variants in immune evasion, antigenicity, and cell-cell fusion

Li, P., Liu, Y., Faraone, J. N., Hsu, C. C., Chamblee, M., Zheng, Y.-M., Carlin, C., Bednash, J. S., Horowitz, J. C., Mallampalli, R. K., et al. (2024) · mBio · doi:10.1128/mbio.00751-24 · Cited by 49 · see citing works

Tetravalent SARS-CoV-2 Neutralizing Antibodies Show Enhanced Potency and Resistance to Escape Mutations

Miersch, S., Li, Z., Saberianfar, R., Ustav, M., Case, J. B., Blazer, L. L., Chen, C., Ye, W., Pavlenco, A., Gorelik, M., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167177 · Cited by 5 · see citing works

Leveraging vaccination-induced protective antibodies to define conserved epitopes on influenza N2 neuraminidase

Lei, R., Kim, W., Lv, H., Mou, Z., Scherm, M. J., Schmitz, A. J., Turner, J. S., Tan, T. J. C., Wang, Y., Ouyang, W. O., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.10.005 · Cited by 45 · see citing works

Monospecific and bispecific monoclonal SARS-CoV-2 neutralizing antibodies that maintain potency against B.1.617

Peng, L., Hu, Y., Mankowski, M. C., Ren, P., Chen, R. E., Wei, J., Zhao, M., Li, T., Tripler, T. N., Ye, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29288-3 · Cited by 43 · see citing works

Deciphering SARS-CoV-2 Virologic and Immunologic Features

Lebeau, G., Vagner, D., Frumence, É., Ah-Pine, F., Guillot, X., Nobécourt, E., Raffray, L., & Gasque, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165932 · Cited by 43 · see citing works

SARS-CoV-2-neutralising monoclonal antibodies to prevent COVID-19

Hirsch, C., Park, Y. S., Piechotta, V., Chai, K. L., Estcourt, L. J., Monsef, I., Salomon, S., Wood, E. M., So‐Osman, C., McQuilten, Z., et al. (2022) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd014945.pub2 · Cited by 39 · see citing works

Passive Immunotherapy Against SARS-CoV-2: From Plasma-Based Therapy to Single Potent Antibodies in the Race to Stay Ahead of the Variants

Strohl, W. R., Ku, Z., An, Z., Carroll, S. F., Keyt, B. A., & Strohl, L. M. (2022) · BioDrugs · doi:10.1007/s40259-022-00529-7 · Cited by 34 · see citing works

SARS-CoV-2 immunity in animal models

Chen, Z., Yuan, Y., Hu, Q., Zhu, A.-R., Chen, F., Li, S., Guan, X., Lv, C., Tang, T., He, Y.-Y., et al. (2024) · Cellular & Molecular Immunology · doi:10.1038/s41423-023-01122-w · Cited by 34 · see citing works

An ultrapotent pan-β-coronavirus lineage B (β-CoV-B) neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope

Liu, Z.-Z., Xu, W., Chen, Z., Fu, W.-J., Zhan, W., Gao, Y.-D., Zhou, J., Zhou, Y., Wu, J.-B., Wang, Q., et al. (2021) · Protein & Cell · doi:10.1007/s13238-021-00871-6 · Cited by 36 · see citing works

The receptor binding domain of SARS-CoV-2 spike is the key target of neutralizing antibody in human polyclonal sera

Steffen, T. L., Stone, E. T., Hassert, M., Geerling, E., Grimberg, B. T., Espino, A. M., Pantoja, P., Climent, C., Hoft, D. F., George, S. L., et al. (2020) · doi:10.1101/2020.08.21.261727 · Cited by 25 · see citing works

Function Is More Reliable than Quantity to Follow Up the Humoral Response to the Receptor-Binding Domain of SARS-CoV-2-Spike Protein after Natural Infection or COVID-19 Vaccination

Sariol, C. A., Pantoja, P., Serrano-Collazo, C., Rosa-Arocho, T., Armina-Rodríguez, A., Cruz, L. A., Stone, E. T., Arana, T., Climent, C., Latoni, G., et al. (2021) · Viruses · doi:10.3390/v13101972 · Cited by 31 · see citing works

A pandemic-enabled comparison of discovery platforms demonstrates a naïve antibody library can match the best immune-sourced antibodies

Ferrara, F., Erasmus, M. F., D'Angelo, S., Leal-Lopes, C., Teixeira, A. A. R., Choudhary, A., Honnen, W., Calianese, D., Huang, D.-L., Peng, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27799-z · Cited by 36 · see citing works

Bromodomain and Extraterminal Protein Inhibitor, Apabetalone (RVX-208), Reduces ACE2 Expression and Attenuates SARS-Cov-2 Infection In Vitro

Gilham, D., Smith, A. L., Fu, L., Moore, D. Y., Muralidharan, A., Reid, S. P., Stotz, S. C., Johansson, J. O., Sweeney, M., Wong, N. C. W., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9040437 · Cited by 33 · see citing works

Elicitation of potent SARS-CoV-2 neutralizing antibody responses through immunization with a versatile adenovirus-inspired multimerization platform

Chevillard, C., Amen, A., Besson, S., Hannani, D., Bally, I., Dettling, V., Gout, E., Moreau, C., Buisson, M., Gallet, S., et al. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.02.011 · Cited by 32 · see citing works

SARS CoV-2 Delta variant exhibits enhanced infectivity and a minor decrease in neutralization sensitivity to convalescent or post-vaccination sera

Kuzmina, A., Wattad, S., Khalaila, Y., Ottolenghi, A., Rosental, B., Engel, S., Rosenberg, E., & Taube, R. (2021) · iScience · doi:10.1016/j.isci.2021.103467 · Cited by 30 · see citing works

Seroprevalence of SARS-CoV-2 Antibodies in Children and Adults in St. Louis, Missouri, USA

Smith, B. K., Janowski, A. B., Danis, J. E., Harvey, I. B., Zhao, H., Dai, Y.-N., Farnsworth, C. W., Gronowski, A. M., Roper, S. M., Fremont, D. H., et al. (2021) · mSphere · doi:10.1128/msphere.01207-20 · Cited by 31 · see citing works

Lipid Nanoparticle RBD-hFc mRNA Vaccine Protects hACE2 Transgenic Mice against a Lethal SARS-CoV-2 Infection

Elia, U., Rotem, S., Bar‐Haim, E., Ramishetti, S., Naidu, G. S., Gur, D., Aftalion, M., Israeli, M., Bercovich-Kinori, A., Alcalay, R., et al. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c01284 · Cited by 31 · see citing works

Mouse models of COVID-19 recapitulate inflammatory pathways rather than gene expression

Bishop, C., Dumenil, T. D., Rawle, D. J., Le, T. T., Yan, K., Tang, B., Härtel, G., & Suhrbier, A. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010867 · Cited by 31 · see citing works

Rapid discovery of monoclonal antibodies by microfluidics-enabled FACS of single pathogen-specific antibody-secreting cells

Fischer, K., Lulla, A., So, T. Y., Pereyra-Gerber, P., Raybould, M. I. J., Kohler, T. N., Yam‐Puc, J. C., Kamiński, T. S., Hughes, R., Pyeatt, G. L., et al. (2024) · Nature Biotechnology · doi:10.1038/s41587-024-02346-5 · Cited by 30 · see citing works

High neutralizing potency of swine glyco‐humanized polyclonal antibodies against SARS‐CoV‐2

Vanhove, B., Duvaux-Miret, O., Rousse, J., Royer, P., Evanno, G., Ciron, C., Lhériteau, E., Vacher, L., Gervois, N., Oger, R., et al. (2021) · European Journal of Immunology · doi:10.1002/eji.202049072 · Cited by 28 · see citing works

Therapeutic antibodies for COVID-19: is a new age of IgM, IgA and bispecific antibodies coming?

Zhang, J., Zhang, H., & Sun, L.-T. (2022) · mAbs · doi:10.1080/19420862.2022.2031483 · Cited by 23 · see citing works

Phage-like particle vaccines are highly immunogenic and protect against pathogenic coronavirus infection and disease

Davenport, B. J., Catala, A., Weston, S., Johnson, R. M., Ardanuy, J., Hammond, H., Dillen, C., Frieman, M., Catalano, C., & Morrison, T. (2021) · npj Vaccines · doi:10.1038/s41541-022-00481-1 · Cited by 20 · see citing works

The Rheumatology Drugs for COVID-19 Management: Which and When?

Atzeni, F., Masala, I. F., Rodríguez‐Carrio, J., Garcés, R. R., Gerratana, E., Corte, L. L., Giallanza, M., Nucera, V., Riva, A., Espinosa, G., et al. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10040783 · Cited by 27 · see citing works

SARS-CoV-2: Origin, Evolution, and Targeting Inhibition

Ning, S., Yu, B., Wang, Y., & Wang, F. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.676451 · Cited by 27 · see citing works

Human immunoglobulin from transchromosomic bovines hyperimmunized with SARS-CoV-2 spike antigen efficiently neutralizes viral variants

Liu, Z., Wu, H., Egland, K. A., Gilliland, T. C., Dunn, M. D., Luke, T. C., Sullivan, E. J., Klimstra, W. B., Bausch, C. L., & Whelan, S. P. J. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1940652 · Cited by 26 · see citing works

Inference of B cell clonal families using heavy/light chain pairing information

Ralph, D., & Matsen, F. A., IV (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010723 · Cited by 27 · see citing works

Pathophysiological Response to SARS-CoV-2 Infection Detected by Infrared Spectroscopy Enables Rapid and Robust Saliva Screening for COVID-19

Kazmer, S. T., Härtel, G., Robinson, H., Richards, R. S., Yan, K., van Hal, S. J., Chan, R., Hind, A., Bradley, D. A., Zieschang, F., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10020351 · Cited by 26 · see citing works

Antibody-mediated immunity to SARS-CoV-2 spike

Errico, J. M., Adams, L. J., & Fremont, D. H. (2022) · Advances in immunology · doi:10.1016/bs.ai.2022.07.001 · Cited by 20 · see citing works

Neutralizing Monoclonal Anti-SARS-CoV-2 Antibodies Isolated from Immunized Rabbits Define Novel Vulnerable Spike-Protein Epitope

Makdasi, E., Levy, Y., Alcalay, R., Noy-Porat, T., Zahavy, E., Mechaly, A., Epstein, E., Peretz, E., Cohen, H., Bar-On, L., et al. (2021) · Viruses · doi:10.3390/v13040566 · Cited by 25 · see citing works

Kinetics of Neutralizing Antibodies of COVID-19 Patients Tested Using Clinical D614G, B.1.1.7, and B 1.351 Isolates in Microneutralization Assays

Virtanen, J. M. E., Uusitalo, R., Korhonen, E. M., Aaltonen, K., Smura, T., Kuivanen, S. H., Pakkanen, S. H., Mero, S., Patjas, A., Riekkinen, M., et al. (2021) · Viruses · doi:10.3390/v13060996 · Cited by 24 · see citing works

A review of monoclonal antibodies in COVID-19: Role in immunotherapy, vaccine development and viral detection

Tabll, A., Shahein, Y., Omran, M., Elnakib, M., Ragheb, A., & Amer, K. (2021) · Human Antibodies · doi:10.3233/hab-200441 · Cited by 17 · see citing works

Structural mechanism of SARS-CoV-2 neutralization by two murine antibodies targeting the RBD

Errico, J. M., Zhao, H., Chen, R. E., Liu, Z., Case, J. B., Ma, M., Schmitz, A. J., Rau, M., Fitzpatrick, J. A. J., Shi, P., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109881 · Cited by 22 · see citing works

Uncovering a conserved vulnerability site in SARS‐CoV‐2 by a human antibody

Li, T.-Y., Cai, H., Zhao, Y.-P., Li, Y., Lai, Y., Yao, H., Liu, L. D., Sun, Z., van Vlissingen, M. F., Kuiken, T., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202114544 · Cited by 23 · see citing works

Structure-guided antibody cocktail for prevention and treatment of COVID-19

Su, S.-C., Yang, T.-J., Yu, P.-Y., Liang, K., Chen, W.-Y., Yang, C.-T., Lin, H.-T., Wang, M., Lu, R.-M., Tso, H.-C., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009704 · Cited by 19 · see citing works

Murine Monoclonal Antibodies against the Receptor Binding Domain of SARS-CoV-2 Neutralize Authentic Wild-Type SARS-CoV-2 as Well as B.1.1.7 and B.1.351 Viruses and Protect In Vivo in a Mouse Model in a Neutralization-Dependent Manner

Amanat, F., Strohmeier, S., Lee, W.-H., Bangaru, S., Ward, A. B., Coughlan, L., & Krammer, F. (2021) · mBio · doi:10.1128/mbio.01002-21 · Cited by 16 · see citing works

A Sars-Cov-2 Neutralizing Antibody Protects from Lung Pathology in a Covid-19 Hamster ModelPreprint

Kreye, J., Reincke, S. M., Kornau, H.-C., Sánchez-Sendín, E., Corman, V. M., Liu, H., Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., et al. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3680870

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

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

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

Idiopathic Intracranial Hypertension is Associated with a Higher Burden of Visible Cerebral Perivascular Spaces: The Glymphatic Connection

Jones, O., Cutsforth-Gregory, J., Chen, J., Bhatti, M. T., Huston, J., & Brinjikji, W. (2021) · American Journal of Neuroradiology · doi:10.3174/ajnr.a7326 · Cited by 33 · see citing works