Enhanced SARS-CoV-2 neutralization by dimeric IgA

A pneumonia outbreak associated with a new coronavirus of probable bat origin

Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969 · see citing works

SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286 · see citing works

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

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

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

Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897 · see citing works

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

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

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

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

Targets of T Cell Responses to SARS-CoV-2 Coronavirus in Humans with COVID-19 Disease and Unexposed Individuals

Grifoni, A., Weiskopf, D., Ramirez, S. I., Mateus, J., Dan, J. M., Moderbacher, C. R., Rawlings, S. A., Sutherland, A., Premkumar, L., Jadi, R. S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.015 · Cited by 3,595 · see citing works

Germinal Centers

Victora, G. D., & Nussenzweig, M. C. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075032 · Cited by 1,878 · see citing works

Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals

Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853 · see citing works

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

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

Correlates of protection induced by vaccination

Plotkin, S. A. (2010) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00131-10 · Cited by 1,745 · see citing works

Human neutralizing antibodies elicited by SARS-CoV-2 infection

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

Longitudinal observation and decline of neutralizing antibody responses in the three months following SARS-CoV-2 infection in humans

Seow, J., Graham, C., Merrick, B., Acors, S., Pickering, S., Steel, K. J. A., Hemmings, O., O’Byrne, A., Kouphou, N., Galao, R. P., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-00813-8 · Cited by 1,419 · 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

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

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

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

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

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

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

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

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

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

IgBLAST: an immunoglobulin variable domain sequence analysis tool

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

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

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

Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning

Tiller, T., Meffre, E., Yurasov, S., Tsuiji, M., Nussenzweig, M. C., & Wardemann, H. (2007) · Journal of Immunological Methods · doi:10.1016/j.jim.2007.09.017 · Cited by 1,078 · 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

IgA dominates the early neutralizing antibody response to SARS-CoV-2

Sterlin, D., Mathian, A., Miyara, M., Mohr, A., Anna, F., Claër, L., Quentric, P., Fadlallah, J., Devilliers, H., Ghillani, P., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd2223 · Cited by 1,037 · see citing works

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

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

Antibody Status and Incidence of SARS-CoV-2 Infection in Health Care Workers

Lumley, S. F., O’Donnell, D., Stoesser, N. E., Matthews, P. C., Howarth, A., Hatch, S. B., Marsden, B. D., Cox, S., James, T., Warren, F., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2034545 · Cited by 940 · 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

Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals

Scheid, J. F., Mouquet, H., Feldhahn, N., Seaman, M. S., Velinzon, K., Pietzsch, J., Ott, R. G., Anthony, R. M., Zebroski, H. A., Hurley, A., et al. (2009) · Nature · doi:10.1038/nature07930 · Cited by 865 · see citing works

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

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

COVID-19 neutralizing antibodies predict disease severity and survivalPreprint

Garcia-Beltran, W., Lam, E., Astudillo, M., Yang, D., Miller, T., Feldman, J., Hauser, B., Caradonna, T. M., Clayton, K., Nitido, A. D., et al. (2020) · medRxiv · doi:10.1101/2020.10.15.20213512 · Cited by 683 · see citing works

New concepts in the generation and functions of IgA

Pabst, O. (2012) · Nature reviews. Immunology · doi:10.1038/nri3322 · Cited by 656 · see citing works

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

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

Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses

Schmidt, F., Weisblum, Y., Muecksch, F., Hoffmann, H.-H., Michailidis, E., Lorenzi, J. C. C., Mendoza, P., Rutkowska, M., Bednarski, E., Gaebler, C., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201181 · Cited by 572 · 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

REGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters

Baum, A., Ajithdoss, D., Copin, R., Zhou, A., Lanza, K., Negron, N., Ni, M., Wei, Y., Mohammadi, K., Musser, B., et al. (2020) · Science · doi:10.1126/science.abe2402 · Cited by 517 · see citing works

Serum IgA, IgM, and IgG responses in COVID-19

Ma, H., Zeng, W., He, H., Zhao, D., Yang, Y., Jiang, D., Qi, P. Y., He, W., Zhao, C., Yi, R., et al. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0474-z · Cited by 500 · see citing works

Immunoglobulin A: Strategic Defense Initiative at the Mucosal Surface

Underdown, B. J., & Schiff, J. M. (1986) · Annual Review of Immunology · doi:10.1146/annurev.iy.04.040186.002133 · Cited by 410 · see citing works

Analysis of a SARS-CoV-2-Infected Individual Reveals Development of Potent Neutralizing Antibodies with Limited Somatic Mutation

Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.001 · Cited by 364 · see citing works

Distinct Early Serological Signatures Track with SARS-CoV-2 Survival

Atyeo, C., Fischinger, S., Zohar, T., Slein, M. D., Burke, J., Loos, C., McCulloch, D. J., Newman, K. L., Wolf, C., Yu, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.020 · Cited by 349 · see citing works

Rethinking mucosal antibody responses: IgM, IgG and IgD join IgA

Chen, K., Magri, G., Grasset, E. K., & Cerutti, A. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-019-0261-1 · Cited by 339 · see citing works

Recurrent Potent Human Neutralizing Antibodies to Zika Virus in Brazil and Mexico

Robbiani, D. F., Bozzacco, L., Keeffe, J. R., Khouri, R., Olsen, P. C., Gazumyan, A., Schaefer-Babajew, D. J., Ávila‐Ríos, S., Nogueira, L., Patel, R., et al. (2017) · Cell · doi:10.1016/j.cell.2017.04.024 · Cited by 335 · see citing works

Distinct features of SARS-CoV-2-specific IgA response in COVID-19 patients

Yu, H.-Q., Sun, B.-Q., Fang, Z., et al. (2020) · European Respiratory Journal · doi:10.1183/13993003.01526-2020 · Cited by 326 · see citing works

Longitudinal Isolation of Potent Near-Germline SARS-CoV-2-Neutralizing Antibodies from COVID-19 Patients

Kreer, C., Zehner, M., Weber, T., Ercanoglu, M. S., Gieselmann, L., Rohde, C., Halwe, S., Korenkov, M., Schommers, P., Vanshylla, K., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.044 · Cited by 313 · see citing works

High frequency of shared clonotypes in human B cell receptor repertoires

Soto, C., Bombardi, R. G., Branchizio, A., Kose, N., Matta, P., Sevy, A. M., Sinkovits, R. S., Gilchuk, P., Finn, J. A., & Crowe, J. E. (2019) · Nature · doi:10.1038/s41586-019-0934-8 · Cited by 294 · see citing works

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

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

Antibody Affinity Shapes the Choice between Memory and Germinal Center B Cell Fates

Viant, C., Weymar, G. H. J., Escolano, A., Chen, S., Hartweger, H., Cipolla, M., Gazumyan, A., & Nussenzweig, M. C. (2020) · Cell · doi:10.1016/j.cell.2020.09.063 · Cited by 233 · see citing works

Evaluating the Association of Clinical Characteristics With Neutralizing Antibody Levels in Patients Who Have Recovered From Mild COVID-19 in Shanghai, China

Wu, F., Liu, M., Wang, A., Lu, L., Wang, Q., Gu, C., Chen, J., Wu, Y., Xia, S., Ling, Y., et al. (2020) · JAMA Internal Medicine · doi:10.1001/jamainternmed.2020.4616 · Cited by 219 · see citing works

The Coming of Age of the Immunoglobulin J Chain

Koshland, M. E. (1985) · Annual Review of Immunology · doi:10.1146/annurev.iy.03.040185.002233 · Cited by 214 · 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

A recombinant Salmonella typhimurium vaccine induces local immunity by four different routes of immunization

Hopkins, S., Kraehenbühl, J. P., Schödel, F. P., Potts, A., Peterson, D. L., Grandi, P. D., & Nardelli‐Haefliger, D. (1995) · Infection and Immunity · doi:10.1128/iai.63.9.3279-3286.1995 · Cited by 180 · see citing works

Differences in Immune Responses Induced by Oral and Rectal Immunizations withSalmonella typhiTy21a: Evidence for Compartmentalization within the Common Mucosal Immune System in Humans

Kantele, A., Hakkinen, M., Moldoveanu, Z., Lu, A., Savilahti, E. M., Alvarez, R. D., Michalek, S. M., & Mestecky, J. F. (1998) · Infection and Immunity · doi:10.1128/iai.66.12.5630-5635.1998 · Cited by 158 · see citing works

Relationship of the quaternary structure of human secretory IgA to neutralization of influenza virus

Suzuki, T., Kawaguchi, A., Ainai, A., Tamura, S., Ito, R., Multihartina, P., Setiawaty, V., Pangesti, K. N. A., Odagiri, T., Tashiro, M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1503885112 · Cited by 150 · see citing works

A Combination of Human Broadly Neutralizing Antibodies against Hepatitis B Virus HBsAg with Distinct Epitopes Suppresses Escape Mutations

Wang, Q., Michailidis, E., Yu, Y., Wang, Z., Hurley, A., Oren, D. A., Mayer, C. T., Gazumyan, A., Liu, Z., Zhou, Y., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.05.010 · Cited by 76 · see citing works

Specific-Antibody-Secreting Cells in the Rectums and Genital Tracts of Nonhuman Primates following Vaccination

Eriksson, K., Quiding‐Järbrink, M., Osek, J., Möller, Å. J. R., Björk, S., Holmgren, J. R., & Czerkinsky, C. C. (1998) · Infection and Immunity · doi:10.1128/iai.66.12.5889-5896.1998 · Cited by 73 · see citing works

IgA tetramerization improves target breadth but not peak potency of functionality of anti-influenza virus broadly neutralizing antibody

Saito, S., Sano, K., Suzuki, T., Ainai, A., Taga, Y., Ueno, T., Tabata, K., Saito, K., Wada, Y., Ohara, Y., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007427 · Cited by 68 · see citing works

cAb-Rep: A Database of Curated Antibody Repertoires for Exploring Antibody Diversity and Predicting Antibody Prevalence

Guo, Y., Chen, K. C., Kwong, P. D., Shapiro, L. S., & Sheng, Z. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02365 · Cited by 67 · see citing works

Antibodies to SARS-CoV-2 are associated with protection against reinfectionPreprint

Lumley, S., O’Donnell, D., Stoesser, N. E., et al. (2020) · medRxiv · doi:10.1101/2020.11.18.20234369 · Cited by 60 · see citing works

IgA polymerization contributes to efficient virus neutralization on human upper respiratory mucosa after intranasal inactivated influenza vaccine administration

Terauchi, Y., Sano, K., Ainai, A., Saito, S., Taga, Y., Ogawa‐Goto, K., Tamura, S., Odagiri, T., Tashiro, M., Fujieda, M., et al. (2018) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2018.1438791 · Cited by 59 · see citing works

COVID-19 neutralizing antibodies predict disease severity and survival

Garcia-Beltran, W., Lam, E., Astudillo, M., Yang, D., Miller, T., Feldman, J., Hauser, B., Caradonna, T. M., Clayton, K., Nitido, A. D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.12.015 · Cited by 56 · see citing works

Neutralization Takes Precedence Over IgG or IgA Isotype-related Functions in Mucosal HIV-1 Antibody-mediated Protection

Astronomo, R. D., Santra, S., Ballweber-Fleming, L., Westerberg, K., Mach, L. V., Hensley‐McBain, T., Sutherland, L. L., Mildenberg, B., Morton, G., Yates, N. L., et al. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.11.024 · Cited by 54 · see citing works

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

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

Correlates of protection against symptomatic and asymptomatic SARS-CoV-2 infection

Feng, S., Phillips, D. J., White, T., Sayal, H., Aley, P. K., Bibi, S., Dold, C., Fuskova, M., Gilbert, S. C., Hirsch, I., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01540-1 · Cited by 1,163 · see citing works

IgA dominates the early neutralizing antibody response to SARS-CoV-2

Sterlin, D., Mathian, A., Miyara, M., Mohr, A., Anna, F., Claër, L., Quentric, P., Fadlallah, J., Devilliers, H., Ghillani, P., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd2223 · Cited by 1,037 · see citing works

Naturally enhanced neutralizing breadth against SARS-CoV-2 one year after infection

Wang, Z., Muecksch, F., Schaefer-Babajew, D., Finkin, S., Viant, C., Gaebler, C., Hoffmann, H. H., Barnes, C. O., Cipolla, M., Ramos, V., et al. (2021) · Nature · doi:10.1038/s41586-021-03696-9 · Cited by 721 · see citing works

Increased memory B cell potency and breadth after a SARS-CoV-2 mRNA boost

Muecksch, F., Wang, Z., Cho, A., Gaebler, C., Ben Tanfous, T., DaSilva, J., Bednarski, E., Ramos, V., Zong, S., Johnson, B., et al. (2022) · Nature · doi:10.1038/s41586-022-04778-y · Cited by 297 · see citing works

Kinetics and correlates of the neutralizing antibody response to SARS-CoV-2 infection in humans

Vanshylla, K., Di Cristanziano, V., Kleipass, F., Dewald, F., Schommers, P., Gieselmann, L., Gruell, H., Schlotz, M., Ercanoglu, M. S., Stumpf, R., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.04.015 · Cited by 153 · see citing works

Anti- SARS-CoV-2 Receptor Binding Domain Antibody Evolution after mRNA Vaccination

Cho, A., Muecksch, F., Schaefer-Babajew, D., Wang, Z., Finkin, S., Gaebler, C., Ramos, V., Cipolla, M., Mendoza, P., Agudelo, M., et al. (2021) · doi:10.1101/2021.07.29.454333 · Cited by 275 · see citing works

Decay of Fc-dependent antibody functions after mild to moderate COVID-19

Lee, W. S., Selva, K. J., Davis, S. K., Wines, B. D., Reynaldi, A., Esterbauer, R., Kelly, H. G., Haycroft, E. R., Tan, H.-X., Juno, J. A., et al. (2020) · doi:10.1101/2020.12.13.20248143 · Cited by 80 · see citing works

Systematic Investigation of Selected Bio-molecules Potentially Effective in Inhibiting SARS-CoV-2/COVID-19 via In-Silico Analysis

Vanzara, A., Ambasan, S., Shrivastav, A., et al. (2024) · Fine Chemical Engineering · doi:10.37256/fce.5220244193

Detection of SARS-CoV-2 through pool testing for COVID-19: an integrative review

Costa, M. S., Guimarães, N. S., de Andrade, A. B., Vaz-Tostes, L. P., Oliveira, R. B., Simões, M. D. S., Gelape, G. D. O., Alves, C. R. L., Machado, E. L., da Fonseca, F. G., et al. (2021) · Revista da Sociedade Brasileira de Medicina Tropical · doi:10.1590/0037-8682-0276-2021 · Cited by 8 · see citing works

Coronial cases: SARS-CoV-2 infection and Covid-19

Iles, L. E. (2021) · Pathology · doi:10.1016/j.pathol.2021.05.026

Limits of Detection of 6 Approved RT–PCR Kits for the Novel SARS-Coronavirus-2 (SARS-CoV-2)

Wang, X., Yao, H., Xu, X., et al. (2020) · Clinical Chemistry · doi:10.1093/clinchem/hvaa099 · Cited by 146 · see citing works

Background, testing methods, and laboratory approaches to SARS coronavirus-2 (SARS-CoV-2) and Covid19

Rawlinson, W. D., van Hal, S. J., Yeang, M., et al. (2021) · Pathology · doi:10.1016/j.pathol.2021.05.025