Comparison of Four SARS-CoV-2 Neutralization Assays

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

WHO Coronavirus Disease (COVID-19) Dashboard

(2020) · Bangladesh Physiotherapy Journal · doi:10.46945/bpj.10.1.03.01 · Cited by 5,545 · see citing works

Antibody responses to SARS-CoV-2 in patients with COVID-19

Long, Q.-X., Liu, B.-Z., Deng, H.-J., Wu, G.-C., Deng, K., Chen, Y.-K., Liao, P., Qiu, J.-F., Lin, Y., Cai, X.-F., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0897-1 · Cited by 2,876 · see citing works

Antibody Responses to SARS-CoV-2 in Patients With Novel Coronavirus Disease 2019

Zhao, J., Yuan, Q., Wang, H., Liu, W., Liao, X., Su, Y., Wang, X., Yuan, J., Li, T., Li, J., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa344 · Cited by 2,607 · see citing works

Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity

Cantuti-Castelvetri, L., Ojha, R., Pedro, L. D., Djannatian, M., Franz, J., Kuivanen, S., van der Meer, F., Kallio, K., Kaya, T., Anastasina, M., et al. (2020) · Science · doi:10.1126/science.abd2985 · Cited by 1,925 · see citing works

A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells

Hoffmann, M., Kleine-Weber, H., & Pöhlmann, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.022 · Cited by 1,852 · 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

Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies

Baum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253 · see citing works

Coronavirus Disease 2019 (COVID-19) Re-infection by a Phylogenetically Distinct Severe Acute Respiratory Syndrome Coronavirus 2 Strain Confirmed by Whole Genome Sequencing

To, K. K.-W., Hung, I. F.-N., Ip, J. D., Chu, A. W.-H., Chan, W.-M., Tam, A. R., Fong, C. H.-Y., Yuan, S., Tsoi, H.-W., Ng, A. C.-K., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1275 · Cited by 746 · see citing works

Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays

Crawford, K. H. D., Eguia, R. T., Dingens, A. S., Loes, A. N., Malone, K. D., Wolf, C. R., Chu, H. Y., Tortorici, M. A., Veesler, D., Murphy, M., et al. (2020) · Viruses · doi:10.3390/v12050513 · Cited by 727 · see citing works

Establishment and validation of a pseudovirus neutralization assay for SARS-CoV-2

Nie, J., Li, Q., Wu, J., Zhao, C., Hao, H., Liu, H., Zhang, L., Nie, L., Qin, H., Wang, M., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1743767 · Cited by 711 · 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

The dynamics of humoral immune responses following SARS-CoV-2 infection and the potential for reinfection

Kellam, P., & Barclay, W. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001439 · Cited by 351 · see citing works

A comparison of four serological assays for detecting anti–SARS-CoV-2 antibodies in human serum samples from different populations

Grzelak, L., Temmam, S., Planchais, C., Demeret, C., Tondeur, L., Huon, C., Guivel-Benhassine, F., Staropoli, I., Chazal, M., Dufloo, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.abc3103 · Cited by 310 · see citing works

Protocol and reagents for pseudotyping lentiviral particles with SARS-CoV-2 Spike protein for neutralization assaysPreprint

Crawford, K. H. D., Eguia, R. T., Dingens, A. S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.20.051219 · Cited by 230 · see citing works

Asymptomatic Reinfection in 2 Healthcare Workers From India With Genetically Distinct Severe Acute Respiratory Syndrome Coronavirus 2

Gupta, V., Bhoyar, R. C., Jain, A. K., Srivastava, S., Upadhayay, R., Imran, M., Jolly, B., Divakar, M. K., Sharma, D., Sehgal, P., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa1451 · Cited by 187 · see citing works

An In Vitro Microneutralization Assay for SARS‐CoV‐2 Serology and Drug Screening

Amanat, F., White, K. M., Miorin, L., Strohmeier, S., McMahon, M., Meade, P. S., Liu, W., Albrecht, R. A., Simon, V. R., Martínez‐Sobrido, L., et al. (2020) · Current Protocols in Microbiology · doi:10.1002/cpmc.108 · Cited by 171 · see citing works

Validation of a commercially available SARS-CoV-2 serological immunoassay

Meyer, B., Torriani, G., Yerly, S., Mazza, L., Calame, A., Arm‐Vernez, I., Zimmer, G., Agoritsas, T., Stirnemann, J., Spechbach, H., et al. (2020) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2020.06.024 · Cited by 156 · see citing works

Retroviral Vectors Pseudotyped with Severe Acute Respiratory Syndrome Coronavirus S Protein

Giroglou, T., Cinatl, J., Rabenau, H., Drosten, C., Schwalbe, H., Doerr, H., & von Laer, D. (2004) · Journal of Virology · doi:10.1128/jvi.78.17.9007-9015.2004 · Cited by 147 · see citing works

A highly specific and sensitive serological assay detects SARS-CoV-2 antibody levels in COVID-19 patients that correlate with neutralization

Peterhoff, D., Glück, V., Vogel, M., Schuster, P., Schütz, A., Neubert, P., Albert, V., Frisch, S., Kießling, M., Pervan, P., et al. (2020) · Infection · doi:10.1007/s15010-020-01503-7 · Cited by 136 · see citing works

Fusion-active glycoprotein G mediates the cytotoxicity of vesicular stomatitis virus M mutants lacking host shut-off activity

Hoffmann, M., Wu, Y.-J., Gerber, M. A., Rentsch, M. B., Heimrich, B., Schwemmle, M., & Zimmer, G. (2010) · Journal of General Virology · doi:10.1099/vir.0.023978-0 · Cited by 96 · see citing works

Rapid Quantification of SARS-CoV-2-Neutralizing Antibodies Using Propagation-Defective Vesicular Stomatitis Virus Pseudotypes

Zettl, F., Meister, T. L., Vollmer, T., Fischer, B., Steinmann, J., Krawczyk, A., V’kovski, P., Tödt, D., Steinmann, E., Pfaender, S., et al. (2020) · Vaccines · doi:10.3390/vaccines8030386 · Cited by 86 · see citing works

High SARS-CoV-2 seroprevalence in children and adults in the Austrian ski resort of Ischgl

Knabl, L., Mitra, T., Kimpel, J., Rössler, A., Volland, A., Walser, A., Ulmer, H., Pipperger, L., Binder, S. C., Riepler, L., et al. (2021) · Communications Medicine · doi:10.1038/s43856-021-00007-1 · Cited by 70 · see citing works

VSV-GP: a Potent Viral Vaccine Vector That Boosts the Immune Response upon Repeated Applications

Tober, R., Bánki, Z., Egerer, L., Muik, A., Behmüller, S., Kreppel, F., Greczmiel, U., Oxenius, A., von Laer, D., & Kimpel, J. (2014) · Journal of Virology · doi:10.1128/jvi.03276-13 · Cited by 69 · see citing works

Asymptomatic reinfection in two healthcare workers from India with genetically distinct SARS-CoV-2Preprint

Gupta, V., Bhoyar, R. C., Jain, A. K., Srivastava, S., Upadhayay, R., Imran, M., Jolly, B., Divakar, M. K., Sharma, D., Sehgal, P., et al. (2020) · doi:10.31219/osf.io/4fmrg · Cited by 62 · see citing works

Mutations in gp120 Contribute to the Resistance of Human Immunodeficiency Virus Type 1 to Membrane-Anchored C-Peptide maC46

Hermann, F. G., Egerer, L., Brauer, F., Gerum, C., Schwalbe, H., Dietrich, U., & von Laer, D. (2009) · Journal of Virology · doi:10.1128/jvi.00666-08 · Cited by 40 · see citing works

High SARS-CoV-2 Seroprevalence in Children and Adults in the Austrian Ski Resort IschglPreprint

Knabl, L., Mitra, T., Kimpel, J., et al. (2020) · medRxiv · doi:10.1101/2020.08.20.20178533 · Cited by 34 · see citing works

Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry

Lin, H.-X., Feng, Y., Tu, X., Zhao, X., Hsieh, C.-H., Griffin, L., Junop, M. S., & Zhang, C. (2011) · Virus Research · doi:10.1016/j.virusres.2011.06.029 · Cited by 30 · see citing works

Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity

Garcia-Beltran, W. F., Lam, E. C., St. Denis, K., Nitido, A. D., Garcia, Z. H., Hauser, B. M., Feldman, J., Pavlovic, M. N., Gregory, D. J., Poznansky, M. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.013 · Cited by 1,353 · see citing works

mRNA-based COVID-19 vaccine boosters induce neutralizing immunity against SARS-CoV-2 Omicron variant

Garcia-Beltran, W. F., St. Denis, K. J., Hoelzemer, A., Lam, E. C., Nitido, A. D., Sheehan, M. L., Berrios, C., Ofoman, O., Chang, C. C., Hauser, B. M., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.033 · Cited by 1,045 · see citing works

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

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

SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies

Hoffmann, M., Arora, P., Groß, R., Seidel, A., Hörnich, B. F., Hahn, A. S., Krüger, N., Graichen, L., Hofmann-Winkler, H., Kempf, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.036 · Cited by 897 · see citing works

The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic

Hoffmann, M., Krüger, N., Schulz, S., Cossmann, A., Rocha, C., Kempf, A., Nehlmeier, I., Graichen, L., Moldenhauer, A.-S., Winkler, M. S., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.032 · Cited by 889 · see citing works

SARS-CoV-2 Omicron Variant Neutralization in Serum from Vaccinated and Convalescent Persons

Rössler, A., Riepler, L., Bante, D., von Laer, D., & Kimpel, J. (2022) · New England Journal of Medicine · doi:10.1056/nejmc2119236 · Cited by 466 · see citing works

Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity

García-Beltrán, W. F., Lam, E. C., Denis, K. S., Nitido, A. D., Garcia, Z. H., Hauser, B. M., Feldman, J. E., Pavlovic, M., Gregory, D. J., Poznansky, M. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.006 · Cited by 446 · see citing works

SARS-CoV-2 variant evasion of monoclonal antibodies based on in vitro studies

Cox, M., Peacock, T. P., Harvey, W. T., Hughes, J., Wright, D. W., Willett, B. J., Thomson, E. C., Gupta, R. K., Peacock, S. J., Robertson, D. L., et al. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00809-7 · Cited by 336 · see citing works

Postacute COVID-19 is Characterized by Gut Viral Antigen Persistence in Inflammatory Bowel Diseases

Zollner, A., Koch, R., Jukic, A., Pfister, A., Meyer, M., Rössler, A., Kimpel, J., Adolph, T. E., & Tilg, H. (2022) · Gastroenterology · doi:10.1053/j.gastro.2022.04.037 · Cited by 313 · see citing works

SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination

Hoffmann, M., Hofmann-Winkler, H., Krüger, N., Kempf, A., Nehlmeier, I., Graichen, L., Arora, P., Sidarovich, A., Moldenhauer, A.-S., Winkler, M. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109415 · Cited by 258 · see citing works

ADAM10 and ADAM17 promote SARS‐CoV‐2 cell entry and spike protein‐mediated lung cell fusion

Jocher, G., Grass, V., Tschirner, S. K., Riepler, L., Breimann, S., Kaya, T., Oelsner, M., Hamad, M. S., Hofmann, L. I., Blobel, C., et al. (2022) · EMBO Reports · doi:10.15252/embr.202154305 · Cited by 123 · see citing works

Neutralizing Antibodies Against Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Variants Induced by Natural Infection or Vaccination: A Systematic Review and Pooled Analysis

Chen, X., Chen, Z., Azman, A. S., Sun, R., Lu, W., Zheng, N., Zhou, J., Wu, Q., Deng, X., Zhao, Z., et al. (2022) · Clinical Infectious Diseases · doi:10.1093/cid/ciab646 · Cited by 113 · see citing works

SARS-CoV-2 BA.2.86 enters lung cells and evades neutralizing antibodies with high efficiency

Zhang, L., Kempf, A. M., Nehlmeier, I., Cossmann, A., Richter, A. M., Bdeir, N., Graichen, L., Moldenhauer, A.-S., Dopfer‐Jablonka, A., Stankov, M. V., et al. (2024) · Cell · doi:10.1016/j.cell.2023.12.025 · Cited by 113 · see citing works

Determinants of Spike infectivity, processing, and neutralization in SARS-CoV-2 Omicron subvariants BA.1 and BA.2

Pastorio, C., Zech, F., Noettger, S., Jung, C., Jacob, T., Sanderson, T., Sparrer, K. M. J., & Kirchhoff, F. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.07.006 · Cited by 90 · see citing works

Serology as a Tool to Assess Infectious Disease Landscapes and Guide Public Health Policy

Haselbeck, A., Im, J., Prifti, K., Marks, F., Holm, M., & Zellweger, R. M. (2022) · Pathogens · doi:10.3390/pathogens11070732 · Cited by 91 · see citing works

BA.2 and BA.5 omicron differ immunologically from both BA.1 omicron and pre-omicron variants

Rössler, A., Netzl, A., Knabl, L., Schäfer, H., Wilks, S., Bante, D., Falkensammer, B., Borena, W., von Laer, D., Smith, D. J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35312-3 · Cited by 77 · see citing works

B and T cell response to SARS-CoV-2 vaccination in health care professionals with and without previous COVID-19

Zollner, A., Watschinger, C., Rössler, A., Farcet, M. R., Penner, A., Böhm, V., Zollner-Kiechl, S., Stampfel, G., Hintenberger, R., Tilg, H., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103539 · Cited by 75 · see citing works

B.1.617.2 enters and fuses lung cells with increased efficiency and evades antibodies induced by infection and vaccination

Arora, P., Sidarovich, A., Krüger, N., Kempf, A. M., Nehlmeier, I., Graichen, L., Moldenhauer, A.-S., Winkler, M. S., Schulz, S. R., Jäck, H., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109825 · Cited by 76 · see citing works

Highly synergistic combinations of nanobodies that target SARS-CoV-2 and are resistant to escape

Mast, F. D., Fridy, P. C., Ketaren, N. E., Wang, J., Jacobs, E. Y., Olivier, J. P., Sanyal, T., Molloy, K., Schmidt, F., Rutkowska, M., et al. (2021) · eLife · doi:10.7554/elife.73027 · Cited by 62 · see citing works

Mutations in the SARS-CoV-2 spike receptor binding domain and their delicate balance between ACE2 affinity and antibody evasion

Xue, S., Han, Y., Wu, F., & Wang, Q. (2024) · Protein & Cell · doi:10.1093/procel/pwae007 · Cited by 72 · see citing works

Clinical validation of the Siemens quantitative SARS-CoV-2 spike IgG assay (sCOVG) reveals improved sensitivity and a good correlation with virus neutralization titers

Irsara, C., Egger, A., Prokop, W., Nairz, M., Loacker, L., Sahanic, S., Pizzini, A., Sonnweber, T., Holzer, B., Mayer, W., et al. (2021) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2021-0214 · Cited by 65 · see citing works

Intranasal inoculation of an MVA-based vaccine induces IgA and protects the respiratory tract of hACE2 mice from SARS-CoV-2 infection

Americo, J. L., Cotter, C. A., Earl, P. L., Liu, R., & Moss, B. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2202069119 · Cited by 60 · see citing works

Preclinical evaluation of a SARS-CoV-2 mRNA vaccine PTX-COVID19-B

Liu, J., Budylowski, P., Samson, R., Griffin, B. D., Babuadze, G., Rathod, B., Colwill, K., Abioye, J. A., Schwartz, J. A., Law, R., et al. (2022) · Science Advances · doi:10.1126/sciadv.abj9815 · Cited by 56 · see citing works

Persistence of Anti-SARS-CoV-2 Antibodies Depends on the Analytical Kit: A Report for Up to 10 Months after Infection

Favresse, J., Eucher, C., Elsen, M., Gillot, C., Eeckhoudt, S. V., Dogné, J., & Douxfils, J. (2021) · Microorganisms · doi:10.3390/microorganisms9030556 · Cited by 54 · see citing works

Clinical Utility of Elecsys Anti-SARS-CoV-2 S Assay in COVID-19 Vaccination: An Exploratory Analysis of the mRNA-1273 Phase 1 Trial

Jochum, S., Kirste, I., Hortsch, S., Grunert, V. P., Legault, H. M., Eichenlaub, U., Kashlan, B., & Pajón, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.798117 · Cited by 54 · see citing works

SARS-CoV-2 Omicron sublineages show comparable cell entry but differential neutralization by therapeutic antibodies

Arora, P., Zhang, L., Krüger, N., Rocha, C., Sidarovich, A., Schulz, S. R., Kempf, A. M., Graichen, L., Moldenhauer, A.-S., Cossmann, A., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.04.017 · Cited by 44 · see citing works

Diagnostic assay and technology advancement for detecting SARS-CoV-2 infections causing the COVID-19 pandemic

Dhar, B. (2022) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-022-03918-7 · Cited by 45 · see citing works

Characterizing SARS-CoV-2 neutralization profiles after bivalent boosting using antigenic cartography

Rössler, A., Netzl, A., Knabl, L., Bante, D., Wilks, S. H., Borena, W., von Laer, D., Smith, D. J., & Kimpel, J. (2023) · Nature Communications · doi:10.1038/s41467-023-41049-4 · Cited by 45 · see citing works

A third dose of inactivated vaccine augments the potency, breadth, and duration of anamnestic responses against SARS-CoV-2Preprint

Wang, K., Cao, Y., Zhou, Y., Wu, J., Jia, Z., Hu, Y., Yisimayi, A., Fu, W., Wang, L., Liu, P., et al. (2021) · medRxiv · doi:10.1101/2021.09.02.21261735 · Cited by 38 · see citing works

Marked Increase in Avidity of SARS-CoV-2 Antibodies 7–8 Months After Infection Is Not Diminished in Old Age

Pichler, D., Baumgartner, M. R., Kimpel, J., Rössler, A., Riepler, L., Bates, K., Fleischer, V., von Laer, D., Borena, W., & Würzner, R. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab300 · Cited by 39 · see citing works

Fetal bovine serum: how to leave it behind in the pursuit of more reliable science

Weber, T., Malakpour‐Permlid, A., Chary, A., D’Alessandro, V., Haut, L., Seufert, S., Wenzel, E. V., Hickman, J. J., Bieback, K., Wiest, J., et al. (2025) · Frontiers in Toxicology · doi:10.3389/ftox.2025.1612903 · Cited by 45 · see citing works

Ad26.COV2.S breakthrough infections induce high titers of neutralizing antibodies against Omicron and other SARS-CoV-2 variants of concern

Kitchin, D., Richardson, S. I., van der Mescht, M. A., Motlou, T. P., Mzindle, N. B., Moyo-Gwete, T., Makhado, Z., Ayres, F., Manamela, N. P., Spencer, H., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100535 · Cited by 35 · see citing works

Different Neutralization Sensitivity of SARS-CoV-2 Cell-to-Cell and Cell-Free Modes of Infection to Convalescent Sera

Kruglova, N., Siniavin, A., Gushchin, V., & Mazurov, D. (2021) · Viruses · doi:10.3390/v13061133 · Cited by 37 · see citing works

Heterologous ChAdOx1/BNT162b2 vaccination induces stronger immune response than homologous ChAdOx1 vaccination: The pragmatic, multi-center, three-arm, partially randomized HEVACC trial

Bánki, Z., Mateus, J., Rössler, A., Schäfer, H., Bante, D., Riepler, L., Grifoni, A., Sette, A., Simon, V. R., Falkensammer, B., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104073 · Cited by 37 · see citing works

Immune response against SARS-CoV-2 variants: the role of neutralization assays

Chmielewska, A., Czarnota, A., Bieńkowska-Szewczyk, K., & Grzyb, K. (2021) · npj Vaccines · doi:10.1038/s41541-021-00404-6 · Cited by 33 · see citing works

Rapid spread of the SARS-CoV-2 JN.1 lineage is associated with increased neutralization evasion

Zhang, L., Dopfer‐Jablonka, A., Cossmann, A., Stankov, M. V., Graichen, L., Moldenhauer, A.-S., Fichter, C., Aggarwal, A., Turville, S. G., Behrens, G. M. N., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109904 · Cited by 29 · see citing works

Scalable, Micro-Neutralization Assay for Assessment of SARS-CoV-2 (COVID-19) Virus-Neutralizing Antibodies in Human Clinical Samples

Bennett, R. S., Postnikova, E. N., Liang, J. Y., Gross, R., Mazur, S., Dixit, S., Lukin, V. V., Kocher, G., Yu, S., Georgia, S., et al. (2021) · Viruses · doi:10.3390/v13050893 · Cited by 29 · see citing works

Homogeneous surrogate virus neutralization assay to rapidly assess neutralization activity of anti-SARS-CoV-2 antibodies

Kim, S. J., Yao, Z., Marsh, M., Eckert, D. M., Kay, M. S., Lyakisheva, A., Pasic, M. D., Bansal, A., Birnboim, C., Jha, P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31300-9 · Cited by 27 · see citing works

Neutralization of alpha, gamma, and D614G SARS‐CoV‐2 variants by CoronaVac vaccine‐induced antibodies

Fernández, J., Bruneau, N., Fasce, R., Martín, H. S., Balanda, M., Bustos, P., Ulloa, S., Mora, J., & Ramírez, E., V (2021) · Journal of Medical Virology · doi:10.1002/jmv.27310 · Cited by 25 · see citing works

Uses and Challenges of Antiviral Polyclonal and Monoclonal Antibody Therapies

Struble, E. B., Rawson, J. M. O., Stantchev, T. S., Scott, D., & Shapiro, M. A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15051538 · 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

Multiplexed LNP-mRNA vaccination against pathogenic coronavirus species

Peng, L., Fang, Z., Renauer, P. A., McNamara, A., Park, J. J.-Y., Lin, Q., Zhou, X., Dong, M. B., Zhu, B., Zhao, H., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111160 · Cited by 25 · see citing works

A pseudovirus-based platform to measure neutralizing antibodies in Mexico using SARS-CoV-2 as proof-of-concept

Cruz-Cárdenas, J. A., Gutiérrez, M., López-Arredondo, A., Castañeda‐Delgado, J. E., Rojas‐Martínez, A., Nakamura, Y., Enciso‐Moreno, J. A., Palomares, L. A., & Brunck, M. E. G. (2022) · Scientific Reports · doi:10.1038/s41598-022-22921-7 · Cited by 25 · see citing works

The Anti-Histamine Azelastine, Identified by Computational Drug Repurposing, Inhibits Infection by Major Variants of SARS-CoV-2 in Cell Cultures and Reconstituted Human Nasal Tissue

Konrat, R., Papp, H., Kimpel, J., Rössler, A., Szijártó, V., Nagy, G., Madai, M., Zeghbib, S., Kuczmog, A., Lanszki, Z., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.861295 · Cited by 23 · see citing works

Development and optimization of diagnostic assays for infectious diseases

Ciotti, M., Nicolai, E., & Pieri, M. (2024) · LabMed discovery. · doi:10.1016/j.lmd.2024.100032 · Cited by 26 · see citing works

Optimization and evaluation of a live virus SARS-CoV-2 neutralization assay

Frische, A., Brooks, P. T., Gybel‐Brask, M., Sækmose, S. G., Jensen, B. A., Mikkelsen, S., Bruun, M. T., Boding, L., Polacek, C., Jørgensen, C. S., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0272298 · Cited by 22 · see citing works

Increased lung cell entry of B.1.617.2 and evasion of antibodies induced by infection and BNT162b2 vaccinationPreprint

Arora, P., Kempf, A. M., Nehlmeier, I., Sidarovich, A., Krüger, N., Graichen, L., Moldenhauer, A.-S., Winkler, M. S., Schulz, S. R., Jäck, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.23.449568 · Cited by 20 · see citing works

Persistence of immunity to SARS-CoV-2 over time in the ski resort Ischgl

Borena, W., Bánki, Z., Bates, K., Winner, H., Riepler, L., Rössler, A., Pipperger, L., Theurl, I., Falkensammer, B., Ulmer, H., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103534 · Cited by 18 · see citing works

Impact of mutations defining SARS-CoV-2 Omicron subvariants BA.2.12.1 and BA.4/5 on Spike function and neutralization

Pastorio, C., Noettger, S., Nchioua, R., Zech, F., Sparrer, K. M. J., & Kirchhoff, F. (2023) · iScience · doi:10.1016/j.isci.2023.108299 · Cited by 19 · see citing works

Spectrum Bias and Individual Strengths of SARS-CoV-2 Serological Tests—A Population-Based Evaluation

Einhauser, S., Peterhoff, D., Niller, H. H., Beileke, S., Günther, F., Steininger, P. A., Burkhardt, R., Heid, I. M., Pfahlberg, A. B., Überla, K., et al. (2021) · Diagnostics · doi:10.3390/diagnostics11101843 · Cited by 17 · see citing works

Persistence of humoral response upon SARS‐CoV‐2 infection

Knies, A., Ladage, D., Braun, R. J., Kimpel, J., & Schneider, M. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2272 · Cited by 14 · see citing works

Liposome-based high-throughput and point-of-care assays toward the quick, simple, and sensitive detection of neutralizing antibodies against SARS-CoV-2 in patient sera

Streif, S., Neckermann, P., Spitzenberg, C., Weiß, K. T., Hoecherl, K., Kulikowski, K., Hahner, S., Nölting, C., Einhauser, S., Peterhoff, D., et al. (2023) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-023-04548-3 · Cited by 15 · see citing works

No evidence for epitranscriptomic m5C modification of SARS-CoV-2, HIV and MLV viral RNA

Huang, A., Riepler, L., Rieder, D., Kimpel, J., & Lusser, A. (2023) · RNA · doi:10.1261/rna.079549.122 · Cited by 16 · see citing works

SARS-CoV-2 vaccination of convalescents boosts neutralization capacity against Omicron subvariants BA.1, BA.2 and BA.5 and can be predicted by anti-S antibody concentrations in serological assays

Seidel, A., Hoffmann, S., Jahrsdörfer, B., Körper, S., Ludwig, C., Vieweg, C., Albers, D., von Maltitz, P., Müller, R., Lotfi, R., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1170759 · Cited by 16 · see citing works

Comparative analysis of SARS-CoV-2 neutralization titers reveals consistency between human and animal model serum and across assays

Mühlemann, B., Wilks, S. H., Baracco, L., Bekliz, M., Carreño, J. M., Corman, V. M., Davis-Gardner, M. E., Dejnirattisai, W., Diamond, M., Douek, D. C., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adl1722 · Cited by 18 · see citing works

Practical guidance for clinical laboratories for SARS-CoV-2 serology testing

Charlton, C. L., Kanji, J. N., Tran, V., Kus, J. V., Gubbay, J. B., Osiowy, C., Robinson, J. L., Sekirov, I., DREBOT, M. A., Hatchette, T. F., et al. (2021) · Canada Communicable Disease Report · doi:10.14745/ccdr.v47i04a01 · Cited by 14 · see citing works

Development of a Cell-Based SARS-CoV-2 Pseudovirus Neutralization Assay Using Imaging and Flow Cytometry Analysis

Izac, J. R., Kwee, E. J., Tian, L., Elsheikh, E. B., Gaigalas, A. K., Elliott, J. T., & Wang, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512332 · Cited by 13 · see citing works

Validation of a Pseudovirus Neutralization Assay for Severe Acute Respiratory Syndrome Coronavirus 2: A High-Throughput Method for the Evaluation of Vaccine Immunogenicity

Cai, Z., Kalkeri, R., Wang, M., Haner, B., Dent, D., Osman, B., Skonieczny, P., Ross, J., Feng, S.-L. Y., Cai, R., et al. (2024) · Microorganisms · doi:10.3390/microorganisms12061201 · Cited by 12 · see citing works

A Recombinant Protein XBB.1.5 RBD/Alum/CpG Vaccine Elicits High Neutralizing Antibody Titers against Omicron Subvariants of SARS-CoV-2

Thimmiraju, S. R., Adhikari, R., Villar, M. J., Lee, J., Liu, Z., Kundu, R. T., Chen, Y., Sharma, S., Ghei, K., Keegan, B. P., et al. (2023) · Vaccines · doi:10.3390/vaccines11101557 · Cited by 11 · see citing works

Serological Survey of Retrovirus and Coronavirus Infections, including SARS-CoV-2, in Rural Stray Cats in The Netherlands, 2020–2022

Duijvestijn, M. B. H. M., Schuurman, N., Vernooij, J. C. M., van Leeuwen, M. A. J. M., Bosch, B., van den Brand, J. M. A., Wagenaar, J. A., van Kuppeveld, F. J. M., Egberink, H. F., & Verhagen, J. H. (2023) · Viruses · doi:10.3390/v15071531 · Cited by 11 · see citing works

Antiviral Potential of Azelastine against Major Respiratory Viruses

Fischhuber, K., Bánki, Z., Kimpel, J., Kragl, N., Rössler, A., Bolze, A., Müllauer, B., Angerer, J., Nagy, G., Nagy, E., et al. (2023) · Viruses · doi:10.3390/v15122300 · Cited by 10 · see citing works

Prevalence of SARS-CoV-2 antibodies in healthy blood donors from the state of Tyrol, Austria, in summer 2020

Siller, A., Wachter, G. A., Neururer, S. B., Pfeifer, B. E., Astl, M., Borena, W., Kimpel, J., Elmer, S., Spöck, F., Vales, A., et al. (2021) · Wiener klinische Wochenschrift · doi:10.1007/s00508-021-01963-3 · Cited by 9 · see citing works

SARS-CoV-2 Antibody Neutralization Assay Platforms Based on Epitopes Sources: Live Virus, Pseudovirus, and Recombinant S Glycoprotein RBD

Septisetyani, E. P., Prasetyaningrum, P. W., Anam, K., & Santoso, A. (2021) · Immune Network · doi:10.4110/in.2021.21.e39 · Cited by 10 · see citing works

Development of a Rapid Live SARS-CoV-2 Neutralization Assay Based on a qPCR Readout

Lichtenegger, S., Saiger, S., Hardt, M., Kulnik, S., Wagner, G. E., Kleinhappl, B., Assig, K., Zauner, A., Ober, M., Kimpel, J., et al. (2022) · Journal of Clinical Microbiology · doi:10.1128/jcm.00376-22 · Cited by 10 · see citing works

Advances in Surrogate Neutralization Tests for High-Throughput Screening and the Point-of-Care

Streif, S., & Baeumner, A. J. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c00666 · Cited by 8 · see citing works

Reduced levels of convalescent neutralizing antibodies against SARS-CoV-2 B.1+L249S+E484K lineage

Álvarez-Díaz, D. A., Laiton‐Donato, K., Torres, O., Ruiz-Moreno, H. A., Franco-Muñoz, C., Beltran, M. A., Mercado, M., Rueda, M. G., & Muñoz, A. L. (2021) · Virus Research · doi:10.1016/j.virusres.2021.198629 · Cited by 8 · see citing works

Leveraging South African HIV research to define SARS‐CoV ‐2 immunity triggered by sequential variants of concern

Bhiman, J. N., & Moore, P. L. (2022) · Immunological Reviews · doi:10.1111/imr.13086 · Cited by 6 · see citing works

A Global Collaborative Comparison of SARS-CoV-2 Antigenicity Across 15 Laboratories

Brangel, P., Türeli, S., Mühlemann, B., Liechti, N., Zysset, D., Engler, O. B., Hunger‐Glaser, I., Ghiga, I., Mattiuzzo, G., Eckerle, I., et al. (2024) · Viruses · doi:10.3390/v16121936 · Cited by 8 · see citing works

Establishment of national standard for anti-SARS-Cov-2 neutralizing antibody in China: The first National Standard calibration traceability to the WHO International Standard

Guan, L., Mao, Q., Tan, D., Liu, J., Zhang, X., Li, L., Liu, M., Wang, Z., Cheng, F., Cui, B., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1107639 · Cited by 7 · see citing works

Pharmacokinetic and Environmental Risk Assessment of Prime-2-CoV, a Non-Replicating Orf Virus-Based Vaccine against SARS-CoV-2

Metz, C., Haug, V., Müller, M., & Amann, R. (2024) · Vaccines · doi:10.3390/vaccines12050492 · Cited by 7 · see citing works

Assessing the Reliability of SARS-CoV-2 Neutralization Studies That Use Post-Vaccination Sera

Jacobsen, H., Sitaras, I., Jurgensmeyer, M., Mulders, M. N., Goldblatt, D., Feikin, D. R., Bar‐Zeev, N., Higdon, M. M., & Knoll, M. D. (2022) · Vaccines · doi:10.3390/vaccines10060850 · Cited by 7 · see citing works

Role of tannic acid against SARS-cov-2 cell entry by targeting the interface region between S-protein-RBD and human ACE2

Chen, X., Wang, Z., Wang, J., Yao, Y., Wang, Q., Huang, J., Xiang, X., Zhou, Y., Xue, Y., Li, Y., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.940628 · Cited by 7 · see citing works

Antibody response in elderly vaccinated four times with an mRNA anti-COVID-19 vaccine

Rouvinski, A., Friedman, A., Kirillov, S., Attal, J. H., Kumari, S., Fahoum, J., Wiener, R., Magen, S., Plotkin, Y., Chemtob, D., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-41399-5 · Cited by 7 · see citing works

Exposure to two antigenically distinct SARS-CoV-2 variants broadens neutralization patterns

Schmitt, M. M., Rössler, A., Netzl, A., Knabl, L., Falch, A., Neckermann, P., Bermejo‐Jambrina, M., Borena, W., Singh, G., Krammer, F., et al. (2025) · Vaccine · doi:10.1016/j.vaccine.2025.127459 · Cited by 8 · see citing works

Treatment with integrase inhibitors alters SARS‐CoV‐2 neutralization levels measured with HIV‐based pseudotypes in people living with HIV

Tarazona, E. D. L. T., González-Robles, A., Cascajero, A., Jiménez, P., Miró, J. M., Sánchez‐Palomino, S., Alcamı́, J., Buzón, M. J., & García‐Pérez, J. (2023) · Journal of Medical Virology · doi:10.1002/jmv.28543 · Cited by 6 · see citing works

Characterization of Immune Responses to SARS-CoV-2 and Other Human Pathogenic Coronaviruses Using a Multiplex Bead-Based Immunoassay

Borena, W., Kimpel, J., Gierer, M., Rössler, A., Riepler, L., Oehler, S., von Laer, D., & Miholits, M. (2021) · Vaccines · doi:10.3390/vaccines9060611 · Cited by 6 · see citing works

Exploring Rapid and Effective Screening Methods for Anti-SARS-CoV-2 Neutralizing Antibodies in COVID-19 Convalescent Patients and Longitudinal Vaccinated Populations

Hu, C.-Q., Li, D., Liu, Z., Ren, L., Su, J.-W., Zhu, M., Feng, Y., Wang, Z., Liu, Q., Zhu, B., et al. (2022) · Pathogens · doi:10.3390/pathogens11020171 · Cited by 5 · see citing works

Performance and correlation of ten commercial immunoassays for the detection of SARS-CoV-2 antibodies

Lokida, D., Karyana, M., Kosasih, H., Mardian, Y., Sugiyono, R. I., Arlinda, D., Lukman, N., Salim, G., Butar-butar, D. P., Naysilla, A. M., et al. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12614 · Cited by 6 · see citing works

Maternal Immunization Using a Protein Subunit Vaccine Mediates Passive Immunity against Zaire ebolavirus in a Murine Model

Williams, C. A., Wong, T. A. S., Ball, A. H., Lieberman, M. M., & Lehrer, A. T. (2022) · Viruses · doi:10.3390/v14122784 · Cited by 5 · see citing works

Borderline and weakly positive antibody levels against the S-protein of SARS-CoV-2 exhibit limited agreement with virus neutralization titres

Egger, A., Irsara, C., Holzer, B., Winkler, C., Bellmann‐Weiler, R., Weiß, G., Hartmann, B., Prokop, W., Hoermann, G., Griesmacher, A., et al. (2021) · Journal of Clinical Virology Plus · doi:10.1016/j.jcvp.2021.100058 · Cited by 5 · see citing works

Evaluation of different platforms for the detection of anti-SARS coronavirus-2 antibodies, Thailand

Lerdsamran, H., Mungaomklang, A., Iamsirithaworn, S., Prasertsopon, J., Prasert, K., Intalapaporn, P., Siriyakorn, N., Wiriyarat, W., Thinpan, N., Sawadpongpan, S., et al. (2021) · BMC Infectious Diseases · doi:10.1186/s12879-021-06921-y · Cited by 5 · see citing works

Development and Validation of a Standardized Pseudotyped Virus-Based Neutralization Assay for Assessment of Anti-Nipah Virus Neutralizing Activity in Candidate Nipah Vaccines

Alam, M., Rana, M. J., Salauddin, A., Bentley, E. M., Kamuyu, G., Shill, D. K., Jahan, S., Alam, M. M., Raihan, M. A., Rahman, M. Z., et al. (2025) · Vaccines · doi:10.3390/vaccines13070753 · Cited by 4 · see citing works

Development of a Novel Homogeneous Liposome-Based One-Step Assay for SARS-CoV‑2 Antibody Detection in Human Serum Based on Fluorescent Liposomes and Complement Activity

Reiner, C., Hoecherl, K., Einhauser, S., Streif, S., Spitzenberg, C., Konrad, J., Neckermann, P., Breunig, M., Pauly, D., Wagner, R., et al. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c04506 · Cited by 3 · see citing works

Host cell lectins ASGR1 and DC-SIGN jointly with TMEM106B confer ACE2 independence and imdevimab resistance to SARS-CoV-2 pseudovirus with spike mutation E484D

Arora, P., Zhang, L., Nehlmeier, I., Kempf, A. M., Graichen, L., Kreitz, E., Sidarovich, A., Rocha, C., Gärtner, S., Winkler, M., et al. (2025) · Journal of Virology · doi:10.1128/jvi.01230-24 · Cited by 4 · see citing works

Entry Efficiency, Protease Dependence, and Antibody-Mediated Neutralization of SARS-CoV-2 Sublineages KP.3.1.1 and XEC

Arora, P., Kempf, A. M., Nehlmeier, I., Schulz, S. R., Jäck, H., Hoffmann, M., & Pöhlmann, S. (2025) · Vaccines · doi:10.3390/vaccines13040385 · Cited by 4 · see citing works

Comparative Analysis of SARS-CoV-2 Antigenicity across Assays and in Human and Animal Model SeraPreprint

Mühlemann, B., Wilks, S., Baracco, L., Bekliz, M., Carreño, J. M., Corman, V. M., Davis-Gardner, M. E., Dejnirattisai, W., Diamond, M., Douek, D. C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.27.559689 · Cited by 4 · see citing works

A critical residue in a conserved RBD epitope determines neutralization breadth of pan-sarbecovirus antibodies with recurring YYDRxxG motifs

Stein, S. C., Ssebyatika, G. L., Benecke, T., Stroh, L. J., Rajak, M. K., Vollmer, B., Menz, S., Waldmann, J.-Y., Tipp, S. N., Ochulor, O., et al. (2025) · mBio · doi:10.1128/mbio.00606-25 · Cited by 3 · see citing works

Novel neutralizing mouse-human chimeric monoclonal antibodies against the SARS-CoV-2 receptor binding domain

Vanan, A. G., Maghsood, F., Yadegari, H., Bahadori, T., Zarnani, A., Razavi, S. A., Jeddi‐Tehrani, M., Amiri, M. M., & Shokri, F. (2023) · Journal of Medical Microbiology · doi:10.1099/jmm.0.001728 · Cited by 3 · see citing works

B and T Cell Responses to SARS-CoV-2 Vaccination in Kidney and Liver Transplant Recipients with and without Previous COVID-19

Watschinger, C., Stampfel, G., Zollner, A., Hoog, A., Rössler, A., Reiter, S., Dax, K., Kimpel, J., Tilg, H., Antlanger, M., et al. (2023) · Viruses · doi:10.3390/v16010001 · Cited by 3 · see citing works

Impedance‐based monitoring of titration and neutralization assays with VSV‐G and SARS‐CoV‐2‐spike pseudoviruses

Mildner, A., Einhauser, S., Michaelis, S., von Bieberstein, K. R., Wagner, R., & Wegener, J. (2024) · Applied Research · doi:10.1002/appl.202400097 · Cited by 3 · see citing works

High Prevalence of Undocumented SARS-CoV-2 Infections in the Pediatric Population of the Tyrolean District of Schwaz

Harthaller, T., Borena, W., Bante, D., Schäfer, H., Strallhofer, O., Zöggeler, T., Hochmuth, E., Hoch, L., Rössler, A., von Laer, D., et al. (2022) · Viruses · doi:10.3390/v14102294 · Cited by 3 · see citing works

Neutralization of five SARS-CoV-2 variants of concern by convalescent and BBIBP-CorV vaccinee serum

Zhu, Y., Yang, X., Xun, J., Liu, J., Wen, Q., Lin, Y., Shen, X., Chen, J., Yuan, S., Zhao, X., et al. (2022) · Virologica Sinica · doi:10.1016/j.virs.2022.10.006 · Cited by 3 · see citing works

Detection of infectious SARS-CoV-2 in ocular samples is linked to viral load in the nasopharynx

Kimpel, J., Rössler, A., Bante, D., Borena, W., von Laer, D., Zehetner, C., Rauchegger, T., Seiwald, S., & Falkensammer, B. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1332157 · Cited by 3 · see citing works

Seroprevalence of SARS-CoV-2 infection in the Tyrolean district of Schwaz at the time of the rapid mass vaccination in March 2021 following B.1.351-variant outbreak

Willeit, P., Kimpel, J., Winner, H., Harthaller, T., Schäfer, H., Bante, D., Falkensammer, B., Rössler, A., Riepler, L., Ower, C., et al. (2022) · Frontiers in Public Health · doi:10.3389/fpubh.2022.989337 · Cited by 3 · see citing works

Severe Acute Respiratory Syndrome Corona Virus-2 (SARS-CoV-2) Serology in the Vaccination Era and Post Booster Vaccination

Dulipsingh, L., Lang, M., Diffenderfer, M. R., Cook, L., Puff, J., Diaz, L., He, L., & Schaefer, E. J. (2022) · Journal of Clinical Virology Plus · doi:10.1016/j.jcvp.2022.100130 · Cited by 3 · see citing works

Immune response to 2-dose BNT162b2 vaccination and risk of SARS-CoV-2 breakthrough infection: The Shieldvacc-2 studyPreprint

Seekircher, L., Bánki, Z., Kimpel, J., Rössler, A., Schäfer, H., Falkensammer, B., Bante, D., Forer, L., Schönherr, S., Harthaller, T., et al. (2022) · medRxiv · doi:10.1101/2022.04.19.22273872 · Cited by 3 · see citing works

An innovative nasal nanovaccine against SARS-CoV-2 induces systemic and upper airway immunity controlling viral replication

Pagni, R. L., Cunha-Neto, E., Santos, Y. D. S., Postól, E., de Alencar, R. E., Moretti, A. I. S., dos Santos, J. J., Silva, T. L., Daher, I. P., Knirsch, M. C., et al. (2026) · npj Vaccines · doi:10.1038/s41541-026-01407-x · Cited by 2 · see citing works

Interchangeability of the Assays Used to Assess the Activity of Anti-SARS-CoV-2 Monoclonal Antibodies

Hickerson, B. T., Khalenkov, A. M., Xie, T., Frucht, D. M., Scott, D. E., & Ilyushina, N. A. (2023) · Viruses · doi:10.3390/v15081698 · Cited by 2 · see citing works

Validation of a focus reduction neutralization test (FRNT) to rapidly titrate human SARS-CoV-2 neutralizing antibodies by using the CTL Immunospot S6 universal analyzer

Puglia, I., Caporale, M., Casaccia, C., Valleriani, F., Salini, R., Berjaoui, S., Marfoglia, C., Ricci, L., & Lorusso, A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34925 · Cited by 2 · see citing works

The Anti-SARS-CoV-2 S-Protein IgG, Which Is Detected Using the Chemiluminescence Microparticle Immunoassay (CMIA) in Individuals Having Either a History of COVID-19 Vaccination and/or SARS-CoV-2 Infection, Showed a High-Titer Neutralizing Effect

Çin, D., Soğuksu, P., Ören, M. M., Özgülnar, N., Ağaçfidan, A., & Meşe, S. (2024) · Viruses · doi:10.3390/v16091409 · Cited by 2 · see citing works

Comparative assessment of four virus neutralization assays for detection of SARS-CoV-2 neutralizing antibodies

Maghsood, F., Dashti, N., Bahadori, T., Golsaz‐Shirazi, F., Moog, C., Amiri, M. M., & Shokri, F. (2025) · Analytical Biochemistry · doi:10.1016/j.ab.2025.115860 · Cited by 1 · see citing works

Evaluation of cell-based and surrogate SARS-CoV-2 neutralization assays

Lu, J., Kaiser, H., Corey, L., Lempp, F. A., Strong, R. K., Ford, E. S., Stuart, A. B., Hou, Y. J., Fiore-Gartland, A. J., Miner, M. D., et al. (2022) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/870f-kk74

Reconciliation of titer differences between SARS-CoV-2 neutralizing antibody assays

Stadler, E., Mordant, F. L., Gartner, M. J., Docken, S. S., Davenport, M. P., Khoury, D. S., & Subbarao, K. (2026) · Journal of Virology · doi:10.1128/jvi.00823-26

Evaluation of SARS-CoV-2 neutralization assays for antibody monitoring in natural infection and vaccine trialsPreprint

Sholukh, A. M., Fiore-Gartland, A., Ford, E. S., Hou, Y., Tse, L.-P. V., Lempp, F., Kaiser, H., Germain, R. S., Bossard, E. L., Jia, J.-K., et al. (2020) · medRxiv · doi:10.1101/2020.12.07.20245431 · Cited by 25 · see citing works

Detection of SARS-CoV-2 Neutralizing Antibodies and Vaccine Development

(2026) · MDPI eBooks · doi:10.3390/books978-3-7258-6535-2