The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Monoclonal antibodies isolated without screening by analyzing the variable-gene repertoire of plasma cells
Abstract
Isolation of antigen-specific monoclonal antibodies (mAbs) and antibody fragments relies on high-throughput screening of immortalized B cells or recombinant antibody libraries. We bypassed the screening step by using high-throughput DNA sequencing and bioinformatic analysis to mine antibody variable region (V)-gene repertoires from bone marrow plasma cells (BMPC) of immunized mice. BMPCs, which cannot be immortalized, produce the vast majority of circulating antibodies. We found that the V-gene repertoire of BMPCs becomes highly polarized after immunization, with the most abundant sequences represented at frequencies between approximately 1% and >10% of the total repertoire. We paired the most abundant variable heavy (V(H)) and variable light (V(L)) genes based on their relative frequencies, reconstructed them using automated gene synthesis, and expressed recombinant antibodies in bacteria or mammalian cells. Antibodies generated in this manner from six mice, each immunized with one of three antigens were overwhelmingly antigen specific (21/27 or 78%). Those generated from a mouse with high serum titers had nanomolar binding affinities.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“A similar approach based on identifying highly abundant sequences was used to select antigen-specific molecules in immunized mice [216].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [216]
In the citing paper
“Sequencing a sample of the repertoire and identifying newly abundant sequence-similar BCRs is being used as a simple bioinformatic method to identify new antibodies specific for the antigen of interest.”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [216]
Citations
Cites
Continuous cultures of fused cells secreting antibody of predefined specificity
Köhler, G., & Milstein, C. (1975) · Nature · doi:10.1038/256495a0 · Cited by 17,200
Next-generation DNA sequencing
Shendure, J., & Ji, H. (2008) · Nature Biotechnology · doi:10.1038/nbt1486 · Cited by 4,509
Brochet, X., Lefranc, M., & Giudicelli, V. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn316 · Cited by 1,220
Making antibody fragments using phage display libraries
Clackson, T., Hoogenboom, H. R., Griffiths, A. D., & Winter, G. P. (1991) · Nature · doi:10.1038/352624a0 · Cited by 1,211
Competence and competition: the challenge of becoming a long-lived plasma cell
Radbruch, A., Muehlinghaus, G., Luger, E., Inamine, A., Smith, K. G. C., Dörner, T., & Hiepe, F. (2006) · Nature reviews. Immunology · doi:10.1038/nri1886 · Cited by 1,033
Rapid cloning of high-affinity human monoclonal antibodies against influenza virus
Wrammert, J., Smith, K., Miller, J., Langley, W. A., Kokko, K. E., Larsen, C. P., Zheng, N., Mays, I., Garman, L., Helms, C., et al. (2008) · Nature · doi:10.1038/nature06890 · Cited by 1,026
Selecting and screening recombinant antibody libraries
Hoogenboom, H. R. (2005) · Nature Biotechnology · doi:10.1038/nbt1126 · Cited by 975
Regulation of plasma-cell development
Shelef, M. A., & Calame, K. L. (2005) · Nature reviews. Immunology · doi:10.1038/nri1572 · Cited by 917
Lifetime of plasma cells in the bone marrow
Manz, R. A., Thiel, A., & Radbruch, A. (1997) · Nature · doi:10.1038/40540 · Cited by 866
Traggiai, E., Becker, S., Subbarao, K., Kolesnikova, L., Uematsu, Y., Gismondo, M. R., Murphy, B. R., Rappuoli, R., & Lanzavecchia, A. (2004) · Nature Medicine · doi:10.1038/nm1080 · Cited by 697
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 294
Forecasting of emerging therapeutic monoclonal antibodies patents based on a decision model
Pereira, C. G., Lavoie, J. R., Garces, E., Basso, F. G., Dabić, M., Porto, G. S., & Daim, T. U. (2018) · Technological Forecasting and Social Change · doi:10.1016/j.techfore.2018.11.002 · Cited by 40
Eliyahu, S., Sharabi, O., Elmedvi, S., Timor, R., Davidovich, A., Vigneault, F., Clouser, C., Hope, R., Assy, N., Braun, M., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.03004 · Cited by 37
Lee, E. S., Thomas, P. G., Mold, J. E., & Yates, A. J. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005313 · Cited by 39
Adler, A. S., Mizrahi, R. A., Spindler, M. J., Adams, M. S., Asensio, M. A., Edgar, R. C., Leong, J., Leong, R., & Johnson, D. S. (2017) · mAbs · doi:10.1080/19420862.2017.1371386 · Cited by 40
Applications of Machine and Deep Learning in Adaptive Immunity
Pertseva, M., Gao, B., Neumeier, D., Yermanos, A., & Reddy, S. T. (2021) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-101420-125021 · Cited by 38
Self-citationSvilenov, H. L., Arosio, P., Menzen, T., Tessier, P. M., & Sormanni, P. (2023) · mAbs · doi:10.1080/19420862.2022.2164459 · Cited by 40
From deep sequencing to actual clones
D’Angelo, S., Kumar, S., Naranjo, L. A., Ferrara, F., Kiss, C., & Bradbury, A. M. (2014) · Protein Engineering Design and Selection · doi:10.1093/protein/gzu032 · Cited by 38
Benchmarking Tree and Ancestral Sequence Inference for B Cell Receptor Sequences
Davidsen, K., & Matsen, F. A., IV (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02451 · Cited by 35
An array of 60,000 antibodies for proteome-scale antibody generation and target discovery
Wang, Z., Li, Y., Hou, B., Pronobis, M. I., Wang, M., Wang, Y., Cheng, G., Zhang, Z., Wang, Y., Tang, Y., et al. (2020) · Science Advances · doi:10.1126/sciadv.aax2271 · Cited by 39
Richardson, E., Galson, J. D., Kellam, P., Kelly, D. F., Smith, S. E., Palser, A. L., Watson, S. J., & Deane, C. M. (2021) · mAbs · doi:10.1080/19420862.2020.1869406 · Cited by 41
Intrinsic bias and public rearrangements in the human immunoglobulin Vλ light chain repertoire
Hoi, K. H., & Ippolito, G. C. (2013) · Genes and Immunity · doi:10.1038/gene.2013.10 · Cited by 37
Self-citationStructure-based cross-docking analysis of antibody–antigen interactions
Kilambi, K. P., & Gray, J. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-08414-y · Cited by 37
Jorgolli, M., Nevill, T., Winters, A. G., Chen, I., Chong, S., Lin, F., Mock, M. L., Chen, C., Le, K., Tan, C., et al. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.27024 · Cited by 35
Guan, Q., Wang, X., Wang, X., Teng, D., Mao, R., Zhang, Y., & Wang, J. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6339-6 · Cited by 37
Miyazaki, N., Kiyose, N., Akazawa, Y., Takashima, M., Hagihara, Y., Inoue, N., Matsuda, T., Ogawa, R., Inoue, S., & Ito, Y. (2015) · The Journal of Biochemistry · doi:10.1093/jb/mvv038 · Cited by 36
Fitzgerald, V., Manning, B., O’Donnell, B., O’Reilly, B., O’Sullivan, D., O’Kennedy, R. J., & Leonard, P. (2014) · Analytical Chemistry · doi:10.1021/ac503547j · Cited by 36
De novo design of antibody complementarity determining regions binding a FLAG tetra-peptide
Entzminger, K. C., Hyun, J., Pantazes, R. J., Patterson-Orazem, A. C., Qerqez, A. N., Frye, Z., Hughes, R. A., Ellington, A. D., Lieberman, R. L., Maranas, C. D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10737-9 · Cited by 36
Self-citationThe Application of Next Generation Sequencing to the Understanding of Antibody Repertoires
Mathonet, P., & Ullman, C. G. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00265 · Cited by 36
Asensio, M. A., Lim, Y. W., Wayham, N. P., Stadtmiller, K., Edgar, R. C., Leong, J., Leong, R., Mizrahi, R. A., Adams, M. S., Simons, J. F., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1583995 · Cited by 34
Lü, J., Panavas, T., Thys, K., Aerssens, J., Naso, M. F., Fisher, J., Rycyzyn, M. A., & Sweet, R. W. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.09.008 · Cited by 33
Friedensohn, S., Lindner, J. M., Cornacchione, V., Iazeolla, M., Miho, E., Zingg, A., Meng, S. M., Traggiai, E., & Reddy, S. T. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01401 · Cited by 33
Self-citationParola, C., Neumeier, D., Friedensohn, S., Csepregi, L., Tacchio, M. D., Mason, D. M., & Reddy, S. T. (2019) · mAbs · doi:10.1080/19420862.2019.1662691 · Cited by 33
Self-citationFrontier of therapeutic antibody discovery: The challenges and how to face them
Lu, Z. (2012) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v3.i12.187 · Cited by 30
Wang, B., Lee, C., Johnson, E. L., Kluwe, C., Cunningham, J. C., Tanno, H., Crooks, R. M., Georgiou, G., & Ellington, A. D. (2016) · mAbs · doi:10.1080/19420862.2016.1190059 · Cited by 31
Self-citationDrabek, D., Janssens, R., de Boer, E., Rademaker, R., Kloess, J., Skehel, J. J., & Grosveld, F. G. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00619 · Cited by 31
Fast, accurate antibody structure prediction from deep learning on massive set of natural antibodiesPreprint
Ruffolo, J. A., Chu, L., Mahajan, S. P., & Gray, J. J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.20.488972 · Cited by 33
Hémadou, A., Giudicelli, V., Smith, M. L., Lefranc, M., Duroux, P., Κοσσίδα, Σ., Heiner, C. R., Hepler, N. L., Kuijpers, J., Groppi, A., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01796 · Cited by 29
Hillman, Y., Lustiger, D., & Wine, Y. (2019) · Nanotechnology · doi:10.1088/1361-6528/ab12f4 · Cited by 29
The role of structural proteomics in vaccine development: recent advances and future prospects
Donnarumma, D., Faleri, A., Costantino, P., Rappuoli, R., & Norais, N. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2016.1121113 · Cited by 30
Moeller, T. D., Shah, S. B., Lai, K., Lopez‐Barbosa, N., Desai, P., Wang, W., Zhong, Z., Redmond, D., Singh, A. K., & DeLisa, M. P. (2023) · ACS Central Science · doi:10.1021/acscentsci.2c01473 · Cited by 28
Identification of highly selective MMP‐14 inhibitory Fabs by deep sequencing
Lopez, T., Nam, D. H., Kaihara, E., Mustafa, Z., & Ge, X. (2017) · Biotechnology and Bioengineering · doi:10.1002/bit.26248 · Cited by 29
Self-citationSpoendlin, F. C., Abanades, B., Raybould, M. I. J., Wong, W. K., Georges, G., & Deane, C. M. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1237621 · Cited by 26
Systems analysis of adaptive immunity by utilization of high-throughput technologies
Reddy, S. T., & Georgiou, G. (2011) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2011.04.015 · Cited by 26
Self-citationWang, X., Teng, D., Guan, Q., Mao, R., Hao, Y., Wang, X., Yao, J., & Wang, J. (2017) · AMB Express · doi:10.1186/s13568-017-0452-8 · Cited by 25
Venet, S., Ravn, U., Buatois, V., Gueneau, F., Calloud, S., Kosco‐Vilbois, M. H., & Fischer, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043471 · Cited by 24
Phenotypic determinism and stochasticity in antibody repertoires of clonally expanded plasma cells
Neumeier, D., Yermanos, A., Agrafiotis, A., Csepregi, L., Chowdhury, T., Ehling, R. A., Kuhn, R., Cotet, T., Roberto, R. B. D., Tacchio, M. D., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113766119 · Cited by 24
Self-citationImpact of new sequencing technologies on studies of the human B cell repertoire
Finn, J. A., & Crowe, J. E. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.09.010 · Cited by 23
Yang, X., Wang, M., Wu, J., Shi, D., Zhang, Y., Zeng, H., Zhu, Y., Lan, C., Deng, Y., Guo, S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109110 · Cited by 23
Li, Z., Liu, G., Tong, Y., Zhang, M., Xu, Y., Li, Q., Wang, Z., Chen, X., & He, J. (2015) · Scientific Reports · doi:10.1038/srep10092 · Cited by 22
Zhang, Y., Li, Q., Luo, L., Duan, C., Shen, J., & Wang, Z. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108143 · Cited by 23
Immunological principles regulating immunomodulation with biomaterials
Khan, T. A., & Reddy, S. T. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.12.011 · Cited by 22
Self-citationDevelopment of Antibody-Based Therapeutics
Tabrizi, M. A., Klakamp, S. L., & Bornstein, G. G. (2012) · Springer eBooks · doi:10.1007/978-1-4419-5955-3 · Cited by 23
High-throughput retrieval of physical DNA for NGS-identifiable clones in phage display library
Noh, J., Kim, O., Jung, Y., Han, H., Kim, J., Kim, S., Lee, S., Park, J., Jung, R. H., Kim, S. I., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1571878 · Cited by 22
ASAP - A Webserver for Immunoglobulin-Sequencing Analysis Pipeline
Avram, O., Vaisman‐Mentesh, A., Yehezkel, D., Ashkenazy, H., Pupko, T., & Wine, Y. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01686 · Cited by 21
Ehling, R. A., Weber, C. R., Mason, D. M., Friedensohn, S., Wagner, B., Bieberich, F., Kapetanovic, E., Vazquez-Lombardi, R., Roberto, R. B. D., Hong, K., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110242 · Cited by 27
Self-citationPélissier, A., Luo, S., Stratigopoulou, M., Guikema, J. E. J., & Martínez, M. R. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1123968 · Cited by 21
The dengue-specific immune response and antibody identification with machine learning
Natali, E. N., Horst, A., Meier, P., Greiff, V., Nuvolone, M., Babrak, L. M., Fink, K., & Miho, E. (2024) · npj Vaccines · doi:10.1038/s41541-023-00788-7 · Cited by 21
Characterization of human IgG repertoires in an acute HIV-1 infection
Chen, W., Prabakaran, P., Zhu, Z., Feng, Y., Streaker, E. D., & Dimitrov, D. S. (2012) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2012.09.022 · Cited by 21
Discovery of Novel Candidate Therapeutics and Diagnostics Based on Engineered Human Antibody Domains
Chen, W., Gong, R., Ying, T., Prabakaran, P., Zhu, Z., Feng, Y., & Dimitrov, D. S. (2014) · Current Drug Discovery Technologies · doi:10.2174/15701638113109990032 · Cited by 21
Mankowska, S. A., Gatti‐Lafranconi, P., Chodorge, M., Sridharan, S., Minter, R., & Hollfelder, F. (2016) · Scientific Reports · doi:10.1038/srep36391 · Cited by 20
Identification of high affinity HER2 binding antibodies using CHO Fab surface display
Nguyen, A. W., Le, K. C., & Maynard, J. A. (2018) · Protein Engineering Design and Selection · doi:10.1093/protein/gzy004 · Cited by 21
Chen, H.-S., Hou, S.-C., Jian, J.-W., Goh, K.-S., Shen, S.-T., Lee, Y., You, J.-J., Peng, H., Kuo, W., Chen, S., et al. (2015) · Scientific Reports · doi:10.1038/srep12411 · Cited by 21
Kacskovıcs, I., Cervenak, J., Erdei, A., Goldsby, R. A., & Butler, J. E. (2011) · mAbs · doi:10.4161/mabs.3.5.17023 · Cited by 20
Systems Biology Approach for New Target and Biomarker Identification
Wang, I., Stone, D. J., Nickle, D. C., Loboda, A. P., Puig, Ó., & Roberts, C. (2012) · Current topics in microbiology and immunology · doi:10.1007/82_2012_252 · Cited by 19
Fine epitope signature of antibody neutralization breadth at the HIV-1 envelope CD4-binding site
Cheng, H. D., Grimm, S. K., Gilman, M. S. A., Gwom, L. C., Sok, D., Sundling, C., Donofrio, G. C., Hedestam, G. B. K., Bonsignori, M., Haynes, B. F., et al. (2018) · JCI Insight · doi:10.1172/jci.insight.97018 · Cited by 19
Castro, R., Navelsaker, S., Krasnov, A., Pasquier, L. D., & Boudinot, P. (2017) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2017.02.018 · Cited by 17
Kiguchi, Y., Oyama, H., Morita, I., Morikawa, M., Nakano, A., Fujihara, W., Inoue, Y., Sasaki, M., Saijo, Y., Kanemoto, Y., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71037-3 · Cited by 18
Moutai, T., Yamana, H., Nojima, T., & Kitamura, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092732 · Cited by 18
Promdonkoy, P., Sornlek, W., Preechakul, T., Tanapongpipat, S., & Runguphan, W. (2022) · Fermentation · doi:10.3390/fermentation8090429 · Cited by 18
Agrafiotis, A., Neumeier, D., Hong, K., Chowdhury, T., Ehling, R. A., Kuhn, R., Sandu, I., Kreiner, V., Cotet, T., Shlesinger, D., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106055 · Cited by 15
Self-citationDevelopment of proteome‐wide binding reagents for research and diagnostics
Taussig, M., Schmidt, R., Cook, E. A., & Stoevesandt, O. (2013) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201300060 · Cited by 17
Henry, K. A. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7447-4_24 · Cited by 17
Devulapally, P. R., Bürger, J., Mielke, T., Konthur, Z., Lehrach, H., Yaspo, M., Glökler, J., & Warnatz, H.-J. (2018) · Genome Medicine · doi:10.1186/s13073-018-0542-5 · Cited by 17
Tschumper, R. C., Asmann, Y. W., Hossain, A., Huddleston, P. M., Wu, X., Dispenzieri, A. A., Eckloff, B. W., & Jelinek, D. F. (2012) · Oncotarget · doi:10.18632/oncotarget.469 · Cited by 17
High‐throughput sequencing of immune repertoires in multiple sclerosis
Lossius, A., Johansen, J. N., Vartdal, F., & Holmøy, T. (2016) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.295 · Cited by 16
Chen, Y., Kim, S. H., Shang, Y., Guillory, J., Stinson, J., Zhang, Q., Hötzel, I., & Hoi, K. H. (2018) · Journal of Immunological Methods · doi:10.1016/j.jim.2018.01.004 · Cited by 16
Self-citationAntibody–antigen complex modelling in the era of immunoglobulin repertoire sequencing
Raybould, M. I. J., Wong, W. K., & Deane, C. M. (2019) · Molecular Systems Design & Engineering · doi:10.1039/c9me00034h · Cited by 14
Cervenak, J., Kurrle, R., & Kacskovıcs, I. (2015) · Immunological Reviews · doi:10.1111/imr.12364 · Cited by 16
Wang, X., Guan, Q., Wang, X., Teng, D., Mao, R., Yao, J., & Wang, J. (2015) · Process Biochemistry · doi:10.1016/j.procbio.2015.05.001 · Cited by 16
Single B Cell Cloning and Production of Rabbit Monoclonal Antibodies
Rashidian, J., & Lloyd, J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9853-1_23 · Cited by 16
Dudzic, P., Chomicz, D., Bielska, W., Jaszczyszyn, I., Zieliński, M., Janusz, B., Wróbel, S., Pannérer, M.-M. L., Phillips, A., Prabakaran, P., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08388-y · Cited by 15
Advances in antibody discovery from human BCR repertoires
Xu, Z., Ismanto, H. S., Zhou, H., Saputri, D. S., Sugihara, F., & Standley, D. M. (2022) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2022.1044975 · Cited by 18
A Microfluidic Chip for Screening and Sequencing of Monoclonal Antibody at a Single-Cell Level
Zhang, W., Li, Q., Jia, F., Hu, Z., & Wei, Z. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c00918 · Cited by 15
Trends in computational biology—2010
Mak, H. C. (2011) · Nature Biotechnology · doi:10.1038/nbt.1747 · Cited by 14
Bai, C., Zhou, L., Tang, J. X., He, J., Han, J., Niu, H., & Zhu, B. (2020) · Vaccines · doi:10.3390/vaccines8040715 · Cited by 14
Pan, X., Acevedo, S. N. L., Cuziol, C., Tavernier, E. D., Fahad, A. S., Longjam, P. S., Rao, S. P., Aguilera, D., Rezé, M., Bricault, C. A., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1137069 · Cited by 14
Chen, Z., Ren, X., Yang, J., Dong, J., Xue, Y., Sun, L., Zhu, Y., & Jin, Q. (2016) · mAbs · doi:10.1080/19420862.2016.1267086 · Cited by 13
Landscape of infection enhancing antibodies in COVID-19 and healthy donors
Ismanto, H. S., Xu, Z., Saputri, D. S., Wilamowski, J., Li, S., Nugraha, D. K., Horiguchi, Y., Okada, M., Arase, H., & Standley, D. M. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.11.001 · Cited by 13
Houimel, M. (2014) · Human Immunology · doi:10.1016/j.humimm.2014.05.005 · Cited by 13
ScaffoldSeq: Software for characterization of directed evolution populations
Woldring, D., Holec, P. V., & Hackel, B. J. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25040 · Cited by 12
Monitoring Phage Biopanning by Next-Generation Sequencing
Vaisman‐Mentesh, A., & Wine, Y. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7447-4_26 · Cited by 12
Rafique, A., Satake, K., Kishimoto, S., Khan, K. H., Kato, D., & Ito, Y. (2019) · Monoclonal Antibodies in Immunodiagnosis and Immunotherapy · doi:10.1089/mab.2019.0027 · Cited by 12
Kelil, A., Gallo, E., Banerjee, S., Adams, J., & Sidhu, S. S. (2021) · Communications Biology · doi:10.1038/s42003-021-02066-5 · Cited by 12
The Cloning and Expression of Human Monoclonal Antibodies: Implications for Allergen Immunotherapy
James, L. K. (2016) · Current Allergy and Asthma Reports · doi:10.1007/s11882-015-0588-z · Cited by 12
Foster, M. H. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00275.2016 · Cited by 12
Liao, H., Li, S., Yu, Y., Yue, Y., Su, K., Zheng, Q., Jiang, N., & Zhang, Z. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.03163 · Cited by 12
Isolation of Monoclonal Antibodies with Predetermined Conformational Epitope Specificity
Sholukh, A. M., Mukhtar, M. M., Humbert, M., Essono, S., Watkins, J. D., Vyas, H. K., Shanmuganathan, V., Hemashettar, G., Kahn, M., Hu, S., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038943 · Cited by 12
Profiling the IgOme: Meeting the challenge
Weiss-Ottolenghi, Y., & Gershoni, J. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.11.005 · Cited by 11
Morgan, D. M., Zhang, Y. J., Kim, J. H., Murillo, M., Singh, S., Loschko, J., Surendran, N., Sekulović, O., Feng, E., Shi, S., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06823-0 · Cited by 10
Gallo, E. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01018-5 · Cited by 13
Pabst, O., Hazanov, H., & Mehr, R. (2014) · Mucosal Immunology · doi:10.1038/mi.2014.103 · Cited by 11
In Vivo VL-Targeted Microbial Superantigen Induced Global Shifts in the B Cell Repertoire
Grönwall, C., Pond, S. L. K., Young, J. A., & Silverman, G. J. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200245 · Cited by 11
Yan, Q., Zhang, Y., Hou, R., Pan, W., Liang, H., Gao, X., Deng, W., Huang, X., Qu, L., Tang, C., et al. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2290841 · Cited by 9
Hussack, G., Baral, T. N., Baardsnes, J., van Faassen, H., Raphael, S., Henry, K. A., Zhang, J., & MacKenzie, C. R. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01406 · Cited by 10
Animal immunization merges with innovative technologies: A new paradigm shift in antibody discovery
Prabakaran, P., Rao, S. P., & Wendt, M. (2021) · mAbs · doi:10.1080/19420862.2021.1924347 · Cited by 11
Strategies to Obtain Diverse and Specific Human Monoclonal Antibodies From Transgenic Animals
Brüggemann, M., Osborn, M. J., Ma, B., & Buelow, R. (2017) · Transplantation · doi:10.1097/tp.0000000000001702 · Cited by 9
Wang, Z., Li, D., Chen, Y., Sun, Y., Jin, C., Hu, C., Feng, Y., Su, J., Ren, L., Hao, Y., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1160283 · Cited by 8
Membrane-anchored stalk domain of influenza HA enhanced immune responses in mice
Gao, D., Chen, Y., Han, D., Qi, Q., Sun, X., Zhang, H., Feng, H., & Wang, M. (2017) · Microbial Pathogenesis · doi:10.1016/j.micpath.2017.11.025 · Cited by 9
Medina‐Cucurella, A. V., Mizrahi, R. A., Asensio, M. A., Edgar, R. C., Leong, J., Leong, R., Lim, Y. W., Nelson, A. L., Niedecken, A. R., Simons, J. F., et al. (2019) · Antibodies · doi:10.3390/antib8010017 · Cited by 9
Antigen-Specific Human Monoclonal Antibodies from Transgenic Mice
Magadán, S., & González‐Fernández, Á. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-586-6_13 · Cited by 9
Metadata
- Authors
- Reddy, S. T., Ge, X., Miklos, A. E., Hughes, R. A., Kang, S. H., Hoi, K. H., Chrysostomou, C., Hunicke-Smith, S. P., Iverson, B. L., Tucker, P. W., Ellington, A. D., & Georgiou, G.
- Affiliations
- The University of Texas at Austin (US)
- Applied Research Laboratories, The University of Texas at Austin (US)
- Corresponding author
- Georgiou, George
- ORCID
- Venue
- Nature Biotechnology
- Published
- 2010-08-29
- Volume
- 28
- Issue
- 9
- Pages
- 965-969
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W1968091806
- Cited by
- 292
- References
- 32
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 10 · 2023: 16 · 2022: 20 · 2021: 18 · 2020: 14 · 2019: 17 · 2018: 24 · 2017: 31 · 2016: 23 · 2015: 20 · 2014: 24 · 2013: 27 · 2012: 23
- FWCI
- 16.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- monoclonal antibodies, antibody repertoire, plasma cells, antigen-specific antibodies, antibody fragments, immunization, antibody affinity, recombinant antibody production, next-generation sequencing
- MeSH terms
- Animals, Antibodies, Monoclonal, Antigens, Base Sequence, Humans, Immunization, Immunoglobulin Variable Region, Immunoglobulin Heavy Chains, Molecular Sequence Data, Plasma Cells, Complementarity Determining Regions, Mice, High-Throughput Screening Assays, High-Throughput Nucleotide Sequencing
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review