A strategy for risk mitigation of antibodies with fast clearance

Cross validatory choice and assessment of statistical predictions

Stone, M. (1974) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1974.tb00994.x · Cited by 10,881 · see citing works

The Predictive Sample Reuse Method with Applications

Geisser, S. (1975) · Journal of the American Statistical Association · doi:10.1080/01621459.1975.10479865 · Cited by 2,748 · see citing works

Monoclonal Antibody Pharmacokinetics and Pharmacodynamics

Wang, W., Wang, E., & Balthasar, J. (2008) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2008.170 · Cited by 978 · see citing works

Clinical Pharmacokinetics of Therapeutic Monoclonal Antibodies

Keizer, R. J., Huitema, A. D. R., Schellens, J. H. M., & Beijnen, J. H. (2010) · Clinical Pharmacokinetics · doi:10.2165/11531280-000000000-00000 · Cited by 725 · see citing works

Enhanced antibody half-life improves in vivo activity

Zalevsky, J., Chamberlain, A. K., Horton, H. M., Karki, S., Leung, I., Sproule, T. J., Lazar, G. A., Roopenian, D. C., & Desjarlais, J. R. (2010) · Nature Biotechnology · doi:10.1038/nbt.1601 · Cited by 657 · see citing works

Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn)

Dall’Acqua, W. F., Kiener, P. A., & Wu, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604292200 · Cited by 648 · see citing works

Elimination mechanisms of therapeutic monoclonal antibodies

Tabrizi, M. A., Tseng, C.-M. L., & Roskos, L. K. (2006) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03638-x · Cited by 479 · see citing works

Development of Motavizumab, an Ultra-potent Antibody for the Prevention of Respiratory Syncytial Virus Infection in the Upper and Lower Respiratory Tract

Wu, H., Pfarr, D. S., Johnson, S., Brewah, Y. A., Woods, R. M., Patel, N., White, W. I., Young, J. F., & Kiener, P. A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.024 · Cited by 374 · see citing works

Marketed therapeutic antibodies compendium

Reichert, J. M. (2012) · mAbs · doi:10.4161/mabs.19931 · Cited by 368 · see citing works

Projecting human pharmacokinetics of therapeutic antibodies from nonclinical data: What have we learned?

Deng, R., Iyer, S., Theil, F.-P., Mortensen, D. L., Fielder, P. J., & Prabhu, S. (2011) · mAbs · doi:10.4161/mabs.3.1.13799 · Cited by 285 · see citing works

An Engineered Human IgG1 Antibody with Longer Serum Half-Life

Hinton, P. R., Xiong, J. M., Johlfs, M. G., Tang, M. T., Keller, S., & Tsurushita, N. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.1.346 · Cited by 282 · see citing works

The Influence of Charge Distribution on Self-Association and Viscosity Behavior of Monoclonal Antibody Solutions

Yadav, S., Laue, T. M., Kalonia, D. S., Singh, S. N., & Shire, S. J. (2012) · Molecular Pharmaceutics · doi:10.1021/mp200566k · Cited by 282 · see citing works

Reduced elimination of IgG antibodies by engineering the variable region

Igawa, T., Tsunoda, H., Tachibana, T., Maeda, A., Mimoto, F., Moriyama, C., Nanami, M., Sekimori, Y., Nabuchi, Y., Aso, Y., et al. (2010) · Protein Engineering Design and Selection · doi:10.1093/protein/gzq009 · Cited by 265 · cited 2× · see citing works

Target-mediated drug disposition and dynamics

Mager, D. E. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.12.041 · Cited by 245 · see citing works

A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody

Angal, S., King, D. J., Bodmer, M., Turner, A. V., Lawson, A. D. G., Roberts, G., Pedley, B. R., & Adair, J. R. (1993) · Molecular Immunology · doi:10.1016/0161-5890(93)90432-b · Cited by 245 · see citing works

Engineering Human IgG1 Affinity to Human Neonatal Fc Receptor: Impact of Affinity Improvement on Pharmacokinetics in Primates

Yeung, Y. A., Leabman, M. K., Marvin, J. S., Qiu, J., Adams, C. W., Lien, S., Starovasnik, M. A., & Lowman, H. B. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804182 · Cited by 237 · see citing works

Neonatal Fc receptor and IgG-based therapeutics

Kuo, T. T., & Aveson, V. G. (2011) · mAbs · doi:10.4161/mabs.3.5.16983 · Cited by 236 · see citing works

High-affinity Human Antibodies from Phage-displayed Synthetic Fab Libraries with a Single Framework Scaffold

Lee, C. V., Liang, W., Dennis, M. S., Eigenbrot, C. W., Sidhu, S. S., & Fuh, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.051 · Cited by 228 · see citing works

Pharmacokinetics and Pharmacodynamics of Monoclonal Antibodies

Mould, D. R., & Green, B. (2010) · BioDrugs · doi:10.2165/11530560-000000000-00000 · Cited by 207 · see citing works

Proteomics of the Autographa californica Nucleopolyhedrovirus Budded Virions

Wang, R., Dèng, F., Hou, D., Zhao, Y. B., Guo, L., Wáng, H., & Hú, Z. (2010) · Journal of Virology · doi:10.1128/jvi.00040-10 · Cited by 182 · see citing works

Monoclonal Antibodies with Identical Fc Sequences Can Bind to FcRn Differentially with Pharmacokinetic Consequences

Wang, W., Lü, P., Fang, Y., Hamuro, L., Pittman, T. J., Carr, B. I., Hochman, J. H., & Prueksaritanont, T. (2011) · Drug Metabolism and Disposition · doi:10.1124/dmd.111.039453 · Cited by 166 · see citing works

Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection

Marheineke, K., Grünewald, S., Christie, W. W., & Reiländer, H. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01523-3 · Cited by 159 · see citing works

Pharmacokinetics of Humanized Monoclonal Anti-Tumor Necrosis Factor-α Antibody and Its Neonatal Fc Receptor Variants in Mice and Cynomolgus Monkeys

Deng, R., Loyet, K. M., Lien, S., Iyer, S., DeForge, L. E., Theil, F., Lowman, H. B., Fielder, P. J., & Prabhu, S. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.031310 · Cited by 113 · see citing works

Screening antibody–antigen interactions in parallel using Biacore A100

Säfsten, P., Klakamp, S. L., Drake, A. W., Karlsson, R., & Myszka, D. G. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.01.041 · Cited by 112 · see citing works

Highly specific off-target binding identified and eliminated during the humanization of an antibody against FGF receptor 4

Bumbaca, D., Wong, A., Drake, E. A., Reyes, A. E., Lin, B. C., Stéphan, J.-P., Desnoyers, L., Shen, B., & Dennis, M. S. (2011) · mAbs · doi:10.4161/mabs.3.4.15786 · Cited by 105 · see citing works

Determination of the net charge (valence) of a protein: a fundamental but elusive parameter

Winzor, D. J. (2003) · Analytical Biochemistry · doi:10.1016/j.ab.2003.09.035 · Cited by 79 · see citing works

A Therapeutic Anti–VEGF Antibody with Increased Potency Independent of Pharmacokinetic Half-life

Yeung, Y. A., Wu, X., Reyes, A. E., Vernes, J.-M., Lien, S., Lowe, J. A., III, Maia, M., Forrest, W. F., Meng, Y. G., Damico, L. A., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4580 · Cited by 78 · see citing works

Complex Pharmacokinetics of a Humanized Antibody Against Human Amyloid Beta Peptide, Anti-Abeta Ab2, in Nonclinical Species

Vugmeyster, Y., Szklut, P., Wensel, D. L., Ross, J. E., Xu, X., Awwad, M., Gill, D. S., Tchistiakov, L., & Warner, G. L. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0405-x · Cited by 50 · see citing works

In vitro potency, pharmacokinetic profiles and pharmacological activity of optimized anti-IL-21R antibodies in a mouse model of lupus

Vugmeyster, Y., Guay, H., Szklut, P., Qian, M., Jin, M., Widom, A., Spaulding, V., Bennett, F., Lowe, L. D., Andreyeva, T. A., et al. (2010) · mAbs · doi:10.4161/mabs.2.3.11850 · Cited by 48 · see citing works

Efficient production of antibodies against a mammalian integral membrane protein by phage display

Hötzel, I., Chiang, V., Diao, J., Pantua, H., Maun, H. R., & Kapadia, S. B. (2011) · Protein Engineering Design and Selection · doi:10.1093/protein/gzr039 · Cited by 38 · see citing works

Pharmacokinetics of Monoclonal Antibodies

Ryman, J. T., & Meibohm, B. (2017) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12224 · Cited by 815 · see citing works

Next generation antibody drugs: pursuit of the 'high-hanging fruit'

Carter, P. J., & Lazar, G. A. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.227 · Cited by 760 · see citing works

Biophysical properties of the clinical-stage antibody landscape

Jain, T., Sun, T., Durand, S., Hall, A., Houston, N. R., Nett, J. H., Sharkey, B., Bobrowicz, B., Caffry, I., Yu, Y., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616408114 · Cited by 629 · see citing works

Pharmacokinetics of monoclonal antibodies and Fc-fusion proteins

Liming, L. (2017) · Protein & Cell · doi:10.1007/s13238-017-0408-4 · Cited by 394 · see citing works

Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development

Ovacik, M., & Lin, K. (2018) · Clinical and Translational Science · doi:10.1111/cts.12567 · Cited by 299 · see citing works

Phage Display Derived Monoclonal Antibodies: From Bench to Bedside

Alfaleh, M. A., Alsaab, H. O., Mahmoud, A. B., Alkayyal, A. A., Jones, M. L., Mahler, S. M., & Hashem, A. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01986 · Cited by 280 · see citing works

Structure, heterogeneity and developability assessment of therapeutic antibodies

Xu, Y., Wang, D., Mason, B. D., Rossomando, T., Li, N., Liu, D., Cheung, J. K., Xu, W., Raghava, S., Katiyar, A., et al. (2018) · mAbs · doi:10.1080/19420862.2018.1553476 · Cited by 268 · see citing works

In silico selection of therapeutic antibodies for development: Viscosity, clearance, and chemical stability

Sharma, V. K., Patapoff, T. W., Kabakoff, B., Pai, S., Hilario, E., Zhang, B., Li, C., Borisov, O., Kelley, R. F., Chorny, I., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421779112 · Cited by 256 · see citing works

Developability Assessment During the Selection of Novel Therapeutic Antibodies

Jarasch, A., Koll, H., Regula, J. T., Bader, M., Papadimitriou, A., & Kettenberger, H. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24430 · Cited by 242 · see citing works

Predicting antibody developability profiles through early stage discovery screening

Bailly, M., Mieczkowski, C., Juan, V., Metwally, E., Tomazela, D., Baker, J., Uchida, M., Kofman, E., Raoufi, F., Motlagh, S., et al. (2020) · mAbs · doi:10.1080/19420862.2020.1743053 · Cited by 228 · see citing works

Preclinical pharmacokinetics, pharmacodynamics, tissue distribution, and tumor penetration of anti-PD-L1 monoclonal antibody, an immune checkpoint inhibitor

Deng, R., Bumbaca, D., Pastuskovas, C. V., Boswell, C. A., West, D., Cowan, K. J., Chiu, H., McBride, J., Johnson, C., Xin, Y., et al. (2016) · mAbs · doi:10.1080/19420862.2015.1136043 · Cited by 199 · see citing works

Emerging Strategies for Developing Next-Generation Protein Therapeutics for Cancer Treatment

Kintzing, J. R., Interrante, M. V. F., & Cochran, J. R. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.10.005 · Cited by 192 · see citing works

Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: a FACS-based, high-throughput selection and analytical tool

Xu, Y., Roach, W., Sun, T., Jain, T. S., Prinz, B., Yu, T. Y., Torrey, J., Thomas, J., Bobrowicz, P., Vásquez, M., et al. (2013) · Protein Engineering Design and Selection · doi:10.1093/protein/gzt047 · Cited by 178 · see citing works

A single molecular descriptor to predict solution behavior of therapeutic antibodies

Kingsbury, J. S., Saini, A., Auclair, S. M., Fu, L., Lantz, M. M., Halloran, K. T., Calero‐Rubio, C., Schwenger, W. J., Airiau, C. Y., Zhang, J., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb0372 · Cited by 158 · see citing works

Translational pharmacokinetics and pharmacodynamics of monoclonal antibodies

Kamath, A. V. (2016) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.09.004 · Cited by 158 · see citing works

Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility

Rabia, L. A., Desai, A. A., Jhajj, H. S., & Tessier, P. M. (2018) · Biochemical Engineering Journal · doi:10.1016/j.bej.2018.06.003 · Cited by 159 · see citing works

Antibody Aggregation: Insights from Sequence and Structure

Li, W., Prabakaran, P., Chen, W., Zhu, Z., Feng, Y., & Dimitrov, D. S. (2016) · Antibodies · doi:10.3390/antib5030019 · Cited by 152 · see citing works

Balancing charge in the complementarity-determining regions of humanized mAbs without affecting pI reduces non-specific binding and improves the pharmacokinetics

Datta‐Mannan, A., Thangaraju, A., Leung, D., Tang, Y., Witcher, D. R., Lu, J., & Wroblewski, V. J. (2015) · mAbs · doi:10.1080/19420862.2015.1016696 · Cited by 141 · see citing works

Reducing Immunogenicity by Design: Approaches to Minimize Immunogenicity of Monoclonal Antibodies

Harris, C. T., & Cohen, S. (2024) · BioDrugs · doi:10.1007/s40259-023-00641-2 · Cited by 140 · see citing works

High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy

Liu, Y., Caffry, I., Wu, J., Geng, S. B., Jain, T. S., Sun, T., Reid, F., Cao, Y., Estep, P., Yu, Y., et al. (2013) · mAbs · doi:10.4161/mabs.27431 · Cited by 139 · see citing works

Framework selection can influence pharmacokinetics of a humanized therapeutic antibody through differences in molecule charge

Li, B., Tesar, D. B., Boswell, C. A., Cahaya, H. S., Wong, A., Zhang, J., Meng, Y. G., Eigenbrot, C. W., Pantua, H., Diao, J., et al. (2014) · mAbs · doi:10.4161/mabs.29809 · Cited by 122 · see citing works

Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo

Dobson, C., Devine, P. W. A., Phillips, J. J., Higazi, D. R., Lloyd, C., Popovic, B., Arnold, J., Buchanan, A. G., Lewis, A. R., Goodman, J., et al. (2016) · Scientific Reports · doi:10.1038/srep38644 · Cited by 121 · see citing works

Preclinical Development of a Bispecific Antibody that Safely and Effectively Targets CD19 and CD47 for the Treatment of B-Cell Lymphoma and Leukemia

Buatois, V., Johnson, Z., Salgado-Pires, S., Papaioannou, A., Hatterer, E., Chauchet, X., Richard, F., Barba, L., Daubeuf, B., Cons, L., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-1095 · Cited by 115 · see citing works

A High Through-put Platform for Recombinant Antibodies to Folded Proteins

Hornsby, M. J., Paduch, M., Miersch, S., Sääf, A. M., Matsuguchi, T., Lee, B. H., Wypisniak, K., Doak, A. K., King, D., Usatyuk, S., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.052209 · Cited by 106 · see citing works

Linear pharmacokinetic parameters for monoclonal antibodies are similar within a species and across different pharmacological targets: A comparison between human, cynomolgus monkey and hFcRn Tg32 transgenic mouse using a population-modeling approach

Betts, A. M., Keunecke, A., van Steeg, T. J., van der Graaf, P. H., Avery, L. B., Jones, H. M., & Berkhout, J. (2018) · mAbs · doi:10.1080/19420862.2018.1462429 · Cited by 114 · see citing works

Effects of altered FcγR binding on antibody pharmacokinetics in cynomolgus monkeys

Leabman, M. K., Meng, Y. G., Kelley, R. F., DeForge, L. E., Cowan, K. J., & Iyer, S. (2013) · mAbs · doi:10.4161/mabs.26436 · Cited by 110 · see citing works

Utility of a human FcRn transgenic mouse model in drug discovery for early assessment and prediction of human pharmacokinetics of monoclonal antibodies

Avery, L. B., Wang, M., Kavosi, M. S., Joyce, A. P., Kurz, J. C., Fan, Y., Dowty, M. E., Zhang, M., Zhang, Y., Cheng, A., et al. (2016) · mAbs · doi:10.1080/19420862.2016.1193660 · Cited by 110 · see citing works

Mechanisms Influencing the Pharmacokinetics and Disposition of Monoclonal Antibodies and Peptides

Datta‐Mannan, A. (2019) · Drug Metabolism and Disposition · doi:10.1124/dmd.119.086488 · Cited by 110 · see citing works

Characterization and screening of IgG binding to the neonatal Fc receptor

Neuber, T., Frese, K., Jaehrling, J., Jäger, S., Daubert, D., Felderer, K., Linnemann, M., Höhne, A., Kaden, S., Kölln, J., et al. (2014) · mAbs · doi:10.4161/mabs.28744 · Cited by 109 · see citing works

Tracking Antibody Distribution with Near-Infrared Fluorescent Dyes: Impact of Dye Structure and Degree of Labeling on Plasma Clearance

Cilliers, C., Nessler, I., Christodolu, N., & Thurber, G. M. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01091 · Cited by 109 · see citing works

Development of a Human Antibody Cocktail that Deploys Multiple Functions to Confer Pan-Ebolavirus Protection

Wec, A. Z., Bornholdt, Z. A., He, S., Herbert, A. S., Goodwin, E. C., Wirchnianski, A. S., Gunn, B. M., Zhang, Z., Zhu, W., Liu, G., et al. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2018.12.004 · Cited by 106 · see citing works

Affinity Maturation Enhances Antibody Specificity but Compromises Conformational Stability

Shehata, L., Maurer, D. P., Wec, A. Z., Lilov, A., Champney, E. R., Sun, T., Archambault, K., Burnina, I., Lynaugh, H., Zhi, X., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.056 · Cited by 104 · see citing works

In vitro and in silico assessment of the developability of a designed monoclonal antibody library

Wolf Pérez, A.-M., Sormanni, P., Andersen, J. S., Sakhnini, L. I., Rodriguez-Leon, I., Bjelke, J. R., Gajhede, A. J., De Maria, L., Otzen, D. E., Vendruscolo, M., et al. (2019) · mAbs · doi:10.1080/19420862.2018.1556082 · Cited by 97 · see citing works

Establishing in vitro in vivo correlations to screen monoclonal antibodies for physicochemical properties related to favorable human pharmacokinetics

Avery, L. B., Wade, J. M., Wang, M., Tam, A. S. P., King, A. C., Piche‐Nicholas, N., Kavosi, M. S., Penn, S., Cirelli, D. J., Kurz, J. C., et al. (2017) · mAbs · doi:10.1080/19420862.2017.1417718 · Cited by 97 · see citing works

Assessing developability early in the discovery process for novel biologics

Fernández‐Quintero, M. L., Ljungars, A., Waibl, F., Greiff, V., Andersen, J. T., Gjølberg, T. T., Jenkins, T. P., Voldborg, B. G. R., Grav, L. M., Kumar, S., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2171248 · Cited by 99 · see citing works

A human endothelial cell-based recycling assay for screening of FcRn targeted molecules

Grevys, A., Nilsen, J., Sand, K. M. K., Daba, M. B., Øynebråten, I., Bern, M., McAdam, M. B., Foss, S., Schlothauer, T., Michaelsen, T. E., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03061-x · Cited by 98 · see citing works

B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV

Scheid, J. F., Barnes, C. O., Eraslan, B., Hudak, A., Keeffe, J. R., Cosimi, L. A., Brown, E., Muecksch, F., Weisblum, Y., Zhang, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.032 · Cited by 90 · see citing works

High throughput cross-interaction measures for human IgG1 antibodies correlate with clearance rates in mice

Kelly, R. L., Sun, T., Jain, T. S., Caffry, I., Yu, Y., Cao, Y., Lynaugh, H., Brown, M. E., Vásquez, M., Wittrup, K. D., et al. (2015) · mAbs · doi:10.1080/19420862.2015.1043503 · Cited by 90 · see citing works

Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope

Schoofs, T., Barnes, C. O., Suh-Toma, N., Golijanin, J., Schommers, P., Gruell, H., West, A. P., Bach, F., Lee, Y. E., Nogueira, L., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.04.014 · Cited by 89 · see citing works

The interplay of non-specific binding, target-mediated clearance and FcRn interactions on the pharmacokinetics of humanized antibodies

Datta‐Mannan, A., Lu, J., Witcher, D. R., Leung, D., Tang, Y., & Wroblewski, V. J. (2015) · mAbs · doi:10.1080/19420862.2015.1075109 · Cited by 85 · see citing works

Selecting and engineering monoclonal antibodies with drug-like specificity

Starr, C. G., & Tessier, P. M. (2019) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2019.01.008 · Cited by 81 · see citing works

Evaluating the Use of Antibody Variable Region (Fv) Charge as a Risk Assessment Tool for Predicting Typical Cynomolgus Monkey Pharmacokinetics

Bumbaca Yadav, D., Sharma, V. K., Boswell, C. A., Hotzel, I., Tesar, D., Shang, Y., Ying, Y., Fischer, S. K., Grogan, J. L., Chiang, E. Y., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.692434 · Cited by 82 · see citing works

Net charge of antibody complementarity-determining regions is a key predictor of specificity

Rabia, L. A., Zhang, Y., Ludwig, S. D., Julian, M. C., & Tessier, P. M. (2018) · Protein Engineering Design and Selection · doi:10.1093/protein/gzz002 · Cited by 81 · see citing works

Non-specificity as the sticky problem in therapeutic antibody development

Ausserwöger, H., Schneider, M. M., Herling, T. W., Arosio, P., Invernizzi, G., Knowles, T. P. J., & Lorenzen, N. (2022) · Nature Reviews Chemistry · doi:10.1038/s41570-022-00438-x · Cited by 80 · see citing works

Polyreactivity and polyspecificity in therapeutic antibody development: risk factors for failure in preclinical and clinical development campaigns

Cunningham, O., Scott, M. J., Zhou, Z., & Finlay, W. J. J. (2021) · mAbs · doi:10.1080/19420862.2021.1999195 · Cited by 72 · see citing works

Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics

Zhang, W., Wang, H., Feng, N., Li, Y., Gu, J., & Wang, Z. (2022) · Antibody Therapeutics · doi:10.1093/abt/tbac029 · Cited by 74 · see citing works

Toward Drug-Like Multispecific Antibodies by Design

Sawant, M. S., Streu, C. N., Wu, L., & Tessier, P. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207496 · Cited by 74 · see citing works

Anti-PD1 ‘SHR-1210ʹ aberrantly targets pro-angiogenic receptors and this polyspecificity can be ablated by paratope refinement

Finlay, W. J. J., Coleman, J. E., Edwards, J. S., & Johnson, K. S. (2018) · mAbs · doi:10.1080/19420862.2018.1550321 · Cited by 72 · see citing works

Identifying developability risks for clinical progression of antibodies using high-throughput in vitro and in silico approaches

Jain, T. S., Boland, T., & Vásquez, M. (2023) · mAbs · doi:10.1080/19420862.2023.2200540 · Cited by 71 · see citing works

Heparin chromatography as an in vitro predictor for antibody clearance rate through pinocytosis

Kraft, T. E., Richter, W. F., Emrich, T., Knaupp, A., Schuster, M., Wolfert, A., & Kettenberger, H. (2019) · mAbs · doi:10.1080/19420862.2019.1683432 · Cited by 68 · see citing works

Beyond affinity: selection of antibody variants with optimal biophysical properties and reduced immunogenicity from mammalian display libraries

Dyson, M. R., Masters, E. W., Pazeraitis, D., Perera, R. L., Syrjänen, J. L., Surade, S. B., Thorsteinson, N., Parthiban, K., Jones, P. C., Sattar, M., et al. (2020) · mAbs · doi:10.1080/19420862.2020.1829335 · Cited by 68 · see citing works

Reduction of Nonspecificity Motifs in Synthetic Antibody Libraries

Kelly, R. L., Le, D., Zhao, J., & Wittrup, K. D. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.11.008 · Cited by 67 · see citing works

Industrial bioprocessing perspectives on managing therapeutic protein charge variant profiles

Chung, S., Tian, J., Tan, Z., Chen, J., Lee, J., Borys, M., & Li, Z. J. (2018) · Biotechnology and Bioengineering · doi:10.1002/bit.26587 · Cited by 66 · see citing works

Anin vitroFcRn- dependent transcytosis assay as a screening tool for predictive assessment of nonspecific clearance of antibody therapeutics in humans

Chung, S., Nguyen, V., Lin, Y. L., Lafrance‐Vanasse, J., Scales, S. J., Lin, K., Deng, R., Williams, K., Sperinde, G. V., Li, J. J., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1605270 · Cited by 65 · see citing works

Improving Monoclonal Antibody Selection and Engineering using Measurements of Colloidal Protein Interactions

Geng, S. B., Cheung, J. K., Narasimhan, C. N., Shameem, M., & Tessier, P. M. (2014) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24130 · Cited by 65 · see citing works

Blueprint for antibody biologics developability

Mieczkowski, C., Zhang, X., Lee, D., Nguyen, K., Lv, W., Wang, Y., Zhang, Y., Way, J., & Gries, J. (2023) · mAbs · doi:10.1080/19420862.2023.2185924 · Cited by 65 · see citing works

An alternative assay to hydrophobic interaction chromatography for high-throughput characterization of monoclonal antibodies

Estep, P., Caffry, I., Yu, Y., Sun, T., Cao, Y., Lynaugh, H., Jain, T. S., Vásquez, M., Tessier, P. M., & Xu, Y. (2015) · mAbs · doi:10.1080/19420862.2015.1016694 · Cited by 64 · see citing works

Deep Sequencing-guided Design of a High Affinity Dual Specificity Antibody to Target Two Angiogenic Factors in Neovascular Age-related Macular Degeneration

Koenig, P. S., Lee, C. V., Sanowar, S., Wu, P., Stinson, J., Harris, S. F., & Fuh, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662783 · Cited by 63 · see citing works

Effect of variable domain charge on in vitro and in vivo disposition of monoclonal antibodies

Liu, S., Verma, A., Kettenberger, H., Richter, W. F., & Shah, D. K. (2021) · mAbs · doi:10.1080/19420862.2021.1993769 · Cited by 61 · see citing works

Drug-like antibodies with high affinity, diversity and developability directly from next-generation antibody libraries

Teixeira, A. A. R., Erasmus, M. F., D’Angelo, S., Naranjo, L. A., Ferrara, F., Leal‐Lopes, C., Durrant, O., Galmiche, C., Morelli, A., Scott-Tucker, A., et al. (2021) · mAbs · doi:10.1080/19420862.2021.1980942 · Cited by 60 · see citing works

Discovery-stage identification of drug-like antibodies using emerging experimental and computational methods

Makowski, E. K., Wu, L., Gupta, P., & Tessier, P. M. (2021) · mAbs · doi:10.1080/19420862.2021.1895540 · Cited by 60 · see citing works

Antibody engineering for increased potency, breadth and half-life

Sievers, S. A., Scharf, L., West, A. P., & Björkman, P. J. (2015) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0000000000000148 · Cited by 59 · see citing works

An in silico method to assess antibody fragment polyreactivity

Harvey, E. P., Shin, J.-E., Skiba, M. A., Nemeth, G. R., Hurley, J. D., Wellner, A., Shaw, A. Y., Miranda, V. G., Min, J., Liu, C. C., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35276-4 · Cited by 57 · see citing works

Pharmacokinetic and pharmacodynamic considerations for the next generation protein therapeutics

Shah, D. K. (2015) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-015-9447-8 · Cited by 55 · see citing works

Engineering a bispecific antibody with a common light chain: Identification and optimization of an anti-CD3 epsilon and anti-GPC3 bispecific antibody, ERY974

Shiraiwa, H., Narita, A., Kamata‐Sakurai, M., Ishiguro, T., Sano, Y., Hironiwa, N., Tsushima, T., Segawa, H., Tsunenari, T., Ikeda, Y., et al. (2018) · Methods · doi:10.1016/j.ymeth.2018.10.005 · Cited by 55 · see citing works

Biochemical patterns of antibody polyreactivity revealed through a bioinformatics-based analysis of CDR loops

Boughter, C. T., Borowska, M. T., Guthmiller, J. J., Bendelac, A. S., Wilson, P. C., Roux, B., & Adams, E. J. (2020) · eLife · doi:10.7554/elife.61393 · Cited by 56 · 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

Identifying biophysical assays and <i>in silico</i> properties that enrich for slow clearance in clinical-stage therapeutic antibodies

Grinshpun, B., Thorsteinson, N., Pereira, J. N., Rippmann, F., Nannemann, D., Sood, V. D., & Fomekong Nanfack, Y. (2021) · mAbs · doi:10.1080/19420862.2021.1932230 · Cited by 52 · see citing works

The Fab region of IgG impairs the internalization pathway of FcRn upon Fc engagement

Brinkhaus, M., Pannecoucke, E., van der Kooi, E. J., Bentlage, A. E. H., Derksen, N. I. L., Andries, J., Balbino, B., Sips, M., Ulrichts, P., Verheesen, P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33764-1 · Cited by 51 · see citing works

Aberrant bispecific antibody pharmacokinetics linked to liver sinusoidal endothelium clearance mechanism in cynomolgus monkeys

Datta‐Mannan, A., Croy, J. E., Schirtzinger, L., Torgerson, S., Breyer, M. D., & Wroblewski, V. J. (2016) · mAbs · doi:10.1080/19420862.2016.1178435 · Cited by 51 · see citing works

Target-independent variable region mediated effects on antibody clearance can be FcRn independent

Kelly, R. L., Yu, Y., Sun, T., Caffry, I., Lynaugh, H., Brown, M. E., Jain, T. S., Xu, Y., & Wittrup, K. D. (2016) · mAbs · doi:10.1080/19420862.2016.1208330 · Cited by 51 · see citing works

Optimization of therapeutic antibodies for reduced self-association and non-specific binding via interpretable machine learning

Makowski, E. K., Wang, T., Zupancic, J. M., Huang, J., Wu, L., Schardt, J. S., Groot, A. S. D., Elkins, S. L., Martin, W. D., & Tessier, P. M. (2023) · Nature Biomedical Engineering · doi:10.1038/s41551-023-01074-6 · Cited by 49 · see citing works

Physicochemical Rules for Identifying Monoclonal Antibodies with Drug-like Specificity

Zhang, Y., Wu, L., Gupta, P., Desai, A. A., Smith, M. D., Rabia, L. A., Ludwig, S. D., & Tessier, P. M. (2020) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00257 · Cited by 46 · see citing works

Highly sensitive detection of antibody nonspecific interactions using flow cytometry

Makowski, E. K., Wu, L., Desai, A. A., & Tessier, P. M. (2021) · mAbs · doi:10.1080/19420862.2021.1951426 · Cited by 46 · see citing works

Antibodies with Weakly Basic Isoelectric Points Minimize Trade-offs between Formulation and Physiological Colloidal Properties

Gupta, P., Makowski, E. K., Kumar, S., Zhang, Y., Scheer, J. M., & Tessier, P. M. (2022) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00373 · Cited by 45 · see citing works

Pharmacokinetic de-risking tools for selection of monoclonal antibody lead candidates

Dostalek, M., Prueksaritanont, T., & Kelley, R. F. (2017) · mAbs · doi:10.1080/19420862.2017.1323160 · Cited by 45 · see citing works

Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods

Pérez, A.-M. W., Lorenzen, N., Vendruscolo, M., & Sormanni, P. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1450-1_4 · Cited by 40 · see citing works

Quantitative prediction of therapeutic antibody pharmacokinetics after intravenous and subcutaneous injection in human

Haraya, K., Tachibana, T., & Nezu, J. (2017) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2017.05.002 · Cited by 43 · see citing works

Ultradilute Measurements of Self-Association for the Identification of Antibodies with Favorable High-Concentration Solution Properties

Starr, C. G., Makowski, E. K., Wu, L., Berg, B., Kingsbury, J. S., Gokarn, Y. R., & Tessier, P. M. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00280 · Cited by 43 · see citing works

Microfluidic Approaches for the Characterization of Therapeutic Proteins

Kopp, M. R. G., & Arosio, P. (2018) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2018.01.001 · Cited by 43 · see citing works

Preclinical and translational pharmacokinetics of a novel THIOMAB™ antibody-antibiotic conjugate againstStaphylococcus aureus

Deng, R., Zhou, C., Li, D., Cai, H., Sukumaran, S., Carrasco‐Triguero, M., Saad, O. M., Nazzal, D., Lowe, C., Ramanujan, S., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1627152 · Cited by 42 · see citing works

Engineered Multivalent Nanobodies Potently and Broadly Neutralize SARS‐CoV‐2 Variants

Zupancic, J. M., Schardt, J. S., Desai, A. A., Makowski, E. K., Smith, M. D., Pornnoppadol, G., Barbosa, M. G. D. M., Cascalho, M., Lanigan, T. M., & Tessier, P. M. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202100099 · Cited by 39 · see citing works

Physiologic Changes During Pregnancy and Impact on Small‐Molecule Drugs, Biologic (Monoclonal Antibody) Disposition, and Response

Eke, A. C., Gebreyohannes, R. D., Fernandes, M. F. S., & Pillai, V. C. (2023) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.2227 · Cited by 59 · see citing works

Development and Preclinical Characterization of a Humanized Antibody Targeting CXCL12

Zhong, C., Wang, J., Li, B., Xiang, H., Ultsch, M. H., Coons, M. M., Wong, T., Chiang, N. Y., Clark, S., Clark, R., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0943 · Cited by 39 · see citing works

Mechanistic and quantitative insight into cell surface targeted molecular imaging agent design

Zhang, L., Bhatnagar, S., Deschenes, E., & Thurber, G. M. (2016) · Scientific Reports · doi:10.1038/srep25424 · Cited by 38 · see citing works

Antibody-siRNA conjugates: drugging the undruggable for anti-leukemic therapy

Tushir‐Singh, J. (2016) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2017.1273344 · Cited by 38 · see citing works

The biodistribution of therapeutic proteins: Mechanism, implications for pharmacokinetics, and methods of evaluation

Conner, K. P., Devanaboyina, S. C., Thomas, V. A., & Rock, D. A. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107574 · Cited by 38 · see citing works

Evolving strategies and application of proteins and peptide therapeutics in cancer treatment

Mukherjee, A. G., Wanjari, U. R., Gopalakrishnan, A. V., Bradu, P., Biswas, A., Ganesan, R., Renu, K., Dey, A., Vellingiri, B., Allali, A. E., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114832 · Cited by 37 · see citing works

Nanoscale integration of single cell biologics discovery processes using optofluidic manipulation and monitoring

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 · see citing works

Predicting monoclonal antibody pharmacokinetics following subcutaneous administration via whole-body physiologically-based modeling

Hu, S., & D’Argenio, D. Z. (2020) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-020-09691-3 · Cited by 38 · see citing works

An accelerated surface-mediated stress assay of antibody instability for developability studies

Kopp, M. R. G., Pérez, A.-M. W., Zucca, M. V., Palmiero, U. C., Friedrichsen, B., Lorenzen, N., & Arosio, P. (2020) · mAbs · doi:10.1080/19420862.2020.1815995 · Cited by 36 · see citing works

Pharmacokinetics of novel Fc-engineered monoclonal and multispecific antibodies in cynomolgus monkeys and humanized FcRn transgenic mouse models

Valente, D., Mauriac, C., Schmidt, T., Focken, I., Beninga, J., Mackness, B. C., Qiu, H., Vicat, P., Kandira, A., Radošević, K., et al. (2020) · mAbs · doi:10.1080/19420862.2020.1829337 · Cited by 34 · see citing works

Measurements of Monoclonal Antibody Self-Association Are Correlated with Complex Biophysical Properties

Geng, S. B., Wittekind, M. G., Vigil, A., & Tessier, P. M. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b00071 · Cited by 34 · see citing works

Recent Advances in Translational Pharmacokinetics and Pharmacodynamics Prediction of Therapeutic Antibodies Using Modeling and Simulation

Haraya, K., Tsutsui, H., Komori, Y., & Tachibana, T. (2022) · Pharmaceuticals · doi:10.3390/ph15050508 · Cited by 35 · see citing works

Improvement of pharmacokinetic properties of therapeutic antibodies by antibody engineering

Haraya, K., Tachibana, T., & Igawa, T. (2018) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2018.10.003 · Cited by 33 · see citing works

Novel in Vivo and in Vitro Pharmacokinetic/Pharmacodynamic-Based Human Starting Dose Selection for Glofitamab

Frances, N., Bacac, M., Bray, K. M., Christen, F., Hinton, H. J., Husar, E., Quackenbush, E. J., Schäfer, M. K.-H., Schick, E., Vyver, A. J. V. D., et al. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2021.12.019 · Cited by 33 · see citing works

Chaperone proteins as single component reagents to assess antibody nonspecificity

Kelly, R. L., Geoghegan, J. C., Feldman, J. E., Jain, T. S., Kauke, M. J., Le, D., Zhao, J., & Wittrup, K. D. (2017) · mAbs · doi:10.1080/19420862.2017.1356529 · Cited by 33 · see citing works

Molecular surface descriptors to predict antibody developability: sensitivity to parameters, structure models, and conformational sampling

Park, E., & Izadi, S. (2024) · mAbs · doi:10.1080/19420862.2024.2362788 · Cited by 32 · see citing works

Preclinical development of AMG 139, a human antibody specifically targeting IL ‐23

Köck, K., Pan, W., Gow, J. M., Horner, M. J., Gibbs, J. P., Colbert, A., Goletz, T. J., Newhall, K. J., Rees, W. A., Sun, Y., et al. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12904 · Cited by 32 · see citing works

Pharmacologic Considerations in the Disposition of Antibodies and Antibody-Drug Conjugates in Preclinical Models and in Patients

Lucas, A. T., Robinson, R., Schorzman, A. N., Piscitelli, J. A., Razo, J. F., & Zamboni, W. C. (2019) · Antibodies · doi:10.3390/antib8010003 · Cited by 31 · see citing works

Target-independent variable region mediated effects on antibody clearance can be FcRn independent

Kelly, R. L., Yu, Y., Sun, T., Caffry, I., Lynaugh, H., Brown, M. E., Jain, T. S., Xu, Y., & Wittrup, K. D. (2016) · mAbs · doi:10.1080/19420862.2016.1208330 · Cited by 51 · see citing works

The interplay of non-specific binding, target-mediated clearance and FcRn interactions on the pharmacokinetics of humanized antibodies

Datta‐Mannan, A., Lu, J., Witcher, D. R., Leung, D., Tang, Y., & Wroblewski, V. J. (2015) · mAbs · doi:10.1080/19420862.2015.1075109 · Cited by 85 · see citing works

Cellular Neonatal Fc Receptor Recycling Efficiencies can Differentiate Target-Independent Clearance Mechanisms of Monoclonal Antibodies

Bryniarski, M. A., Tuhin, M. T. H., Acker, T. M., Wakefield, D. L., Sethaputra, P., Cook, K. D., Soto, M., Ponce, M., Primack, R., Jagarapu, A., et al. (2024) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2024.06.013 · Cited by 8 · see citing works

Anin vitroFcRn- dependent transcytosis assay as a screening tool for predictive assessment of nonspecific clearance of antibody therapeutics in humans

Chung, S., Nguyen, V., Lin, Y. L., Lafrance‐Vanasse, J., Scales, S. J., Lin, K., Deng, R., Williams, K., Sperinde, G. V., Li, J. J., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1605270 · Cited by 65 · see citing works

Heparin chromatography as an in vitro predictor for antibody clearance rate through pinocytosis

Kraft, T. E., Richter, W. F., Emrich, T., Knaupp, A., Schuster, M., Wolfert, A., & Kettenberger, H. (2019) · mAbs · doi:10.1080/19420862.2019.1683432 · Cited by 68 · see citing works