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

Sequences of proteins of immunological interest

Kabat, B. E. A. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90805-4 · Cited by 3,387 · see citing works

Clinical development success rates for investigational drugs

Hay, M., Thomas, D. W., Craighead, J. L., Economides, C., & Rosenthal, J. (2014) · Nature Biotechnology · doi:10.1038/nbt.2786 · Cited by 2,536 · see citing works

Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab

Cho, H., Mason, K., Ramyar, K. X., Stanley, A. M., Gabelli, S. B., Denney, D. W., & Leahy, D. J. (2003) · Nature · doi:10.1038/nature01392 · Cited by 1,615 · see citing works

High-Resolution Epitope Mapping of hGH-Receptor Interactions by Alanine-Scanning Mutagenesis

Cunningham, B. C., & Wells, J. A. (1989) · Science · doi:10.1126/science.2471267 · Cited by 1,361 · 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

CNS Delivery Via Adsorptive Transcytosis

Hervé, F., Ghinea, N., & Scherrmann, J.-M. (2008) · The AAPS Journal · doi:10.1208/s12248-008-9055-2 · Cited by 676 · see citing works

Interspecies scaling, allometry, physiological time, and the ground plan of pharmacokinetics

Boxenbaum, H. (1982) · Journal of Pharmacokinetics and Biopharmaceutics · doi:10.1007/bf01062336 · Cited by 648 · see citing works

Differences in promiscuity for antibody–FcRn interactions across species: implications for therapeutic antibodies

Ober, R. J., Radu, C. G., Ghetie, V. F., & Ward, E. S. (2001) · International Immunology · doi:10.1093/intimm/13.12.1551 · Cited by 502 · see citing works

Effects of Charge on Antibody Tissue Distribution and Pharmacokinetics

Boswell, C. A., Tesar, D. B., Mukhyala, K., Theil, F.-P., Fielder, P. J., & Khawli, L. A. (2010) · Bioconjugate Chemistry · doi:10.1021/bc100261d · Cited by 398 · see citing works

Species similarities and differences in pharmacokinetics.

Lin, J. H. (1995) · Drug Metabolism and Disposition · doi:10.1016/s0090-9556(25)06742-x · Cited by 397 · see citing works

Mechanistic Determinants of Biotherapeutics Absorption Following SC Administration

Richter, W. F., Bhansali, S. G., & Morris, M. E. (2012) · The AAPS Journal · doi:10.1208/s12248-012-9367-0 · Cited by 377 · see citing works

Marketed therapeutic antibodies compendium

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

Immunogenicity to Therapeutic Proteins: Impact on PK/PD and Efficacy

Chirmule, N. B., Jawa, V., & Meibohm, B. (2012) · The AAPS Journal · doi:10.1208/s12248-012-9340-y · Cited by 338 · see citing works

Identification and Multidimensional Optimization of an Asymmetric Bispecific IgG Antibody Mimicking the Function of Factor VIII Cofactor Activity

Sampei, Z., Igawa, T., Soeda, T., Okuyama-Nishida, Y., Moriyama, C., Wakabayashi, T., Tanaka, E., Muto, A., Kojima, T., Kitazawa, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057479 · Cited by 338 · see citing works

Biodistribution Mechanisms of Therapeutic Monoclonal Antibodies in Health and Disease

Tabrizi, M. A., Bornstein, G. G., & Suria, H. (2009) · The AAPS Journal · doi:10.1208/s12248-009-9157-5 · Cited by 307 · 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

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

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

A strategy for risk mitigation of antibodies with fast clearance

Hötzel, I., Theil, F.-P., Bernstein, L. J., Prabhu, S., Deng, R., Quintana, L., Lutman, J., Sibia, R., Chan, P., Bumbaca, D., et al. (2012) · mAbs · doi:10.4161/mabs.22189 · Cited by 245 · see citing works

Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics

Schoch, A., Kettenberger, H., Mundigl, O., Winter, G., Engert, J., Heinrich, J., & Emrich, T. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408766112 · Cited by 202 · see citing works

Development of humanized bispecific antibodies reactive with cytotoxic lymphocytes and tumor cells overexpressing the HER2 protooncogene.

Shalaby, M. R., Shepard, H. M., Presta, L. G., Rodrigues, M. L., Beverley, P. C. L., Feldmann, M., & Carter, P. M. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.175.1.217 · Cited by 176 · see citing works

Quantitative Prediction of Human Pharmacokinetics for Monoclonal Antibodies: Retrospective Analysis of Monkey as a Single Species for First-in-Human Prediction

Dong, J. Q., Salinger, D. H., Endres, C. J., Gibbs, J. P., Hsu, C.-P., Stouch, B. J., Hurh, E., & Gibbs, M. A. (2011) · Clinical Pharmacokinetics · doi:10.2165/11537430-000000000-00000 · Cited by 156 · 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

Comparison of IgG diffusion and extracellular matrix composition in rhabdomyosarcomas grown in mice versus in vitro as spheroids reveals the role of host stromal cells

Davies, C. D. L., Berk, D. A., Pluen, A., & Jain, R. K. (2002) · British Journal of Cancer · doi:10.1038/sj.bjc.6600270 · Cited by 121 · see citing works

Physiochemical and Biochemical Factors Influencing the Pharmacokinetics of Antibody Therapeutics

Bumbaca, D., Boswell, C. A., Fielder, P. J., & Khawli, L. A. (2012) · The AAPS Journal · doi:10.1208/s12248-012-9369-y · Cited by 119 · see citing works

Glycan Shifting on Hepatitis C Virus (HCV) E2 Glycoprotein Is a Mechanism for Escape from Broadly Neutralizing Antibodies

Pantua, H., Diao, J., Ultsch, M. H., Hazen, M., Mathieu, M. A., McCutcheon, K. M., Takeda, K., Date, S. V., Cheung, T. K., Phung, Q. T., et al. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.025 · Cited by 113 · 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

Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis.

Sharp, L. L., Zhou, J., & Blair, D. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7946 · Cited by 104 · see citing works

Properties of a general PK/PD model of antibody-ligand interactions for therapeutic antibodies that bind to soluble endogenous targets

Davda, J. P., & Hansen, R. J. (2010) · mAbs · doi:10.4161/mabs.2.5.12833 · Cited by 94 · see citing works

Incorporating target-mediated drug disposition in a minimal physiologically-based pharmacokinetic model for monoclonal antibodies

Cao, Y., & Jusko, W. J. (2014) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-014-9372-2 · Cited by 92 · see citing works

Monoclonal Antibody Radiopharmaceuticals: Cationization, Pegylation, Radiometal Chelation, Pharmacokinetics, and Tumor Imaging

Lee, H., & Pardridge, W. M. (2003) · Bioconjugate Chemistry · doi:10.1021/bc0256648 · Cited by 79 · see citing works

The pharmacokinetic characteristics of glycolated humanized anti-Tac Fabs are determined by their isoelectric points.

Kobayashi, H., Le, N., Kim, I. S., Kim, M. K., Pie, J.-E., Drumm, D., Paik, D. S., Waldmann, T. A., Paik, C. H., & Carrasquillo, J. A. (1999) · PubMed · Cited by 73 · see citing works

Electrostatic Interactions of Monoclonal Antibodies With Subcutaneous Tissue

Mach, H., Gregory, S., Mackiewicz, A. L., Mittal, S., Lalloo, A., Kirchmeier, M. J., & Shameem, M. (2011) · Therapeutic Delivery · doi:10.4155/tde.11.31 · Cited by 60 · see citing works

Enhanced cellular uptake and in vivo biodistribution of a monoclonal antibody following cationization

Pardridge, W. M., Kang, Y., Yang, J., & Buciak, J. L. (1995) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.2600840808 · Cited by 56 · see citing works

CheA Kinase of Bacterial Chemotaxis: Chemical Mapping of Four Essential Docking Sites

Miller, A. S., Kohout, S. C., Gilman, K. A., & Falke, J. J. (2006) · Biochemistry · doi:10.1021/bi060580y · Cited by 55 · 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

Off-Target Platelet Activation in Macaques Unique to a Therapeutic Monoclonal Antibody

Santostefano, M. J., Kirchner, J., Vissinga, C. S., Fort, M. M., Lear, S. P., Pan, W., Prince, P. J., Hensley, K. M., Tran, D. T., Rock, D. A., et al. (2012) · Toxicologic Pathology · doi:10.1177/0192623312444029 · Cited by 43 · see citing works

Pharmacokinetic and Pharmacodynamic Analysis of Circulating Biomarkers of Anti-NRP1, a Novel Antiangiogenesis Agent, in Two Phase I Trials in Patients with Advanced Solid Tumors

Xin, Y., Li, J., Wu, J., Kinard, R., Weekes, C., Patnaik, A., LoRusso, P., Brachmann, R., Tong, R. K., Yan, Y.-B., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-1652 · Cited by 41 · see citing works

Dimerization of LTβR by LTα 1 β 2 is necessary and sufficient for signal transduction

Sudhamsu, J., Yin, J., Chiang, E. Y., Starovasnik, M. A., Grogan, J. L., & Hymowitz, S. G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310838110 · Cited by 39 · see citing works

Mapping Out Regions on the Surface of the Aspartate Receptor That Are Essential for Kinase Activation

Mehan, R. S., White, N. C., & Falke, J. J. (2003) · Biochemistry · doi:10.1021/bi027127g · Cited by 28 · see citing works

Improved Tumor Localization and Radioimaging with Chemically Modified Monoclonal Antibodies

Khawli, L. A., Glasky, M. S., Alauddin, M. M., & Epstein, A. L. (1996) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/cbr.1996.11.203 · Cited by 27 · see citing works

Unexpected Thrombocytopenia and Anemia in Cynomolgus Monkeys Induced by a Therapeutic Human Monoclonal Antibody

Everds, N. E., Li, N., Bailey, K. L., Fort, M. M., Stevenson, R., Jawando, R., Salyers, K. L., Jawa, V., Narayanan, P. K., Stevens, E., et al. (2013) · Toxicologic Pathology · doi:10.1177/0192623312474727 · Cited by 25 · see citing works

In Vivo Depletion of Lymphotoxin-Alpha Expressing Lymphocytes Inhibits Xenogeneic Graft-versus-Host-Disease

Chiang, E. Y., Kolumam, G. A., McCutcheon, K. M., Young, J., Lin, Z., Balázs, M., & Grogan, J. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033106 · Cited by 21 · see citing works

Methods to Engineer and Identify IgG1 Variants with Improved FcRn Binding or Effector Function

Kelley, R. F., & Meng, Y. G. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-931-0_18 · Cited by 13 · see citing works

The PICM Chemical Scanning Method for Identifying Domain–Domain and Protein–Protein Interfaces: Applications to the Core Signaling Complex of E. coli Chemotaxis

Bass, R. B., Miller, A. S., Gloor, S. L., & Falke, J. J. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)23001-0 · Cited by 12 · see citing works

Biosimilar Monoclonal Antibodies

Pippig, S. D., Brockmeyer, C., & Zoubek, R. E. (2014) · doi:10.1002/9783527682423.ch24 · Cited by 2 · 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

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

Considerations for the Design of Antibody-Based Therapeutics

Goulet, D. R., & Atkins, W. M. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.05.031 · Cited by 305 · 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

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

Subcutaneous delivery of monoclonal antibodies: How do we get there?

Viola, M., Sequeira, J. A. D., Seiça, R. M. F., Veiga, F., Serra, J. P., Paiva‐Santos, A. C., & Ribeiro, A. J. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.08.001 · Cited by 238 · see citing works

Challenges and Opportunities for the Subcutaneous Delivery of Therapeutic Proteins

Turner, M. R., & Balu‐Iyer, S. V. (2018) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2018.01.007 · Cited by 177 · 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

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

Oxidation and Deamidation of Monoclonal Antibody Products: Potential Impact on Stability, Biological Activity, and Efficacy

Gupta, S., Jiskoot, W., Schöneich, C., & Rathore, A. S. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2021.11.024 · Cited by 156 · see citing works

Progress and challenges for the machine learning-based design of fit-for-purpose monoclonal antibodies

Akbar, R., Bashour, H., Rawat, P., Robert, P. A., Smorodina, E., Cotet, T., Karlsen, K. F., Frank, R., Mehta, B. B., Vu, M. H., et al. (2022) · mAbs · doi:10.1080/19420862.2021.2008790 · Cited by 117 · see citing works

Brain Disposition of Antibody-Based Therapeutics: Dogma, Approaches and Perspectives

Kouhi, A., Pachipulusu, V., Kapenstein, T., Hu, P., Epstein, A. L., & Khawli, L. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126442 · Cited by 107 · 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

Structure Based Prediction of Asparagine Deamidation Propensity in Monoclonal Antibodies

Yan, Q., Huang, M., Lewis, M. J., & Hu, P. (2018) · mAbs · doi:10.1080/19420862.2018.1478646 · Cited by 93 · 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

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

Machine Learning Applied to Determine the Molecular Descriptors Responsible for the Viscosity Behavior of Concentrated Therapeutic Antibodies

Lai, P., Fernando, A., Cloutier, T. K., Gokarn, Y. R., Zhang, J., Schwenger, W. J., Chari, R. V. J., Calero‐Rubio, C., & Trout, B. L. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c01073 · Cited by 79 · see citing works

Alternative Routes of Administration for Therapeutic Antibodies—State of the Art

Pitiot, A., Heuzé‐Vourc'h, N., & Sécher, T. (2022) · Antibodies · doi:10.3390/antib11030056 · Cited by 77 · see citing works

Trends in industrialization of biotherapeutics: a survey of product characteristics of 89 antibody-based biotherapeutics

Martin, K., Grimaldi, C. M., Grempler, R., Hansel, S. B., & Kumar, S. (2023) · mAbs · doi:10.1080/19420862.2023.2191301 · 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

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

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

Influence of Charge, Hydrophobicity, and Size on Vitreous Pharmacokinetics of Large Molecules

Crowell, S. R., Wang, K., Famili, A., Shatz-Binder, W., Loyet, K. M., Chang, V., Liu, Y., Prabhu, S., Kamath, A. V., & Kelley, R. F. (2019) · Translational Vision Science & Technology · doi:10.1167/tvst.8.6.1 · Cited by 62 · 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

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

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 in the Design of Therapeutic Antibodies

Leipold, D. D., & Prabhu, S. (2018) · Clinical and Translational Science · doi:10.1111/cts.12597 · 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

Developability considerations for bispecific and multispecific antibodies

Amash, A., Volkers, G., Farber, P. J., Griffin, D., Davison, K. S., Goodman, A., Tonikian, R., Yamniuk, A. P., Barnhart, B. C., & Jacobs, T. M. (2024) · mAbs · doi:10.1080/19420862.2024.2394229 · Cited by 50 · 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

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

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

Therapeutic antibodies – natural and pathological barriers and strategies to overcome them

Ojaimi, Y. A., Blin, T., Lamamy, J., Gracia, M., Pitiot, A., Denevault‐Sabourin, C., Joubert, N., Pouget, J., Gouilleux‐Gruart, V., Heuzé‐Vourc'h, N., et al. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108022 · Cited by 41 · 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

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

Anti‐CD22 and anti‐CD79b antibody‐drug conjugates preferentially target proliferating B cells

Fuh, F. K., Looney, C., Li, D., Poon, K. A., Dere, R. C., Danilenko, D. M., McBride, J., Reed, C., Chung, S., Zheng, B., et al. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13697 · Cited by 30 · see citing works

Nature-inspired design and evolution of anti-amyloid antibodies

Julian, M. C., Rabia, L. A., Desai, A. A., Arsiwala, A., Gerson, J. E., Paulson, H. L., Kane, R. S., & Tessier, P. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004731 · Cited by 30 · see citing works

Development of in silico models to predict viscosity and mouse clearance using a comprehensive analytical data set collected on 83 scaffold-consistent monoclonal antibodies

Mock, M. L., Jacobitz, A. W., LANGMEAD, C. J., Sudom, A. M., Yoo, D., Humphreys, S. C., Alday, M., Alekseychyk, L., Angell, N., Bi, V., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2256745 · Cited by 29 · see citing works

Evaluation of In Vitro Tools to Predict the In Vivo Absorption of Biopharmaceuticals Following Subcutaneous Administration

Bender, C., Eichling, S., Franzen, L., Herzog, V., Ickenstein, L. M., Jere, D., Nonis, L., Schwach, G., Stoll, P., Venczel, M., et al. (2022) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2022.04.005 · Cited by 28 · see citing works

Impact of SPR biosensor assay configuration on antibody: Neonatal Fc receptor binding data

Wang, X., McKay, P., Yee, L. T., Dutina, G., Hass, P. E., Nijem, I., Allison, D., Cowan, K. J., Lin, K., Quarmby, V. E., et al. (2016) · mAbs · doi:10.1080/19420862.2016.1261774 · Cited by 28 · see citing works

Reduction of therapeutic antibody self-association using yeast-display selections and machine learning

Makowski, E. K., Chen, H., Lambert, M. A., Bennett, E. M., Eschmann, N. S., Zhang, Y., Zupancic, J. M., Desai, A. A., Smith, M. D., Lou, W., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2146629 · Cited by 25 · see citing works

Translational Approach for Predicting Human Pharmacokinetics of Engineered Therapeutic Monoclonal Antibodies with Increased FcRn-Binding Mutations

Haraya, K., & Tachibana, T. (2022) · BioDrugs · doi:10.1007/s40259-022-00566-2 · Cited by 18 · see citing works

Physiologically Based Pharmacokinetic Modeling to Characterize the Effect of Molecular Charge on Whole-Body Disposition of Monoclonal Antibodies

Liu, S., & Shah, D. K. (2023) · The AAPS Journal · doi:10.1208/s12248-023-00812-7 · Cited by 17 · see citing works

Single cell-produced and in vitro-assembled anti-FcRH5/CD3 T-cell dependent bispecific antibodies have similar in vitro and in vivo properties

Ovacik, A. M., Li, J., Lemper, M., Danilenko, D. M., Stagg, N. J., Mathieu, M. A., Ellerman, D. A., Gupta, V., Kalia, N., Nguy, T., et al. (2018) · mAbs · doi:10.1080/19420862.2018.1551676 · Cited by 16 · see citing works

Microphysiological endothelial models to characterize subcutaneous drug absorption

Offeddu, G. S. (2022) · ALTEX · doi:10.14573/altex.2207131 · Cited by 15 · see citing works

Nonclinical Pharmacokinetics and Pharmacodynamics Characterization of Anti-CD79b/CD3 T Cell-Dependent Bispecific Antibody Using a Surrogate Molecule: A Potential Therapeutic Agent for B Cell Malignancies

Yadav, R., Sukumaran, S., Zabka, T. S., Li, J., Oldendorp, A., Morrow, G. R., Reyes, A. E., Cheu, M., Li, J. L., Wallin, J. J., et al. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14050970 · Cited by 12 · see citing works

A minimal physiologically based pharmacokinetic model to study the combined effect of antibody size, charge, and binding affinity to FcRn/antigen on antibody pharmacokinetics

Patidar, K., Pillai, N., Dhakal, S., Avery, L. B., & Mavroudis, P. D. (2024) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-023-09899-z · Cited by 11 · see citing works

Improved antibody pharmacokinetics by disruption of contiguous positive surface potential and charge reduction using alternate human framework

Ollier, R., Fuchs, A., Gauye, F., Piorkowska, K., Menant, S., Ratnam, M., Montanari, P., Guilhot, F., Phillipe, D., Audrain, M., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2232087 · Cited by 11 · see citing works

Internalization of therapeutic antibodies into dendritic cells as a risk factor for immunogenicity

Siegel, M., Bolender, A., Ducret, A., Fraidling, J., Hartman, K., Looney, C. M., Rohr, O., Hickling, T. P., Kettenberger, H., Lechmann, M., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1406643 · Cited by 10 · see citing works

Mathematical Models to Characterize the Absorption, Distribution, Metabolism, and Excretion of Protein Therapeutics

Liu, S., & Shah, D. K. (2022) · Drug Metabolism and Disposition · doi:10.1124/dmd.121.000460 · Cited by 10 · see citing works

C-Terminal Lysine Processing of IgG in Human Suction Blister Fluid: Implications for Subcutaneous Administration

Ayalew, L., Chan, P., Hu, Z., Shen, A. Y., Duenas, E. T., Kirschbrown, W. P., Schick, A. J., Chen, Y., & Kim, M. T.-J. (2022) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.2c00506 · Cited by 9 · see citing works

Preferential precipitation of acidic variants from monoclonal antibody pools

Rumanek, T., Kołodziej, M., Piątkowski, W., & Antos, D. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28257 · Cited by 9 · see citing works

SUMO: In Silico Sequence Assessment Using Multiple Optimization Parameters

Evers, A., Malhotra, S., Bolick, W.-G., Najafian, A., Borisovska, M., Warszawski, S., Fomekong‐Nanfack, Y., Kühn, D., Rippmann, F., Crespo, A., et al. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3279-6_22 · Cited by 9 · see citing works

A Cell-Based FcRn-dependent Recycling assay for Predictive Pharmacokinetic assessment of Therapeutic Antibodies

Liu, C., Kim, Y. S., Lowe, J. H.-N., & Chung, S. (2021) · Bioanalysis · doi:10.4155/bio-2021-0099 · Cited by 8 · see citing works

Monoclonal Antibody Pharmacokinetics in Cynomolgus Monkeys Following Subcutaneous Administration: Physiologically Based Model Predictions from Physiochemical Properties

Hu, S., Datta‐Mannan, A., & D’Argenio, D. Z. (2022) · The AAPS Journal · doi:10.1208/s12248-022-00772-4 · Cited by 7 · see citing works

Utility of Cellular Measurements of Non-Specific Endocytosis to Assess the Target-Independent Clearance of Monoclonal Antibodies

Bryniarski, M. A., Tuhin, M. T. H., Shomin, C. D., Nasrollahi, F., Ko, E. C., Soto, M., Chung, K., Poon-Andersen, C., Primack, R., Wong, D., et al. (2024) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2024.07.009 · Cited by 7 · see citing works

Minimal Physiologically-based Pharmacokinetic Model to Investigate the Effect of Charge on the Pharmacokinetics of Humanized anti-HCV-E2 IgG Antibodies in Sprague–Dawley Rats

Hardiansyah, D., & Ng, C. M. (2022) · Pharmaceutical Research · doi:10.1007/s11095-022-03204-2 · Cited by 7 · see citing works

Utility of physiologically based pharmacokinetic modeling to predict inter-antibody variability in monoclonal antibody pharmacokinetics in mice

Liu, S., Humphreys, S. C., Cook, K. D., Conner, K. P., Correia, A. R., Jacobitz, A. W., Yang, M., Primack, R., Soto, M., Padaki, R., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2263926 · Cited by 6 · see citing works

Utilizing PK and PD Biomarkers to Guide the First-in-Human Starting Dose Selection of MTBT1466A: A Novel Humanized Monoclonal Anti-TGFβ3 Antibody for the Treatment of Fibrotic Diseases

Yadav, R., Sukumaran, S., Lutman, J., Mitra, M. S., Halpern, W., Sun, T., Setiadi, A., Neighbors, M., Sheng, X. R., Yip, V., et al. (2023) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2023.07.005 · Cited by 6 · see citing works

Leveraging protein language and structural models for early prediction of antibodies with fast clearancePreprint

Mazrooei, P., O’Neil, D., Izadi, S., Chen, B., & Ramanujan, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.08.597997 · Cited by 6 · see citing works

Does one model fit all mAbs? An evaluation of population pharmacokinetic models

van den Berg, S. P. H., Adolfsen, P. E. A., Dorlo, T. P. C., & Rispens, T. (2025) · mAbs · doi:10.1080/19420862.2025.2512217 · Cited by 5 · see citing works

Impact of DO, agitation, aeration and copper concentration on lactate metabolism and charge heterogeneity for monoclonal antibody production by CHO cells in fed-batch culture

Yin, P., Lin, H., Zhou, Q., Tong, J., & Guo, M. (2025) · Cytotechnology · doi:10.1007/s10616-025-00816-5 · Cited by 5 · see citing works

Monoclonal Antibodies: From Structure to Therapeutic Application

Deng, R., Li, J., Boswell, C. A., Joshi, A., & Li, C. (2024) · Springer eBooks · doi:10.1007/978-3-031-30023-3_8 · Cited by 5 · see citing works

A role for macromolecular crowding in off-target binding of therapeutic antibodies

Klinger, M. (2017) · Protein Engineering Design and Selection · doi:10.1093/protein/gzx035 · Cited by 5 · see citing works

Delivery science: Its increasing importance for the next generation of medicines

Ashford, M. B., & Bak, A. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.114663 · Cited by 4 · see citing works

Algorithmic multiscale analysis for the FcRn mediated regulation of antibody PK in human

Patsatzis, D. G., Wu, S., Shah, D. K., & Goussis, D. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-09846-x · Cited by 4 · see citing works

Novel Perspectives on the Design and Development of a Long-Acting Subcutaneous Raltegravir Injection for Treatment of HIV—In Vitro and In Vivo Evaluation

Abd-Ellah, H. S., Mudududdla, R., Carter, G. P., & Baell, J. B. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15051530 · Cited by 4 · see citing works

Nonspecific Cellular Interactions Are a Key Determinant in the Disposition of Fc-Fused Proteins

Bryniarski, M. A., Wang, S., Chen, A., Coventry, B., Korkmaz, E. N., Tuhin, M. T. H., Ko, E. C., Wakefield, D. L., LaGory, E. L., Wu, H., et al. (2026) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5c01228 · Cited by 4 · see citing works

Monoclonal Antibodies: From Structure to Therapeutic Application

Deng, R., Boswell, C. A., Putnam, W. S., Tang, M. T., Garg, A., Li, C., Chung, S., & Girish, S. (2019) · Springer eBooks · doi:10.1007/978-3-030-00710-2_8 · Cited by 3 · see citing works

Improvement of tumor-to-blood ratio of radioimmunoconjugates by poly(ethyleneimine)-containing chelating agent

Nakashima, K., Shimohara, H., Watanabe, H., & Ono, M. (2024) · Annals of Nuclear Medicine · doi:10.1007/s12149-024-02003-6 · Cited by 2 · see citing works

PK/PD of Positively Charged ADC in Mice

Chang, H., Le, H. K., Liu, S., & Shah, D. K. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17030377 · Cited by 2 · see citing works

Isoelectric point, net charge and amino acid analysis of experimentally validated therapeutic antibodies

Nagraj, A. K., Patel, R., Gavade, A., Pais, R., Verma, P., & Patil, J. (2025) · In Silico Pharmacology · doi:10.1007/s40203-025-00356-y · Cited by 1 · see citing works

Long lasting complement neutralisation by RAY121, an engineered anti-C1s antibody with C1q displacement function

Ho, A. W. S., Fukuzawa, T., Koga, H., Ohmine, K., Kawauchi, H., Muraoka, M., Ikuta, Y., Gupta, G., Okuda, M., Onami, I., et al. (2025) · EBioMedicine · doi:10.1016/j.ebiom.2025.106009 · Cited by 1 · see citing works

Comparison between a chimeric anti-methamphetamine monoclonal antibody and humanized antibodies on pharmacological effects of methamphetamine

Berquist, M. D., Gunnell, M. G., Henry, R. L., Gentry, W. B., & Stevens, M. W. (2025) · Psychopharmacology · doi:10.1007/s00213-025-06959-9 · Cited by 1 · see citing works

Human Dose and Pharmacokinetic Predictions for Biologics at Boehringer Ingelheim: A Retrospective Analysis

Grempler, R., Ahlberg, J., Germovsek, E., Gupta, P., Li, H., Pilvankar, M., Sharma, A., Stopfer, P., & Hansel, S. B. (2023) · Advances in Therapy · doi:10.1007/s12325-023-02710-y · Cited by 1 · see citing works

Biotherapeutics ADME and PK/PD Principles

Yadav, D. B., Gadkar, K. G., & Figueroa, I. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821044-4.00009-1

Preferential precipitation for reducing acidic variant content in monoclonal antibody poolsPreprint

Rumanek, T., Kołodziej, M., Piątkowski, W., & Antos, D. (2022) · doi:10.22541/au.164873336.66745488/v1

Preferential Precipitation for Reducing Acidic Variant Contentin Monoclonal Antibody PoolsPreprint

Antos, D., Rumanek, T., Kołodziej, M., & Piątkowski, W. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4072650

Physiologically based pharmacokinetic (PBPK) model that describes enhanced FcRn-dependent distribution of monoclonal antibodies (mAbs) by pI-engineering in mice

Naoi, S., Yamane, M., Nemoto, T., Kato, M., Saito, R., & Tachibana, T. (2023) · Drug Metabolism and Pharmacokinetics · doi:10.1016/j.dmpk.2023.100506

Tagatose as a Charge Variants Regulator of Mab by Decreasing Sialic Acid LevelPreprint

Gu, L., Cao, Y., & Zhou, H. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4883614

Monoclonal Antibody Pharmacokinetics in Cynomolgus Monkeys Following Subcutaneous Administration: Physiologically Based Model Predictions from Physiochemical Properties

Hu, S., Datta‐Mannan, A., & D’Argenio, D. Z. (2022) · The AAPS Journal · doi:10.1208/s12248-022-00772-4 · Cited by 7 · 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

Simple Approach to Accurately Predict Pharmacokinetics of Therapeutic Monoclonal Antibodies after Subcutaneous Injection in Humans

Haraya, K., & Tachibana, T. (2020) · Clinical Pharmacokinetics · doi:10.1007/s40262-020-00917-8 · Cited by 11 · 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

A strategy for risk mitigation of antibodies with fast clearance

Hötzel, I., Theil, F.-P., Bernstein, L. J., Prabhu, S., Deng, R., Quintana, L., Lutman, J., Sibia, R., Chan, P., Bumbaca, D., et al. (2012) · mAbs · doi:10.4161/mabs.22189 · Cited by 245 · see citing works