Structural and Functional Characterization of Disulfide Isoforms of the Human IgG2 Subclass

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Post-translational modifications in the context of therapeutic proteins

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Crystal Structure of a Neutralizing Human IgG Against HIV-1: A Template for Vaccine Design

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Downstream processing of monoclonal antibodies—Application of platform approaches

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Probing conformational changes in proteins by mass spectrometry

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Disulfide bonds as switches for protein function.

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Therapeutic antibodies for human diseases at the dawn of the twenty-first century

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Heterogeneity of Monoclonal Antibodies

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Advances in refolding of proteins produced in E. coli

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Reduced FcRn-mediated transcytosis of IgG2 due to a missing Glycine in its lower hinge

Stapleton, N. M., Brinkhaus, M., Armour, K. L., Bentlage, A. E. H., de Taeye, S. W., Temming, A. R., Mok, J. Y., Brasser, G., Maas, M. J., van Esch, W. J. E., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40731-2 · Cited by 38

Systematic analysis of Fc mutations designed to reduce binding to Fc-gamma receptors

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Investigation of antibody disulfide reduction and re-oxidation and impact to biological activities

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Three-Dimensional Structure of the Human Myeloma IgG2

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Field flow fractionation for assessing neonatal Fc receptor and Fcγ receptor binding to monoclonal antibodies in solution

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The structure-function relationship of disulfide bonds in etanercept

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Engineering an Improved IgG4 Molecule with Reduced Disulfide Bond Heterogeneity and Increased Fab Domain Thermal Stability

Peters, S. J., Smales, C. M., Henry, A. J., Stephens, P. E., West, S. M., & Humphreys, D. P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.369744 · Cited by 32

Characterization of Cysteinylation and Trisulfide Bonds in a Recombinant Monoclonal Antibody

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Current Mass Spectrometric Tools for the Bioanalyses of Therapeutic Monoclonal Antibodies and Antibody-Drug Conjugates

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Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect Fc gamma receptor or C1q binding

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Structural mass spectrometry in biologics discovery: advances and future trends

Mo, J., Tymiak, A. A., & Chen, G. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.07.006 · Cited by 30

Generation and characterization of a target-selectively activated antibody against epidermal growth factor receptor with enhanced anti-tumor potency

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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

Interchain Disulfide Bonding in Human IgG2 Antibodies Probed by Site-Directed Mutagenesis

Allen, M. J., Guo, A., Martinez, T., Han, M., Flynn, G. C., Wypych, J., Liu, D., Shen, W. D., Dillon, T. M., Vezina, C., et al. (2009) · Biochemistry · doi:10.1021/bi8022174 · Cited by 29

IgG2 disulfide isoform conversion kinetics

Liu, D., Wang, T., Chou, R., Chen, L., Kannan, G., Stevenson, R., Goetze, A. M., Jiang, X. G., Huang, G., Dillon, T. M., et al. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2012.12.005 · Cited by 29

6thAnnual European Antibody Congress 2010

Beck, A., & Wurch, T. (2011) · mAbs · doi:10.4161/mabs.3.2.14788 · Cited by 27

Cysteine Racemization on IgG Heavy and Light Chains

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Quantification of immunoglobulin G and characterization of process related impurities using coupled Protein A and size exclusion high performance liquid chromatography

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Production of a PEGylated Fab′ of the anti-LINGO-1 Li33 Antibody and Assessment of Its Biochemical and Functional Properties in Vitro and in a Rat Model of Remyelination

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The solution structure of the human IgG2 subclass is distinct from those for human IgG1 and IgG4 providing an explanation for their discrete functions

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MS-based conformation analysis of recombinant proteins in design, optimization and development of biopharmaceuticals

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Unlocking the potential of agonist antibodies for treating cancer using antibody engineering

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Domain-specific free thiol variant characterization of an IgG1 by reversed-phase high-performance liquid chromatography mass spectrometry

Cheng, Y., Chen, M. T., Patterson, L. C., Yu, X., Zhang, Y. T., Burgess, B. L., & Chen, Y. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.12.003 · Cited by 25

Agonist Antibodies for Cancer Immunotherapy: History, Hopes, and Challenges

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Viremic HIV Controllers Exhibit High Plasmacytoid Dendritic Cell–Reactive Opsonophagocytic IgG Antibody Responses against HIV-1 p24 Associated with Greater Antibody Isotype Diversification

Tjiam, M. C., Taylor, J. P. A., Morshidi, M. A., Sariputra, L., Burrows, S., Martin, J. N., Deeks, S. G., Tan, D. B. A., Lee, S., Fernández, S., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402918 · Cited by 25

Characterization of free thiol variants of an IgG1 by reversed phase ultra high pressure liquid chromatography coupled with mass spectrometry

Liu, H., Jeong, J., Kao, Y., & Zhang, Y. T. (2015) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2015.02.015 · Cited by 24

Automated in-solution protein digestion using a commonly available high-performance liquid chromatography autosampler

Richardson, J., Shah, B., Xiao, G., Bondarenko, P. V., & Zhang, Z. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.01.019 · Cited by 24

Relative stabilities of IgG1 and IgG4 Fab domains: Influence of the light–heavy interchain disulfide bond architecture

Heads, J. T., Adams, R., D’Hooghe, L. E., Page, M., Humphreys, D. P., Popplewell, A. G., Lawson, A. D. G., & Henry, A. J. (2012) · Protein Science · doi:10.1002/pro.2118 · Cited by 24

Direct mass spectrometric characterization of disulfide linkages

Guan, X., Zhang, L., & Wypych, J. (2018) · mAbs · doi:10.1080/19420862.2018.1442998 · Cited by 24

Production of IgG antibodies to pneumococcal polysaccharides is associated with expansion of ICOS+ circulating memory T follicular-helper cells which is impaired by HIV infection

Abudulai, L. N., Fernández, S., Corscadden, K. J., Burrows, S., Hunter, M., Tjiam, M. C., Kirkham, L. S., Post, J. J., & French, M. A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176641 · Cited by 23

In-Depth Characterization of Protein Disulfide Bonds by Online Liquid Chromatography-Electrochemistry-Mass Spectrometry

Switzar, L., Nicolardi, S., Rutten, J. W., Oberstein, S. A. J. L., Aartsma-Rus, A. M., & van der Burgt, Y. E. M. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1258-z · Cited by 24

Characterization of recombinant monoclonal antibody charge variants using WCX chromatography, icIEF and LC-MS/MS

Liu, H., Ren, W., Zong, L., Zhang, J., & Wang, Y. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.10.002 · Cited by 23

Evidence of disulfide bond scrambling during production of an antibody-drug conjugate

Liu-Shin, L. P.-Y., Fung, A., Malhotra, A., & Ratnaswamy, G. (2018) · mAbs · doi:10.1080/19420862.2018.1521128 · Cited by 23

Enabling development, manufacturing, and regulatory approval of biotherapeutics through advances in mass spectrometry

Apostoł, I., Bondarenko, P. V., Ren, D., Semin, D. J., Wu, C., Zhang, Z., & Goudar, C. T. (2021) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2021.08.001 · Cited by 22

Antibody C Region Influences TGN1412-like Functional Activity In Vitro

Ball, C., Fox, B. J., Hufton, S. E., Sharp, G., Poole, S., Stebbings, R., Eastwood, D., Findlay, L., Parren, P. W. H. I., Thorpe, R., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201795 · Cited by 22

Development 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

Influence of disulfide bond isoforms on drug conjugation sites in cysteine-linked IgG2 antibody-drug conjugates

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Anticorps thérapeutiques et dérivés : une palette de structures pour une pléthore d’indications

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Middle Level IM–MS and CIU Experiments for Improved Therapeutic Immunoglobulin Subclass Fingerprinting

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Development of a Novel, Fully Human, Anti-PCSK9 Antibody with Potent Hypolipidemic Activity by Utilizing Phage Display-Based Strategy

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Non–antigen-contacting region of an asymmetric bispecific antibody to factors IXa/X significantly affects factor VIII-mimetic activity

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The Properties of Cysteine-Conjugated Antibody-Drug Conjugates Are Impacted by the IgG Subclass

Datta‐Mannan, A., Choi, H., Stokell, D. J., Tang, J. X., Murphy, A., Wrobleski, A. D., & Feng, Y. (2018) · The AAPS Journal · doi:10.1208/s12248-018-0263-0 · Cited by 20

Non-targeted characterization of attributes affecting antibody-FcγRIIIa V158 (CD16a) binding via online affinity chromatography-mass spectrometry

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Characterization of IgG2 Disulfide Bonds with LC/MS/MS and Postcolumn Online Reduction

Liu, H., Lei, Q. P., & Washabaugh, M. W. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04368 · Cited by 19

Development issues: antibody stability, developability, immunogenicity, and comparability

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Rapid and refined separation of human IgG2 disulfide isomers using superficially porous particles

Wang, Q., Lacher, N. A., Muralidhara, B. K., Schlittler, M. R., Aykent, S., & Demarest, C. W. (2010) · Journal of Separation Science · doi:10.1002/jssc.201000230 · Cited by 19

Improvement of heavy and light chain assembly by modification of heavy chain constant region 1 (CH1): Application for the construction of an anti-paclitaxel fragment antigen-binding (Fab) antibody

Yusakul, G., Sakamoto, S., Tanaka, H., & Morimoto, S. (2018) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2018.10.009 · Cited by 19

IgG Structure and Function

Thomson, C. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.05002-5 · Cited by 24

One-pot stapling of interchain disulfides of antibodies using an isobutylene motif

Sun, S., Akkapeddi, P., Marques, M. C., Martínez‐Sáez, N., Torres, V. M., CORDEIRO, C. A., Boutureira, O., & Bernardes, G. J. L. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob02877j · Cited by 18

High resolution separations of charge variants and disulfide isomers of monoclonal antibodies and antibody drug conjugates using ultra-high voltage capillary electrophoresis with high electric field strength

Henley, W. H., He, Y., Mellors, J. S., Batz, N. G., Ramsey, J. M., & Jorgenson, J. W. (2017) · Journal of Chromatography A · doi:10.1016/j.chroma.2017.07.059 · Cited by 18

Rapid, automated characterization of disulfide bond scrambling and IgG2 isoform determination

Resemann, A., Liu-Shin, L. P.-Y., Tremintin, G., Malhotra, A., Fung, A., Wang, F., Ratnaswamy, G., & Suckau, D. (2018) · mAbs · doi:10.1080/19420862.2018.1512328 · Cited by 18

Rethinking the INN system for therapeutic antibodies

Pottier, J., Chastang, R., Dumet, C., & Watier, H. (2016) · mAbs · doi:10.1080/19420862.2016.1255520 · Cited by 18

LC-MS characterization of antibody-based therapeutics

Robotham, A. C., & Kelly, J. F. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-103019-6.00001-1 · Cited by 17

Evolution of Mass Spectrometers for High m/z Biological Ion Formation, Transmission, Analysis and Detection: A Personal Perspective

Campuzano, I. D. G., & Loo, J. A. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00348 · Cited by 20

Current status and future prospects for ion-mobility mass spectrometry in the biopharmaceutical industry

Skeene, K., Khatri, K., Soloviev, Z., & Lapthorn, C. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140697 · Cited by 18

Protected hinge in the immunoglobulin G2‐A2 disulfide isoform

Liu, D., Chou, R., Dillon, T. M., Poppe, L., Spahr, C. S., Shi, S. D. ‐., & Flynn, G. C. (2014) · Protein Science · doi:10.1002/pro.2557 · Cited by 16

Reversed-phase chromatography with large pore superficially porous particles for high throughput immunoglobulin G 2 disulfide isoform separation

Wei, B., Zhang, B., Boyes, B. E., & Zhang, Y. T. (2017) · Journal of Chromatography A · doi:10.1016/j.chroma.2017.10.040 · Cited by 16

Methodology for Determining Disulfide Linkage Patterns of Closely Spaced Cysteine Residues

Zhang, B., & Cockrill, S. L. (2009) · Analytical Chemistry · doi:10.1021/ac901161e · Cited by 16

Separation Methods and Orthogonal Techniques

Michels, D. A., Ip, A. Y., Dillon, T. M., Brorson, K., Lute, S. C., Chavez, B. K., Prentice, K. M., Brady, L. J., & Miller, K. J. (2015) · ACS symposium series · doi:10.1021/bk-2015-1201.ch005 · Cited by 15

The Best IgG Subclass for the Development of Therapeutic Monoclonal Antibody Drugs and their Commercial Production: A Review

Muhammed, Y. (2020) · Immunome Research · doi:10.35248/1745-7580.20.16.173 · Cited by 15

Dynamics of Intact Immunoglobulin G Explored by Drift‐Tube Ion‐Mobility Mass Spectrometry and Molecular Modeling

Pacholarz, K. J., Porrini, M., Garlish, R. A., Burnley, R. J., Taylor, R. J., Henry, A. J., & Barran, P. E. (2014) · Angewandte Chemie · doi:10.1002/ange.201402863 · Cited by 15

Antibody Engineering

Lo, K.-M., Léger, O. J. P., & Hock, B. M. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.aid-0007-12 · Cited by 14

Stability of monoclonal antibodies (mAbs)

Shire, S. J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-08-100296-4.00003-8 · Cited by 15

Drying for Stabilization of Protein Formulations

Horn, J., Mahler, H., & Frieß, W. (2020) · doi:10.1002/9783527802104.ch4 · Cited by 15

Use of the 2D 1H-13C HSQC NMR Methyl Region to Evaluate the Higher Order Structural Integrity of Biopharmaceuticals

Hwang, T., Batabyal, D., Knutson, N., & Wikström, M. (2021) · Molecules · doi:10.3390/molecules26092714 · Cited by 14

Chemically generated IgG2 bispecific antibodies through disulfide bridging

Patterson, J. T., Gros, E., Zhou, H., Atassi, G., Kerwin, L., Carmody, L., Zhu, T., Jones, B., Fu, Y., & Kaufmann, G. F. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.07.021 · Cited by 14

Isotype Selection and Fc Engineering: Design and Construction of Fit-for-Purpose Therapeutic Antibodies

Strohl, W. R. (2011) · Modecular medicine and medicinal · doi:10.1142/9781848166295_0005 · Cited by 13

High-Throughput Mass Spectrometry for Biopharma: A Universal Modality and Target Independent Analytical Method for Accurate Biomolecule Characterization

Campuzano, I. D. G., Pelegri-O’Day, E. M., Srinivasan, N., Lippens, J. L., Egea, P. F., Umeda, A., Aral, J., Zhang, T., Laganowsky, A. D., & Netirojjanakul, C. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00138 · Cited by 13

Assessment of naturally occurring covalent and total dimer levels in human IgG1 and IgG2

Yang, J., Goetze, A. M., & Flynn, G. C. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.11.011 · Cited by 13

Reprogramming the Constant Region of Immunoglobulin G Subclasses for Enhanced Therapeutic Potency against Cancer

Kang, T. H., & Jung, S. T. (2020) · Biomolecules · doi:10.3390/biom10030382 · Cited by 14

Stability of monoclonal antibodies after simulated subcutaneous administration

Schuster, J., Mahler, H., Joerg, S., Kamuju, V., Huwyler, J., & Mathaes, R. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2021.03.007 · Cited by 13

Analytical Challenges Assessing Protein Aggregation and Fragmentation Under Physiologic Conditions

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Application of a label-free and domain-specific free thiol method in monoclonal antibody characterization

Pu, Y., Chen, Y., Nguyen, T. T. T., Xu, C., Zang, L., Sosic, Z., & Carlage, T. (2019) · Journal of Chromatography B · doi:10.1016/j.jchromb.2019.03.032 · Cited by 12

5th European Antibody Congress 2009

Beck, A., Reichert, J. M., & Wurch, T. (2010) · mAbs · doi:10.4161/mabs.2.2.11302 · Cited by 12

Fast and Efficient non-reduced Lys-C digest using pressure cycling technology for antibody disulfide mapping by LC–MS

Cheng, Y., Chen, Y., & Yu, C. (2016) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2016.07.002 · Cited by 11

Impact of antibody subclass and disulfide isoform differences on the biological activity of CD200R and βklotho agonist antibodies

Grujic, O., Stevens, J. L., Chou, R., Weiszmann, J., Sekirov, L., Thomson, C. A., Badh, A., Grauer, S., Chan, B., Graham, K. C., et al. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.03.145 · Cited by 10

Characterization of cysteine related variants in an IgG2 antibody by LC–MS with an automated data analysis approach

Zhang, Y., Bailey, R. W., Nightlinger, N. S., Gillespie, A. J., Balland, A., & Rogers, R. S. (2015) · Journal of Chromatography B · doi:10.1016/j.jchromb.2015.04.035 · Cited by 10

Quantification of protein posttranslational modifications using stable isotope and mass spectrometry

Jiang, X. G., Apostoł, I., Luo, Q., Lewis, J. K., Keener, R. N., Luo, S., Jerums, M., Zhang, X., Wypych, J., & Huang, G. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.12.004 · Cited by 10

Anti-CD20 Antibody with Multimerized Fc Domains: A Novel Strategy To Deplete B Cells and Augment Treatment of Autoimmune Disease

Zhang, X., Olsen, H. S., Chen, S., So, E. C., Zhou, H., Burch, E. E., Mérigeon, E. Y., Block, D. S., & Strome, S. E. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1501755 · Cited by 10

Characterization of Therapeutic Proteins

Struble, E. B., Kirschbaum, N., Liu, J., Marszal, E., & Shapiro, M. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2015_5005 · Cited by 9

Human Fc receptor-like 5 distinguishes IgG2 disulfide isoforms and deamidated charge variants

Alabi, O., Dement-Brown, J., & Tolnay, M. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.10.020 · Cited by 10

Engineering a human IgG2 antibody stable at low pH

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