Characterization of mAb size heterogeneity originating from a cysteine to tyrosine substitution using denaturing and native LC-MS.

[1]  Patrick K. Quoika,et al.  Structural mechanism of Fab domain dissociation as a measure of interface stability , 2023, Journal of Computer-Aided Molecular Design.

[2]  G. Walsh,et al.  Biopharmaceutical benchmarks 2022 , 2022, Nature biotechnology.

[3]  Hsin-Jung Li,et al.  Development of therapeutic antibodies for the treatment of diseases , 2022, Molecular Biomedicine.

[4]  P. Dalby,et al.  The global landscape of approved antibody therapies , 2022, Antibody therapeutics.

[5]  Weichen Xu,et al.  Monoclonal antibody sequence variants disguised as fragments: identification, characterization, and their removal by purification process optimization. , 2022, Journal of pharmaceutical sciences.

[6]  K. Sandra,et al.  Similarity demonstrated between isolated charge variants of MB02, a biosimilar of bevacizumab, and Avastin® following extended physicochemical and functional characterization. , 2022, Biologicals : journal of the International Association of Biological Standardization.

[7]  A. Heck,et al.  High-Resolution Native Mass Spectrometry , 2021, Chemical reviews.

[8]  Katsuyoshi Yamazaki,et al.  Identification and characterization of a monoclonal antibody variant species with a clipping in the complementarity determining region isolated by size exclusion chromatography under native conditions. , 2021, Journal of pharmaceutical sciences.

[9]  Asher Mullard.  FDA approves 100th monoclonal antibody product , 2021, Nature Reviews Drug Discovery.

[10]  W. Sandoval,et al.  Denaturing and Native Mass Spectrometric Analytics for Biotherapeutic Drug Discovery Research: Historical, Current, and Future Personal Perspectives. , 2021, Journal of the American Society for Mass Spectrometry.

[11]  Matthew T. Aspelund,et al.  Characterization and monitoring of a novel light-heavy-light chain mispair in a therapeutic bispecific antibody. , 2021, Journal of pharmaceutical sciences.

[12]  A. Hunter,et al.  Identification of a CE-SDS shoulder peak as disulfide-linked fragments from common CH2 cleavages in IgGs and IgG-like bispecific antibodies , 2021, mAbs.

[13]  M. Taverna,et al.  Investigation of monoclonal antibody dimers in a final formulated drug by separation techniques coupled to native mass spectrometry , 2020, mAbs.

[14]  Weichen Xu,et al.  Identification and characterization of an IgG sequence variant with an 11 kDa heavy chain C-terminal extension using a combination of mass spectrometry and high-throughput sequencing analysis , 2019, mAbs.

[15]  M. Lewis,et al.  Specific and high-resolution identification of monoclonal antibody fragments detected by capillary electrophoresis–sodium dodecyl sulfate using reversed-phase HPLC with top-down mass spectrometry analysis , 2019, mAbs.

[16]  Douglas S Rehder,et al.  Expression vector-derived heterogeneity in a therapeutic IgG4 monoclonal antibody , 2018, mAbs.

[17]  C. Spahr,et al.  Discovery, characterization, and remediation of a C-terminal Fc-extension in proteins expressed in CHO cells , 2018, mAbs.

[18]  Anita P Liu,et al.  Characterization of product‐related low molecular weight impurities in therapeutic monoclonal antibodies using hydrophilic interaction chromatography coupled with mass spectrometry , 2018, Journal of pharmaceutical and biomedical analysis.

[19]  A. Ambrogelly,et al.  Isolation and characterization of a monoclonal antibody containing an extra heavy-light chain Fab arm , 2018, mAbs.

[20]  Reb J. Russell,et al.  Identification and quantification of signal peptide variants in an IgG1 monoclonal antibody produced in mammalian cell lines. , 2017, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

[21]  S. Jusuf,et al.  Mapping the Binding Interface in a Noncovalent Size Variant of a Monoclonal Antibody Using Native Mass Spectrometry, Hydrogen-Deuterium Exchange Mass Spectrometry, and Computational Analysis. , 2017, Journal of pharmaceutical sciences.

[22]  Zhongqi Zhang,et al.  Amino acid misincorporation in recombinant proteins. , 2017, Biotechnology advances.

[23]  Li Zang,et al.  Discovery and Characterization of Histidine Oxidation Initiated Cross-links in an IgG1 Monoclonal Antibody. , 2017, Analytical chemistry.

[24]  W. Suen,et al.  Identification and characterization of monoclonal antibody fragments cleaved at the complementarity determining region using orthogonal analytical methods. , 2017, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

[25]  J. Stracke,et al.  Assessment of disulfide and hinge modifications in monoclonal antibodies , 2017, Electrophoresis.

[26]  Tongtong Wang,et al.  Identification and characterization of a -1 reading frameshift in the heavy chain constant region of an IgG1 recombinant monoclonal antibody produced in CHO cells , 2016, mAbs.

[27]  Davy Guillarme,et al.  Chromatographic, Electrophoretic, and Mass Spectrometric Methods for the Analytical Characterization of Protein Biopharmaceuticals. , 2016, Analytical chemistry.

[28]  A. Balland,et al.  Rapid identification of an antibody DNA construct rearrangement sequence variant by mass spectrometry , 2014, mAbs.

[29]  Pat Sandra,et al.  Modern chromatographic and mass spectrometric techniques for protein biopharmaceutical characterization. , 2014, Journal of chromatography. A.

[30]  Wei Wu,et al.  Investigation of monoclonal antibody fragmentation artifacts in non-reducing SDS-PAGE. , 2013, Journal of pharmaceutical and biomedical analysis.

[31]  Trevor J. Morin,et al.  Analytical characterization of a monoclonal antibody therapeutic reveals a three-light chain species that is efficiently removed using hydrophobic interaction chromatography , 2013, mAbs.

[32]  Amy Shen,et al.  Eliminating tyrosine sequence variants in CHO cell lines producing recombinant monoclonal antibodies , 2013, Biotechnology and bioengineering.

[33]  Alain Van Dorsselaer,et al.  Characterization of therapeutic antibodies and related products. , 2013, Analytical chemistry.

[34]  P. Motchnik,et al.  Characterization of monoclonal antibody size variants containing extra light chains , 2013, mAbs.

[35]  Simon J. Henderson,et al.  Monoclonal antibody therapeutics: history and future. , 2012, Current opinion in pharmacology.

[36]  J. Zhu-Shimoni,et al.  Identification of a single base-pair mutation of TAA (Stop codon) → GAA (Glu) that causes light chain extension in a CHO cell derived IgG1 , 2012, mAbs.

[37]  A. Ambrogelly,et al.  Characterization of antibody variants during process development: The tale of incomplete processing of N-terminal secretion peptide , 2012, mAbs.

[38]  John F. Valliere-Douglass,et al.  Native intact mass determination of antibodies conjugated with monomethyl Auristatin E and F at interchain cysteine residues. , 2012, Analytical chemistry.

[39]  María Vázquez-Rey,et al.  Aggregates in monoclonal antibody manufacturing processes , 2011, Biotechnology and bioengineering.

[40]  R. Ionescu,et al.  Fragmentation of monoclonal antibodies , 2011, mAbs.

[41]  Shujun Bai,et al.  Fragmentation of a highly purified monoclonal antibody attributed to residual CHO cell protease activity. , 2011, Biotechnology and bioengineering.

[42]  Paul Chen,et al.  Control of misincorporation of serine for asparagine during antibody production using CHO cells , 2010, Biotechnology and bioengineering.

[43]  A. Raghani,et al.  Analysis of monoclonal antibody product heterogeneity resulting from alternate cleavage sites of signal peptide. , 2010, Analytical biochemistry.

[44]  M. Matsumura,et al.  Elucidation of two major aggregation pathways in an IgG2 antibody. , 2009, Journal of pharmaceutical sciences.

[45]  Gang Xiao,et al.  Identification and quantification of degradations in the Asp-Asp motifs of a recombinant monoclonal antibody. , 2008, Journal of pharmaceutical and biomedical analysis.

[46]  J. Rouvinen,et al.  Structure-based stability engineering of the mouse IgG1 Fab fragment by modifying constant domains. , 2006, Journal of molecular biology.

[47]  D. Röthlisberger,et al.  Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability. , 2005, Journal of molecular biology.

[48]  Ziping Wei,et al.  Characterization of a novel modification to monoclonal antibodies: thioether cross-link of heavy and light chains. , 2005, Analytical chemistry.

[49]  G. Wang,et al.  Variant antibody identification by peptide mapping. , 1999, Biotechnology and bioengineering.

[50]  G. Cohen,et al.  Antibody Fab assembly: the interface residues between CH1 and CL. , 1986, Molecular immunology.

[51]  C. Chothia,et al.  Domain association in immunoglobulin molecules. The packing of variable domains. , 1985, Journal of molecular biology.

[52]  D. Burton.  Immunoglobulin G: functional sites. , 1985, Molecular immunology.

[53]  K. J. Dorrington.  The structural basis for the functional versatility of immunoglobulin G1. , 1978, Canadian journal of biochemistry.

[54]  D. Brems,et al.  Active dimer of Epratuzumab provides insight into the complex nature of an antibody aggregate. , 2006, Journal of pharmaceutical sciences.

[55]  J. Tainer,et al.  Recognition and interactions controlling the assemblies of beta barrel domains. , 1986, Biophysical journal.