Characterization of outcomes of amino acid modifications using a combinatorial approach to reveal physical and structural perturbations: A case study using trastuzumab biosimilar.

[1]  J. O'mahony,et al.  Raman based chemometric model development for glycation and glycosylation real time monitoring in a manufacturing scale CHO cell bioreactor process , 2021, Biotechnology progress.

[2]  A. Rathore,et al.  Freeze thaw and lyophilization induced alteration in mAb therapeutics: Trastuzumab as a case study. , 2021, Journal of pharmaceutical and biomedical analysis.

[3]  Robin Rajan,et al.  Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials , 2021, Materials Advances.

[4]  A. Rathore,et al.  An application of Nano Differential Scanning Fluorimetry for Higher Order Structure assessment between mAb originator and biosimilars: Trastuzumab and Rituximab as case studies. , 2020, Journal of pharmaceutical and biomedical analysis.

[5]  A. Ishii‐Watabe,et al.  Establishment of a highly precise multi-attribute method for the characterization and quality control of therapeutic monoclonal antibodies , 2020, Bioengineered.

[6]  B. Ruotolo,et al.  Assessment of biosimilarity under native and heat-stressed conditions: rituximab, bevacizumab, and trastuzumab originators and biosimilars , 2019, Analytical and Bioanalytical Chemistry.

[7]  Yingda Xu,et al.  Deamidation and isomerization liability analysis of 131 clinical-stage antibodies , 2018, mAbs.

[8]  J. Prados,et al.  Study of aggregation in therapeutic monoclonal antibodies subjected to stress and long-term stability tests by analyzing size exclusion liquid chromatographic profiles. , 2018, International journal of biological macromolecules.

[9]  M. Hammel,et al.  Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. , 2018, Structure.

[10]  F. Bauss,et al.  Assessment of susceptible chemical modification sites of trastuzumab and endogenous human immunoglobulins at physiological conditions , 2018, Communications Biology.

[11]  Jihun Lee,et al.  Evaluation of analytical similarity between trastuzumab biosimilar CT-P6 and reference product using statistical analyses , 2018, mAbs.

[12]  M. Lewis,et al.  Quantitative analysis of glycation and its impact on antigen binding , 2018, mAbs.

[13]  H. Beck,et al.  Oxidation of M252 but not M428 in hu-IgG1 is responsible for decreased binding to and activation of hu-FcγRIIa (His131). , 2017, Biologicals : journal of the International Association of Biological Standardization.

[14]  Hongcheng Liu,et al.  Forced degradation of recombinant monoclonal antibodies: A practical guide , 2017, mAbs.

[15]  John F. Carpenter,et al.  Some Lessons Learned From a Comparison Between Sedimentation Velocity Analytical Ultracentrifugation and Size Exclusion Chromatography to Characterize and Quantify Protein Aggregates. , 2017, Journal of pharmaceutical sciences.

[16]  Y. Zhang,et al.  Glycation of antibodies: Modification, methods and potential effects on biological functions , 2017, mAbs.

[17]  T. Jain,et al.  Rapid assessment of oxidation via middle-down LCMS correlates with methionine side-chain solvent-accessible surface area for 121 clinical stage monoclonal antibodies , 2017, mAbs.

[18]  I. E. Sánchez,et al.  Prediction of Spontaneous Protein Deamidation from Sequence-Derived Secondary Structure and Intrinsic Disorder , 2015, PloS one.

[19]  W. Jiskoot,et al.  Small Amounts of Sub-Visible Aggregates Enhance the Immunogenic Potential of Monoclonal Antibody Therapeutics , 2015, Pharmaceutical Research.

[20]  Tilman Schlothauer,et al.  Assessment of chemical modifications of sites in the CDRs of recombinant antibodies , 2014, mAbs.

[21]  Hanns-Christian Mahler,et al.  Forced degradation of therapeutic proteins. , 2012, Journal of pharmaceutical sciences.

[22]  Linda O. Narhi,et al.  Chemical Modifications in Therapeutic Protein Aggregates Generated under Different Stress Conditions , 2011, The Journal of Biological Chemistry.

[23]  Yang Wang,et al.  Impact of methionine oxidation in human IgG1 Fc on serum half-life of monoclonal antibodies. , 2011, Molecular immunology.

[24]  H. Cölfen,et al.  Analytical ultracentrifugation of colloids. , 2010, Nanoscale.

[25]  Aditya A Wakankar,et al.  Physicochemical stability of the antibody-drug conjugate Trastuzumab-DM1: changes due to modification and conjugation processes. , 2010, Bioconjugate chemistry.

[26]  Damian Houde,et al.  Post-translational Modifications Differentially Affect IgG1 Conformation and Receptor Binding* , 2010, Molecular & Cellular Proteomics.

[27]  W. Ens,et al.  Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis. , 2006, Analytical chemistry.

[28]  Thomas R. Slaney,et al.  Unique impacts of methionine oxidation, tryptophan oxidation and asparagine deamidation on antibody stability and aggregation. , 2019, Journal of pharmaceutical sciences.

[29]  Min Huang,et al.  An Industry Perspective on Forced Degradation Studies of Biopharmaceuticals: Survey Outcome and Recommendations. , 2019, Journal of pharmaceutical sciences.

[30]  Patrick G. Swann,et al.  A View on the Importance of “Multi-Attribute Method” for Measuring Purity of Biopharmaceuticals and Improving Overall Control Strategy , 2017, The AAPS Journal.

[31]  Ritesh M Pabari,et al.  Physical and structural stability of the monoclonal antibody, trastuzumab (Herceptin®), intravenous solutions. , 2013, Current pharmaceutical biotechnology.