[1] Goldin A,Beckman JA,Schmidt AM,et al.AdvancedGlycation End Products:Sparking the Development ofDiabetic Vascular Injury[J].Circulation,2006,114(6):597-605.
[2] Monnier VM,Sell DR,Genuth S.Glycation Products asMarkers and Predictors of the Progression of DiabeticComplications[J].Ann N Y Acad Sci,2005,1043(1):567-581.
[3] Agarwal N,Mason A,Pradhan R,et al.Kinetic Modeling asa Tool to Understand the Influence of Cell Culture ProcessParameters on the Glycation of Monoclonal AntibodyBiotherapeutics[J].Biotechnol Prog,2019,35(5):e2865.
[4] Jacobitz AW,Dykstra AB,Spahr C,et al.Effects of BufferComposition on Site-Specific Glycation of Lysine Residuesin Monoclonal Antibodies[J].J Pharm Sci,2020,109(1):293-300.
[5] Awotwe-Otoo D,Agarabi C,Read EK,et al.Product andProcess Understanding to Relate the Effect of FreezingMethod on Glycation and Aggregation of LyophilizedMonoclonal Antibody Formulations[J].Int J Pharm,2015,490(1-2):341-350.
[6] Mo J,Jin R,Yan Q,et al.Quantitative Analysis of Glycationand Its Impact on Antigen Binding[J].mAbs,2018,10(3):406-415.
[7] Vlasak J,Ionescu R.Heterogeneity of MonoclonalAntibodies Revealed by Charge-Sensitive Methods[J].CurrPharm Biotechnol,2008,9(6):468-481.
[8] Quan C,Alcala E,Petkovska I,et al.A Study in Glycationof a Therapeutic Recombinant Humanized MonoclonalAntibody:Where It Is,How It Got There,and How It AffectsCharge-Based Behavior[J].Analytical Biochemistry,2008,373(2):179-191.
[9] Miller AK,Hambly DM,Kerwin BA,et al.Characterizationof Site-Specific Glycation During Process Developmentof a Human Therapeutic Monoclonal Antibody[J].Journalof Pharmaceutical Sciences,2011,100(7):2543-2550.
[10] Gadgil HS,Bondarenko PV,Pipes G,et al.The Lc/Ms Analysis of Glycation of Igg Molecules in SucroseContaining Formulations[J].Journal of PharmaceuticalSciences,2007,96(10):2607-2621.
[11] Zhang B,Yang Y,Yuk I,et al.Unveiling a Glycation HotSpot in a Recombinant Humanized Monoclonal Antibody[J].Analytical Chemistry,2008,80(7):2379-2390.
[12] Chung S,Tian J,Tan Z,et al.Modulating Cell CultureOxidative Stress Reduces Protein Glycation and AcidicCharge Variant Formation[J].mAbs,2019,11(1):205-216.
[13] Venkatraman J,Aggarwal K,Balaram P.Helical PeptideModels for Protein Glycation:Proximity Effects in Catalysisof the Amadori Rearrangement[J].Chemistry & Biology,2001,8(7):611-625.
[14] Gstottner C,Reusch D,Haberger M,et al.MonitoringGlycation Levels of a Bispecific Monoclonal Antibody atSubunit Level by Ultrahigh-Resolution Maldi Ft-Icr MassSpectrometry[J].mAbs,2020,12(1):1682403.
[15] Fischer S,Hoernschemeyer J,Mahler HC.GlycationDuring Storage and Administration of Monoclonal AntibodyFormulations[J].Eur J Pharm Biopharm,2008,70(1):42-50.
[16] Brady LJ,Martinez T,Balland A.Characterization ofNonenzymatic Glycation on a Monoclonal Antibody[J].AnalChem,2007,79(24):9403-9413.
[17] Wei B,Berning K,Quan C,et al.Glycation of Antibodies:Modification,Methods and Potential Effects on BiologicalFunctions[J].mAbs,2017,9(4):586-594.
[18] Madren S,McElroy W,Schultz-Kuszak K,et al.GlobalIntercompany Assessment of Icief Platform Comparabilityfor the Characterization of Therapeutic Proteins[J].Electrophoresis,2022,43(9-10):1050-1058.
[19] Schmailzl J,Vorage MW,Stutz H.Intact and MiddleDown Cief of Commercial Therapeutic MonoclonalAntibody Products under Non-Denaturing Conditions[J].Electrophoresis,2020,41(12):1109-1117.
[20] Baran K,Zimoch P,Stanczak A,et al.Separation of ChargeVariants of a Monoclonal Antibody by Overloaded IonExchange Chromatography[J].Journal of chromatography,2021,1658:462607.
[21] Meyer RM,Berger L,Nerkamp J,et al.Identification ofMonoclonal Antibody Variants Involved in AggregateFormation-Part 1:Charge Variants[J].Eur J PharmBiopharm,2021,158:123-131.
[22] Banks DD,Hambly DM,Scavezze JL,et al.The Effect ofSucrose Hydrolysis on the Stability of Protein TherapeuticsDuring Accelerated Formulation Studies[J].Journal ofPharmaceutical Sciences,2009,98(12):4501-4510.
[23] Butko M,Pallat H,Cordoba A,et al.RecombinantAntibody Color Resulting from Advanced Glycation EndProduct Modifications[J].Analytical Chemistry,2014,86(19):9816-9823.
[24] Kennedy DM,Skillen AW,Self CH.Glycation ofMonoclonal Antibodies Impairs Their Ability to BindAntigen[J].Clinical and Experimental Immunology,1994,98(2):245-251.
[25] Ahmad S,Moinuddin,Ali A.Immunological Studies on Glycated Human Igg[J].Life Sciences,2012,90(25-26):980-987.
[26] Newkirk MM,Goldbach-Mansky R,Lee J,et al.AdvancedGlycation End-Product(Age)-Damaged Igg and IgmAutoantibodies to Igg-Age in Patients with Early Synovitis[J].Arthritis Research & Therapy,2003,5(2):R82-90.
[27] Ligier S,Fortin PR,Newkirk MM.A New Antibody inRheumatoid Arthritis Targeting Glycated Igg:Igm AntiIgg-Age[J].British Journal of Rheumatology,1998,37(12):1307-1314.
[28] Bosley A,Cook K,Lin S,et al.Improved ProcessIntermediate Stability through the Identification andElimination of Reactive Glycation Residues-a MonoclonalAntibody Case Study[J].Bioengineered,2022,13(6):14402-14412.
[29] Faid V,Leblanc Y,Berger M,et al.C-TerminalLysine Clipping of Igg1:Impact on Binding to HumanFcgammariiia and Neonatal Fc Receptors[J].Eur J PharmSci,2021,159:105730.
[30] Kaur H.Characterization of Glycosylation in MonoclonalAntibodies and Its Importance in Therapeutic AntibodyDevelopment[J].Critical Reviews in Biotechnology,2021,41(2):300-315.
[31] Mimura Y,Saldova R,Mimura-Kimura Y,et al.Importanceand Monitoring of Therapeutic Immunoglobulin GGlycosylation[J].Experientia Supplementum,2021,112:481-517.