{"product_id":"co-and-post-translational-modifications-of-therapeutic-antibodies-and-proteins-isbn-9781119053316","title":"Co- and Post-Translational Modifications of Therapeutic Antibodies and Proteins","description":"\u003cp\u003e\u003cb\u003eA Comprehensive Guide to Crucial Attributes of Therapeutic Proteins in Biological Pharmaceuticals\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eWith this book, Dr. Raju offers a valuable resource for professionals involved in research and development of biopharmaceutical and biosimilar drugs. This is a highly relevant work, as medical practitioners have increasingly turned to biopharmaceutical medicines in their search for safe and reliable treatments for complex diseases, while pharmaceutical researchers seek to expand the availability of biopharmaceuticals and create more affordable biosimilar alternatives. \u003c\/p\u003e \u003cp\u003eReaders receive a thorough overview of the major co-translational modifications (CTMs) and post-translational modifications (PTMs) of therapeutic proteins relevant to the development of biotherapeutics. The majority of chapters detail individual CTMs and PTMs that may affect the physicochemical, biochemical, biological, pharmacokinetic, immunological, toxicological etc. properties of proteins. In addition, readers are guided on the methodology necessary to analyze and characterize these modifications. Thus, readers gain not only an understanding of CTMs\/PTMs, but also the ability to design and assess their own structure-function studies for experimental molecules. Specific features and topics include: \u003c\/p\u003e \u003cul\u003e \u003cli\u003eDiscussion of the research behind and expansion of biopharmaceuticals\u003c\/li\u003e \u003cli\u003eTwenty chapters detailing relevant CTMs and PTMs of proteins, such as glycosylation, oxidation, phosphorylation, methylation, proteolysis, etc.\u003c\/li\u003e \u003cli\u003eEach chapter offers an introduction and guide to the mechanisms and biological significance of an individual CTM or PTM, including practical guidance for experiment design and analysis\u003c\/li\u003e \u003cli\u003eAn appendix of biologic pharmaceuticals currently on the market, along with an assessment of their PTMs and overall safety and efficacy\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eThis volume will prove a key reference on the shelves of industry and academic researchers involved in the study and development of biochemistry, molecular biology, biopharmaceuticals and proteins in medicine, particularly as biopharmaceuticals and biosimilars become ever more prominent tools in the field of healthcare.\u003c\/p\u003e \u003cp\u003ePreface xv\u003c\/p\u003e \u003cp\u003eAbout the Author xix\u003c\/p\u003e \u003cp\u003eAbbreviations xxi\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction to Co- and Post-translational Modifications of Proteins \u003c\/b\u003e\u003cb\u003e1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eBrief Introductions to Individual Chapters 8\u003c\/p\u003e \u003cp\u003eChapter 2: Acetylation of Proteins 8\u003c\/p\u003e \u003cp\u003eChapter 3: C-Terminal Lys or Arg Clipping of Proteins 8\u003c\/p\u003e \u003cp\u003eChapter 4: Cysteinylation of Proteins 8\u003c\/p\u003e \u003cp\u003eChapter 5: Deamidation of Proteins 8\u003c\/p\u003e \u003cp\u003eChapter 6: Glycation of Proteins 9\u003c\/p\u003e \u003cp\u003eChapter 7: Glycosylation of Proteins 9\u003c\/p\u003e \u003cp\u003eChapter 8: N-glycosylation of Proteins 9\u003c\/p\u003e \u003cp\u003eChapter 9: O-glycosylation of Proteins 10\u003c\/p\u003e \u003cp\u003eChapter 10: Hydroxylation of Proteins 10\u003c\/p\u003e \u003cp\u003eChapter 11: Methylation of Proteins 10\u003c\/p\u003e \u003cp\u003eChapter 12: Oxidation of Proteins 11\u003c\/p\u003e \u003cp\u003eChapter 13: Phosphorylation of Proteins 11\u003c\/p\u003e \u003cp\u003eChapter 14: Prenylation of Proteins 11\u003c\/p\u003e \u003cp\u003eChapter 15: Proteolysis of Proteins 11\u003c\/p\u003e \u003cp\u003eChapter 16: Selenylation of Proteins 12\u003c\/p\u003e \u003cp\u003eChapter 17: Signal Peptides of Proteins 12\u003c\/p\u003e \u003cp\u003eChapter 18: Sulfation of Proteins and Glycoproteins 12\u003c\/p\u003e \u003cp\u003eChapter 19: SUMOylation 12\u003c\/p\u003e \u003cp\u003eChapter 20: Ubiquitination 13\u003c\/p\u003e \u003cp\u003eChapter 21: Other PTMs 13\u003c\/p\u003e \u003cp\u003eReferences 13\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Acetylation of Proteins \u003c\/b\u003e\u003cb\u003e17\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 17\u003c\/p\u003e \u003cp\u003eMechanism of N-acetylation at the N-termini of Proteins 19\u003c\/p\u003e \u003cp\u003eMechanism of N-acetylation and N-deacetylation of Lysine Residues 21\u003c\/p\u003e \u003cp\u003eMechanism of O-acetylation of Sugar Residues 21\u003c\/p\u003e \u003cp\u003eBiological Significance of Protein Acetylation 22\u003c\/p\u003e \u003cp\u003eAcetylation in Recombinant Therapeutic Proteins 23\u003c\/p\u003e \u003cp\u003eMethods to Analyze Acetylation in Proteins and Carbohydrates 23\u003c\/p\u003e \u003cp\u003eReferences 24\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 C-terminal Lys or Arg Clipping in Proteins \u003c\/b\u003e\u003cb\u003e31\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 31\u003c\/p\u003e \u003cp\u003eBiological Significance of C-terminal Lys or Arg Clipping in Proteins 31\u003c\/p\u003e \u003cp\u003eAnalysis of C-terminal Lys or Arg Clipping in Proteins 32\u003c\/p\u003e \u003cp\u003eReferences 32\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Cysteinylation of Proteins \u003c\/b\u003e\u003cb\u003e35\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 35\u003c\/p\u003e \u003cp\u003eBiological Significance of Cysteinylation of Proteins 35\u003c\/p\u003e \u003cp\u003eCysteinylation and Trisulfide Bonds in Recombinant Therapeutic Proteins 36\u003c\/p\u003e \u003cp\u003eAnalysis of Cysteinylation of Proteins 36\u003c\/p\u003e \u003cp\u003eReferences 37\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Deamidation of Proteins \u003c\/b\u003e\u003cb\u003e39\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 39\u003c\/p\u003e \u003cp\u003eMechanism of Deamidation of Proteins 40\u003c\/p\u003e \u003cp\u003ePhysicochemical Characteristics of Deamidated Proteins 42\u003c\/p\u003e \u003cp\u003eBiological Significance of Deamidation of Proteins 43\u003c\/p\u003e \u003cp\u003eDeamidation and Immunogenicity 43\u003c\/p\u003e \u003cp\u003eDeamidation and Pharmacokinetics Properties of Proteins 44\u003c\/p\u003e \u003cp\u003eDeamidation in Recombinant Therapeutic Proteins 44\u003c\/p\u003e \u003cp\u003eMethods for the Analysis of Deamidation in Proteins 44\u003c\/p\u003e \u003cp\u003eReferences 45\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Glycation of Proteins \u003c\/b\u003e\u003cb\u003e51\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 51\u003c\/p\u003e \u003cp\u003eMechanism of Protein Glycation 52\u003c\/p\u003e \u003cp\u003eGlycation of Proteins in Human 54\u003c\/p\u003e \u003cp\u003eProtein Glycation and Human Diseases 55\u003c\/p\u003e \u003cp\u003eGlycation in Recombinant Therapeutic Proteins 56\u003c\/p\u003e \u003cp\u003eMethods to Analyze Protein Glycation 57\u003c\/p\u003e \u003cp\u003eReferences 58\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Glycosylation of Proteins \u003c\/b\u003e\u003cb\u003e63\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 63\u003c\/p\u003e \u003cp\u003eGlycans and Aglycans 64\u003c\/p\u003e \u003cp\u003eGlycosidic Bonds 64\u003c\/p\u003e \u003cp\u003eAldoses and Ketoses 66\u003c\/p\u003e \u003cp\u003eAnomeric Groups: α- and β-Configurations 69\u003c\/p\u003e \u003cp\u003eNatural Diversity of Glycans 70\u003c\/p\u003e \u003cp\u003eGlycans and Enzymes 71\u003c\/p\u003e \u003cp\u003eN-glycosylation 71\u003c\/p\u003e \u003cp\u003eO-glycosylation 72\u003c\/p\u003e \u003cp\u003ePhospho-Serine Glycosylation 72\u003c\/p\u003e \u003cp\u003eGPI-Anchors (Glypiation) 72\u003c\/p\u003e \u003cp\u003eC-mannosylation 73\u003c\/p\u003e \u003cp\u003eReferences 73\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 N-glycosylation of Proteins \u003c\/b\u003e\u003cb\u003e77\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 77\u003c\/p\u003e \u003cp\u003eMechanism of N-glycosylation of Proteins 81\u003c\/p\u003e \u003cp\u003eBiosynthesis of \u003ci\u003eN\u003c\/i\u003e-Glycans 81\u003c\/p\u003e \u003cp\u003eBiosynthesis of Lipid-linked Precursor Oligosaccharide 81\u003c\/p\u003e \u003cp\u003eEn Bloc Transfer of the Precursor Oligosaccharide to Nascent Polypeptide Chain 82\u003c\/p\u003e \u003cp\u003eProcessing of the Glycan 82\u003c\/p\u003e \u003cp\u003eAdditional Processing of Oligosaccharide Unit for Chain Elongation and\/or Modifications 83\u003c\/p\u003e \u003cp\u003eMicroheterogeneity of \u003ci\u003eN\u003c\/i\u003e-Glycans 84\u003c\/p\u003e \u003cp\u003eSpecies-Specific N-glycosylation 85\u003c\/p\u003e \u003cp\u003eFunctions of \u003ci\u003eN\u003c\/i\u003e-glycans 87\u003c\/p\u003e \u003cp\u003ePhysicochemical Functions of \u003ci\u003eN\u003c\/i\u003e-glycans 87\u003c\/p\u003e \u003cp\u003eBiological Functions of \u003ci\u003eN\u003c\/i\u003e-glycans 88\u003c\/p\u003e \u003cp\u003eImpact of \u003ci\u003eN\u003c\/i\u003e-Glycans on Pharmacokinetic Properties of Proteins 88\u003c\/p\u003e \u003cp\u003e\u003ci\u003eN\u003c\/i\u003e-Glycans and Human Diseases 89\u003c\/p\u003e \u003cp\u003eN-glycosylation of RTPs 89\u003c\/p\u003e \u003cp\u003eMethods to Analyze \u003ci\u003eN\u003c\/i\u003e-Glycans 90\u003c\/p\u003e \u003cp\u003eReferences 92\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 O-glycosylation of Proteins \u003c\/b\u003e\u003cb\u003e101\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 101\u003c\/p\u003e \u003cp\u003eBiosynthesis of O-Glycans 103\u003c\/p\u003e \u003cp\u003eBiosynthesis of Mucin Type O-Glycans 103\u003c\/p\u003e \u003cp\u003eBiosynthesis of O-linked GlcNAc on Proteins 105\u003c\/p\u003e \u003cp\u003eBiosynthesis of O-linked Fucose on Proteins 106\u003c\/p\u003e \u003cp\u003eBiosynthesis of O-linked Glc Residues 107\u003c\/p\u003e \u003cp\u003eBiosynthesis of O-linked Gal Residues 107\u003c\/p\u003e \u003cp\u003eBiosynthesis of O-linked Man Residues 107\u003c\/p\u003e \u003cp\u003eO-Glycans on Hydroxyproline Residues 108\u003c\/p\u003e \u003cp\u003ePhysicochemical Properties of O-Glycosylated Proteins 108\u003c\/p\u003e \u003cp\u003eBiological Functions of O-Glycans 108\u003c\/p\u003e \u003cp\u003eO-glycosylation in RTPs 110\u003c\/p\u003e \u003cp\u003eAnalysis of O-Glycans 111\u003c\/p\u003e \u003cp\u003eReferences 113\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Hydroxylation of Proteins \u003c\/b\u003e\u003cb\u003e119\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 119\u003c\/p\u003e \u003cp\u003eMechanism of Hydroxylation 120\u003c\/p\u003e \u003cp\u003eMechanism of Hydroxylation in Organic Molecules 120\u003c\/p\u003e \u003cp\u003eMechanism of Hydroxylation in Biomolecules 121\u003c\/p\u003e \u003cp\u003eProlyl 4-Hydroxylase 123\u003c\/p\u003e \u003cp\u003eProlyl 3-Hydroxylase 123\u003c\/p\u003e \u003cp\u003eLysyl 5-Hydroxylase 123\u003c\/p\u003e \u003cp\u003ePhenylalanine Hydroxylase 123\u003c\/p\u003e \u003cp\u003eTyrosine Hydroxylase 124\u003c\/p\u003e \u003cp\u003eBiological Significance of Hydroxylation 124\u003c\/p\u003e \u003cp\u003eHydroxylation in RTPs 126\u003c\/p\u003e \u003cp\u003eAnalysis of Hydroxylation 126\u003c\/p\u003e \u003cp\u003eReferences 127\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Methylation of Proteins \u003c\/b\u003e\u003cb\u003e133\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 133\u003c\/p\u003e \u003cp\u003eMechanism of Protein Methylation 135\u003c\/p\u003e \u003cp\u003eChemical Methylation Reactions 135\u003c\/p\u003e \u003cp\u003eBiological Methylation Reactions 135\u003c\/p\u003e \u003cp\u003eMethylation of Arg Residues 135\u003c\/p\u003e \u003cp\u003eMethylation of Lys Residues 137\u003c\/p\u003e \u003cp\u003eMethylation of Prenylcysteine Residues 137\u003c\/p\u003e \u003cp\u003eMethylation of Protein Phosphatase 2A 137\u003c\/p\u003e \u003cp\u003eMethylation of Isoaspartyl Residues 138\u003c\/p\u003e \u003cp\u003eO-Methylation of Sugar Residues 138\u003c\/p\u003e \u003cp\u003ePhysicochemical and Biological Significance of Methylation of Proteins 139\u003c\/p\u003e \u003cp\u003eMethylation in RTPs 140\u003c\/p\u003e \u003cp\u003eMethods to Analyze Methylation in Proteins and Glycoproteins 140\u003c\/p\u003e \u003cp\u003eReferences 141\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Oxidation of Proteins \u003c\/b\u003e\u003cb\u003e147\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 147\u003c\/p\u003e \u003cp\u003eMechanism of Protein Oxidation 149\u003c\/p\u003e \u003cp\u003eMethionine (Met) Oxidation 149\u003c\/p\u003e \u003cp\u003eCysteine (Cys) Oxidation 150\u003c\/p\u003e \u003cp\u003eTryptophan (Trp) Oxidation 151\u003c\/p\u003e \u003cp\u003eTyrosine (Tyr) Oxidation 153\u003c\/p\u003e \u003cp\u003eOxidation of Other Amino Acid Residues and Protein Backbone 155\u003c\/p\u003e \u003cp\u003eOxidation in RTPs 155\u003c\/p\u003e \u003cp\u003eMet Oxidation in mAbs 157\u003c\/p\u003e \u003cp\u003eAnalytical Methods to Measure Protein Oxidation 157\u003c\/p\u003e \u003cp\u003eReferences 158\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Phosphorylation of Proteins \u003c\/b\u003e\u003cb\u003e163\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 163\u003c\/p\u003e \u003cp\u003eMechanism of Protein Phosphorylation in Living Cells 164\u003c\/p\u003e \u003cp\u003eMg\u003csup\u003e2+\u003c\/sup\u003e Mediated Mechanism of Protein Phosphorylation 165\u003c\/p\u003e \u003cp\u003eProtein Kinase-Based Mechanism of Protein Phosphorylation 166\u003c\/p\u003e \u003cp\u003eMechanism of Dephosphorylation of Proteins by Phosphatases 166\u003c\/p\u003e \u003cp\u003eProtein Kinases 167\u003c\/p\u003e \u003cp\u003eSerine Kinases 167\u003c\/p\u003e \u003cp\u003eTyrosine Kinases 168\u003c\/p\u003e \u003cp\u003ePhysicochemical and Biological Functions of Protein Phosphorylation 169\u003c\/p\u003e \u003cp\u003ePhosphorylation in RTPs 169\u003c\/p\u003e \u003cp\u003eMethods to Analyze Protein Phosphorylation 170\u003c\/p\u003e \u003cp\u003eGel Electrophoresis 170\u003c\/p\u003e \u003cp\u003eMass Spectrometry 171\u003c\/p\u003e \u003cp\u003eEnrichment of Phosphoproteins 171\u003c\/p\u003e \u003cp\u003eEnrichment of Phosphorylated Peptides 171\u003c\/p\u003e \u003cp\u003eReferences 171\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Prenylation of Proteins \u003c\/b\u003e\u003cb\u003e177\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 177\u003c\/p\u003e \u003cp\u003eMechanism of Protein Prenylation 177\u003c\/p\u003e \u003cp\u003eBiological Significance of Prenylation of Proteins 179\u003c\/p\u003e \u003cp\u003eAnalysis of Prenylation of Proteins 179\u003c\/p\u003e \u003cp\u003eReferences 179\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Proteolysis of Proteins \u003c\/b\u003e\u003cb\u003e183\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 183\u003c\/p\u003e \u003cp\u003eChemical Proteolysis 184\u003c\/p\u003e \u003cp\u003eEnzymatic Proteolysis 185\u003c\/p\u003e \u003cp\u003eBiological Significance of Proteolysis 187\u003c\/p\u003e \u003cp\u003ePost-translational Processing of Proteins by Proteolysis 187\u003c\/p\u003e \u003cp\u003eIntracellular and Extracelluar Degradation of Proteins by Proteases 189\u003c\/p\u003e \u003cp\u003eProteolysis and Food Digestion 190\u003c\/p\u003e \u003cp\u003eRole of Proteases in Apoptosis 190\u003c\/p\u003e \u003cp\u003eRole of Proteolysis in Human Diseases 191\u003c\/p\u003e \u003cp\u003eUse of Proteases in Laboratories 191\u003c\/p\u003e \u003cp\u003eSources of Proteases 193\u003c\/p\u003e \u003cp\u003eProteolysis in RTPs 193\u003c\/p\u003e \u003cp\u003eChemical Proteolysis in RTPs 193\u003c\/p\u003e \u003cp\u003eEnzymatic Proteolysis in RTPs 194\u003c\/p\u003e \u003cp\u003eAnalytical Methods for the Detection of Proteolysis of Proteins 195\u003c\/p\u003e \u003cp\u003eReferences 196\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Selenylation \u003c\/b\u003e\u003cb\u003e203\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 203\u003c\/p\u003e \u003cp\u003eBiological Significance of Selenylation of Proteins 203\u003c\/p\u003e \u003cp\u003eReferences 205\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Signal Peptides \u003c\/b\u003e\u003cb\u003e207\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 207\u003c\/p\u003e \u003cp\u003eBiological Significance of Signal Peptides 207\u003c\/p\u003e \u003cp\u003eSignal Peptides in RTPs 208\u003c\/p\u003e \u003cp\u003eReferences 208\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Sulfation of Proteins and Glycoproteins \u003c\/b\u003e\u003cb\u003e211\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 211\u003c\/p\u003e \u003cp\u003eBiosynthesis of PAPS 212\u003c\/p\u003e \u003cp\u003eSulfation Reactions in the Cytosol 213\u003c\/p\u003e \u003cp\u003eSulfation in the Golgi Compartments 215\u003c\/p\u003e \u003cp\u003eSulfation of Tyrosine Residues 215\u003c\/p\u003e \u003cp\u003eMechanism of Tyrosine Sulfation 216\u003c\/p\u003e \u003cp\u003eBiological Functions of Tyr Sulfation 216\u003c\/p\u003e \u003cp\u003eSulfation of Glycosaminoglycans (GAGs) and Proteoglycans 217\u003c\/p\u003e \u003cp\u003eBiological Functions of GAGs 219\u003c\/p\u003e \u003cp\u003eSulfation in RTPs 220\u003c\/p\u003e \u003cp\u003eAnalysis of Sulfation in Biomolecules 221\u003c\/p\u003e \u003cp\u003eAnalysis of Tyr Sulfation 222\u003c\/p\u003e \u003cp\u003eAnalysis of Sulfated Glycoconjugates 222\u003c\/p\u003e \u003cp\u003eColorimetric Methods to Analyze Sulfated Glycoconjugates 222\u003c\/p\u003e \u003cp\u003eElectrophoretic Methods to Analyze Sulfated Glycoconjugates 223\u003c\/p\u003e \u003cp\u003eChromatographic Methods to Analyze Sulfated Glycoconjugates 223\u003c\/p\u003e \u003cp\u003eAnalysis of Sulfated Glycoconjugates by Mass Spectrometry 224\u003c\/p\u003e \u003cp\u003eReferences 224\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 SUMOylation \u003c\/b\u003e\u003cb\u003e231\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 231\u003c\/p\u003e \u003cp\u003eMechanism of SUMOylation 232\u003c\/p\u003e \u003cp\u003eBiological Significance of SUMOylation 232\u003c\/p\u003e \u003cp\u003eReferences 232\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 Ubiquitination \u003c\/b\u003e\u003cb\u003e235\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 235\u003c\/p\u003e \u003cp\u003eMechanism of Ubiquitination 235\u003c\/p\u003e \u003cp\u003eBiological Significance of Ubiquitination 236\u003c\/p\u003e \u003cp\u003eReferences 236\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 Other CTMs and PTMs of Proteins \u003c\/b\u003e\u003cb\u003e239\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eAdenylylation or AMPylation 239\u003c\/p\u003e \u003cp\u003eADP-Ribosylation 239\u003c\/p\u003e \u003cp\u003eAmidation 239\u003c\/p\u003e \u003cp\u003eArginylation 240\u003c\/p\u003e \u003cp\u003eButyrylation 240\u003c\/p\u003e \u003cp\u003eCarbamylation 240\u003c\/p\u003e \u003cp\u003eCarbonylation 240\u003c\/p\u003e \u003cp\u003eγ-Carboxylation 241\u003c\/p\u003e \u003cp\u003eCitrullination 241\u003c\/p\u003e \u003cp\u003eDiphthamide 241\u003c\/p\u003e \u003cp\u003eFormylation 241\u003c\/p\u003e \u003cp\u003eGlypiation 242\u003c\/p\u003e \u003cp\u003eHypusine Formation 242\u003c\/p\u003e \u003cp\u003eIodination 242\u003c\/p\u003e \u003cp\u003eLipoylation 243\u003c\/p\u003e \u003cp\u003eMalonylation 243\u003c\/p\u003e \u003cp\u003eMyristoylation 243\u003c\/p\u003e \u003cp\u003eNeddylation 243\u003c\/p\u003e \u003cp\u003ePalmitoylation 244\u003c\/p\u003e \u003cp\u003ePolyglutamylation 244\u003c\/p\u003e \u003cp\u003ePolyglycylation 244\u003c\/p\u003e \u003cp\u003ePropionylation 245\u003c\/p\u003e \u003cp\u003ePupylation 245\u003c\/p\u003e \u003cp\u003ePyroglutamate Formation 245\u003c\/p\u003e \u003cp\u003eS-Glutathionylation 245\u003c\/p\u003e \u003cp\u003eS-Nitrosylation 247\u003c\/p\u003e \u003cp\u003eReferences 247\u003c\/p\u003e \u003cp\u003eAppendix A 253\u003c\/p\u003e \u003cp\u003eIndex 271\u003c\/p\u003e   \u003cp\u003e\u003cb\u003eT. Shantha Raju\u003c\/b\u003e has more than 20 years of experience in the research and development of biotherapeutics, including monoclonal antibodies and glycoproteins. Dr. Raju has published over 40 research articles, several reviews and book chapters and serves on the editorial boards of several leading journals.    \u003c\/p\u003e\u003cp\u003e\u003cb\u003eA Comprehensive Guide to Critical Attributes of Therapeutic Antibodies and Proteins\u003c\/b\u003e \u003c\/p\u003e\u003cp\u003eWith this book, Dr. Raju offers a valuable resource for professionals involved in research and development of biopharmaceutical and biosimilar drugs. This is a highly relevant work, as medical practitioners have increasingly turned to biopharmaceutical medicines in their search for safe and reliable treatments for complex diseases, while pharmaceutical researchers seek to expand the availability of biopharmaceuticals and create more affordable biosimilar alternatives. \u003c\/p\u003e\u003cp\u003eReaders receive a thorough overview of the major co-translational modifications (CTMs) and post-translational modifications (PTMs) of therapeutic proteins relevant to the development of biotherapeutics. The majority of chapters detail individual CTMs and PTMs that may affect the physicochemical, biochemical, biological, pharmacokinetic, immunological, toxicological etc. properties of proteins. In addition, readers are guided on the methodology necessary to analyze and characterize these modifications. Thus, readers gain not only an understanding of CTMs\/PTMs, but also the ability to design and assess their own structure-function studies for experimental molecules. Specific features and topics include: \u003c\/p\u003e\u003cul\u003e \u003cli\u003eDiscussion of the research behind and expansion of biopharmaceuticals.\u003c\/li\u003e \u003cli\u003eTwenty chapters detailing relevant CTMs and PTMs of proteins, such as glycosylation, oxidation, phosphorylation, methylation, proteolysis, etc.\u003c\/li\u003e \u003cli\u003eEach chapter offers an introduction and guide to the mechanisms and biological significance of an individual CTM or PTM, including practical guidance for experiment design and analysis.\u003c\/li\u003e \u003cli\u003eAn appendix of biologic pharmaceuticals currently on the market, along with an assessment of their PTMs and overall safety and efficacy.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eThis volume will prove to be a key reference on the shelves of industry and academic researchers involved in the study and development of biochemistry and molecular biology of proteins in medicine, particularly as biopharmaceuticals and biosimilars become ever more prominent tools in the field of healthcare.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47988937556197,"sku":"NP9781119053316","price":161.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781119053316.jpg?v=1761782126","url":"https:\/\/k12savings.com\/es\/products\/co-and-post-translational-modifications-of-therapeutic-antibodies-and-proteins-isbn-9781119053316","provider":"K12savings","version":"1.0","type":"link"}