{"text_format":"2","workbook":"xls","n_sheets":1,"sheets":["report2"],"not_rendered":{"charts":0,"images":0,"macros":0,"external_links":1,"defined_names":2,"comments":0,"pivot_tables":0},"unopened":[],"bounds":{"document_bytes":16777216,"sheet_cells":100000,"run_cost":"one","rows_first":2000,"rows_last":500,"rows_between":2000,"halvings":0,"cell_chars":16384,"cell_head_chars":4096},"cells_cut":0,"cells_raw":0,"read":"whole","date_system":"1900","formulas":"cached_only"}

{"sheet":"report2","index":0,"n_rows":42,"n_cols":5,"rows_kept":42,"cut":false,"hidden":false,"merged":[[0,2,0,3],[0,4,0,5],[1,2,1,3],[1,4,1,5],[2,2,2,3],[4,2,4,3],[5,2,5,3],[6,2,6,3],[7,2,7,3],[8,2,8,3],[11,2,11,3],[12,2,12,3],[15,2,15,3],[15,4,15,5],[16,2,16,3],[16,4,16,5],[17,2,17,3],[19,2,19,3],[20,2,20,3],[21,2,21,3],[22,2,22,3],[23,2,23,3],[29,2,29,3],[30,2,30,3],[33,2,33,3]],"flags":["formulas_cached_only"]}
[null,"1.","Record Nr.",null,"UNINA9910160267103321"]
[null,null,"Titolo",null,"Cinematic social studies : a resource for teaching and learning social studies with film / / edited by William B. Russell, III, University of Central Florida, Stewart Waters, University of Tennessee"]
[null,null,"Pubbl/distr/stampa",null,"Charlotte, NC : , : Information Age Publishing, Incorporated, , [2017]"]
[{"$nulls":4},"©2017"]
[null,null,"ISBN",null,"1-68123-735-0"]
[null,null,"Descrizione fisica",null,"1 online resource (533 pages) : illustrations"]
[null,null,"Collana",null,"Teaching and learning social studies"]
[null,null,"Disciplina",null,"300.71"]
[null,null,"Soggetti",null,"Social sciences"]
[{"$nulls":4},"Motion pictures"]
[{"$nulls":4},"Electronic books."]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Nota di bibliografia","Includes bibliographical references."]
[null,"2.","Record Nr.",null,"UNINA9910506382203321"]
[null,null,"Titolo",null,"Antibody glycosylation / / edited by Marija Pezer"]
[null,null,"Pubbl/distr/stampa",null,"Cham, Switzerland : , : Springer, , [2021]"]
[{"$nulls":4},"©2021"]
[null,null,"ISBN",null,"3-030-76912-7"]
[null,null,"Descrizione fisica",null,"1 online resource (585 pages)"]
[null,null,"Collana",null,"Experientia Supplementum Ser ; ; v.112"]
[null,null,"Disciplina",null,"571.967"]
[null,null,"Soggetti",null,"Biochemical markers"]
[{"$nulls":4},"Pharmacology"]
[{"$nulls":4},"Immunology"]
[{"$nulls":4},"Enginyeria de proteïnes"]
[{"$nulls":4},"Enginyeria bioquímica"]
[{"$nulls":4},"Llibres electrònics"]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Nota di bibliografia","Includes bibliographical references and index."]
[null,null,"Nota di contenuto",null,"Intro -- Foreword -- Contents -- Editor and Contributors -- Chapter 1: Micro-Heterogeneity of Antibody Molecules -- 1.1 Introduction -- 1.2 Disulfide Bond-Related Modifications -- 1.3 N- and C-Terminal Modifications -- 1.3.1 N-Terminal Modifications -- 1.3.2 C-Terminal Modifications -- 1.4 Chemical Modifications of Main-Chain Amino Acid Residues -- 1.4.1 Deamidation -- 1.4.2 Glycation -- 1.4.3 Oxidation -- 1.5 Aggregation -- 1.6 Glycosylation -- 1.6.1 IgG-Fc Oligosaccharide Chain -- 1.6.2 Fab Oligosaccharide Chain -- 1.7 Conclusion -- References -- Part I: Analytical Methods -- Chapter 2: Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 2.1 Introduction -- 2.1.1 Glycosylation -- 2.1.2 Immunoglobulins -- 2.2 Liquid Chromatography -- 2.2.1 Immunoglobulin Purification by Liquid Chromatography -- 2.2.1.1 Affinity Chromatography -- 2.2.1.2 Melon Gel Chromatography -- 2.2.1.3 Size-Exclusion Chromatography (SEC) -- 2.2.1.4 Ion-Exchange Chromatography (IEX) -- 2.2.2 N-Glycan Analysis by Liquid Chromatography -- 2.2.2.1 Glycan Release -- 2.2.2.2 Fluorescent Labeling Methods -- 2.2.2.3 Reducing Agent -- 2.2.2.4 Clean-Up Strategies -- 2.2.2.5 Detection of Labeled Glycans with (U)HPLC -- 2.2.2.6 N-Glycan Sequencing by Exoglycosidases -- 2.2.3 O-Glycan Analysis by Liquid Chromatography -- 2.2.4 Liquid Chromatography "]
[{"$nulls":4},"Coupled to Mass Spectrometry -- 2.2.4.1 Proteolytic Cleavage -- 2.2.4.2 Glycopeptide and Glycan Enrichment -- 2.2.4.3 Glycopeptide and Glycan Analysis by LC-MS -- 2.2.4.4 Analysis of Ig Glycosylation on the Subunit and Whole Protein Level -- 2.3 Lectin Techniques -- 2.3.1 Lectin Chromatography -- 2.3.2 Lectin Microarrays -- 2.4 Perspectives -- References -- Chapter 3: Mass Spectrometry-Based Methods for Immunoglobulin G N-Glycosylation Analysis -- 3.1 Basic Principles of Mass Spectrometry."]
[{"$nulls":4},"3.1.1 Ionization -- 3.1.2 Gas-Phase Separation and Detection -- 3.1.3 Tandem MS -- 3.2 Levels of IgG N-Glycosylation Analysis -- 3.3 Sample Preparation for IgG Glycosylation Analysis -- 3.3.1 Protein A, G, and L Affinity Chromatography for IgG Enrichment from Biological Samples -- 3.3.1.1 Protein A -- 3.3.1.2 Protein G -- 3.3.1.3 Protein L -- 3.3.1.4 Recombinant Fusion Proteins and Alternative Scaffolds -- 3.3.2 Sample Preparation for Released IgG Glycan Analysis -- 3.3.2.1 Chemical and Enzymatic Glycan Release -- 3.3.3 Fluorescent and Isotopic Glycan Labeling -- 3.3.4 Sample Preparation for Glycopeptide Mapping and Subclass-Specific IgG Fc Glycosylation Analysis -- 3.3.4.1 Enzymatic Digestion -- 3.3.4.2 Stable Isotope Glycopeptide Labeling -- 3.3.4.3 Glycan and Glycopeptide Enrichment and Purification Strategies -- 3.4 Deciphering the IgG Glycan Structure -- 3.4.1 Fragmentation -- 3.4.2 Fragmentation Nomenclature -- 3.4.3 Fragmentation Candidates -- 3.4.3.1 Fragmentation of Glycopeptides -- 3.4.3.2 Fragmentation of Released Glycans -- 3.4.4 Ionization Polarity of MS Analysis -- 3.4.4.1 Example of Positive Ion Mode Fragmentation -- 3.4.4.2 Example of Negative Ion Mode Fragmentation -- 3.4.5 Exoglycosidase Digestion Monitored by MS -- 3.5 Selected Approaches for IgG Glycosylation Analysis -- 3.5.1 MALDI-MS -- 3.5.1.1 Intact Proteins and Glycopeptides -- 3.5.1.2 Released N-Glycans -- 3.5.1.3 Sialic Acid Stability -- 3.5.1.4 Matrix Substances for MALDI-MS -- 3.5.1.5 MALDI-MS for High-Throughput and Quantitative Analysis -- 3.5.2 LC-MS for IgG Glycosylation Analysis -- 3.5.2.1 Coupling LC to MS for Enhanced Separation and Structural Characterization -- 3.5.2.2 HILIC-UHPLC-MS -- 3.5.2.3 RP-LC-MS -- 3.5.2.4 PGC for Enhanced Isomeric Glycan Separation -- 3.5.2.5 Anion Exchange LC-MS -- 3.5.2.6 Challenges of Miniaturization."]
[{"$nulls":4},"3.5.3 Capillary Electrophoresis-Mass Spectrometry -- 3.6 Perspectives -- References -- Chapter 4: Capillary (Gel) Electrophoresis-Based Methods for Immunoglobulin (G) Glycosylation Analysis -- 4.1 Historical Background -- 4.2 Background: Principles of Capillary (Gel) Electrophoresis (C(G)E) -- 4.3 Performance, Benefits, and Potentials of Capillary (Gel) Electrophoresis C(G)E -- 4.4 Data Analysis and Interpretation -- 4.5 Exoglycosidase Sequencing of Glycans -- 4.6 Coupling Capillary Electrophoresis with Mass Spectrometry -- 4.7 Latest Developments: Miniaturization of CE Systems-Microchip CE -- 4.8 Application of C(G)E for Immunoglobulin Analysis -- 4.9 Conclusion -- References -- Chapter 5: Automation of Immunoglobulin Glycosylation Analysis -- 5.1 Introduction -- 5.1.1 Biopharmaceutical Glycomics -- 5.1.2 Clinical Glycomics -- 5.1.3 Towards High-Throughput Glycomics -- 5.1.4 Robotics: The Ultimate High-Throughput Solution? -- 5.2 Automation of Glycomics Sample Preparation -- 5.2.1 Sample Origins and Protein Purification -- 5.2.1.1 Serum and Plasma -- 5.2.1.2 Therapeutic Antibody Glycoproteins -- 5.2.2 Preparing Glycans for Analysis: Glycan Release, Derivatization and Clean-Up -- 5.2.2.1 Plasma and Serum -- Automated Methods for N-Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.2.2 Therapeutic "]
[{"$nulls":4},"Antibody Glycoproteins -- Automated Methods for N-Glycan Preparation Employing Anomeric Fluorescent Labeling Strategies -- Automated Methods for N-Glycan Preparation Employing Permethylation Derivatization Strategies -- 5.2.3 Automated Methods for Glycopeptide Preparation -- 5.3 Commentary -- 5.4 Future Perspectives -- 5.5 Conclusions -- References -- Chapter 6: Bioinformatics in Immunoglobulin Glycosylation Analysis -- 6.1 Introduction."]
[{"$nulls":4},"6.2 Glycomic Data Collection and Processing -- 6.2.1 Reference Databases -- 6.2.2 Identification and Quantification Software Tools -- 6.3 Glycoproteomics Data Collection and Processing -- 6.3.1 Reference Databases -- 6.3.2 Identification Software Tools -- 6.3.3 Quantification Software Tools -- 6.4 Data Integration with Other Omics -- 6.5 Practical Examples -- 6.5.1 Glycomic Data Processing -- 6.5.1.1 Software Required -- 6.5.1.2 Glycan Composition Determination -- 6.5.1.3 Annotation of MS and MS/MS Glycomics Spectra -- 6.5.1.4 Convert Raw Mass Spectrometry Data to mzXML -- 6.5.1.5 Skyline for Glycomics Quantitation -- 6.5.1.6 Setting Up Transition List -- 6.5.2 Glycopeptide Data Processing for Enriched Immunoglobulins -- 6.5.2.1 Software Required -- 6.5.2.2 Glycosylation Site Identification Based on MS2 -- 6.5.2.3 Glycoform Identification Based on MS1 -- 6.5.2.4 Targeted Glycopeptide Quantification -- 6.5.3 Visualizing Profiles -- 6.5.3.1 Structural Dependencies Brought Out by GlyConnect Compozitor -- 6.5.3.2 Comparing Profiles with Glynsight -- 6.6 Conclusion -- References -- Part II: Biosynthesis and Regulation -- Chapter 7: N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome -- 7.1 Introduction -- 7.2 Biosynthesis of N-Glycans in the Endoplasmic Reticulum -- 7.2.1 Building Blocks for N-Glycan Synthesis -- 7.2.2 Precursor Synthesis and Its Attachment to Nascent Polypeptide Chains -- 7.2.3 N-Glycan Processing in the ER and Quality Control -- 7.3 N-Glycan Processing in the Golgi Apparatus -- 7.3.1 N-Glycosylation of Immunoglobulins -- 7.4 Golgi Microenvironment Is Important for Normal Processing and Maturation of N-Glycans -- 7.4.1 Golgi pH Homeostasis -- 7.4.2 Golgi Ion Homeostasis -- 7.4.3 Golgi Redox State -- 7.5 Concluding Remarks -- References -- Chapter 8: Genetic Regulation of Immunoglobulin G Glycosylation."]
[{"$nulls":4},"8.1 Introduction -- 8.2 Heritability of the Human IgG N-Glycome -- 8.3 Linkage Studies of Mouse N-glycome -- 8.4 Genome-Wide Association Studies of Human N-Glycome -- 8.4.1 Genomic Loci Associated with IgG N-Glycosylation -- 8.4.1.1 Chromosome 1 -- 8.4.1.2 Chromosome 3 -- 8.4.1.3 Chromosome 5 -- 8.4.1.4 Chromosome 6 -- 8.4.1.5 Chromosome 7 -- 8.4.1.6 Chromosome 9 -- 8.4.1.7 Chromosome 11 -- 8.4.1.8 Chromosome 14 -- 8.4.1.9 Chromosome 17 -- 8.4.1.10 Chromosome 21 -- 8.4.1.11 Chromosome 22 -- 8.4.2 Suggestive Associations -- 8.4.3 Functional Network of Loci Associated with IgG Glycosylation -- 8.5 Pleiotropy with Complex Traits and Diseases -- 8.6 Conclusions -- References -- Chapter 9: Epigenetics of Immunoglobulin G Glycosylation -- 9.1 Introduction -- 9.2 Regulation of Glycosyltransferases by Transcription Factors -- 9.3 Epigenetic Regulation of IgG Glycosylation -- 9.4 The Role of miRNAs in Protein N-Glycosylation -- 9.5 Conclusions -- References -- Chapter 10: Immunoglobulin G Glycosylation Changes in Aging and Other Inflammatory Conditions -- 10.1 Premise -- 10.2 IgG Glycosylation -- 10.3 Changes in IgG Asn297 Glycans Associated with Inflammatory Diseases -- 10.4 IgG Glycosylation as a Predictor of Disease Onset, Progression, and Therapy Response -- 10.4.1 Prediction of Disease Onset -- 10.4.2 Prediction of Progression and Therapy Response -- 10.5 IgG Glycosylation in Aging -- 10.6 The Inflammaging Is a Link "]
[{"$nulls":4},"Between Aging and Inflammation -- 10.7 How Altered IgG Glycosylation Drives Inflammation -- 10.7.1 Activation of Complement Through the Lectin or the Classical Pathways -- 10.7.2 Binding to Fcγ Receptors -- 10.7.3 Binding on Lectin Receptors of Antigen-Presenting Cells: Role in the Intravenous Administration of High Doses IgG (IVIG) -- 10.7.4 Anti IgG Autoantibodies -- 10.8 Molecular Bases of N-Glycosylation Changes -- 10.9 Conclusions."]
[{"$nulls":4},"References."]