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Note: Cover -- Synthetic Glycomes -- Preface -- Contents -- Chapter 1 - Introduction: Glycome and theGlyco-toolbox -- 1.1 Introduction -- 1.2 Diversity of Glycans -- 1.3 Limited Glycan Backbone Structures -- 1.4 Access -- 1.5 Application -- 1.6 Conclusion -- References -- Chapter 2 - Methodologies in Chemical Syntheses of Carbohydrates -- 2.1 Introduction -- 2.2 Before Glycosylation -- 2.2.1 Protecting Groups -- 2.2.2 De Novo Syntheses of Carbohydrates -- 2.3 Amidst Glycosylation -- 2.3.1 Reactivity -- 2.3.2 Stereochemistry -- 2.4 Applications Beyond Glycosylation -- 2.4.1 Oligosaccharides and Polysaccharides -- 2.4.2 Glycoconjugates -- 2.4.3 Natural Products -- 2.5 Conclusion -- References -- Chapter 3 - Synthetically Useful Glycosyltransferases for the Access of Mammalian Glycomes -- 3.1 Introduction -- 3.2 Glycosyltransferases (GTs) and Their Usage in Mammalian Glycan Preparation -- 3.2.1 Leloir GTs and Non-LeloirGTs -- 3.2.2 Mammalian GTs and Bacterial GTs -- 3.2.3 Wild-typeGTs and Engineered GTs -- 3.3 Synthetically Useful Glycosyltransferases -- 3.3.1 N-Acetylglucosaminyltransferases(GlcNAcTs) -- 3.3.2 Galactosyltransferases (GalTs) -- 3.3.3 Fucosyltransferases (FucTs) -- 3.3.4 Sialyltransferases (SiaTs) -- 3.3.5 N-Acetylgalactosaminyltransferases(GalNAcTs) -- 3.3.6 Glucuronosyltransferases (GlcATs) -- 3.3.7 Mannosyltransferases (ManTs) -- 3.4 Strategies in GT-catalyzed Glycan Syntheses -- 3.4.1 Direct GT-catalyzedReactions -- 3.4.2 GT-catalyzed Reaction with Sugar Nucleotide In Situ Regeneration -- 3.4.3 One-pot Multienzyme (OPME) Syntheses and Enzymatic Modular Assembly (EMA) -- 3.4.4 Whole-cellCatalysis -- 3.4.5 Living Cell Factory -- 3.5 Prospective -- References -- Chapter 4 - Chemical Synthesis of N-Glycans -- 4.1 Introduction -- 4.2 Chemical Synthesis of N-Glycans -- 4.2.1 Chemical Synthesis of Core Trisaccharide in N-Glycans. , 4.2.2 Chemical Synthesis of High-mannose Type N-Glycans -- 4.2.3 Chemical Synthesis of Hybrid Type N-Glycans -- 4.2.4 Chemical Synthesis of Complex Type N-Glycans -- 4.2.4.1 Synthesis of Symmetric Biantennary Complex Type N-Glycans -- 4.2.4.2 Synthesis of Symmetric Triantennary Complex Type N-Glycans -- 4.2.4.2.1 Synthesis of Symmetric 2,2,6-Armed Triantennary Complex Type N-Glycans -- 4.2.4.2.2 Synthesis of Symmetric 2,4,2-ArmedTriantennary Complex Type N-Glycans. -- 4.2.4.3 Synthesis of Symmetric Tetraantennary Complex Type N-Glycans -- 4.2.5 Synthesis of Neu5Ac-containing Complex Type N-Glycans -- 4.2.6 Synthesis of Asymmetric Complex Type N-Glycans -- 4.2.7 Synthesis of Bisecting Type N-Glycans -- 4.2.8 Synthesis of Core-fucosylated N-Glycans -- 4.3 Discussion -- 4.4 Summary -- References -- Chapter 5 - Chemoenzymatic Synthesis of N-Glycans -- 5.1 Introduction -- 5.2 Enzymes Employed in the Preparation of N-Glycans -- 5.2.1 Sialyltransferases -- 5.2.2 Galactosyltransferases -- 5.2.3 Fucosyltransferases -- 5.2.4 N-Acetylhexosaminyltransferases -- 5.2.5 Glycosidases -- 5.2.6 Glycosynthases -- 5.3 Enzymatic Preparation of N-Glycans -- 5.4 Chemoenzymatic Preparation of N-GlycanLibraries -- 5.4.1 A General Strategy for Chemoenzymatic Synthesis of Asymmetric Complex Type N-Glycans -- 5.4.2 Core Synthesis/Enzymatic Extension (CSEE) Strategy forthe Synthesis of Hybrid and Complex Type N-Glycans -- 5.4.3 Enzymatic Synthesis of Complex Type N-Glycansfrom One Chemically Prepared Precursor -- 5.5 Modular Synthesis of All Types of N-Glycans -- 5.6 Summary -- References -- Chapter 6 - Chemoenzymatic Synthesis of α-Dystroglycan O-Mannose Glycans -- 6.1 Introduction -- 6.2 Biosynthetic Pathway and Functional Roles of O-Mannose Glycans -- 6.2.1 Biosynthesis Pathway of O-MannosylGlycans -- 6.2.2 Dystroglycanopathies and Implicated Genes. , 6.2.3 Roles of O-Mannosylationin Tumor Metastasis -- 6.2.4 Function of Core M1 and M2 Structures -- 6.2.5 O-MannosylatedSubstrates Beyond α-DG -- 6.3 Synthesis of O-MannoseGlycans -- 6.3.1 Chemical or Chemoenzymatic Synthesis of Core M1 Structures -- 6.3.2 Chemical or Chemoenzymatic Synthesis of Core M2 O-Mannose Glycans -- 6.3.3 Chemical Synthesis of Phosphorylated Core M3 Trisaccharide -- 6.4 Conclusion -- Abbreviations -- Acknowledgement -- References -- Chapter 7 - Chemical Synthesis of Glycopeptides and Glycoproteins -- 7.1 Introduction -- 7.2 Synthesis of Glycopeptide -- 7.2.1 Synthesis of Polypeptide Chain -- 7.2.2 Synthesis of PSGL-1 -- 7.2.3 Synthesis of CD52 -- 7.3 Ligation Method -- 7.3.1 Basic Strategies -- 7.3.2 Glycopeptide Thioester Synthesis -- 7.4 Synthesis of O-linkedGlycoproteins -- 7.4.1 Synthesis of Antifreeze Glycoprotein -- 7.4.2 Synthesis of MUC2 Model -- 7.4.3 Synthesis of Interleukin-2 -- 7.5 Synthesis of N-linkedGlycoprotein -- 7.5.1 Strategies for N-linked Glycoprotein Synthesis -- 7.5.2 Synthesis of Human Interferon-β -- 7.5.3 Synthesis of TIM-3 -- 7.5.4 Synthesis of Ig Domain of Emmprin -- 7.6 Conclusion -- References -- Chapter 8 - Synthesis of Chondroitin Sulfate Oligosaccharides and Chondroitin Sulfate Glycopeptides -- 8.1 Introduction to Chondroitin Sulfate (CS) and Chondroitin Sulfate Proteoglycan (CSPG) -- 8.2 Chemical Synthesis of CS -- 8.2.1 General Synthetic Design for Chemical Synthesis of CS -- 8.2.2 Strategies Addressing N-protective Groups -- 8.2.2.1 Azide Protective Group -- 8.2.2.2 N-AcetamideGroup -- 8.2.2.3 N-Trichloroacetamide Group -- 8.2.2.4 N-Trifluoroacetamide -- 8.2.2.5 N-Tetrachlorophthalimide Group -- 8.2.2.6 Lactose Derived CS Mimetics -- 8.2.3 Semi-synthesisof CS, Expediting Building Block Preparation Using Natural Sources -- 8.2.4 Solid Phase Synthesis of CS Oligosaccharides. , 8.2.5 Chemical Synthesis of a CS Disaccharide Library and Biotinylated CS -- 8.2.6 Chemical Synthesis of Heterologous Sulfated CS Oligosaccharides -- 8.2.7 Chemical Synthesis of CS Oligosaccharides with Linkage Region -- 8.3 Chemoenzymatic Synthesis of CS Oligosaccharides -- 8.4 Chemical Synthesis of CS Glycopolymers and Glycoconjugates -- 8.5 Synthesis of CS Glycopeptide -- 8.6 Conclusions -- Abbreviations -- Acknowledgement -- References -- Chapter 9 - Chemoenzymatic Synthesis of Heparan Sulfate and Heparin -- 9.1 Introduction -- 9.1.1 Heparan Sulfate -- 9.1.2 Heparin -- 9.1.3 Chemoenzymatic Synthesis of HS and Heparin -- 9.2 Key Techniques of Synthesis -- 9.2.1 Design of Sugar Nucleotides for the Chemoenzymatic Synthesis of HS -- 9.2.2 Sequences of Enzymatic Modifications for the Synthesis of Different Oligosaccharides -- 9.3.1 Synthesis of HS Oligosaccharide Library and a New Antithrombin-binding Octasaccharide -- 9.3.2 HS Microarray to Target HS and Protein Interaction -- 9.3.3 Design of Heparin Drugs -- 9.3.4 Scale-up Synthesis of HS 12-mer -- 9.4 Conclusion -- References -- Chapter 10 - Synthesis of Glycosphingolipids (GSLs) -- 10.1 Introduction -- 10.2 Chemical Strategies for Synthesizing Glycosphingolipids -- 10.2.1 Synthesis Using Glycosyl Trichloroacetimidate Donors -- 10.2.2 Synthesis with Glycosyl N-Phenyl Trifluoroacetimidates -- 10.2.3 Synthesis Using Glycosyl Fluoride Donors -- 10.2.4 Synthesis Using Koenigs-Knorr Glycosylation Reactions -- 10.2.5 Synthesis Using Thioglycoside Glycosyl Donors -- 10.2.6 Synthesis Using α-GlycosylIodide Donors -- 10.2.7 Synthesis Using Glycosyl Mesylate Donors -- 10.2.8 Synthesis Using Glycal Donors -- 10.2.9 Synthesis of α-Galactosylceramide Analogs from Naturally Configured α-Galactosides -- 10.3 Chemoenzymatic Synthesis of GSLs -- 10.3.1 Endoglycoceramidase-derived Glycosynthase-catalyzed Synthesis. , 10.3.2 Enzymatic Synthesis of Gb3 and iGb3 Using Lactosyl Ceramide as Acceptor Substrate -- 10.3.3 Enzymatic Assembly of Oligosaccharides Followed by Chemical Glycosylation -- 10.3.4 Enzymatic Sialylation of Glycolipids -- 10.3.5 One-pot Multienzyme (OPME) Chemoenzymatic Strategies -- 10.4 Conclusion -- Acknowledgement -- References -- Chapter 11 - Enzymatic and Chemoenzymatic Synthesis of Human Milk Oligosaccharides (HMOS) -- 11.1 Introduction -- 11.2 Bacterial and Mammalian Glycosyltransferases (GTs) that Have Been Used for the Synthesis of HMOS -- 11.3 Synthesis of HMOS via One-pot Multienzyme(OPME) Approaches -- 11.3.1 One-potMultienzyme (OPME) Glycosylation Systems -- 11.3.2 OPME Synthesis of Core Glycans LNTri II (Lc3) and LNnT -- 11.3.3 OPME Enzymatic Synthesis of Fucose-containing HMOS -- 11.3.3.1 OPME Synthesis of LNFP I -- 11.3.3.2 OPME Synthesis of LNFP III -- 11.3.3.3 OPME Synthesis of 3- FL, LNFP III, LNDFH II, and LNDFH III -- 11.3.4 OPME Synthesis of Sialylated HMOS -- 11.3.4.1 OPME Synthesis of 3′-SLand 6′-SL -- 11.3.4.2 OPME Synthesis of LST a, LST d, Sialylated LNFP III -- 11.3.4.3 OPME Synthesis of LSTc -- 11.3.4.4 OPME Synthesis of Disialylated HMOS -- 11.4 Glycosyltransferase-catalyzed Enzymatic Synthesis of HMOS -- 11.5 Enzymatic Synthesis of HMOS Using Transglycosidases, Glycosidases and Mutants -- 11.6 Chemoenzymatic Synthesis of HMOS -- 11.7 Whole-cell Production and Fermentation of Engineered E. coli Cells -- 11.8 Conclusion -- Acknowledgement -- References -- Chapter 12 - Synthesis of Marine Polysaccharides/Oligosaccharides and Their Derivatives -- 12.1 Introduction -- 12.2 Synthesis of Marine Polysaccharides -- 12.2.1 Biosynthesis of Marine Polysaccharides -- 12.2.2 Semi-synthesisof Marine-derived Polysaccharides -- 12.2.3 Synthesis of Glycopolymers and Glycoclusters to Mimic Natural Marine Polysaccharides. , 12.2.4 Synthesis and Modification of Marine Polysaccharide Derivatives.

Note: Intro -- Title -- Copyright -- Preface -- Contents -- CHAPTER 1 Introduction: General Aspects of the Chemical Biology of Glycoproteins -- 1.1 Introduction -- 1.1.1 Complexity of Protein Glycosylation -- 1.1.2 Strategies and Methods to Study Protein Glycosylation -- 1.2 Chemical Biology of Glycoproteins -- 1.2.1 Types of Protein Glycosylation -- 1.2.2 Biosynthesis of Glycoproteins -- 1.2.3 Structural and Functional Consequences of Protein Glycosylation -- 1.2.4 Methods to Prepare Homogeneous Glycopeptides and Glycoproteins -- 1.2.5 Chemical Glycobiology and Applications -- 1.3 Conclusion -- References -- CHAPTER 2 Chemical Biology of Protein N-Glycosylation -- 2.1 Introduction -- 2.2 Biosynthesis and Intracellular Functions of N-Glycans of Glycoproteins -- 2.3 Inhibitors of Glycan-Processing Enzymes for Controlling Protein N-Glycosylation -- 2.4 Global Metabolic Enzyme Inhibitors for Perturbing Protein N-Glycosylation -- 2.5 Metabolic Glycoengineering of Cell-Surface Glycoproteins -- 2.6 Chemoenzymatic Synthesis and Glycosylation Remodeling Toward Homogeneous N-Glycoproteins -- 2.6.1 Generation of Novel ENGase-Based Glycosynthases for N-Glycosylation Remodeling and N-Glycoprotein Synthesis -- 2.6.2 Chemoenzymatic Fc Glycan Remodeling of Therapeutic Monoclonal Antibodies -- 2.6.3 Combined E. coli Expression and Chemoenzymatic Glycan Remodeling to Produce Humanized N-Glycoproteins -- 2.7 Conclusion -- Acknowledgements -- References -- CHAPTER 3 Chemical Biology of Protein O-Glycosylation -- 3.1 Introduction -- 3.2 Biosynthesis of O-Glycoproteins -- 3.2.1 α-O-GalNAc -- 3.2.2 α-O-Man -- 3.2.3 α-O-Fuc -- 3.2.4 β-O-Glc -- 3.2.5 β-O-GlcNAc -- 3.3 Chemical Biology in Studying the Structural and Functional Consequences of Protein O-Glycosylation -- 3.3.1 α-O-GalNAc -- 3.3.1.1 Substrate Preferences of ppGalNAcTs. , 3.3.1.2 Structural Effects of O-GalNAc Glycosylation -- 3.3.1.3 Functional Effects of O-GalNAc Glycosylation -- 3.3.2 α-O-Man -- 3.3.2.1 Biosynthetic Pathway of O-Man Glycans -- 3.3.2.2 Biophysical and Biological Effects of O-Mannosylation -- 3.3.3 α-O-Fuc -- 3.3.4 β-O-Glc -- 3.3.5 β-O-GlcNAc -- 3.4 Chemical Biology in Studying the Composition of Mixtures of O-Glycoproteins -- 3.4.1 Glycoprotein Purification and Enrichment -- 3.4.2 Glycoprotein Digestion and Glycopeptide Separation -- 3.4.3 Glycopeptide Analysis -- 3.4.4 Importance of Synthetic Glycopeptides in Protein Glycosylation Analysis -- 3.5 Conclusion -- References -- CHAPTER 4 Chemical Biology of O-GlcNAc Glycosylation -- 4.1 Introduction -- 4.2 Chemical Blockade of O-GlcNAc Addition -- 4.2.1 Inhibitors of UDP-GlcNAc Biosynthesis -- 4.2.2 Product Inhibition of OGT: UDP -- 4.2.3 Alloxan -- 4.2.4 Screening Approaches to Discover OGT Inhibitors -- 4.2.5 Substrate Mimicry Approach to Discover OGT Inhibitors -- 4.2.6 New Directions in OGT Inhibitor Development -- 4.3 Chemical Blockade of O-GlcNAc Removal: OGA Inhibitors -- 4.3.1 Streptozotocin -- 4.3.2 PUGNAc -- 4.3.3 NAG-Thiazoline -- 4.3.4 GlcNAcstatins -- 4.3.5 Thiamet-G -- 4.3.6 Other Approaches to OGA Inhibition -- 4.4 Detection of O-GlcNAcylated Substrates: Lectins and Antibodies -- 4.5 Detection of O-GlcNAcylated Substrates: Mass Spectrometry-Based Methods -- 4.5.1 Electron Transfer Dissociation MS -- 4.5.2 MS Approaches to Complement ETD -- 4.5.3 Chemical Derivatization of MS Samples for O-GlcNAc Enrichment and Detection -- 4.6 Detection of O-GlcNAcylated Substrates: A Chemoenzymatic Approach -- 4.7 Detection of O-GlcNAcylated Substrates: Metabolic Labeling Approaches -- 4.7.1 N-Azidoacetylglucosamine (GlcNAz) -- 4.7.2 N-Azidoacetylgalactosamine (GalNAz) -- 4.7.3 N-Butynyl-Glucosamine (GlcNAlk) and Other Alkynylsugars. , 4.7.4 Other Metabolic Labeling Reagents -- 4.8 Methods to Deduce the Biochemical and Cellular Functions of O-GlcNAc -- 4.8.1 Live-Cell Assays of OGT or OGA Activity -- 4.8.2 Chemical Modification and Semi-Synthesis of Model Glycoproteins and Glycopeptides -- 4.8.3 Photocrosslinking Tools to Capture O-GlcNAc-Mediated Protein-Protein Interactions -- 4.9 Conclusions and Outlook -- References -- CHAPTER 5 Chemical Synthesis and Engineering of N-Linked Glycoproteins -- 5.1 Introduction -- 5.2 Semisynthesis of N-Glycosylated Proteins -- 5.2.1 Semisynthesis of N-Glycoprotein Mimics with Unnatural Glycosyl Linkages at Cysteines -- 5.2.2 Semisynthesis of Glycoproteins with Natural N-Linkages on Asparagines -- 5.3 Total Chemical Synthesis of N-Linked Glycoproteins -- 5.3.1 Total Synthesis of N-Linked Glycoproteins Bearing N-Chitobioses -- 5.3.2 Total Synthesis of N-Linked Glycoproteins Bearing "Wild-Type" N-Glycans -- 5.3.3 Representative Synthetic Attempts Towards Producing N-Linked Glycoproteins with Multiple Disulfide Linkages -- 5.4 Application of Chemically Synthesized N-Linked Glycoproteins to Biological Processes -- 5.5 Conclusion -- References -- CHAPTER 6 Chemoenzymatic Synthesis of N-Glycans -- 6.1 Introduction -- 6.2 Chemical Synthesis of Complex N-Glycans -- 6.2.1 Assembly Strategy and Method of Glycosylation in Chemical Synthesis of N-Glycans -- 6.2.2 Total Synthesis of Complex N-Glycans by Global Glycosylation of a Core Pentasaccharide -- 6.2.3 Convergent Synthesis of Complex N-Glycans by Glycosylation of Core Trisaccharide -- 6.3 Chemoenzymatic Synthesis of Complex N-Glycans -- 6.3.1 A General Strategy for the Chemoenzymatic Synthesis of Asymmetrically Branched N-Glycans -- 6.3.1.1 Chemical Synthesis of Asymmetric N-Glycans by Orthogonal Protection Strategy -- 6.3.1.2 Enzymatic Extension to Synthesize Asymmetrically Branched N-Glycans. , 6.3.2 Core Synthesis/Enzymatic Extension (CSEE) Strategy for Efficient Synthesis of N-Glycan Libraries -- 6.3.2.1 Chemical Synthesis of N-Glycan Core Structures Through Convergent Block Coupling -- 6.3.2.2 Enzymatic Extension to Obtain a N-Glycan Library -- 6.4 Conclusion -- References -- CHAPTER 7 Towards Synthesis of Heparan Sulfate Glycopeptides and Proteoglycans -- 7.1 Structures, Biological Functions and Biosynthesis of Proteoglycans -- 7.2 Chemical Synthesis of the PG Linker-Peptide Conjugates -- 7.3 Synthesis of HS Glycopeptides -- 7.4 Conclusion and Future Outlook -- Acknowledgements -- References -- CHAPTER 8 Chemoenzymatic Synthesis of Low-Molecular-Weight Heparin and Heparan Sulfate -- 8.1 Introduction -- 8.1.1 What are Heparan Sulfate, Heparin and Heparin-Derivatives? -- 8.1.2 Why are Synthetic Heparins and Heparan Sulfates Needed? -- 8.1.3 Types of Chemoenzymatic Synthesis -- 8.2 Enzymes Required for Chemoenzymatic Synthesis -- 8.2.1 Glycosyltransferases -- 8.2.2 Sulfotransferases and C5-Epimerase -- 8.3 Building Blocks Prepared for Chemoenzymatic Synthesis -- 8.3.1 Acceptors -- 8.3.2 Donors -- 8.3.2.1 Natural UDP-Sugars -- 8.3.2.2 Unnatural UDP-Sugars -- 8.3.3 Polysaccharide and Oligosaccharide Backbone -- 8.4 Control of Product Through Sequential Enzymatic Modification -- 8.5 Novel Chemoenzymatic Synthesis -- 8.5.1 One-Pot Multienzyme System -- 8.5.2 Fluorous-Tagging Techniques -- 8.5.3 Solid-Phase Synthesis -- 8.5.4 Immobilized Enzymes -- 8.5.5 Immobilized Enzyme Cofactors -- 8.6 Conclusion and Future Perspectives -- References -- CHAPTER 9 Synthetic Studies of GPI-Anchored Peptides, Glycopeptides, and Proteins -- 9.1 Introduction -- 9.2 Biosynthesis of GPIs and GPI-Anchored Proteins -- 9.2.1 Biosynthesis of GPI Anchors -- 9.2.2 Posttranslational Attachment of GPIs to Proteins. , 9.3 Synthesis of GPI-Anchored Proteins and Glycoproteins -- 9.3.1 Chemical Total Synthesis of GPI-Anchored Peptides and Glycopeptides -- 9.3.2 Synthesis of GPI-Anchored Peptides and Proteins via NCL -- 9.3.3 Synthesis of GPI-Anchored Peptides, Glycopeptides, and Proteins via Enzymatic Ligation -- 9.4 GPI-Anchored Proteomics Studies -- 9.5 Concluding Remarks -- Acknowledgements -- References -- CHAPTER 10 Chemical Approaches to Image Protein Glycosylation -- 10.1 Background -- 10.2 Structure, Biosynthesis, and Function of Protein Glycans -- 10.2.1 N-Linked Glycans -- 10.2.2 Mucin-Type O-Linked Glycans -- 10.2.3 Sialic Acids -- 10.2.4 O-GlcNAc -- 10.3 Methods for Glycan Labeling and Imaging -- 10.3.1 Lectins and Antibodies -- 10.3.2 Metabolic Glycan Labeling -- 10.3.3 Chemoenzymatic Labeling -- 10.4 Imaging Protein Glycosylation -- 10.4.1 General Principles of the Dual-Labeling-Based Methods -- 10.4.2 FRET-Based Protein-Specific Imaging of Glycosylation -- 10.4.3 PLA-Based Protein-Specific Imaging of Glycosylation -- 10.4.4 Protein-Specific Imaging of Glycosylation Based on PEBL -- 10.4.5 Protein-Specific Imaging of Glycosylation Based on SERS -- 10.5 Conclusion and Perspective -- References -- CHAPTER 11 Targeting Glycans of HIV Envelope Glycoproteins for Vaccine Design -- 11.1 The Human Immunodeficiency Virus -- 11.1.1 Structure, Genome and Viral Lifecycle -- 11.1.2 Transmission and Pathogenesis -- 11.1.3 The Viral Envelope is the Main Target for the Immune System -- 11.1.4 Immune Response -- 11.1.5 Current Therapies and Steps towards a Vaccine -- 11.2 The Viral Envelope Spike -- 11.2.1 Biosynthesis -- 11.2.2 Structure and Function of Env -- 11.2.3 The Glycan Shield -- 11.2.4 Site-specific N-Linked Glycan Analysis -- 11.2.5 Glycans in Immune Escape -- 11.3 A Target for Broadly Neutralizing Antibodies -- 11.3.1 Sites of Vulnerability. , 11.3.2 Unusual Features of Broadly Neutralizing Antibodies.

Note: Intro -- Nitric Oxide Donors -- Contents -- Preface -- List of Contributors -- Part 1 Chemistry of NO Donors -- 1 NO and NO Donors -- 1.1 Introduction to NO Biosynthesis and NO donors -- 1.1.1 Nitric Oxide Synthases -- 1.1.2 Chemistry of Reactive Nitrogen Species -- 1.2 Classification of NO Donors -- 1.3 New Classes of NO Donors under Development -- 1.3.1 Nitroarene -- 1.3.2 Hydroxamic Acids -- 1.4 Development of NO-Drug Hybrid Molecules -- 1.4.1 Nitrate Hybrid Molecules -- 1.4.2 Furoxan Hybrid Molecules -- 1.5 New Therapeutic Applications of NO Donors -- 1.5.1 NO Donors against Cancer -- 1.5.1.1 Diazeniumdiolates (NONOates) as Promising Anticancer Drugs -- 1.5.1.2 The Synergistic Effect of NO and Anticancer Drugs -- 1.5.1.3 NO-NSAIDs as a New Generation of Anti-tumoral Agents -- 1.5.1.4 Other NO Donors with Anticancer Activity -- 1.5.2 NO against Virus -- 1.5.2.1 HIV-1 Induces NO Production -- 1.5.2.2 Antiviral and Proviral Activity of NO -- 1.5.3 Inhibition of Bone Resorption -- 1.5.4 Treatment of Diabetes -- 1.5.5 Thromboresistant Polymeric Films -- 1.5.6 Inhibition of Cysteine Proteases -- 1.6 Conclusion -- References -- 2 Organic Nitrates and Nitrites -- 2.1 Organic Nitrates -- 2.1.1 Direct Chemical Reaction between Organic Nitrates and Thiols -- 2.1.2 Glutathione-S-transferase -- 2.1.3 Cytochrome P-450-dependent Systems -- 2.1.4 Membrane-bound Enzyme of Vascular Smooth Muscle Cells -- 2.1.5 Xanthine Oxidoreductase -- 2.1.6 Mitochondrial Aldehyde Dehydrogenase -- 2.1.7 Tolerance -- 2.2 Organic Nitrites -- 2.3 Conclusions -- References -- 3 N-Nitroso Compounds -- 3.1 Introduction -- 3.2 N-Nitrosamines -- 3.2.1 Synthesis of Nitrosamines -- 3.2.2 Physical Properties and Reactions of N-Nitrosamines -- 3.2.3 Structure-Activity Relationship of N-Nitrosamines -- 3.2.4 Application of N-Nitrosamines -- 3.3 N-Hydroxy-N-nitrosoamines. , 3.3.1 Biologically Active N-Hydroxy-N-nitrosamine Compounds -- 3.3.2 Synthesis of N-Hydroxy-N-nitrosamines -- 3.3.3 Properties of N-Hydroxy-N-nitrosamines -- 3.3.4 Reactivity of N-Hydroxo-N-nitrosamines -- 3.4 N-Nitrosimines -- 3.4.1 Mechanism of Thermal Reaction of N-Nitrosoimine -- 3.4.2 Properties of N-Nitrosoimines -- 3.4.3 Synthesis of N-Nitrosoimines -- 3.5 N-Diazeniumdiolates -- 3.5.1 Mechanism of NO Release -- 3.5.2 Synthesis of N-Diazeniumdiolates -- 3.5.2.1 Ionic Diazeniumdiolates -- 3.5.2.2 O-derivatized Diazeniumdiolates -- 3.5.3 Reactions of N-Diazeniumdiolates -- 3.5.4 Clinical Applications -- 3.5.4.1 Reversal of Cerebral Vasospasm -- 3.5.4.2 Treatment of Impotency -- 3.5.4.3 Nonthrombogenic Blood-contact Surfaces -- 3.5.5 Future Directions -- References -- 4 The Role of S-Nitrosothiols in the Biological Milieu -- 4.1 Structure and Cellular Reactivity of RSNOs -- 4.1.1 RSNO Structure -- 4.1.1.1 Enzymatic Consumption of RSNOs -- 4.1.2 Formation of RSNOs in the Biological Milieu -- 4.1.2.1 Nitrite Mediated -- 4.1.2.2 NO Mediated -- 4.1.2.3 NO Oxidation Products Mediated -- 4.1.2.4 Metalloprotein Mediated -- 4.1.2.5 Transnitrosation -- 4.2 Postulated Physiological roles of RSNOs -- 4.2.1 Regulation of Blood Flow by HbSNO -- 4.2.2 Regulation of Ventilatory Response in the Brain by RSNOs -- 4.2.3 Role of RSNOs in Platelet Function -- 4.3 Conclusion -- References -- 5 Metal-NO complexes: Structures, Syntheses, Properties and NO-releasing Mechanisms -- 5.1 Iron Complexes -- 5.1.1 Nitroprusside -- 5.1.2 Iron Porphyrin Nitrosyls -- 5.1.3 Dinitrosyl Complexes (DNICs) -- 5.1.4 Iron-Sulfur Cluster Nitrosyls -- 5.2 Ruthenium Complexes -- 5.3 Other Metal Nitrosyls -- 5.4 Conclusion -- References -- 6 The NO-releasing Heterocycles -- 6.1 Heterocyclic N-oxides -- 6.1.1 Furoxans -- 6.1.1.1 General Properties -- 6.1.1.2 Synthesis. , 6.1.1.2.1 Dimerisation of nitrile oxides -- 6.1.1.2.2 Dehydrogenation of α-dioximes (glyoximes) -- 6.1.1.2.3 Action of nitrogen oxides on olefins -- 6.1.1.2.4 Other methods -- 6.1.1.3 NO-release -- 6.1.1.4 Biological Actions -- 6.1.1.4.1 Condensed furoxans -- 6.1.1.4.2 Furoxan sulfones and carbonitriles -- 6.1.1.4.3 Furoxancarboxamides -- 6.1.1.5 NO-donor Hybrid Furoxans -- 6.1.2 3,4-Dihydro-1,2-diazete 1,2-dioxides (1,2-diazetine 1,2-dioxides) -- 6.1.2.1 Generalities -- 6.1.2.2 Synthesis -- 6.1.2.3 NO-release -- 6.1.2.4 Biological Properties -- 6.1.3 Other Heterocyclic N-oxides -- 6.1.3.1 4H-pyrazol-4-one 1,2-dioxides (pyrazolone N,N-dioxides) -- 6.1.3.2 2H-1,2,3-triazole 1-oxides -- 6.1.3.3 1,2,3,4-Benzotetrazine 1,3-dioxides and 1,2,3-Benzotriazine 3-oxides -- 6.2 Mesoionic Heterocycles -- 6.2.1 Sydnonimines -- 6.2.1.1 General Properties -- 6.2.1.2 Synthesis -- 6.2.1.3 NO-release -- 6.2.1.4 Biological Properties -- 6.2.2 Mesoionic Oxatriazoles -- 6.2.2.1 Synthesis -- 6.2.2.2 NO-release -- 6.2.2.3 Biological Properties -- 6.3 Other Heterocyclic Systems -- References -- 7 C-Nitroso Compounds, Oximes, N-Hydroxyguanidines and N-Hydroxyureas -- 7.1 Introduction -- 7.2 C-Nitroso Compounds -- 7.2.1 Alkyl and Aryl C-Nitroso Compounds -- 7.2.1.1 Syntheses and Properties -- 7.2.1.2 NO-releasing Mechanisms -- 7.2.2 Acyl C-Nitroso Compounds -- 7.2.2.1 Syntheses and Properties -- 7.2.2.2 NO-releasing Mechanisms -- 7.2.2.3 Structure-Activity Relationships -- 7.3 Oximes -- 7.3.1 Syntheses and Properties -- 7.3.2 NO-releasing Mechanisms -- 7.3.3 Structure-Activity Relationships -- 7.4 N-Hydroxyguanidines -- 7.4.1 Syntheses and Properties -- 7.4.2 NO-releasing Mechanisms -- 7.4.3 Structure-Activity Relationships -- 7.5 N-Hydroxyureas -- 7.5.1 Syntheses and Properties -- 7.5.2 NO-releasing Mechanisms -- 7.5.3 Structure-Activity Relationships -- References. , Part 2 NO Donors' Applications in Biological Research -- 8 Vasodilators for Biological Research -- 8.1 NO-donor Drugs for Biological Research -- 8.2 Sodium Nitrite (NaNO(2)) -- 8.3 S-Nitrosothiols -- 8.4 Metallic Nitrosyls -- 8.5 Sodium Nitroprusside (Na(2)[Fe(CN)(5)NO] · 2H(2)O) -- 8.6 Organic Nitrates -- 8.7 Organic Nitrites -- 8.8 NONOates -- 8.9 NO Inhalation -- NO Gas as an NO Donor -- 8.10 Sydnonimines -- 8.11 Conclusion -- References -- 9 NO Donors as Antiplatelet Agents -- 9.1 Introduction -- 9.2 Molecular Mechanisms of NO-mediated Platelet Inhibition -- 9.2.1 cGMP-dependent NO Signaling Mechanisms -- 9.2.1.1 Regulation of cGMP Levels -- 9.2.1.2 Effector Sites of cGMP -- 9.2.1.3 cGMP-PK I Substrates in Platelets -- 9.2.1.3.1 Inositol triphosphate (IP(3)) receptor -- 9.2.1.3.2 Rap 1b -- 9.2.1.3.3 Vasodilator stimulated phosphoprotein (VASP) -- 9.2.1.3.4 Heat shock protein hsp27 -- 9.2.1.3.5 LASP -- 9.2.1.3.6 Thromboxane A(2) (TxA(2)) receptor -- 9.2.1.3.7 Phosphodiesterase PDE5 -- 9.2.2 cGMP-independent NO Signaling Mechanisms -- 9.3 Effects of Different Groups of NO Donors on Platelets -- 9.3.1 Diazeniumdiolates -- 9.3.1.1 DEA/NO (Sodium 2-(N,N-diethylamino)-diazenolate-2-oxide) -- 9.3.1.2 DETA NONOate ((Z)-1-[N-(2-Aminoethyl)-N-(2-ammonioethyl) amino]diazen-1-ium-1,2-diolate) -- 9.3.1.3 MAHMA NONOate ((Z-1-[N-Methyl-N-[6-(N-methylammoniohexyl) amino]]diazen-1-ium-1,2-diolate) -- 9.3.2 Sodium Nitroprusside (SNP) -- 9.3.3 Molsidomine (3-Morpholino-sidnonimine -- SIN-1) -- 9.3.4 S-Nitrosothiols -- 9.3.4.1 SNAP (S-Nitroso-N-acetyl-d,1-penicillamine) -- 9.3.4.2 SNVP (S-Nitroso-N-valerylpenicillamine) -- 9.3.4.3 GSNO (S-nitroso-glutatione) -- 9.3.4.4 CysNO (S-Nitrosocysteine) -- 9.3.4.5 SNAC (S-Nitroso-N-acetyl-cysteine) -- 9.3.4.6 HomocysNO (S-Nitrosohomocysteine). , 9.3.4.7 RIG200 (N-(S-Nitroso-N-acetylpenicillamine)-2-amino-2-deoxy-1,3,4,6, tetra-O-acetyl-beta-D-glucopyranose) -- 9.3.5 Organic Nitrates -- 9.3.5.1 GTN (Glyceryl Trinitrate, Nitroglycerin, NTG) -- 9.3.6 Mesoionic Oxatriazole Derivatives -- 9.3.6.1 GEA-3162 (1,2,3,4-Oxatriazolium, 5-amino-3-(3,4-dichlorphenyl)-, cloride) -- 9.3.6.2 GEA-3175 (1,2,3, 4-Oxatriazolium, -3-(3-chloro-2-methylphenyl)-5-[[(4-methylphenyl) sulfonyl]amino]-, Hydroxide Inner Salt) -- 9.3.7 Other NO Donors -- 9.3.7.1 OXINO (Sodium trioxdinitrate or Angel's Salt) -- 9.3.7.2 B-NOD (2-Hydroxy-benzoid acid 3-nitrooxymethyl-phenyl ester) -- 9.3.8 L-Arginine (L-Arg) -- 9.4 Activators of Soluble Guanylyl Cyclase -- 9.4.1 YC-1 (3-(5´-Hydroxymethyl-2´-furyl)-1-benzyl indazole) -- 9.4.2 BAY 41-2272 (3-(4-Amino-5-cyclopropylpyrimidine-2-yl)-1-(2-fluorobenzyl)-1H-pyrazolo [3,4-b]pyridine) -- 9.5 cGMP Analogs -- 9.6 Inhaled NO and Platelet Inhibition -- 9.7 Conclusion -- References -- 10 Control of NO Production -- 10.1 Introduction -- 10.2 Structure of Nitric Oxide Synthase -- 10.3 NO Formation -- 10.4 L-Arginine and L-Arginine Derivatives -- 10.4.1 Inhibitors -- 10.4.2 Substrates -- 10.5 Non-amino Acid Inhibitors and Non-amino Acid Substrates -- 10.5.1 Guanidine -- 10.5.1.1 Inhibitor -- 10.5.1.2 Substrates -- 10.5.2 Isothiourea (ITU) -- 10.5.3 Amidine -- 10.5.4 Cyclic Amidines are Potent iNOS Selective Inhibitors -- 10.5.5 Indazole -- 10.6 Inhibition of NOS Function Targeted towards Cofactors -- 10.7 Regulators of NOS Gene Expression -- 10.8 NO Formation by an NOS-independent Pathway -- 10.8.1 Oxime -- 10.8.2 Hydroxyurea -- 10.9 Summary -- References -- Part 3 Clinical Applications of NO Donors -- 11 Nitric Oxide Donors in Cardiovascular Disease -- 11.1 Introduction -- 11.2 Clinical Cardiovascular Applications of NO Donor Therapy - Past and Present. , 11.3 Pharmacological Cardiovascular Mechanism of Action of NO Donors.

Note: Cover -- Half Title -- Title -- Copyright -- Contents -- Foreword -- Preface -- Authors -- Chapter 1 Introduction -- 1.1 Background and Significance -- 1.1.1 Background of Subpixel Mapping -- 1.1.2 Significance of Subpixel Mapping -- 1.2 Research Status of Subpixel Mapping -- 1.2.1 Initialize-Then-Optimize Subpixel Mapping -- 1.2.2 Soft-Then-Hard Subpixel Mapping -- 1.2.3 Other Types of Subpixel Mapping -- 1.2.4 Research Status of Super-Resolution Technology -- 1.3 Problems in Subpixel Mapping -- 1.4 Main Research Contents and Chapter Arrangement -- References -- Chapter 2 Basic Principles of Subpixel Mapping -- 2.1 Introduction -- 2.2 Spectral Unmixing Method -- 2.2.1 Linear Spectral Unmixing Model -- 2.2.2 Non-linear Spectral Unmixing Model -- 2.3 Theoretical Basis of Spatial Correlation -- 2.4 Processing Flow of Subpixel Mapping -- 2.4.1 Subpixel Sharpening Method -- 2.4.2 Class Allocation Method -- 2.5 Evaluation Method of Subpixel Mapping Accuracy -- 2.6 Summary -- References -- Chapter 3 Subpixel Mapping Based on Single Remote Sensing Image -- 3.1 Introduction -- 3.2 Subpixel Mapping Based on Spatial-Spectral Interpolation -- 3.2.1 Interpolation Problem -- 3.2.2 Existing Subpixel Mapping Based on Interpolation -- 3.2.3 Processing Flow of the Proposed Method -- 3.2.4 Experimental Content and Result Analysis -- 3.3 Subpixel Mapping Based on Hopfield Neural Network With More Supervision Information -- 3.3.1 Traditional Subpixel Mapping Method Based on Hopfield Neural Network -- 3.3.2 Hopfield Neural Network With More Prior Information -- 3.3.3 Experiment Content and Result Analysis -- 3.4 Subpixel Mapping Based on Extended Random Walk -- 3.4.1 Multi-Scale Segmentation Algorithm -- 3.4.2 Extended Random Walk Algorithm -- 3.4.3 Class Allocation Method Based on Object Unit -- 3.4.4 Experimental Content and Result Analysis. , 3.5 Subpixel Mapping Based on Spatial-Spectral Correlation for Spectral Imagery -- 3.5.1 Spatial Correlation -- 3.5.2 Spectral Correlation -- 3.5.3 Spatial-Spectral Correlation Implementation -- 3.5.4 Experimental Content and Result Analysis -- 3.6 Summary -- References -- Chapter 4 Subpixel Mapping Based on Multi-Shift Remote Sensing Images -- 4.1 Introduction -- 4.2 Theoretical Basis -- 4.2.1 Multi-Shift Images Problem -- 4.2.2 Existing Subpixel Mapping Method Based on Multi-Shift Images -- 4.3 Subpixel Mapping Method Based on Multi-Shift With Spatial-Spectral Information -- 4.3.1 Multi-Shift Image With More Spatial-Spectral Information -- 4.3.2 Experiment Content and Result Analysis -- 4.4 Subpixel Mapping Based on the Spatial Attraction Model With Multi-Scale Subpixel Shifted Images -- 4.4.1 Subpixel-Pixel Spatial Attraction Model -- 4.4.2 Subpixel-Subpixel Spatial Attraction Model -- 4.4.3 Spatial Attraction Model With Multi-Scale Subpixel Shifted Image -- 4.4.4 Experiment Content and Result Analysis -- 4.5 Utilizing Parallel Networks to Produce Subpixel Shifted Images With Multi-Scale Spatial-Spectral Information for Subpixel Mapping -- 4.5.1 Multi-Scale Network and Spatial-Spectral Network -- 4.5.2 Multi-Scale Spatial-Spectral Information -- 4.5.3 Experimental Content and Result Analysis -- 4.6 Spatiotemporal Subpixel Mapping by Considering the Point Spread Function Effect -- 4.6.1 Spatial Dependence -- 4.6.2 Temporal Dependence -- 4.6.3 Spatiotemporal Dependence -- 4.6.4 Experimental Content and Result Analysis -- 4.7 Summary -- References -- Chapter 5 Subpixel Mapping of Remote Sensing Image Based on Fusion Technology -- 5.1 Introduction -- 5.2 Soft-Then-Hard Subpixel Mapping Based on Pansharpening Technology -- 5.2.1 Pansharpening Technology -- 5.2.2 STHSRM-PAN -- 5.2.3 Experimental Content and Result Analysis. , 5.3 Subpixel Land Cover Mapping Based on Parallel Processing Path for Hyperspectral Image -- 5.3.1 Fusion Path -- 5.3.2 Deep Learning Path -- 5.3.3 Dual Processing Path -- 5.3.4 Experimental Content and Result Analysis -- 5.4 Subpixel Mapping Based on Multi-Source Remote Sensing Fusion Data for Land Cover Classes -- 5.4.1 Data-Level Fusion -- 5.4.2 Feature Fusion -- 5.4.3 Obtaining Mapping Result -- 5.4.4 Experimental Content and Result Analysis -- 5.5 Summary -- References -- Chapter 6 Remote Sensing Image Subpixel Mapping Based on Classification Then Reconstruction -- 6.1 Introduction -- 6.2 Theoretical Basis -- 6.2.1 Super-Resolution Algorithm -- 6.2.2 Fully Supervised Information Classification Algorithm -- 6.3 Subpixel Mapping Based on MAP Super-Resolution Reconstruction Then Classification -- 6.3.1 Transformed MAP-Based Super-Resolution Reconstruction -- 6.3.2 LSSVM Classification Algorithm -- 6.3.3 Experiment Content and Result Analysis -- 6.4 Subpixel Mapping Based on Pansharpening Then Classification -- 6.4.1 Implementation Steps -- 6.4.2 Experiment Content and Result Analysis -- 6.5 Summary -- References -- Chapter 7 Application of Subpixel Mapping Technology in Remote Sensing Imaging -- 7.1 Introduction -- 7.2 Improving Flood Subpixel Mapping for Multispectral Image by Supplying More Spectral Information -- 7.2.1 Existing SRFIM -- 7.2.2 SRFIM-MSI -- 7.2.3 Experiment Content and Result Analysis -- 7.3 Subpixel Mapping of Urban Buildings Based in Multispectral Image With Spatial-Spectral Information -- 7.3.1 Spaceborne Multispectral Remote Sensing Image -- 7.3.2 Experiment Content and Result Analysis -- 7.4 Multispectral Subpixel Burned-Area Mapping Based on Space-Temperature Information -- 7.4.1 Space Part -- 7.4.2 Temperature Part -- 7.4.3 Implementation of STI -- 7.4.4 Experiment Content and Result Analysis -- 7.5 Summary -- References. , Appendix: Abbreviations -- Content Validity -- Index.

Note: Intro -- Preface -- Contents -- Part I: Background -- Chapter 1: Introduction: Computational Pulse Diagnosis -- 1.1 Principle of Pulse Signal -- 1.2 Traditional Pulse Diagnosis -- 1.3 Computational Pulse Signal Analysis -- 1.4 Summary -- References -- Part II: Pulse Signal Acquisition -- Chapter 2: Compound Pressure Signal Acquisition -- 2.1 Introduction -- 2.2 Application Scenario and Requirement Analysis -- 2.3 System Architecture -- 2.3.1 Mechanical Structure -- 2.3.2 Sensor -- 2.3.3 Circuit -- 2.3.4 Summary -- 2.4 System Evaluation -- 2.4.1 Sampled Pulse Signals -- 2.4.2 Computational Pulse Diagnosis -- 2.4.3 Comparisons with Other Pulse Sampling Systems -- 2.5 Summary -- References -- Chapter 3: Pulse Signal Acquisition Using Multi-sensors -- 3.1 Introduction -- 3.2 Framework of the Proposed System -- 3.2.1 Pulse Collecting -- 3.2.2 Pulse Processing and Interaction Design -- 3.3 Design of the Different Sensor Arrays -- 3.3.1 Pressure Sensor -- 3.3.2 Photoelectric Sensor Array -- 3.3.3 Combination of Pressure and Photoelectric Sensor Arrays -- 3.4 Multichannel Optimization -- 3.4.1 Selection of Base Channel -- 3.4.2 Multichannel Selection -- 3.5 The Optimization of Different Sensors Fusion -- 3.6 Experimental Results -- 3.6.1 Experiment 1 -- 3.6.2 Experiment 2 -- 3.7 Summary -- References -- Part III: Pulse Signal Preprocessing -- Chapter 4: Baseline Wander Correction in Pulse Waveforms Using Wavelet-Based Cascaded Adaptive Filter -- 4.1 Introduction -- 4.1.1 Pulse Waveform Analysis -- 4.1.2 Related Works on Baseline Drift Removal -- 4.2 The Proposed CAF -- 4.2.1 The Design of CAF -- 4.2.2 Detection Level of Baseline Drift Using ER -- 4.2.2.1 Why Detect ER -- 4.2.2.2 How to Compute the ER of Pulse Signal -- 4.2.3 The Discrete Meyer Wavelet Filter -- 4.2.3.1 Design of the Discrete Meyer Wavelet Filter. , 4.2.3.2 Performance of Discrete Meyer Wavelet Filter on Pulse Waveform -- 4.2.4 Cubic Spline Estimation Filter -- 4.2.4.1 Detecting Pulse's Onsets -- 4.2.4.2 Cubic Spline Estimation -- 4.3 Simulated Signals: Experimental Results and Analysis -- 4.3.1 Experimental Results of the CAF for Different Baseline Drifts -- 4.3.2 Experimental Results for Different ER Thresholds -- 4.3.3 Experimental Results for Several Typical Pulses -- 4.4 Experimental Results for Actual Pulse Records -- 4.5 Summary -- References -- Chapter 5: Detection of Saturation and Artifact -- 5.1 Introduction -- 5.2 Saturation and Artifact -- 5.2.1 Saturation -- 5.2.2 Artifact -- 5.3 The Detection of Saturation and Artifact -- 5.3.1 The Preprocessing and the Priority -- 5.3.2 Saturation Detection -- 5.3.3 Artifact Detection -- 5.4 Experimental Results -- 5.4.1 Saturation Detection -- 5.4.2 Artifact Detection -- 5.5 Summary -- References -- Chapter 6: Optimized Preprocessing Framework for Wrist Pulse Analysis -- 6.1 Introduction -- 6.2 Description of Pulse Database -- 6.2.1 Data Acquisition -- 6.2.2 Time Domain Characteristic -- 6.2.3 Frequency Domain Characteristic -- 6.3 Proposed Pulse Preprocessing Method -- 6.3.1 Pulse Denoising -- 6.3.2 Interval Selection -- 6.3.3 Baseline Drift Removal -- 6.3.4 Period Segmentation and Normalization -- 6.4 Experiments on Actual Pulse Database -- 6.4.1 Comparison of Pulse Denoising -- 6.4.2 Optimal Segmentation Strategy -- 6.4.3 Preprocessing for Pulse Diagnosis -- 6.5 Summary -- References -- Part IV: Pulse Signal Feature Extraction -- Chapter 7: Arrhythmic Pulse Detection -- 7.1 Introduction -- 7.2 Clinical Value of Pulse Rhythm Analysis -- 7.3 The Approach to Automatic Recognition of Pulse Rhythms -- 7.3.1 Lempel-Ziv Complexity Analysis -- 7.3.2 Definitions and Basic Facts -- 7.3.2.1 Definitions -- 7.3.2.2 Rules -- 7.3.2.3 Lemma. , 7.3.2.4 The Seven Pulse Patterns' Characteristics in Rhythms -- 7.3.3 Automatic Recognition of Pulse Patterns Distinctive in Rhythm -- 7.3.3.1 Preprocessing the Pulse Waveform -- 7.3.3.2 Pulse Interval Extraction and Calculation of its VC and VR -- 7.3.3.3 Symbolizing Pulse Interval Series and Subsequence Extraction -- 7.3.3.4 Arrhythmic Pulse Recognition Based on Lempel-Ziv Complexity Analysis -- 7.4 Experiments -- 7.5 Summary -- References -- Chapter 8: Spatial and Spectrum Feature Extraction -- 8.1 Introduction -- 8.2 Data Acquisition and Preprocessing -- 8.3 Feature Extraction -- 8.3.1 Spatial Feature Extraction of Blood Flow Velocity Signal -- 8.3.2 EMD-Based Spectrum Feature Extraction -- 8.3.2.1 Hilbert-Huang Transform -- 8.3.2.2 Feature Extraction by Hilbert-Huang Transform -- 8.4 Experimental Result and Discussion -- 8.5 Summary -- References -- Chapter 9: Generalized Feature Extraction for Wrist Pulse Analysis: From 1-D Time Series to 2-D Matrix -- 9.1 Introduction -- 9.2 Wrist Pulse Acquisition and Preprocessing Methods -- 9.2.1 Wrist Pulse Acquisition Platform -- 9.2.2 Wrist Pulse Preprocessing -- 9.3 Conventional Pulse Feature -- 9.3.1 Time Domain Feature -- 9.3.2 Frequency Domain Feature -- 9.4 2-D Pulse Feature Extraction -- 9.4.1 Motivation -- 9.4.2 Matrix Description for Pulse Waveforms -- 9.5 Experiments -- 9.5.1 Diabetes Diagnosis -- 9.5.2 Pregnancy Diagnosis -- 9.6 Summary -- References -- Chapter 10: Characterization of Inter-Cycle Variations for Wrist Pulse Diagnosis -- 10.1 Introduction -- 10.2 The Quasiperiodic Pulse Signals -- 10.3 Characterization of Inter-Cycle Variations -- 10.3.1 Preprocessing -- 10.3.2 The Simple Combination Method -- 10.3.3 Multi-scale Entropy -- 10.3.4 The Complex Network Method -- 10.4 Experimental Results -- 10.4.1 Datasets -- 10.4.2 Experiments and Results -- 10.5 Summary -- References. , Part V: Pulse Analysis and Diagnosis -- Chapter 11: Edit Distance for Pulse Diagnosis -- 11.1 Introduction -- 11.2 The Pulse Waveform Classification Modules -- 11.2.1 Pulse Waveform Acquisition -- 11.2.2 Pulse Waveform Preprocessing -- 11.2.3 Feature Extraction and Classification -- 11.3 The EDCK and GEKC Classifiers -- 11.3.1 Edit Distance with Real Penalty -- 11.3.2 DFWKNN and KDFKNN -- 11.3.3 The EDKC Classifier -- 11.3.4 The GEKC Classifier -- 11.4 Experimental Results -- 11.5 Summary -- References -- Chapter 12: Modified Gaussian Models and Fuzzy C-Means -- 12.1 Introduction -- 12.2 Wrist Pulse Signal Collection and Preprocessing -- 12.3 Feature Extraction and Feature Selection -- 12.3.1 A Two-Term Gaussian Model -- 12.3.2 Feature Selection -- 12.4 FCM Clustering -- 12.5 Experimental Result -- 12.6 Summary -- References -- Chapter 13: Modified Auto-regressive Models -- 13.1 Introduction -- 13.2 The Proposed Method -- 13.2.1 Feature Extraction via AR Modelling -- 13.2.2 SVM Classification -- 13.2.3 The Selection of Doppler Ultrasonic Diagnostic Parameters -- 13.3 Experimental Results -- 13.3.1 Data Description -- 13.3.2 Experimental Results by Using the AR Features -- 13.3.3 Experimental Results by Using the Doppler Parameters as Additional Features -- 13.4 Conclusions and Future Work -- References -- Chapter 14: Combination of Heterogeneous Features for Wrist Pulse Blood Flow Signal Diagnosis via Multiple Kernel Learning -- 14.1 Introduction -- 14.2 Pulse Signal Feature Extraction -- 14.2.1 Nontransform-Based Feature Extraction -- 14.2.1.1 AR Model -- 14.2.1.2 Time Series Matching -- 14.2.2 Transform-Based Feature Extraction -- 14.3 Pulse Signal Classification Based on MKL -- 14.3.1 Kernel Functions -- 14.3.2 SimpleMKL -- 14.4 Experimental Results and Discussion -- 14.4.1 Classification Experimental of Wrist Blood Flow Signal. , 14.4.2 Other Pulse Classification Application -- 14.5 Summary -- References -- Part VI: Comparison and Discussion -- Chapter 15: Comparison of Three Different Types of Wrist Pulse Signals -- 15.1 Introduction -- 15.2 Measurement Mechanism -- 15.2.1 Measurement Mechanism of Pressure Sensors -- 15.2.2 Measurement Mechanism of Photoelectric Sensors -- 15.2.3 Measurement Mechanism of Ultrasonic Sensors -- 15.3 Dependency and Complementarity -- 15.3.1 Assumptions -- 15.3.2 Relationship Among Blood Velocity, Radius, and Pressure in Steady Laminar Flow -- 15.3.3 Influence of Physiological and Pathological Factors -- 15.3.4 Summary -- 15.4 Case Studies -- 15.4.1 Method -- 15.4.2 Diabetes Experiment -- 15.4.3 Arteriosclerosis Experiment -- 15.5 Summary -- References -- Chapter 16: Comparison Between Pulse and ECG -- 16.1 Introduction -- 16.2 Methods -- 16.2.1 Analysis of ECG and Wrist Pulse Signals -- 16.2.2 Acquisition of ECG and Wrist Pulse Signal -- 16.2.3 Construction of the Dataset -- 16.2.4 Entropy-Based Complexity Analysis -- 16.2.5 Classification Accuracy and Statistical Test -- 16.2.5.1 Feature Extraction of Wrist Pulse Blood Flow Signal -- 16.2.5.2 Feature Extraction of ECG Signal -- 16.2.5.3 Classifiers -- 16.2.5.4 McNemar Test -- 16.3 Results -- 16.3.1 Comparison of Complexity Measures -- 16.3.2 Comparison of Classification Performance -- 16.3.3 Typical Examples of Wrist Pulse Blood Flow and ECG Signals -- 16.3.4 Classification Accuracy and McNemar Test -- 16.4 Summary -- References -- Chapter 17: Discussion and Future Work -- 17.1 Recapitulation -- 17.2 Future Work -- References -- Index.