Note: Includes bibliographical references and index

Note: Literaturverzeichnis: Seite 53-56

Note: Literaturverz. S. 607 - 645

Note: Literaturverzeichnis: Seite 26-28

Note: Literaturverzeichnis: Seite 40-44

Note: Electrochrornisrn: Fundamentals and Applications -- Contents -- List of Tables -- Symbols and Abbreviations -- Part I Introduction -- 1 Electrochromism: Terminology, Scope, Colouration -- 1.1 What is Electrochromism? -- 1.2 Existing Technologies -- 1.3 Electrochromic Displays and Shutters -- 1.4 Terminology of Electrochromism -- 1.4.1 Primary and Secondary Electrochromism -- 1.4.2 Colour and Contrast Ratio -- 1.4.3 Colouration Efficiency -- 1.4.4 Write-erase Efficiency -- 1.4.5 Response Time -- 1.4.6 Cycle Life -- 1.4.7 The Insertion Coefficient -- 1.4.8 ECD Appearanlx -- References -- 2 Electrochromic Systems: Electrochemistry, Kinetics and Mechanism -- 2.1 Introduction -- 2.2 Equilibrium Electrochemistry -- 2.3 Electrochromic Operation Exemplified -- 2.4 Voltammetry -- 2.4.1 Introduction to Dynamic Elecuochemisuy: The Three-Electrode Configuration -- 2.4.2 The Use of Voltammetry -- Cyclic Voltammetry -- 2.5 Charge Transfer and Charge Transport -- 2.5.1 The Kinetics of Electron Transfer -- 2.5.2 The Use of Semiconducting Electrodes -- 2.5.3 The Rate of Mass Transport -- 2.5.3.1 Migration -- 2.5.3.2 Diffusion -- 2.6 AC or RF Electrochemistry: Impedance or Complex Permittivity Studies -- 2.7 Electrodes: Classification of Electrochrome Type -- 2.7.1 Type 1 Electrochromes: Always in Solution -- 2.7.2 Type 2 Electrochromes: Solution-to-Solid -- 2.7.3 Type 3 Electrochromes: All-Solid Systems -- References -- 3 Construction of Electrochromic Devices -- 3.1 Introduction -- 3.2 All-Solid Cells with Reflective Operation -- 3.3 All-Solid Cells with Transmissive Operation -- 3.4 Solid Electrolytes -- 3.5 The Preparation of Solid Electrochromic Films -- 3.6 Liquid Electrolytes -- 3.7 Self-Darkening Electrochromic Rearview Mirror for Cars Employing Type 1 (Solution-phase) Electrochromes -- References -- Part II Electrochromic Systems -- General Introduction. , References -- A Inorganic Systems -- 4 Metal Oxides -- 4.1 Introduction - Colour in Mixed-valence Systems -- 4.2 Cobalt Oxide -- 4.3 Indium Tin Oxide -- 4.4 Iridium Oxide -- 4.5 Molybdenum Trioxide -- 4.6 Nickel Oxide -- 4.7 Tungsten Trioxide -- 4.7.1 Operation of WO3 ECDs -- 4.7.2 Structure, Preparation and Diffusion Characteristics -- 4.7.3 Spectroscopic and Optical Effects -- 4.8 Vanadium Pentoxide -- 4.9 Other Metal Oxides -- 4.9.1 Cerium Oxide -- 4.9.2 Iron Oxide -- 4.9.3 Manganese Oxide -- 4.9.4 Niobium Pentoxide -- 4.9.5 Palladium Oxide -- 4.9.6 Rhodium Oxide -- 4.9.7 Ruthenium Dioxide -- 4.9.8 Titanium Oxide -- 4.10 Mixed Metal Oxides -- 4.10.1 Cobalt Oxide Mixtures -- 4.10.2 Molybdenum Trioxide Mixtures -- 4.10.3 Nickel Oxide Mixtures -- 4.10.4 Tungsten Trioxide Mixtures -- 4.10.5 Vanadium Oxide Mixtures -- 4.10.6 Miscellaneous Metal Oxide Mixtures -- 4.10.7 Ternary Oxide Mixtures -- 4.11 Metal Oxide - Organic Mixtures -- References -- 5 Phthalocyanine Compounds -- 5.1 Introduction -- 5.2 Lutetium bis(Phthalocyanine) -- 5.3 Other Metal Phthalccyanines -- 5.4 Related Species -- References -- 6 Prussian Blue: Its Systems and Analogues -- 6.1 Introduction: Historical and Bulk Properties -- 6.2 Preparation of Prussian Blue Thin Films -- 6.3 Prussian Blue Electrochromic Films: Cyclic Voltammetry, In Situ Spectroscopy and Characterisation -- 6.4 Prussian Blue ECDs -- 6.4.1 ECDs with Prussian Blue as Sole Electrochrome -- 6.4.2 Prussian-Blue - Tungsten-Trioxide ECDs -- 6.4.3 Prussian-Blue - Polyaniline ECDs -- 6.4.4 A Prussian-Blue - Ytterbium - bis(phthalocyanine) ECD -- 6.5 Prussian Blue Analogues -- 6.5.1 Ruthenium Purple and Osmium Purple -- 6.5.2 Vanadium Hexacyanoferrate -- 6.5.3 Nickel Hexacyanoferrate -- 6.5.4 Copper Hexacyanoferrate -- 6.5.5 Miscellaneous Metal Hexacyanometallates -- 6.5.6 Mixed Metal Hexacyanoferrates -- References. , 7 Other Inorganic Systems -- 7.1 Deposition of Metals -- 7.2 Deposition of Colloidal Material -- 7.3 Intercalation Layers -- 7.4 Inclusion and Polymeric Systems -- 7.5 Miscellaneous -- References -- B Organic Systems -- 8 Bipyridilium Systems -- 8.1 Introduction -- 8.2 Bipyridilium Redox Chemistry -- 8.3 Bipyridilium Species for Inclusion Within ECDs -- 8.3.1 Derivatised Electrodes for ECD Inclusion -- 8.3.2 Immobilised Bipyridilium Elechochromes for ECD Inclusion -- 8.3.3 Soluble-to-Insoluble Bipyriddium Electrochromes for ECD Inclusion -- 8.3.3.1 Devices -- 8.3.3.2 The Effect of the Electrode Substrate -- 8.3.3.3 The Effect of the Counter Ion -- 8.3.3.4 Kinetics and Mechanism -- 8.3.3.5 The Write-erase Efficiency -- 8.4 Recent Developments -- 8.4.1 Modulated Light Scattering -- 8.4.2 Pulsed Potentials -- 8.4.3 Polyelectrochromism -- References -- 9 Electroactive Conducting Polymers -- 9.1 Introduction -- 9.2 Polyaniline Electrochromes -- 9.2.1 Polymers Derived from Substituted Anilines -- 9.2.2 Polymers Derived from Other Aromatic Amines -- 9.2.3 Composite Polyaniline Materials -- 9.3 Polypyrrole Elechochromes -- 9.3.1 Polymers Derived from Substituted Pyrroles -- 9.3.2 Polymers Derived from Pyrrole Analogues -- 9.3.3 Composite Polypyrrole Electrochromes -- 9.4 Polythiophene Electrochromes -- 9.4.1 Polymers Derived from Thiophene -- 9.4.2 Polymers Derived from Substituted Thiophenes -- 9.4.3 Polymers Derived from Oligothiophenes -- 9.4.4 Polymers Derived from bis(2-Thienyl) Species -- 9.4.5 Polymers Derived from Fused-ring Thiophenes -- 9.4.6 Polythiophene Copolymers and Composite Materials -- 9.5 Poly(carbazole) -- 9.6 Miscellaneous Polymeric Electrochromes -- 9.7 Recent Developments -- References -- 10 Other Organic Electrochromes -- 10.1 Monomeric Species -- 10.1.1 Carbazoles -- 10.1.2 Methoxybiphenyl Compounds -- 10.1.3 Quinones. , 10.1.4 Diphenylamine and Phenylene Diamines -- 10.1.5 Miscellaneous Monomeric Electrochromes -- 10.2 Tethered Electrochmic Species -- 10.2.1 Pyrazolines -- 10.2.2 Tetracyanoquinodimethane (TCNQ) -- 10.2.3 Tetrathiafulvalene (TTF) -- 10.3 Electrochromes Immobilised by Viscous Solvents -- References -- Part III Elaborations -- 11 Polyelectrochromism -- 11.1 Introduction -- 11.2 Studies of Polyelectrochromic Systems -- 11.2.1 Bipyridiliums -- 11.2.2 Polybipyridyl Systems -- 11.2.3 Metal Hexacyanometallates -- 11.2.4 Phthalocyanines -- 11.2.5 Tris(dicarboxyester-2,2'-bipyridine) Ruthenium Systems -- 11.2.6 Mixed Systems -- References -- 12 Photoelectrochromism and Electrochromic Printing -- 12.1 Introduction and Definitions -- 12.1.1 Mode of Operation -- 12.1.2 Direction of Beam -- 12.2 Device Types -- 12.2.1 Devices Containing a Photocell -- 12.2.2 Devices Containing Photoconductive Layers -- 12.2.3 Cells Containing Photovoltaic Materials -- 12.2.4 Cells Containing Photogalvanic Materials -- 12.2.5 Electrochemically Fixed Photochromic Systems -- 12.3 Electrochromic Printing or Electrochromography -- 12.3.1 Introduction: Monochrome Printing -- 12.3.2 Polyelectrochromic Printing: Single Electrochromes -- 12.3.3 Four-colour Printing with Mixed Electrochromes -- References -- Index.

Note: Cover -- Half Title -- Title Page -- Copyright Page -- Contents -- Preface -- Editors -- Contributors -- Chapter 1: Introduction -- Chapter 2: DNA Replication and Cell Cycle Control -- Chapter 3: DNA Replication Termination and Genomic Instability -- Chapter 4: Mechanisms of DNA Damage Tolerance -- Chapter 5: The Repair of DNA Single-Strand Breaks and DNA Adducts: Mechanisms and Links to Human Disease -- Chapter 6: Homologous Recombination at Replication Forks -- Chapter 7: Mechanism of Double-Strand Break Repair by Non-Homologous End Joining -- Chapter 8: Protein Methylation and the DNA Damage Response -- Chapter 9: Ubiquitin, SUMO and the DNA Double-Strand Break Response -- Chapter 10: Transcription in the Context of Genome Stability Maintenance -- Chapter 11: RNA Binding Proteins and the DNA Damage Response -- Chapter 12: DNA Replication and Inherited Human Disease -- Chapter 13: Ataxia Telangiectasia and Ataxia Telangiectasia-Like Disorders -- Chapter 14: DNA Repair Mechanisms in Stem Cells and Implications during Ageing -- Chapter 15: Targeting Replication Stress in Sporadic Tumours -- Chapter 16: A Few of the Many Outstanding Questions -- Index.

Note: Cover -- Title Page -- Copyright Page -- Contents -- Introduction to the Book -- Long-Lived Proteins Are Ubiquitous -- Aging -- Autoimmunity -- Age-Related Diseases -- Our Lenses in the Vanguard -- Brain and Memory -- Chapter 1 Long-Lived Cells and Long-Lived Proteins in the Human Body -- 1.1 What Constitutes a Long-Lived Cell and a Long-Lived Protein? -- 1.2 Aim of the Chapter -- 1.3 Aging -- 1.4 Location of LLPs Within the Body -- 1.4.1 ECM and Tissue Function -- 1.5 Extracellular LLPs -- 1.5.1 Several ECM Components Are Long Lived -- 1.5.1.1 Elastin -- 1.5.1.2 Structural Glycoproteins and Proteoglycans -- 1.5.1.3 Collagens -- 1.6 Intracellular LLPs and LLCs -- 1.6.1 LLCs and LLPs in the Organs of the Body -- 1.7 Organs and Tissues that Contain LLCs or LLPs -- 1.7.1 Long-Lived Cells -- 1.7.1.1 Eye -- 1.7.1.2 Oocytes -- 1.7.1.3 Kidneys -- 1.7.1.4 Adipose Tissue -- 1.7.1.5 Brain -- 1.7.1.6 Heart -- 1.7.1.7 Lung -- 1.7.1.8 Skeleton -- 1.7.1.9 Teeth -- 1.7.1.10 Hair -- 1.7.1.11 Joints -- 1.7.1.12 Pancreas -- 1.7.1.13 Liver -- 1.7.1.14 Intestine -- 1.7.1.15 Dividing Cells and LLPs -- 1.7.2 Sensory Tissues -- 1.7.2.1 Hearing -- 1.7.2.2 Smell -- 1.8 Protein Changes and DNA Changes with Age -- 1.9 Processes Responsible for the Breakdown of LLPs -- 1.10 Oxidation: Methionine Sulfoxide Reductases and the Glutathione System -- 1.11 Consequences of LLP Decomposition -- 1.11.1 Protein Modification and Cellular Processing -- 1.11.2 Lifelong Proteins and the Consequences -- 1.12 LLPs and Age-Related Disorders -- 1.12.1 Modified LLPs Acting as Novel Antigens: Autoimmune Diseases -- 1.12.2 Defects in Cytosol/Nuclear Communication -- 1.12.3 Defects in Nuclear Transcription -- 1.12.4 Breakdown of Abundant Macromolecules -- 1.12.5 Elastin -- 1.12.6 Collagen -- 1.13 Neurological Diseases Where LLPs May be Implicated -- 1.13.1 Multiple Sclerosis. , 1.13.2 Motor Neuron Disease (MND)/Amyotrophic Lateral Sclerosis (ALS) -- 1.13.3 Alzheimer Disease (AD) -- 1.14 Aging DNA and LLPs -- 1.15 How Can the Role of LLPs in Aging and Disease Be Investigated? What Can Be Done -- 1.15.1 Heterogeneity of Aged LLPs: A Large Hurdle to Overcome -- 1.16 We Will Not Live Forever -- 1.16.1 LLP Degradation and Tissue Function: Is There a Threshold for Decay? -- 1.16.2 Lifelong Proteins May Degrade at Similar Rates -- 1.16.3 Decay in Tissue Function with Age and Its Effect on Fitness, Health, and Mortality -- 1.16.4 LLPs and Life Span -- 1.16.5 Heart -- 1.16.6 Lung -- 1.16.7 Nerves and Brain -- 1.17 Conclusion -- Acknowledgments -- References -- Chapter 2 Imaging Mass Spectrometry of Long-Lived Proteins -- 2.1 Introduction -- 2.2 Imaging Mass Spectrometry Methods -- 2.2.1 General Considerations -- 2.2.2 MALDI-IMS -- 2.2.3 Desorption Electrospray Ionization (DESI)-IMS -- 2.2.4 Secondary Ion Mass Spectrometry (SIMS)-IMS -- 2.2.5 Other IMS Methods -- 2.3 Protein Identification -- 2.4 LLPs in the Body -- 2.4.1 Lens -- 2.4.2 Optic Nerve -- 2.4.3 Retina -- 2.4.4 Brain and CNS -- 2.4.5 Cartilage -- 2.5 Long-Lived Cells and Structures -- 2.6 Future Directions -- References -- Chapter 3 Eye Lens Crystallins: Remarkable Long-Lived Proteins -- 3.1 Introduction -- 3.2 Eye Lens and Its Transparency -- 3.3 Lens Crystallin Proteins -- 3.3.1 α-Crystallins -- 3.3.2 β- and γ-Crystallins -- 3.4 Congenital, Early Onset, and Age-Related Cataract -- 3.5 Protein Aggregation and Disease, Particularly Cataract -- 3.5.1 Protein Unfolding and Aggregation and Molecular Chaperones -- 3.5.2 Amyloid Fibril and Amorphous Protein Aggregates -- 3.5.3 Diseases Associated with Protein Aggregation -- 3.5.4 Crystallin Aggregation and Cataract -- 3.6 Concluding Comments -- References. , Chapter 4 Spontaneous Breakdown of Long-Lived Proteins in Aging and Their Implications in Disease -- 4.1 Introduction -- 4.2 LLPs Are Found Throughout the Body -- 4.3 Spontaneous Modifications of Aging -- 4.3.1 Deamidation, Racemization, and Isomerization -- 4.3.2 Cross-linking -- 4.3.3 Truncation -- 4.3.4 Age, Disease, and Spontaneous PTMs: General Considerations -- 4.4 LLPs and Onset of Disease: Is Correlation the Only Answer? -- 4.4.1 Eye -- 4.4.1.1 Lens and Age-Related Nuclear Cataract -- 4.4.1.2 Retina, Vitreous Humor, and Sclera -- 4.4.2 Central Nervous System -- 4.4.2.1 Multiple Sclerosis -- 4.4.2.2 Alzheimer's Disease -- 4.4.2.3 Parkinson's Disease -- 4.4.2.4 Amyotrophic Lateral Sclerosis/Motor Neuron Disease -- 4.4.2.5 Systemic Lupus Erythematosus -- 4.4.3 Extracellular Matrix Proteins -- 4.4.3.1 Articular Cartilage, Intervertebral Disc, and Osteoarthritis -- 4.4.3.2 Circulatory System -- 4.4.3.3 Respiratory System -- 4.4.4 Digestive System -- 4.4.4.1 Diabetes -- 4.5 Spontaneous Modifications: Detrimental or Beneficial? -- 4.5.1 NGR Motifs -- 4.5.2 Bcl-xL -- 4.6 Protein Turnover Slows with Age -- 4.7 Potential Treatment of Diseases Initiated by LLPs -- 4.8 Future Outlook -- Acknowledgments -- References -- Chapter 5 Modifications of Long-Lived Proteins that Affect Protein Solubility -- 5.1 Introduction -- 5.2 Insoluble Protein Definition -- 5.3 Insolubilization Due to Disulfide Bonding -- 5.3.1 Disulfide Bonding Is Strongly Correlated with Age-Related Cataracts -- 5.3.2 Levels of Disulfide Bonding at Individual Cysteines in Cataractous Lenses -- 5.3.3 Identity of Individual Disulfide Cross-links in Crystallins of Aged Lenses -- 5.4 Insolubilization Due to Nondisulfide Cross-links -- 5.4.1 Cross-links Due to Dehydroalanine Formation -- 5.4.2 Cross-links Due to C-Terminal Anhydrides -- 5.5 Insolublization Due to Protein Fragmentation. , 5.5.1 Introduction: Protein Hydrolysis and Insolubilization -- 5.5.2 Proteolysis as a Driver of Protein Insolublization in Animal Lenses -- 5.5.3 Nonenzymatic Hydrolysis as a Driver of Protein Insolublization in Human Lenses -- 5.6 Insolublization Due to Deamidation, Isomerization, and Racemization -- 5.7 In vitro Studies of How PTMs Alter Protein Structure and Solubility -- 5.7.1 In vitro Studies of Disulfide Bonding -- 5.7.2 In Vitro Studies of Deamidation -- 5.8 Proteomics Methods to Detect Post-translation Modifications Contributing to Protein Insolublization -- 5.8.1 Crystallins as Ideal Proteins to Detect Age-Related PTMs -- 5.8.2 Two-Dimensional Liquid Chromatography/Mass Spectrometry to Detect PTMs -- 5.8.3 Searches for Known PTMs -- 5.8.4 Searches for Unknown PTMs -- 5.8.5 Identifying Disulfide Cross-links -- 5.8.6 Identifying Deamidation Sites -- 5.8.7 Identifying Isomerization Sites -- 5.8.8 Identifying Racemization Sites -- 5.8.9 Peptide Standards to Study Deamidation, Isomerization, and Racemization -- 5.9 Future PTM Studies of Long-Lived Proteins -- 5.10 Concluding Remarks -- Acknowledgments -- References -- Chapter 6 Degradation of Long-Lived Proteins as a Cause of Autoimmune Diseases -- 6.1 Introduction -- 6.1.1 Background -- 6.1.2 Autoimmunity: Long-Lived Proteins and Long-Lived Cells -- 6.1.3 Focus of this Chapter -- 6.2 Long-Lived Cells Are Widespread in the Body -- 6.3 Long-Lived Proteins Are Present in Many Tissues -- 6.4 Long-Lived Proteins Decompose Over Time -- 6.5 Defenses Against LLP Decomposition -- 6.5.1 Rebuilding Degraded Asp and Asn Sites Within a Protein -- 6.5.2 Oxidation-Related Modification Repair Enzymes and Antioxidants -- 6.6 Consequences of Long-Lived Protein Decomposition -- 6.7 Individual Autoimmune Diseases -- 6.7.1 Pancreas -- 6.7.2 Nerves -- 6.7.3 Stomach -- 6.7.4 Blood Vessels. , 6.7.5 Gastrointestinal Tract -- 6.7.6 Liver -- 6.7.7 Thyroid Gland -- 6.7.8 Adrenal Gland -- 6.7.9 Joints -- 6.7.10 Multiple Sites -- 6.7.11 Skin -- 6.7.12 Moisture-Secreting Glands -- 6.7.13 Blood -- 6.7.14 Muscles -- 6.7.15 Heart -- 6.8 Person-to-Person Variability in Breakdown of LLPs: Multiple Sclerosis -- 6.8.1 Why Do Not All Adults Develop Autoimmune Disorders? -- 6.8.2 Widespread LLPs and Modulation of an Immune Response -- 6.9 Conclusions and Future Research -- Acknowledgments -- References -- Chapter 7 How Isomerization and Epimerization in Long-Lived Proteins Affect Lysosomal Degradation and Proteostasis -- 7.1 Proteostasis -- 7.2 Invisible Modifications -- 7.3 Repair -- 7.4 Identification -- 7.5 Protein Turnover -- 7.6 Mechanistic Considerations -- 7.7 Prevention -- 7.8 Conclusion -- Acknowledgments -- References -- Chapter 8 The Maillard Reaction: Protein Modification by Ascorbic Acid -- 8.1 Introduction -- 8.2 Ascorbic Acid Homeostasis in the Lens: A Dual Sword -- 8.3 Ascorbic Acid as a Source of Age-Related Damage to the Lens -- 8.4 Chemical Pathways of Ascorbic Acid Degradation In Vitro and the Human Lens -- 8.5 Advanced Glycation End Products that have been Detected in the Human Lens -- 8.6 Glucose vs. Ascorbic Acid as a Source of Advanced Glycation End Products in the Lens -- 8.7 Ascorbic Acid as a Major Source of Oxoaldehydes in Lens and Brain -- 8.8 Significance of Advanced Glycation/Ascorbylation Products in the Lens and Brain -- 8.9 Conclusions -- Acknowledgments -- References -- Index -- EULA.