{"product_id":"redox-proteomics-from-protein-modifications-to-cellular-dysfunction-and-diseases-hardback-9780471723455","title":"Redox Proteomics; From Protein Modifications to Cellular Dysfunction and Diseases (Hardback) 9780471723455","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eRedox Proteomics\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eFrom Protein Modifications to Cellular Dysfunction and Diseases\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eIsabella Dalle-Donne (Edited by), I Dalle–Donne (Author), Andrea Scaloni (Edited by), D. Allan Butterfield (Edited by), Dominic M. Desiderio (Series edited by), Nico M. Nibbering (Series edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780471723455, Wiley\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 11 July 2006\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e976 pages, Charts: 35 B\u0026amp;W, 0 Color; Photos: 11 B\u0026amp;W, 0 Color; Drawings: 50 B\u0026amp;W, 0 Color; Tables: 29 B\u0026amp;W, 0 Color; Graphs: 68 B\u0026amp;W, 0 Color\u003cbr\u003e24.1 x 16.3 x 4.8 cm, 1.429 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\"...a major book...readers interested in mass spectrometry methods in proteomics will find much that is of interest here.\" (\u003ci\u003eJournal of the American Society for Mass Spectrometry\u003c\/i\u003e, March 2007)  \u003cp\u003e\"Every laboratory that uses redox proteomics in both clinical and academic research should possess a copy of this excellent book.\" (\u003ci\u003eDoody's Health Services\u003c\/i\u003e)\u003c\/p\u003e \u003cp\u003e\"…highly recommended as a reference text…Redox Proteomics is thought to be a milestone in this field…\" (\u003ci\u003eBiotechnology Journal,\u003c\/i\u003e March 2007)\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eMethodology and applications of redox proteomics\u003cbr\u003e \u003cbr\u003e \u003cbr\u003e \u003cbr\u003e The relatively new and rapidly changing field of redox proteomics has the potential to revolutionize how we diagnose disease, assess risks, determine prognoses, and target therapeutic strategies for people with inflammatory and aging-associated diseases. This collection brings together, in one comprehensive volume, a broad array of information and insights into normal and altered physiology, molecular mechanisms of disease states, and new applications of the rapidly evolving techniques of proteomics.\u003cbr\u003e \u003cbr\u003e Written by some of the finest investigators in this area, Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases examines the key topics of redox proteomics and redox control of cellular function, including:\u003cbr\u003e * The role of oxidized proteins in various disorders\u003cbr\u003e * Pioneering studies on the development of redox proteomics\u003cbr\u003e * Analytical methodologies for identification and structural characterization of proteins affected by oxidative\/nitrosative modifications\u003cbr\u003e * The response and regulation of protein oxidation in different cell types\u003cbr\u003e * The pathological implications of protein oxidation for conditions, including asthma, cardiovascular disease, diabetes, preeclampsia, and Alzheimer's disease\u003cbr\u003e \u003cbr\u003e \u003cbr\u003e Distinguished by its in-depth discussions, balanced methodological approach, and emphasis on medical applications and diagnosis development, Redox Proteomics is a rich resource for all professionals with an interest in proteomics, cellular physiology and its alterations in disease states, and related fields.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePreface xxiii\u003c\/p\u003e \u003cp\u003eContributors xxvii\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart I Oxidatively Modified Proteins and Proteomic Technologies 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Chemical Modification of Proteins by Reactive Oxygen Species 3\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eEarl R. Stadtman and Rodney L. Levine\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 3\u003c\/p\u003e \u003cp\u003e1.2 Peptide Bond Cleavage 5\u003c\/p\u003e \u003cp\u003e1.3 β-Scission 6\u003c\/p\u003e \u003cp\u003e1.4 Oxidation of Amino Acid Residue Side Chains 7\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 The Chemistry of Protein Modifications Elicited by Nitric Oxide and Related Nitrogen Oxides 25\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eDouglas D. Thomas, Lisa Ridnour, Sonia Donzelli, Michael Graham Espey, Daniele Mancardi, Jeffery S. Isenberg, Martin Feelisch, David D. Roberts, and David A. Wink\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 25\u003c\/p\u003e \u003cp\u003e2.2 Chemical Biology of NO 26\u003c\/p\u003e \u003cp\u003e2.3 Chemistry of Metabolite Formation 40\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Mass Spectrometry Approaches for the Molecular Characterization of Oxidatively\/Nitrosatively Modified Proteins 59\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAndrea Scaloni\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 59\u003c\/p\u003e \u003cp\u003e3.2 Mass Spectrometry Analysis of Oxidatively\/Nitrosatively Modified Proteins 61\u003c\/p\u003e \u003cp\u003e3.3 Proteomic Strategies for the Identification of ROS\/RNS Protein Targets in Biological Matrices 76\u003c\/p\u003e \u003cp\u003e3.4 Conclusions 84\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Thiol-Disulfide Oxidoreduction of Protein Cysteines: Old Methods Revisited for Proteomics 101\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eValentina Bonetto and Pietro Ghezzi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction: Protein Thiols from Oxidative Stress to Redox Regulation 101\u003c\/p\u003e \u003cp\u003e4.2 Different Redox States of Protein Cysteines 102\u003c\/p\u003e \u003cp\u003e4.3 Methodologies to Identify and Quantify the Redox State of Protein Cysteines 104\u003c\/p\u003e \u003cp\u003e4.4 Methods to Detect Specific Modifications 108\u003c\/p\u003e \u003cp\u003e4.5 Methods for Enriching Redox-Regulated Proteins 111\u003c\/p\u003e \u003cp\u003e4.6 Structural and Physicochemical Determinants for the Susceptibility of Cysteines toward Oxidation 112\u003c\/p\u003e \u003cp\u003e4.7 Perspective 114\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Carbonylated Proteins and Their Implication in Physiology and Pathology 123\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRodney L. Levine and Earl. R. Stadtman\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 123\u003c\/p\u003e \u003cp\u003e5.2 Types of Oxidative Modifications and Choice of Marker 133\u003c\/p\u003e \u003cp\u003e5.3 Methodological Considerations 134\u003c\/p\u003e \u003cp\u003e5.4 Selected Studies 136\u003c\/p\u003e \u003cp\u003e5.5 Carbonylation during Aging 136\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 S-Nitrosation of Cysteine Thiols as a Redox Signal 169\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eYanhong Zhang and Neil Hogg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 169\u003c\/p\u003e \u003cp\u003e6.2 Mechanisms of Formation of S-Nitrosothiols 170\u003c\/p\u003e \u003cp\u003e6.3 Cellular Transduction of the S-Nitroso Group 176\u003c\/p\u003e \u003cp\u003e6.4 S-Nitrosothiols and Redox Proteomics 178\u003c\/p\u003e \u003cp\u003e6.5 S-Nitrosothiols as an Intracellular Signal 179\u003c\/p\u003e \u003cp\u003e6.6 Conclusions 182\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Detection of Glycated and Glyco-Oxidated Proteins 189\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAnnunziata Lapolla, Elisa Basso, and Pietro Traldi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 189\u003c\/p\u003e \u003cp\u003e7.2 MALDI-MS in the Study of In vitro Glycated Proteins 196\u003c\/p\u003e \u003cp\u003e7.3 MALDI-MS in the Evaluation of Glycation Levels of HSA and IgG in Diabetic Patients 201\u003c\/p\u003e \u003cp\u003e7.4 HbA\u003csub\u003e1c\u003c\/sub\u003e and the Real Globin Glycation and Glyco-Oxidation 205\u003c\/p\u003e \u003cp\u003e7.5 Determination of Dicarbonyl Compound Levels in Diabetic and Nephropathic Patients 209\u003c\/p\u003e \u003cp\u003e7.6 AGE\/Peptides: An In vitro Study and In vivo Preliminary Results 212\u003c\/p\u003e \u003cp\u003e7.7 Expected Future Trends 226\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 MudPIT (Multidimensional Protein Identification Technology) for Identification of Post-translational Protein Modifications in Complex Biological Mixtures 233\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eStefani N. Thomas, Bing-Wen Lu, Tatiana Nikolskaya, Yuri Nikolsky, and Austin J. Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 233\u003c\/p\u003e \u003cp\u003e8.2 Proteomic Analysis of Oxidatively Modified Proteins 234\u003c\/p\u003e \u003cp\u003e8.3 Statistical Validation and Interpretation of MudPIT Data 241\u003c\/p\u003e \u003cp\u003e8.4 Concluding Remarks 249\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Use of a Proteomic Technique to Identify Oxidant-Sensitive Thiol Proteins in Cultured Cells 253\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMark B. Hampton, James W. Baty, and Christine C. Winterbourn\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 253\u003c\/p\u003e \u003cp\u003e9.2 Fluorescence Labeling and Proteomic Analysis of Oxidized Thiol Proteins 254\u003c\/p\u003e \u003cp\u003e9.3 Detection of Thiol Protein Oxidation in Jurkat Cells 256\u003c\/p\u003e \u003cp\u003e9.4 Detection of Reversible and Irreversible Thiol Oxidation 258\u003c\/p\u003e \u003cp\u003e9.5 Oxidized Thiol Compared with Reduced Thiol Measurements 259\u003c\/p\u003e \u003cp\u003e9.6 More Selective Thiol Labeling Protocols 260\u003c\/p\u003e \u003cp\u003e9.7 Identification of Oxidant-Sensitive Proteins 261\u003c\/p\u003e \u003cp\u003e9.8 Conclusions and Future Directions 261\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 ICAT (Isotope-Coded Affinity Tag) Approach to Redox Proteomics: Identification and Quantification of Oxidant-Sensitive Protein Thiols 267\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMahadevan Sethuraman, Mark E. McComb, Hua Huang, Sequin Huang, Tyler Heibeck, Catherine E. Costello, and Richard A. Cohen\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 267\u003c\/p\u003e \u003cp\u003e10.2 Oxidant-Sensitive Cys 268\u003c\/p\u003e \u003cp\u003e10.3 Challenges in Redox Proteomics 268\u003c\/p\u003e \u003cp\u003e10.4 Iodoacetamide-Based Redox Proteomics 269\u003c\/p\u003e \u003cp\u003e10.5 ICAT Approach to Redox Proteomics 271\u003c\/p\u003e \u003cp\u003e10.6 Validation of the ICAT Approach Using the Recombinant Protein Creatine Kinase 271\u003c\/p\u003e \u003cp\u003e10.7 ICAT Approach to the Complex Protein Mixtures 275\u003c\/p\u003e \u003cp\u003e10.8 Perspectives 282\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Quantitative Determination of Free and Protein-Associated 3-Nitrotyrosine and S-Nitrosothiols in the Circulation by Mass Spectrometry and Other Methodologies: A Critical Review and Discussion from the Analytical and Review Point of View 287\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eDimitrios Tsikas\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 287\u003c\/p\u003e \u003cp\u003e11.2 Methods of Analysis 295\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e \u003cp\u003e11.3 S-Nitrosothiols and 3-Nitrotyrosine in Health and Disease 314\u003c\/p\u003e \u003cp\u003e11.4 Considerations from the Analytical and Review Points of View 326\u003c\/p\u003e \u003cp\u003e11.5 Concluding Remarks and Future Prospects 329\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II Cellular Aspects of Protein Oxidation 343\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 The Covalent Advantage: A New Paradigm for Cell Signaling Mediated by Thiol Reactive Lipid Oxidation Products 345\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eDale A. Dickinson, Victor M. Darley-Usmar, and Aimee Landar\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 345\u003c\/p\u003e \u003cp\u003e12.2 Cyclooxygenase and the Conversion of Nonreactive Lipids to Thiol Switching Molecules 346\u003c\/p\u003e \u003cp\u003e12.3 Lipid Peroxidation and the Nonenzymatic Formation of Lipid Adducts Capable of Modifying Proteins 349\u003c\/p\u003e \u003cp\u003e12.4 The Thiol Switch and Redox Cell Signaling 351\u003c\/p\u003e \u003cp\u003e12.5 Biological Responses to Endogenous Electrophilic Lipid Production 353\u003c\/p\u003e \u003cp\u003e12.6 A New Paradigm of Oxidized Lipid Signaling—The Covalent Advantage 353\u003c\/p\u003e \u003cp\u003e12.7 Implications for the Pathophysiology of Disease 356\u003c\/p\u003e \u003cp\u003e12.8 Summary 358\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Early Molecular Events during Response to Oxidative Stress in Human Cells by Differential Proteomics 369\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eGianluca Tell\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 369\u003c\/p\u003e \u003cp\u003e13.2 Cellular Response to Oxidative Stress: From Membrane Receptors to Gene Expression Control 374\u003c\/p\u003e \u003cp\u003e13.3 Gene Expression Control during Cell Response to Oxidative Stress: Redox-Regulated Transcription Factors 382\u003c\/p\u003e \u003cp\u003e13.4 The Power of Differential Proteomics in Detecting Early Molecular Markers of Oxidative Stress: Examples from Human Cell Lines 383\u003c\/p\u003e \u003cp\u003e13.5 Conclusions 388\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Oxidative Damage to Proteins: Structural Modifications and Consequences in Cell Function 399\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eElisa Cabiscol and Joaquim Ros\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 399\u003c\/p\u003e \u003cp\u003e14.2 Glycolysis 400\u003c\/p\u003e \u003cp\u003e14.3 Pyruvate Metabolism 426\u003c\/p\u003e \u003cp\u003e14.4 Tricarboxylic Acid Cycle 432\u003c\/p\u003e \u003cp\u003e14.5 Electron Transport Chain and Oxidative Phosphorylation 437\u003c\/p\u003e \u003cp\u003e14.6 Antioxidant Defenses 443\u003c\/p\u003e \u003cp\u003e14.7 Molecular Chaperones 447\u003c\/p\u003e \u003cp\u003e14.8 Cytoskeleton 451\u003c\/p\u003e \u003cp\u003e14.9 Conclusions 454\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Oxidative Damage and Cellular Senescence: Lessons from Bacteria and Yeast 473\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eThomas Nyström\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Microbial Senescence 473\u003c\/p\u003e \u003cp\u003e15.2 Protein Carbonylation—An Irreversible Oxidative Damage to Proteins 474\u003c\/p\u003e \u003cp\u003e15.3 Bacterial Senescence and Protein Carbonylation 476\u003c\/p\u003e \u003cp\u003e15.4 Replicative Senescence and Segregation of Carbonylated Proteins 478\u003c\/p\u003e \u003cp\u003e15.5 Yeast Senescence, Protein Oxidation, and Oncogenesis 479\u003c\/p\u003e \u003cp\u003e15.6 Perspective 479\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III Redox Proteomic Analysis in Human Diseases 485\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Proteins as Sensitive Biomarkers of Human Conditions Associated with Oxidative Stress 487\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eIsabella Dalle-Donne, Ranieri Rossi, Fabrizio Ceciliani, Daniela Giustarini, Roberto Colombo, and Aldo Milzani\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction 487\u003c\/p\u003e \u003cp\u003e16.2 Oxidative Stress in Human Diseases and Animal Models 489\u003c\/p\u003e \u003cp\u003e16.3 Biomarkers of Oxidative Stress Status (BOSS) 493\u003c\/p\u003e \u003cp\u003e16.4 Proteins as Biomarkers of Oxidative Stress Status 504\u003c\/p\u003e \u003cp\u003e16.5 Conclusions 512\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Degradation and Accumulation of Oxidized Proteins in Age-Related Diseases 527\u003cbr\u003e \u003c\/b\u003e\u003ci\u003ePeter Voss and Tilman Grune\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Oxidative Modifications of Amino Acids and Protein Damage 527\u003c\/p\u003e \u003cp\u003e17.2 Degradation and Accumulation of Oxidatively Modified Proteins 532\u003c\/p\u003e \u003cp\u003e17.3 Oxidized Proteins in Age-Related Diseases 543\u003c\/p\u003e \u003cp\u003e17.4 Summary 547\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Redox Proteomics: A New Approach to Investigate Oxidative Stress in Alzheimer’s Disease 563\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eD. Allan Butterfield, Rukhsana Sultana, and H. Fai Poon\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Introduction 563\u003c\/p\u003e \u003cp\u003e18.2 Brain Tissue and Models Used in Studying Aβ(1–42)-Induced Oxidative Stress and Neurotoxicity in AD 565\u003c\/p\u003e \u003cp\u003e18.3 Redox Proteomics 567\u003c\/p\u003e \u003cp\u003e18.4 Oxidatively Modified Proteins in AD and AD Models by Redox Proteomics 572\u003c\/p\u003e \u003cp\u003e18.5 Conclusion 585\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 Oxidized Proteins in Cardiac Ischemia and Reperfusion 605\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJonathan P. Brennan and Philip Eaton\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19.1 Introduction to Cardiac Ischemia and Reperfusion 605\u003c\/p\u003e \u003cp\u003e19.2 Oxidatively Modified Proteins in the Heart 616\u003c\/p\u003e \u003cp\u003e19.3 Established Targets of Post-translational Oxidation 624\u003c\/p\u003e \u003cp\u003e19.4 Oxidative Stress in Myocardial Adaptation to Ischemia and Reperfusion 628\u003c\/p\u003e \u003cp\u003e19.5 Conclusions, Therapeutic Implications, and Future Directions 631\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 Proteome Analysis of Oxidative Stress: Glutathionyl Hemoglobin in Diabetic and Uremic Patients 651\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eToshimitsu Niwa\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20.1 Introduction 651\u003c\/p\u003e \u003cp\u003e20.2 Glutathionyl Hb as a Marker of Oxidative Stress 653\u003c\/p\u003e \u003cp\u003e20.3 Conclusion 663\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 Glyco-oxidative Biochemistry in Diabetic Renal Injury 669\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eToshio Miyata\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e21.1 Presence of Local, but not Generalized, Oxidative Stress in Diabetes 669\u003c\/p\u003e \u003cp\u003e21.2 Oxidative Protein Damage In vivo 670\u003c\/p\u003e \u003cp\u003e21.3 Antioxidative Properties of Medical Agents 671\u003c\/p\u003e \u003cp\u003e21.4 Therapeutic Perspectives for AGE Inhibitors 672\u003c\/p\u003e \u003cp\u003e21.5 AGE Inhibition and Renoprotection 673\u003c\/p\u003e \u003cp\u003e21.6 Future Prospects 676\u003c\/p\u003e \u003cp\u003e\u003cb\u003e22 Quantitative Screening of Protein Glycation, Oxidation, and Nitration Adducts by LC-MS\/MS: Protein Damage in Diabetes, Uremia, Cirrhosis, and Alzheimer’s Disease 681\u003cbr\u003e \u003c\/b\u003e\u003ci\u003ePaul J. Thornalley\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e22.1 Introduction: Derivatization Free Detection with Application to Modified Proteins and Amino Acids 681\u003c\/p\u003e \u003cp\u003e22.2 Physiological Sources of Glycated, Oxidized, and Nitrated Amino Acid Residues and Free Adducts 689\u003c\/p\u003e \u003cp\u003e22.3 Protein Glycation and Oxidation in Diabetes: Damage to Cellular and Extracellular Proteins 694\u003c\/p\u003e \u003cp\u003e22.4 Profound Mishandling of Glycated, Oxidized, and Nitrated Amino Acids in Uremia 702\u003c\/p\u003e \u003cp\u003e22.5 Increased Glycated and Oxidized Amino Acids of Blood Plasma in Liver Cirrhosis—A Signature of Hepatic Oxidative Stress 704\u003c\/p\u003e \u003cp\u003e22.6 Increased Methylglyoxal-Derived Hydroimidazolone and 3-Nitrotyrosine Free Adducts in Cerebrospinal Fluid of Subjects with Alzheimer’s Disease—A Signature of Neuronal Damage 707\u003c\/p\u003e \u003cp\u003e22.7 Glycation Adducts in Food and Beverages 710\u003c\/p\u003e \u003cp\u003e22.8 Concluding Remarks: Physiological Formation and Proteolytic Processing of Glycated, Oxidized, and Nitrated Proteins in Disease Processes—The Importance of Measuring “Damage and Debris” 714\u003c\/p\u003e \u003cp\u003e\u003cb\u003e23 Protein Targets and Functional Consequences of Tyrosine Nitration in Vascular Disease 729\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eLaura M. S. Baker, Bruce A. Freeman, and Mutay Aslan\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e23.1 Association of Vascular Disease with Increased Production of Reactive Oxygen\/Nitrogen Species and Accumulation of Nitrated Proteins 729\u003c\/p\u003e \u003cp\u003e23.2 Production of Reactive Oxygen and Nitrogen Species in the Vasculature 731\u003c\/p\u003e \u003cp\u003e23.3 Tyrosine Nitration Mechanisms 734\u003c\/p\u003e \u003cp\u003e23.4 Methods for Detecting Nitrotyrosine 742\u003c\/p\u003e \u003cp\u003e23.5 Selectivity of Tyrosine Nitration 745\u003c\/p\u003e \u003cp\u003e23.6 Mechanistic Consequences of Nitrotyrosine Formation: Protein Nitration In vivo and Vascular Disease 747\u003c\/p\u003e \u003cp\u003e23.7 Metabolism, Reversibility, and Stability of the Nitrated Tyrosine 764\u003c\/p\u003e \u003cp\u003e23.8 Tyrosine Nitration as a Cell Signaling Event 767\u003c\/p\u003e \u003cp\u003e23.9 Summary 769\u003c\/p\u003e \u003cp\u003e\u003cb\u003e24 Oxidation of Artery Wall Proteins by Myeloperoxidase: A Proteomics Approach 787\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eTomas Vaisar and Jay W. Heinecke\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e24.1 Oxidative Stress in Atherosclerosis 787\u003c\/p\u003e \u003cp\u003e24.2 Potential Role of Redox-Active Metal Ions and Glucose in Oxidative Stress 789\u003c\/p\u003e \u003cp\u003e24.3 Potential Role of Cellular Pathways in Oxidative Stress 790\u003c\/p\u003e \u003cp\u003e24.4 Evidence for Oxidative Modification of LDL in the Human Artery Wall 793\u003c\/p\u003e \u003cp\u003e24.5 Oxidative Modification of HDL 796\u003c\/p\u003e \u003cp\u003e24.6 Oxidative Regulation of Matrix Metalloproteinases 798\u003c\/p\u003e \u003cp\u003e24.7 Conclusions 804\u003c\/p\u003e \u003cp\u003e\u003cb\u003e25 Oxidative Stress and Protein Oxidation in Pre-Eclampsia 813\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMaarten T. M. Raijmakers, Wilbert H. M. Peters, Christianne J. de Groot, and Eric A. P. Steegers\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e25.1 Introduction 813\u003c\/p\u003e \u003cp\u003e25.2 Oxidative Stress and Pre-Eclampsia 814\u003c\/p\u003e \u003cp\u003e25.3 Proteomics 820\u003c\/p\u003e \u003cp\u003e\u003cb\u003e26 Involvement of Oxidants in the Etiology of Chronic Airway Diseases: Proteomic Approaches to Identify Redox Processes in Epithelial Cell Signaling and Inflammation 831\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAlbert van der Vliet, Niki L. Reynaert, Peter F. Bove, Karina Ckless, Anne-Katrin Greul, Milena Hristova, and Yvonne M. Janssen-Heininger\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e26.1 Introduction 831\u003c\/p\u003e \u003cp\u003e26.2 Chronic Airway Inflammation: Conditions Associated with Oxidative and Nitrosative Stress 832\u003c\/p\u003e \u003cp\u003e26.3 Biological Significance of Protein Oxidation 836\u003c\/p\u003e \u003cp\u003e26.4 Proteomic Approaches to Study Protein Oxidation in Airway Disease 847\u003c\/p\u003e \u003cp\u003e26.5 Tissue Proteomics and Application to Study Protein Oxidation 857\u003c\/p\u003e \u003cp\u003e26.6 Summary and Conclusions 861\u003c\/p\u003e \u003cp\u003e\u003cb\u003e27 Sequestering Agents of Intermediate Reactive Aldehydes as Inhibitors of Advanced Lipoxidation End-Products (ALEs) 877\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMarina Carini, Giancarlo Aldini, and Roberto Maffei Facino\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e27.1 Introduction 877\u003c\/p\u003e \u003cp\u003e27.2 Lipoxidation-Derived Reactive Aldehydes 880\u003c\/p\u003e \u003cp\u003e27.3 Intervention against Lipoxidation-Derived Carbonyl Stress: ALE Inhibitors 893\u003c\/p\u003e \u003cp\u003e27.4 Conclusions and Future Perspective 913\u003c\/p\u003e \u003cp\u003eIndex 931\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Chemistry [\u003ca title=\"See our other books on Chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Chemistry%20%5BPN%5D%22\"\u003ePN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Wiley-Interscience","offers":[{"title":"Brand New","offer_id":52298045063448,"sku":"9780471723455","price":147.99,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/files\/9780471723455.jpg?v=1781732510","url":"https:\/\/freshlyprintedbooks.co.uk\/products\/redox-proteomics-from-protein-modifications-to-cellular-dysfunction-and-diseases-hardback-9780471723455","provider":"Freshly Printed Books","version":"1.0","type":"link"}