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Umfang: 1 online resource (390 pages)

ISBN: 0-12-811950-0

Inhalt: Protein Modificomics: From Modifications to Clinical Perspectives comprehensively deals with all of the most recent aspects of post-translational modification (PTM) of proteins, including discussions on diseases involving PTMs, such as Alzheimer's, Huntington's, X-linked spinal muscular atrophy-2, aneurysmal bone cyst, angelman syndrome and OFC10. The book also discusses the role PTMs play in plant physiology and the production of medicinally important primary and secondary metabolites. The understanding of PTMs in plants helps us enhance the production of these metabolites without greatly altering the genome, providing robust eukaryotic systems for the production and isolation of desired products without considerable downstream and isolation processes. Provides thorough insights into the posttranslational modifications (PTMs) of proteins in both the plant and animal kingdom. Presents diagrammatic representations of various protein modification and estimation mechanisms in four-colors. Includes coverage of diseases involving posttranslational modifications.--

Anmerkung: Front Cover -- Protein Modificomics: From Modifications to Clinical Perspectives -- Copyright -- Contents -- Contributors -- Preface -- Chapter 1: Posttranslational Modifications of Proteins and Their Role in Biological Processes and Associated Diseases -- 1. Introduction -- 2. Major Posttranslational Modifications -- 2.1. Acetylation -- 2.2. Glycosylation and Glycation -- 2.3. Hydroxylation -- 2.4. Phosphorylation -- 2.5. Ubiquitination -- 2.6. Methylation -- 2.7. Amidation -- 2.8. Palmitoylation -- 2.9. Myristoylation -- 2.10. Prenylation -- 2.11. Proteolytic Cleavage -- 3. Functions of Posttranslational Modifications -- 3.1. Role of PTM in Apoptosis and Cancer -- 3.1.1. Regulation of Apoptosis by Posttranslational Modifications of Caspases -- 3.1.2. Role in Cancer -- 3.2. Role of PTM in Signaling -- 4. Diseases Associated With Posttranslational Modifications -- 4.1. Relation Between Mutated Posttranslational Modification Sites and Diseases -- 4.2. Acetylation and Related Diseases -- 4.3. Glycosylation and Related Diseases -- 4.4. PTM of Proteins During Intermittent Hypoxia -- 5. Role of Posttranslational Modifications in Protein-Protein Interaction -- 6. Role of PTMs in Replication -- 6.1. Ubiquitinylation by Unperturbed DNA Replication -- 6.2. PTMs of Replication Protein A -- 7. Role of PTMs in Transcription -- 7.1. Regulation of Activity of Transcription Factor by PTMs -- 8. Role of PTMs in Translation -- 9. Chemical and Functional Aspects of Protein PTMs -- 10. Role of PTMs in Histone Modification -- 11. Conclusion and Future Prospectus -- References -- Further Reading -- Chapter 2: Clinical Perspective of Posttranslational Modifications -- 1. Introduction -- 2. Glycosylation -- 2.1. Congenital Diseases -- 2.1.1. Congenital Disorders of Glycosylation (CDGs) -- 2.1.2. Congenital Muscular Dystrophies (CMDs) -- 2.2. Neurodegenerative Diseases. , 2.3. Cancer -- 3. Acetylation -- 4. Phosphorylation -- 5. Carbonylation -- 6. Methylation -- 7. Hydroxylation -- 8. Nitration -- 9. Sulfation -- 10. Palmitoylation -- 11. Conclusion and Future Perspective -- References -- Chapter 3: Phosphorylation and Acetylation of Proteins as Posttranslational Modification: Implications in Human Health an ... -- 1. Introduction -- 2. Phosphorylation -- 2.1. Heat Shock Protein (Hsp27) -- 2.2. KRAS -- 2.3. NF-κB and IκB -- 2.4. Cytochrome c (Cyt-c) -- 2.5. Epidermal Growth Factor Receptor -- 2.6. P53 -- 2.7. Eukaryotic Translation Initiation Factor 2α (elf2α) -- 2.8. Tau Protein -- 2.9. Insulin Resistant Substrate Protein (IRS-1) -- 3. Protein Acetylation -- 3.1. Histone Acetylation -- 3.1.1. Signal Transducer and Activator of Transcription (STAT) Protein -- 3.1.2. Interferon Regulatory Factor (IRF) -- 3.1.3. Hsp 90 -- 3.1.4. Pyruvate Kinase -- 3.1.5. Huntingtin Protein (Htt Protein) -- 4. Conclusion and Future Prospects -- References -- Chapter 4: Protein Modifications and Lifestyle Disorders -- 1. Introduction -- 2. Deregulated Adipocyte Proteome in Obesity -- 3. Proteostasis in Diabetes -- 4. Protein Modification in Cardiovascular Diseases -- 5. Modified Proteome in Rheumatoid Arthritis -- 6. Conclusion and Future Aspects -- References -- Further Reading -- Chapter 5: Ubiquitin Mediated Posttranslational Modification of Proteins Involved in Various Signaling Diseases -- 1. Introduction -- 2. Ubiquitination in Inflammatory Pathways -- 3. Implications of UPS in Cancer -- 3.1. E3 Ubiquitin Ligases in Development of Cancer -- 3.1.1. p53-Associated E3 Ligases -- 3.1.1.1. Mdm2 -- 3.1.1.2. E6-AP -- 3.1.1.3. ARF-BP1 -- 3.1.1.4. COP1 -- 3.1.1.5. Pirh2 -- 3.1.2. Other E3 Ubiquitin Ligases Involved in Cancer Development -- 3.1.2.1. SKP1-Cullin 1-F-Box Protein (SCF) E3 Ligases. , 3.1.2.2. BRCA1 /BARD1 as an E3 Ubiquitin Ligase -- 3.1.2.3. Von Hippel-Lindau (VHL) Tumor Suppressor Gene -- 3.1.2.4. Nedd4-Like E3 Ligases -- 3.2. Role of Deubiquitinating Enzymes (DUBs) in Cancer -- 3.2.1. Herpes Associated Ubiquitin Specific Protease (HAUSP) or USP7 -- 3.2.2. Usp28 -- 3.2.3. USP9x -- 3.2.4. USP2a -- 3.2.5. A20 -- 3.2.6. CYLD -- 4. E3 Ligases in Diabetic Retinopathy (DR) -- 5. Implications of UPS in Neurodegenerative Diseases -- 5.1. Alzheimer's Disease -- 5.2. Parkinson's Disease (PD) -- 5.3. Huntington's Disease -- 5.4. Amyotrophic Lateral Sclerosis (ALS) -- 5.5. Angelman Syndrome -- 6. Implications of UPS in Renal Disorders -- 6.1. Liddle Syndrome -- 6.2. Ischemic Acute Renal Failure -- 7. Conclusion and Future Perspectives -- References -- Chapter 6: Role of Glycosylation in Modulating Therapeutic Efficiency of Protein Pharmaceuticals -- 1. Introduction -- 2. Challenges Associated With Protein Pharmaceuticals -- 2.1. Physical Instability -- 2.2. Aggregation -- 2.3. Solubility Issue -- 2.4. Chemical Degradation -- 2.5. Degradation by Proteases -- 3. Protein Glycosylation and Its Pharmacological Significance -- 4. Modulation of Therapeutically Important Properties of Proteins by Glycoengineering -- 4.1. Physical and Chemical Properties -- 4.2. Aggregation -- 4.3. Half-Life Extension -- 4.4. Immunogenicity -- 4.5. Protein Drug Delivery -- 4.6. Diagnostic Therapeutics -- 5. Conclusion and Future Direction -- References -- Chapter 7: Posttranslational Modification of Heterologous Human Therapeutics in Plant Host Expression Systems -- 1. Introduction -- 2. N-Glycosylation as a Major Posttranslational Modification -- 3. Factors Affecting the Natural Glycosylation of Plant-Farmed Human Pharmaceuticals -- 3.1. Subcellular Compartmentalization -- 3.2. The Protein Structures -- 3.3. Environmental and Physiological Factors. , 4. Plant Cell Culture Versus Whole Plant Cultivation for Biopharmaceutical Production -- 5. Developing Humanized and Improved Glycoproteins -- 6. Glycoengineering: Concept of ``Biobetters´´ and ``Biosimilars´´ -- 7. Success Stories -- 8. Ebola Virus Infection -- 9. Gaucher's Disease -- 10. Monoclonal Antibodies -- 11. Vaccines -- 12. Benefits of Plant Expression System -- 13. Limitations of Plant Expression System -- 14. Conclusion and Future Prospects -- References -- Chapter 8: Protein Modification in Plants in Response to Abiotic Stress -- 1. Introduction -- 2. Abiotic Stress in Plants -- 3. Types of Abiotic Stress in Plants and the Proteins Involved Therein -- 3.1. Drought Stress and Associated Proteins -- 3.2. Cold Stress and Cold-Induced Proteins -- 3.3. Salinity Stress and the Proteins Induced Thereby -- 3.4. Heat Stress and Heat Shock Induced Proteins -- 3.5. Heavy Metal Stress and the Proteins Involved -- 3.6. Flooding Stress in Plants -- 4. Protein Modification in Plants in Response to Stress -- 4.1. Phosphorylation -- 4.2. Acetylation -- 4.3. Glycosylation -- 4.4. Succinylation -- 4.5. Ubiquitination -- 4.6. S-Nitrosylation and Tyrosine Nitration -- 5. Conclusion and Future Perspective -- References -- Further Reading -- Chapter 9: Posttranslational Modifications Associated With Cancer and Their Therapeutic Implications -- 1. Introduction -- 2. Posttranslational Modifications That Regulate the Mdm2-p53 Interaction -- 3. Modification of Retionblastoma Tumor Suppressor Protein (pRB) and Its Association to Cell Cycle Progression -- 4. Regulation of NF-κB by Various Posttranslational Modifications -- 5. Regulation of Gene Expression Via Histone and Histone Deacetylase Modifications -- 6. Deregulation of Tyrosine Kinase by Posttranslational Modifications -- 7. Posttranslational Modifications in Ras/Raf/MEK/ERK in MAPK Pathway. , 8. Modification of Signal Transducers and Activators of Transcription -- 9. Phosphorylation of Cyclin-Dependent Kinases and Their Therapeutic Implications -- 10. Posttranslational Modification in Cadherins -- 11. Prenylation and G-Protein Coupled Receptors -- 12. Summary and Future Perspectives -- References -- Chapter 10: Nonenzymatic Posttranslational Protein Modifications: Mechanism and Associated Disease Pathologies -- 1. Introduction -- 2. Carbamylation -- 2.1. Mechanism -- 2.2. Contribution to Diseases -- 2.2.1. Chronic Kidney Disease -- 2.2.2. Cardiovascular Disease -- 2.2.3. Sickle Cell Disease and Cataracts -- 2.2.4. Rheumatoid Arthritis -- 2.2.5. Other Pathologies -- 3. Carbonylation -- 3.1. Mechanism -- 3.2. Contribution in Diseases -- 3.2.1. Alzheimer's Disease -- 3.2.2. Chronic Lung Disease -- 3.2.3. Disuse Muscle Atrophy -- 3.2.4. Chronic Renal Failure -- 3.2.5. Diabetes -- 4. N-Homocysteinylation -- 4.1. Mechanism -- 4.2. Contribution to Diseases -- 4.2.1. Tau Homocysteinylation -- 4.2.2. Prion Protein -- 5. S-Nitrosylation -- 5.1. Mechanism -- 5.2. Contribution to Diseases -- 5.2.1. Neurodegeneration -- 5.2.2. Cancer -- 6. Glycation -- 6.1. Mechanism -- 6.2. Contribution to Diseases -- 6.2.1. Diabetic Complications -- 6.2.1.1. Retinopathy -- 6.2.1.2. Cardiomyopathy -- 6.2.2. Alzheimer's Disease -- 6.2.3. Parkinson's Disease -- 7. Summary -- Acknowledgment -- References -- Chapter 11: Protein Covalent Modification by Homocysteine: Consequences and Clinical Implications -- 1. Introduction -- 2. Homocysteine and Protein Homocysteinylation -- 3. Protein S-Homocysteinylation -- 4. Protein N-Homocysteinylation -- 4.1. HTL Induced Covalent Modification Leads to Molten Globule State Formation -- 4.2. N-Homocysteinylation-Induced Structural Alteration is Protein Dependent -- 4.3. Reactivity Toward HTL-Induced Covalent Modification. , 4.4. N-Homocysteinylation Induces Aggregate or Amyloid Formation.

Weitere Ausg.: ISBN 0-12-811913-6

Sprache: Englisch