Kooperativer Bibliotheksverbund

UID:

Format: 1 Online-Ressource (VII, 249 p. 36 illus., 16 illus. in color).

ISBN: 978-981-10-3707-8

Additional Edition: Erscheint auch als Druck-Ausgabe ISBN 978-981-10-3706-1

Language: English

Subjects: Biology

DOI: 10.1007/978-981-10-3707-8

URL: Volltext  (URL des Erstveröffentlichers)

URL: Volltext  (URL des Erstveröffentlichers)

UID:

Format: 1 online resource (390 pages)

ISBN: 0-12-811950-0

Content: 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.--

Note: 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.

Additional Edition: ISBN 0-12-811913-6

Language: English

UID:

Format: vii, 249 Seiten : , Illustrationen.

ISBN: 978-981-10-3706-1

Additional Edition: Erscheint auch als Online-Ausgabe ISBN 978-981-10-3707-8

Language: English

Subjects: Biology

UID:

Format: 1 online resource.

Edition: First edition.

ISBN: 9781003145394 , 1003145396 , 9781000344264 , 1000344266 , 9781000344325 , 1000344320 , 9781000344295 , 1000344290

Content: "This volume, The Glycome: Understanding the Diversity and Complexity of Glycobiology, provides a comprehensive understanding of the enigmatic identity of the glycome, a complex but important area of research, one largely ignored because of its complexity. In this volume, the authors thoroughly deal with almost all aspects of the glycome, i.e., elucidation of the glycan identity enigma and its role in regulation of the cellular process and in disease etiology. It bridges the knowledge gap in understanding the glycome, from being a cell signature to its applications in disease etiology. In addition, it details many of the major insights regarding the possible role of the glycome in various diseases as a therapeutic marker. The book systematically covers the major aspects of the glycome, including the significance of substituting the diverse monosaccharide units to glycoproteins, the role of glycans in disease pathologies, and the challenges and advances in glycobiology. The authors stress the significance and huge encoding power of carbohydrates as well as provide helpful insights in framing the bigger picture. The authors begin with an introduction to the trends and developments in glycobiology and then proceed to discussing its role in disease pathologies, followed by its roles in other organisms, including bacteria, plants, and as stress busters. Chapters cover the involvement of the glycome in congenital and noncongenital disorders, the role of glycans in immunological processes, the role of glycans in neurodegeneration and metastasis, the involvement of glycans in host-pathogen interaction, and their role in microbial infection and the immune evasion. The book also provides insights into the therapeutic aspects of acylation as a vital glycosylational modification of proteins. A chapter highlights the scenario of glycans in plants while another discusses glycans as stress coping agents. The Glycome: Understanding the Diversity and Complexity of Glycobiology details state-of-the-art developments and emerging challenges of glycome biology, which are going to be key areas of future research, not only in the glycobiology field but also in pharmaceutics. "--

Note: Trends and Advancements in Glycobiology: Towards Development of Glycan-Based Therapeutics / Yaser Rafiq Mir and Raja Amir H. Kuchay -- Defects in the Human Glycome: Congenital and Non-Congenital Disorders / Mumtaz Anwar -- Glycome in Immunological Processes: Current Scenario and Future Prospects / Zeba Mueed, Manali Singh, Abhay Mishra, and Nitesh Kumar Poddar -- Role of Glycans in Neurodegeneration / Abhai Kumar and Smita Singh -- Glycome in Metastasis: Glycan Remodeling and Tumor Progression / Ayyagari Archana, Durgashree Dutta, Safikur Rahman, and Rinki Minakshi -- Glycans in the Host-Pathogen Interaction / Muzafar Jan and Sunil K. Arora -- Glycome in Microbial Infections and Immune Evasion / Abid Qureshi -- Acylation as a Vital Post-Glycosylation Modification of Proteins: Insights and Therapeutics Prospects / Usma Manzoor, Snowber Shabir Wani, Fasil Ali, Parvaiz A. Dar, and Tanveer Ali Dar -- Glycome Profiling in Plants: Towards Understanding the Scenario of Carbohydrates / Reetika Mahajan, Muslima Nazir, Jahangir A. Dar, Shazia Mukhtar, Muntazir Mushtaq, Susheel Sharma, Jasdeep Chatrath Padaria, Shafiq A. Wani, and Sajad Majeed Zargar -- Sugars: Coping the Stress in Plants / Ritika Rajpoot.

Additional Edition: Print version: Glycome. Palm Bay, FL, USA ; Burlington, ON, Canada : Apple Academic Press ; Boca Raton, FL, USA ; Abingdon, Oxon, UK : CRC Press, 2021 ISBN 1771889977

Additional Edition: ISBN 9781771889971

Language: English

Keywords: Electronic books.

DOI: 10.1201/9781003145394

URL: https://www.taylorfrancis.com/books/9781003145394

UID:

Format: 1 Online-Ressource (VII, 249 p. 36 illus., 16 illus. in color).

ISBN: 978-981-10-3707-8

Additional Edition: Erscheint auch als Druck-Ausgabe ISBN 978-981-10-3706-1

Language: English

Subjects: Biology

DOI: 10.1007/978-981-10-3707-8

URL: Volltext  (URL des Erstveröffentlichers)

UID:

Format: 1 Online-Ressource (VII, 249 p. 36 illus., 16 illus. in color).

ISBN: 978-981-10-3707-8

Additional Edition: Erscheint auch als Druck-Ausgabe ISBN 978-981-10-3706-1

Language: English

Subjects: Biology

DOI: 10.1007/978-981-10-3707-8

URL: Volltext  (URL des Erstveröffentlichers)

UID:

Format: 1 online resource (218 pages)

Edition: 2nd ed. 2024.

ISBN: 9789819760015

Content: The second edition of this book presents the role of osmolytes in human health and diseases. Some of the chapters deal about the possibility of the use of osmolytes as diagnostic biomarkers and potential drug design for neurodegenerative and other human diseases. Other chapters also include reviews on the role of osmolytes in cancer, metastasis, infectious diseases, metabolic disorders, immunological disorders, and tissue regeneration. Importantly, the book also contain recent updates on the role of naturally occurring osmolytes in protein folding pathway, protein stability, and their underlying mechanisms. The book also covers the aspects that osmolytes could promote conformational alterations of transcription factors that favor metastatic behavior. Potential of the osmolytes in the various process of vaccine development, including enhancing the efficacy, production, and purification steps are also succintly described. Towards the end, the book also elucidates the use of specific molecules for the prevention of toxic gain of functions and restoration of function to disease-causing mutant protein. This book is an invaluable asset for the researchers especially working in osmolyte biology and scientists involved in basic and clinical research particularly neurodegeneration, diabetes, cancer, and metabolic disorders.

Note: Chapter 1_Protein folding pathways in the presence of osmolytes -- Chapter 2_Effect of Organic Osmolytes on protein folding Intermediates -- Chapter 3_Role of TMAO on folding behavior of various proteins associated with neurodegeneration -- Chapter 4_Osmolyte-Mediated Protein Stabilization: Unraveling Interactions Across Conformational Landscapes -- Chapter 5_Osmolytes as a promising therapeutic strategy for protein aggregation diseases -- Chapter 6_Involvement of osmolytes in the pathophysiology of various human diseases -- Chapter 7_Role of osmolytes in cancer -- Chapter 8_Harnessing the power of osmolyte for industrial and pharmaceutical applications -- Chapter 9_Diverse biological functions of Myoinositol: A neuro-metabolite, osmoprotectant and diagnostic marker -- Chapter 10_Potential of osmolytes as Diagnostic Biomarkers in various Diseases -- Chapter 11_Osmolytes as stress sensors in plants: Acclimatizing plants under stress conditions.

Additional Edition: Print version: Singh, Laishram Rajendrakumar Cellular Osmolytes Singapore : Springer,c2024 ISBN 9789819760008

Language: English

DOI: 10.1007/978-981-97-6001-5

UID:

Format: XII, 210 p. 21 illus., 17 illus. in color. , online resource.

Edition: 2nd ed. 2024.

ISBN: 9789819760015

Content: The second edition of this book presents the role of osmolytes in human health and diseases. Some of the chapters deal about the possibility of the use of osmolytes as diagnostic biomarkers and potential drug design for neurodegenerative and other human diseases. Other chapters also include reviews on the role of osmolytes in cancer, metastasis, infectious diseases, metabolic disorders, immunological disorders, and tissue regeneration. Importantly, the book also contain recent updates on the role of naturally occurring osmolytes in protein folding pathway, protein stability, and their underlying mechanisms. The book also covers the aspects that osmolytes could promote conformational alterations of transcription factors that favor metastatic behavior. Potential of the osmolytes in the various process of vaccine development, including enhancing the efficacy, production, and purification steps are also succintly described. Towards the end, the book also elucidates the use of specific molecules for the prevention of toxic gain of functions and restoration of function to disease-causing mutant protein. This book is an invaluable asset for the researchers especially working in osmolyte biology and scientists involved in basic and clinical research particularly neurodegeneration, diabetes, cancer, and metabolic disorders.

Note: Chapter 1_Protein folding pathways in the presence of osmolytes -- Chapter 2_Effect of Organic Osmolytes on protein folding Intermediates -- Chapter 3_Role of TMAO on folding behavior of various proteins associated with neurodegeneration -- Chapter 4_Osmolyte-Mediated Protein Stabilization: Unraveling Interactions Across Conformational Landscapes -- Chapter 5_Osmolytes as a promising therapeutic strategy for protein aggregation diseases -- Chapter 6_Involvement of osmolytes in the pathophysiology of various human diseases -- Chapter 7_Role of osmolytes in cancer -- Chapter 8_Harnessing the power of osmolyte for industrial and pharmaceutical applications -- Chapter 9_Diverse biological functions of Myoinositol: A neuro-metabolite, osmoprotectant and diagnostic marker -- Chapter 10_Potential of osmolytes as Diagnostic Biomarkers in various Diseases -- Chapter 11_Osmolytes as stress sensors in plants: Acclimatizing plants under stress conditions.

In: Springer Nature eBook

Additional Edition: Printed edition: ISBN 9789819760008

Additional Edition: Printed edition: ISBN 9789819760022

Additional Edition: Printed edition: ISBN 9789819760039

Language: English

DOI: 10.1007/978-981-97-6001-5

URL: https://doi.org/10.1007/978-981-97-6001-5

UID:

Format: 1 online resource (390 pages)

ISBN: 0-12-811950-0

Content: 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.--

Note: 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.

Additional Edition: ISBN 0-12-811913-6

Language: English

UID:

Format: 1 online resource (390 pages)

ISBN: 0-12-811950-0

Content: 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.--

Note: 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.

Additional Edition: ISBN 0-12-811913-6

Language: English