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Muestra
Ficha Técnica
Descripción

Approx.280 pages

  • Discusses underlying cellular and molecular mechanisms altered in protein-associated neurodegenerative disorders
  • Describes methods for detection and analysis of protein aggregates
  • Features advancements in therapeutics and emerging techniques to treat these disorders
  • Covers implications in a variety of neurodegenerative diseases, including Alzheimer's, Parkinson’s, ALS, Creutzfeldt-Jakob disease, Cystic fibrosis, Gaucher's disease, and Polyglutamine diseases, including Huntington’s and other related proteinopathies

1. 1 Introduction - p. 67 2. 2 Proteostasis with the paradigms of protein folding, misfolding, and aggregation - p. 72 3. 3 Role of protein quality control and unfolded protein response system in neurodegenerative diseases - p. 79 4. 4 Neurodegenerative disorders caused by protein folding, misfolding, and aggregation - p. 87 5. 5 Impact of oxidative stress on cellular proteostasis, autophagy, protein folding, misfolding, and aggregation - p. 97 6. 6 Cellular and molecular mechanisms related to neurodegeneration as a consequence of protein aggregations and misfolding - p. 103 7. 7 Future prospects - p. 105 8. 8 Conclusion - p. 106 9. Chapter Five. Alterations in protein quality control resulting in neurodegeneration and disease - p. 123 10. Chapter six. Role of molecular chaperones and co-chaperones in maintaining proteostasis - p. 177 11. 1 Introduction - p. 177 12. 2 Proteostasis and the paradigm of protein folding and misfolding - p. 179 13. 3 Protein quality control system (PQC) - p. 191 14. 4 Structure and function of molecular chaperones - p. 196 15. 5 Molecular chaperones, cochaperones, and protein homeostasis: General mechanism - p. 216 16. 6 Redox biology and chaperones - p. 223 17. 7 Crosstalk and checkpoints among various chaperones - p. 228 18. 8 Conclusion - p. 234 19. Chapter Seven. Degradation of misfolded proteins by ubiquitin-proteasome system and autophagy lysosomal proteolytic pathways - p. 253 20. Chapter Eight. Advances in developing novel therapeutics, strategies, approaches, and use of emerging techniques - p. 291 21. Chapter Nine. Challenges in translating laboratory findings to drug development - p. 319 22. Chapter Ten. Drug delivery: Tool of protein misfolding disease and its cure - p. 355 23. Chapter Eleven. Advancements in drug delivery technologies to treat protein misfolding diseases - p. 381 24. Chapter Twelve. Intersections of heavy metal toxicity, protein misfolding, and neurodegenerative disorders in humans - p. 413 25. Chapter THIRTEEN. Heavy metal contamination causes protein misfolding, leading to neurodegenerative disorders - p. 463 26. Chapter Fourteen. Protein misfolding in nonneurological diseases - p. 493 27. Chapter Fifteen. Non-neurological diseases versus protein misfolding: Conflicts and opportunities - p. 525 28. Index - p. 551

Descripcion
Descripción

Approx.280 pages

  • Discusses underlying cellular and molecular mechanisms altered in protein-associated neurodegenerative disorders
  • Describes methods for detection and analysis of protein aggregates
  • Features advancements in therapeutics and emerging techniques to treat these disorders
  • Covers implications in a variety of neurodegenerative diseases, including Alzheimer's, Parkinson’s, ALS, Creutzfeldt-Jakob disease, Cystic fibrosis, Gaucher's disease, and Polyglutamine diseases, including Huntington’s and other related proteinopathies

1. 1 Introduction - p. 67 2. 2 Proteostasis with the paradigms of protein folding, misfolding, and aggregation - p. 72 3. 3 Role of protein quality control and unfolded protein response system in neurodegenerative diseases - p. 79 4. 4 Neurodegenerative disorders caused by protein folding, misfolding, and aggregation - p. 87 5. 5 Impact of oxidative stress on cellular proteostasis, autophagy, protein folding, misfolding, and aggregation - p. 97 6. 6 Cellular and molecular mechanisms related to neurodegeneration as a consequence of protein aggregations and misfolding - p. 103 7. 7 Future prospects - p. 105 8. 8 Conclusion - p. 106 9. Chapter Five. Alterations in protein quality control resulting in neurodegeneration and disease - p. 123 10. Chapter six. Role of molecular chaperones and co-chaperones in maintaining proteostasis - p. 177 11. 1 Introduction - p. 177 12. 2 Proteostasis and the paradigm of protein folding and misfolding - p. 179 13. 3 Protein quality control system (PQC) - p. 191 14. 4 Structure and function of molecular chaperones - p. 196 15. 5 Molecular chaperones, cochaperones, and protein homeostasis: General mechanism - p. 216 16. 6 Redox biology and chaperones - p. 223 17. 7 Crosstalk and checkpoints among various chaperones - p. 228 18. 8 Conclusion - p. 234 19. Chapter Seven. Degradation of misfolded proteins by ubiquitin-proteasome system and autophagy lysosomal proteolytic pathways - p. 253 20. Chapter Eight. Advances in developing novel therapeutics, strategies, approaches, and use of emerging techniques - p. 291 21. Chapter Nine. Challenges in translating laboratory findings to drug development - p. 319 22. Chapter Ten. Drug delivery: Tool of protein misfolding disease and its cure - p. 355 23. Chapter Eleven. Advancements in drug delivery technologies to treat protein misfolding diseases - p. 381 24. Chapter Twelve. Intersections of heavy metal toxicity, protein misfolding, and neurodegenerative disorders in humans - p. 413 25. Chapter THIRTEEN. Heavy metal contamination causes protein misfolding, leading to neurodegenerative disorders - p. 463 26. Chapter Fourteen. Protein misfolding in nonneurological diseases - p. 493 27. Chapter Fifteen. Non-neurological diseases versus protein misfolding: Conflicts and opportunities - p. 525 28. Index - p. 551

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