Protein Misfolding, Volume 118, covers the wide spectrum of diseases and disorders that are attributed to protein misfolding, including degenerative and neurodegenerative, cardiovascular, renal, glaucoma, cancer, cystic fibrosis, Gaucher's disease, and many others. Specific chapters cover Mass spectrometric approaches for profiling protein folding and stability, Biomembranes, a key player in protein misfolding, how Genetic and environmental factors interact to disrupt proteostasis and trigger protein misfolding diseases, Formation of oligomers and large amorphous aggregates by intrinsically disordered proteins, Protein misfolding in ER stress with applications to cardiovascular and renal disease, and much more.
1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Copyright - p. iv 5. Contributors - p. xi 6. Chapter One. Theoretical and computational advances in protein misfolding - p. 1 7. Chapter Two. Combining molecular dynamics simulations and experimental analyses in protein misfolding - p. 33 8. Chapter Three. Mass spectrometric approaches for profiling protein folding and stability - p. 111 9. Chapter Four. The intrinsic and extrinsic factors that contribute to proteostasis decline and pathological protein misfolding - p. 145 10. Chapter Five. Functional and dysfunctional folding, association and aggregation of caseins - p. 163 11. Chapter Six. Protein misfolding in endoplasmic reticulum stress with applications to renal diseases - p. 217 12. Chapter Seven. Misfolding of vasopressin receptors: biased agonist pharmacochaperones as potential therapeutics - p. 249 13. Chapter Eight. LOXL1 folding in exfoliation glaucoma - p. 273 14. Chapter Nine. Liquid-liquid phase transitions and amyloid aggregation in proteins related to cancer and neurodegenerative diseases - p. 289 15. Chapter Ten. Cytotoxic species in amyloid-associated diseases: Oligomers or mature fibrils - p. 333 16. Chapter Eleven. Misfolded proteins as a therapeutic target in Alzheimer's disease - p. 371 17. Chapter Twelve. Influence of the reducing environment in the misfolding of wine proteins - p. 413
Protein Misfolding, Volume 118, covers the wide spectrum of diseases and disorders that are attributed to protein misfolding, including degenerative and neurodegenerative, cardiovascular, renal, glaucoma, cancer, cystic fibrosis, Gaucher's disease, and many others. Specific chapters cover Mass spectrometric approaches for profiling protein folding and stability, Biomembranes, a key player in protein misfolding, how Genetic and environmental factors interact to disrupt proteostasis and trigger protein misfolding diseases, Formation of oligomers and large amorphous aggregates by intrinsically disordered proteins, Protein misfolding in ER stress with applications to cardiovascular and renal disease, and much more.
1. Cover image - p. i 2. Title page - p. ii 3. Table of Contents - p. iii 4. Copyright - p. iv 5. Contributors - p. xi 6. Chapter One. Theoretical and computational advances in protein misfolding - p. 1 7. Chapter Two. Combining molecular dynamics simulations and experimental analyses in protein misfolding - p. 33 8. Chapter Three. Mass spectrometric approaches for profiling protein folding and stability - p. 111 9. Chapter Four. The intrinsic and extrinsic factors that contribute to proteostasis decline and pathological protein misfolding - p. 145 10. Chapter Five. Functional and dysfunctional folding, association and aggregation of caseins - p. 163 11. Chapter Six. Protein misfolding in endoplasmic reticulum stress with applications to renal diseases - p. 217 12. Chapter Seven. Misfolding of vasopressin receptors: biased agonist pharmacochaperones as potential therapeutics - p. 249 13. Chapter Eight. LOXL1 folding in exfoliation glaucoma - p. 273 14. Chapter Nine. Liquid-liquid phase transitions and amyloid aggregation in proteins related to cancer and neurodegenerative diseases - p. 289 15. Chapter Ten. Cytotoxic species in amyloid-associated diseases: Oligomers or mature fibrils - p. 333 16. Chapter Eleven. Misfolded proteins as a therapeutic target in Alzheimer's disease - p. 371 17. Chapter Twelve. Influence of the reducing environment in the misfolding of wine proteins - p. 413
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