Protein Misfolding, Aggregation and Conformational Diseases: Part A: Protein Aggregation and Conformational DiseasesVladimir N. Uversky, Anthony Fink Springer Science & Business Media, 24 нояб. 2007 г. - Всего страниц: 419 Research indicates that most neurodegenerative diseases, systemic amyloidoses and many others, arise from the misfolding and aggregation of an underlying protein. This is the first book to discuss significant achievements in protein structure-function relationships in biochemistry, molecular biology and molecular medicine. The authors summarize recent progress in the understanding of the relationships between protein misfolding, aggregation and development of protein deposition disorders. |
Содержание
| 6 | |
| 14 | |
| 21 | |
| 27 | |
| 30 | |
Concluding Remarks | 36 |
Relative Importance of Hydrophobicity Net Charge | 43 |
Importance of the Propensity to a Form Secondary Structure in Protein | 50 |
Protein Aggregation Ion Channel Formation | 223 |
Prion PrP Channels | 227 |
Abbreviations | 233 |
Identification of Amyloid Using Dyes | 241 |
Concerning the Specificity of CR | 249 |
Advice for the Immunohistochemical Classification of Amyloids | 260 |
Novel Techniqes in Amyloid Research | 266 |
Amyloidosis | 277 |
Other Factors Involved in Protein Aggregation | 54 |
Clinical ValidationOligomers in Human Brain Elevated up to 70Fold in AD | 68 |
Glycosaminoglycans Proteoglycans and Conformational | 83 |
Proteoglycans Contribute to Protein Misfolding in Conformational Protein Disorders | 92 |
Apolipoproteins in Different Amyloidoses | 101 |
Apolipoproteins in Prion Diseases | 109 |
Oxidative Stress and Protein Deposition Diseases | 123 |
Abbreviations | 130 |
Wacker and Paul J Muchowski | 137 |
Key Regulators of Protein Aggregation and Toxicity | 143 |
Chaperones as a Potential Drug Target | 155 |
Aggregates by Molecular Chaperones | 165 |
Abbreviation | 171 |
Proteasomes Inclusion Bodies | 175 |
Examples of Aggresomes in Human Health and Disease | 184 |
Mechanisms of Aggresome Formation | 199 |
Future Directions | 207 |
Resorption of Amyloid Fibrils | 282 |
Tight Binding Probes for Amyloid Imaging | 290 |
Abbreviations | 296 |
by Electron Microscopy | 303 |
Prospects for Fibril Structure Determination | 311 |
Studies of αSyn Aggregation and Morphology | 324 |
Studies of Other AmyloidForming Peptides | 330 |
Experimental Procedures | 336 |
Conclusion | 341 |
Modeling Noncoding Trinucleotide Repeat Diseases | 354 |
Abbreviations | 363 |
Neurodegenerative Disorders | 371 |
Frontotemporal Dementias and Tauopathies | 381 |
Amyotrophic Lateral Sclerosis | 390 |
Index | 409 |
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Protein Misfolding, Aggregation and Conformational Diseases: Part A: Protein ... Vladimir N. Uversky,Anthony Fink Недоступно для просмотра - 2006 |
Protein Misfolding, Aggregation and Conformational Diseases: Part A: Protein ... Vladimir N. Uversky,Anthony Fink Недоступно для просмотра - 2006 |
Protein Misfolding, Aggregation and Conformational Diseases: Part A: Protein ... Vladimir N. Uversky,Anthony Fink Недоступно для просмотра - 2006 |
Часто встречающиеся слова и выражения
Acad accumulation acid activity addition aggregation aggresomes Alzheimer’s disease amyloid deposits amyloid fibrils amyloidosis antibodies apolipoprotein appears assembly associated binding Biol bodies brain cause cell cellular changes chaperones Chem color common complex conformation Congo red contain cytoplasmic degradation disorders Dobson domain effect et al expression factor familial fibril formation Figure folding formation fragment function gene Genet heparan sulfate proteoglycans human hydrophobic important inclusions increased indicate induced inhibit interactions involved lead levels Linke loss mechanism membrane mice misfolded molecular mutations native Natl Nature neurodegenerative neurons Neurosci normal observed oligomers oxidative pathology pathway peptide plaques polypeptide potential presence prion Proc promote proteasome protein protein aggregation recent receptor regions regulation residues response role sequence shown soluble specific stability structure studies substrate suggesting sulfate synaptic tion tissue toxicity ubiquitin unfolded vitro
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