Protein Misfolding, Aggregation and Conformational Diseases Part A: Protein Aggregation and Conformational Diseases /
| Autor Corporativo: | |
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| Otros Autores: | , |
| Formato: | eBook |
| Lenguaje: | English |
| Publicado: |
New York, NY :
Springer US : Imprint: Springer,
2006.
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| Edición: | 1st ed. 2006. |
| Colección: | Protein Reviews ;
4 |
| Materias: | |
| Acceso en línea: | https://doi.org/10.1007/b136464 |
Tabla de Contenidos:
- Structural and Conformational Prerequisites of Amyloidogenesis
- Structural and Conformational Prerequisites of Amyloidogenesis
- The Generic Nature of Protein Folding and Misfolding
- The Generic Nature of Protein Folding and Misfolding
- Relative Importance of Hydrophobicity, Net Charge, and Secondary Structure Propensities in Protein Aggregation
- Relative Importance of Hydrophobicity, Net Charge, and Secondary Structure Propensities in Protein Aggregation
- Cytotoxic Intermediates in the Fibrillation Pathway: A? Oligomers in Alzheimer’s Disease as a Case Study
- Cytotoxic Intermediates in the Fibrillation Pathway: A? Oligomers in Alzheimer’s Disease as a Case Study
- Glycosaminoglycans, Proteoglycans, and Conformational Disorders
- Glycosaminoglycans, Proteoglycans, and Conformational Disorders
- Apolipoproteins in Different Amyloidoses
- Apolipoproteins in Different Amyloidoses
- Oxidative Stress and Protein Deposition Diseases
- Oxidative Stress and Protein Deposition Diseases
- Chaperone and Conformational Disorders
- Chaperone Suppression of Aggregated Protein Toxicity
- Mechanisms of Active Solubilization of Stable Protein Aggregates by Molecular Chaperones
- The Aggresome: Proteasomes, Inclusion Bodies, and Protein Aggregation
- The Aggresome: Proteasomes, Inclusion Bodies, and Protein Aggregation
- Protein Aggregation, Ion Channel Formation, and Membrane Damage
- Protein Aggregation, Ion Channel Formation, and Membrane Damage
- Visualization of Protein Deposits In Vivo
- Congo Red Staining of Amyloid: Improvements and Practical Guide for a More Precise Diagnosis of Amyloid and the Different Amyloidoses
- Immunohistological Study of Experimental Murine AA Amyloidosis
- Visualization of Protein Deposits In Vitro
- Reporters of Amyloid Structure
- Three-Dimensional Structural Analysis of Amyloid Fibrils by Electron Microscopy
- Atomic Force Microscopy
- Direct Observation of Amyloid Fibril Growth Monitored by Total Internal Reflection Fluorescence Microscopy
- Animal and Cell Models of Human Neurodegenerative Disorders
- Drosophila and C. elegans Models of Human Age-Associated Neurodegenerative Diseases
- Genetically Engineered Mouse Models of Neurodegenerative Disorders.