Protein Misfolding, Aggregation, and Conformational Diseases [recurso electrónico] : Part A: Protein Aggregation and Conformational Diseases / edited by Vladimir N. Uversky, Anthony L. Fink.

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.

Protein Misfolding, Aggregation, and Conformational Disease, is the first book to discuss significant achievements in protein structure-function relationships in the areas of biochemistry, molecular biology and molecular medicine. This volume summarizes recent achievements in the understanding of the relationships between protein misfolding, aggregation and development of protein deposition disorders. Research indicates that various human disorders, including most neurodegenerative diseases, systemic amyloidoses and many others, arise from the misfolding and aggregation of an underlying protein. Protein Misfolding, Aggregation and Conformational Diseases is an ideal book for biochemists, protein scientists, immunologists, pharmaceutical scientists, and molecular and cellular biologists.