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.
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.
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Taschenbuch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - This volume fills the gap in protein review and protocal literature while summarizing recent achievements in the understanding of the relationships between protein misfoldings, aggregation, and development of protein deposition disorders. It is devoted to the general questions of conformational disorders and includes discussion of involvement of such common factors as molecular chaperones, oxidative damage, proteasome, glycosoaminoglycans, serum amyloid protein P and several others in the development of different disorders. Some experimental techniques applicable for the visualization of protein deposition in vivo and in vitro are also present. Artikel-Nr. 9781441938510
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