Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

Peptides and proteins have been found to possess an inherent tendency to convert from their native functional states into intractable amyloid aggregates. This phenomenon is associated with a range of increasingly common human disorders, including Alzheimer and Parkinson diseases, type II diabetes, a...

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Vydáno v:	Annual review of biochemistry Ročník 86; s. 27
Hlavní autoři:	Chiti, Fabrizio, Dobson, Christopher M
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 20.06.2017
Témata:	Alzheimer Disease - drug therapy Alzheimer Disease - history Alzheimer Disease - metabolism Alzheimer Disease - pathology Amyloid - chemistry Amyloid - genetics Amyloid - metabolism Amyloidosis - drug therapy Amyloidosis - history Amyloidosis - metabolism Amyloidosis - pathology Diabetes Mellitus, Type 2 - drug therapy Diabetes Mellitus, Type 2 - history Diabetes Mellitus, Type 2 - metabolism Diabetes Mellitus, Type 2 - pathology Drugs, Investigational Gene Expression Regulation History, 21st Century Humans Immunoglobulin Light-chain Amyloidosis Molecular Chaperones - genetics Molecular Chaperones - metabolism Molecular Targeted Therapy Parkinson Disease - drug therapy Parkinson Disease - history Parkinson Disease - metabolism Parkinson Disease - pathology Protein Aggregation, Pathological - history Protein Aggregation, Pathological - metabolism Protein Aggregation, Pathological - pathology Protein Aggregation, Pathological - prevention & control Protein Conformation Protein Folding Proteostasis Deficiencies - drug therapy Proteostasis Deficiencies - history Proteostasis Deficiencies - metabolism Proteostasis Deficiencies - pathology Proteostasis Deficiencies - prevention & control amyloidosis quality control protein aggregation protein homeostasis conformational diseases chaperones functional amyloid
ISSN:	1545-4509, 1545-4509
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