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Annual Review of Biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 27 - 68
Peptides and proteins have been found to possess an inherent tendency to convert from their native functional states into intractable amyloid aggregates. This... 
amyloidosis | quality control | protein aggregation | protein homeostasis | conformational diseases | chaperones | functional amyloid | Protein aggregation | Quality control | Functional amyloid | Amyloidosis | Chaperones | Protein homeostasis | Conformational diseases | FIBRIL FORMATION | NUCLEATED CONFORMATIONAL CONVERSION | SOLID-STATE NMR | STOP-CODON MUTATION | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILIAL BRITISH DEMENTIA | ALPHA-SYNUCLEIN AGGREGATION | BETA PRECURSOR PROTEIN | APOLIPOPROTEIN AII GENE | HUMAN PRION PROTEIN | Proteostasis Deficiencies - metabolism | Molecular Chaperones - metabolism | History, 21st Century | Parkinson Disease - history | Humans | Proteostasis Deficiencies - history | Protein Aggregation, Pathological - history | Drugs, Investigational | Parkinson Disease - drug therapy | Amyloid - chemistry | Diabetes Mellitus, Type 2 - metabolism | Diabetes Mellitus, Type 2 - history | Molecular Targeted Therapy | Alzheimer Disease - pathology | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Parkinson Disease - metabolism | Immunoglobulin Light-chain Amyloidosis | Amyloid - genetics | Alzheimer Disease - history | Parkinson Disease - pathology | Amyloidosis - pathology | Amyloidosis - history | Gene Expression Regulation | Molecular Chaperones - genetics | Proteostasis Deficiencies - pathology | Alzheimer Disease - drug therapy | Amyloidosis - drug therapy | Protein Folding | Proteostasis Deficiencies - prevention & control | Alzheimer Disease - metabolism | Protein Conformation | Diabetes Mellitus, Type 2 - pathology | Proteostasis Deficiencies - drug therapy | Diabetes Mellitus, Type 2 - drug therapy | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Physiological aspects | Development and progression | Genetic aspects | Protein folding | Amyloid beta-protein
Journal Article
Science, ISSN 0036-8075, 04/2015, Volume 348, Issue 6231, pp. 239 - 242
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2017, Volume 114, Issue 3, pp. 574 - 579
Journal Article