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Annual review of biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 97 - 122
neurodegenerative diseases | aging | molecular chaperones | proteostasis | protein aggregation | misfolded protein clearance | Aging | Protein aggregation | Misfolded protein clearance | Proteostasis | Molecular chaperones | Neurodegenerative diseases | Proteostasis Deficiencies - metabolism | Protein Biosynthesis | Molecular Chaperones - metabolism | Humans | Amyloidogenic Proteins - chemistry | Prion Proteins - metabolism | Cell Compartmentation | Aging - genetics | Protein Aggregation, Pathological - pathology | Proteolysis | Prion Proteins - chemistry | Prion Proteins - genetics | Protein Aggregation, Pathological - genetics | Amyloidogenic Proteins - genetics | Neurodegenerative Diseases - pathology | Gene Expression Regulation | Molecular Chaperones - genetics | Protein Refolding | Proteostasis Deficiencies - pathology | Neurodegenerative Diseases - genetics | Neurodegenerative Diseases - metabolism | Protein Folding | Aging - pathology | Proteostasis Deficiencies - genetics | Amyloidogenic Proteins - metabolism | Protein Conformation | Protein Aggregation, Pathological - metabolism | Aging - metabolism | Proteins | Nervous system diseases | Quality control | Physiological aspects | Research | Protein folding | Proteomics | Cell survival | Pathogenesis | Homeostasis | Agglomeration | Chaperones | Disease control | Machinery | Diseases | Machinery and equipment | Neurological diseases | Compartments | Amyloid | Aberration | Proteomes | Protein interaction | Neurological disorders | Plaques | Cancer | Fitness | Index Medicus
Journal Article
Amyloid, ISSN 1350-6129, 10/2016, Volume 23, Issue 4, pp. 209 - 213
Journal Article