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Experimental & molecular medicine, ISSN 1226-3613, 2015, Volume 47, Issue 3, pp. e147 - e147
Mammalian cells remove misfolded proteins using various proteolytic systems, including the ubiquitin (Ub)-proteasome system (UPS), chaperone mediated autophagy... 
MEDICINE, RESEARCH & EXPERIMENTAL | UBIQUITIN-PROTEASOME SYSTEM | CHAPERONE-MEDIATED AUTOPHAGY | ALPHA-SYNUCLEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY CONTROL DEGRADATION | CENTRAL-NERVOUS-SYSTEM | AMYOTROPHIC-LATERAL-SCLEROSIS | SOD1 TRANSGENIC MICE | ENDOPLASMIC-RETICULUM STRESS | END RULE PATHWAY | PARKINSONS-DISEASE | Proteostasis Deficiencies - metabolism | Humans | Ubiquitin - metabolism | tau Proteins - metabolism | Parkinson Disease - drug therapy | Molecular Targeted Therapy | Neurodegenerative Diseases - drug therapy | Amyotrophic Lateral Sclerosis - drug therapy | Autophagy - drug effects | DNA-Binding Proteins - metabolism | PrPSc Proteins - metabolism | Lysosomes - metabolism | Proteolysis | Amyloid beta-Peptides - metabolism | Parkinson Disease - metabolism | Huntington Disease - drug therapy | Superoxide Dismutase - metabolism | Prion Diseases - drug therapy | Alzheimer Disease - drug therapy | Neurodegenerative Diseases - metabolism | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Animals | Alzheimer Disease - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Huntington Disease - genetics | Mutation | Proteasome Endopeptidase Complex - metabolism | alpha-Synuclein - metabolism | Prion Diseases - metabolism | Review
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Nature Cell Biology, ISSN 1465-7392, 2009, Volume 11, Issue 2, pp. 219 - 225
Sequence-specific nucleated protein aggregation is closely linked to the pathogenesis of most neurodegenerative diseases and constitutes the molecular basis of... 
IN-VITRO | PROTEIN MISFOLDING DISEASES | PEPTIDES | FIBRILS | MECHANISM | TOXICITY | HUNTINGTIN | PROPAGATION | YEAST PRION | CELL BIOLOGY | Prion Diseases - physiopathology | Humans | Cell Communication - physiology | Cytoplasm - metabolism | Cytoplasm - pathology | Peptides - metabolism | Peptides - toxicity | Amyloid - biosynthesis | Disease Transmission, Infectious | Inclusion Bodies - metabolism | Huntington Disease - physiopathology | Cell Line | Neurodegenerative Diseases - pathology | Amyloidosis - pathology | Amyloidosis - physiopathology | Neurodegenerative Diseases - metabolism | Neurofibrils - pathology | Huntington Disease - metabolism | Endocytosis - physiology | Neurodegenerative Diseases - physiopathology | Proteasome Endopeptidase Complex - ultrastructure | Trinucleotide Repeat Expansion - genetics | Proteasome Endopeptidase Complex - metabolism | Amyloidosis - metabolism | Prion Diseases - metabolism | Neurofibrils - metabolism | Amyloid beta-protein | Physiological aspects | Nervous system | Genetic aspects | Degeneration | Research | Glutamine | Index Medicus | Huntington Disease | Neurodegenerative Diseases | Peptides | Neurofibrils | Cell Communication | Proteasome Endopeptidase Complex | Trinucleotide Repeat Expansion | Life Sciences | Prion Diseases | Endocytosis | Inclusion Bodies | Amyloid | Amyloidosis | Cytoplasm
Journal Article
Nature Reviews Neuroscience, ISSN 1471-003X, 02/2011, Volume 12, Issue 2, pp. 65 - 72
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