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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
Journal Article
Nature, ISSN 0028-0836, 05/2012, Volume 485, Issue 7399, pp. 507 - 511
The mechanisms leading to neuronal death in neurodegenerative disease are poorly understood. Many of these disorders, including Alzheimer's, Parkinson's and... 
UNFOLDED PROTEIN RESPONSE | TOXICITY IN-VIVO | ALZHEIMERS-DISEASE | ER STRESS | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | MICE | ENDOPLASMIC-RETICULUM STRESS | DYSFUNCTION | PRP | PROTEOSTASIS | Neurons - pathology | Neuroprotective Agents | Phosphorylation | Prions - genetics | Eukaryotic Initiation Factor-2 - chemistry | Neurodegenerative Diseases - etiology | PrPSc Proteins - analysis | Synapses - pathology | Thiourea - pharmacology | Phosphoproteins - metabolism | Repressor Proteins - analysis | PrPSc Proteins - metabolism | Synapses - metabolism | Phosphoproteins - analysis | Protein Folding - drug effects | Protein Phosphatase 1 - genetics | Eukaryotic Initiation Factor-2 - metabolism | Synaptic Transmission - drug effects | Cell Death - drug effects | PrPSc Proteins - toxicity | Neurons - drug effects | Repressor Proteins - metabolism | Prions - metabolism | Synapses - drug effects | Repressor Proteins - chemistry | Neurodegenerative Diseases - pathology | Mice, Inbred C57BL | Kaplan-Meier Estimate | Hippocampus - pathology | Prion Diseases - pathology | Neurodegenerative Diseases - metabolism | Hippocampus - cytology | Cinnamates - pharmacology | Eukaryotic Initiation Factor-2 - analysis | Hippocampus - metabolism | Protein Phosphatase 1 - metabolism | Animals | Prions - biosynthesis | Protein Biosynthesis - drug effects | Mice | Unfolded Protein Response - physiology | Thiourea - analogs & derivatives
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2004, Volume 101, Issue 26, pp. 9683 - 9688
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 10/2014, Volume 289, Issue 43, pp. 30144 - 30160
Background: Membrane attachment of PrP via a GPI anchor is critical for conversion into PrPSc. Results: Semisynthetic membrane-anchored PrP variants are... 
Membrane Anchor | SEMISYNTHESIS | Protein Chemistry | CONVERSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | Liposome | GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR | PENETRATION | Pore Formation | CULTURED-CELLS | CELLULAR MEMBRANES | Protein Semisynthesis | PRPSC | Protein Aggregation | FLUORESCENCE | RECOMBINANT | Protein