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1. Full Text Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
by Ciechanover, Aaron and Kwon, Yong T.ae
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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2. Full Text Sustained translational repression by eIF2α-P mediates prion neurodegeneration
by Moreno, Julie A and Radford, Helois and Peretti, Diego and Steinert, Joern R and Verity, Nicholas and Martin, Maria Guerra and Halliday, Mark and Morgan, Jason and Dinsdale, David and Ortori, Catherine A and Barrett, David A and Tsaytler, Pavel and Bertolotti, Anne and Willis, Anne E and Bushell, Martin and Mallucci, Giovanna R
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
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3. Full Text The prion's elusive reason for being
by Aguzzi, Adriano and Baumann, Frank and Bremer, Juliane
Annual Review of Neuroscience, ISSN 0147-006X, 2008, Volume 31, Issue 1, pp. 439 - 477
The protein-only hypothesis posits that the infectious agent causing transmissible spongiform encephalopathies consists of protein and lacks any informational... 
Prion diseases | Transmissible spongiform encephalopathy | PrP | CA2+-ACTIVATED K+ CURRENTS | PrPSc | CEREBELLAR PURKINJE-CELLS | AMYLOID-PRECURSOR-PROTEIN | transmissible spongiform encephalopathy | STRESS-INDUCIBLE PROTEIN-1 | NEUROSCIENCES | SCRAPIE-INFECTED MICE | FATAL FAMILIAL INSOMNIA | prion diseases | PrPC | PRP KNOCKOUT MICE | STRAUSSLER-SCHEINKER-DISEASE | CENTRAL-NERVOUS-SYSTEM | CREUTZFELDT-JAKOB-DISEASE | Prion Diseases - physiopathology | Prions - metabolism | Prion Diseases - genetics | Prions - genetics | Brain - physiopathology | Humans | Cytoprotection - physiology | Nerve Tissue Proteins - genetics | PrPSc Proteins - genetics | Brain - metabolism | Nerve Tissue Proteins - metabolism | PrPSc Proteins - metabolism | Animals | Neurons - metabolism | PrPC Proteins - metabolism | PrPC Proteins - genetics | Cell Survival - physiology | Prion Diseases - metabolism | Cellular proteins | Research | Structure | Index Medicus
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4. Full Text A General Model of Prion Strains and Their Pathogenicity
by John Collinge and Anthony R. Clarke
Science, ISSN 0036-8075, 11/2007, Volume 318, Issue 5852, pp. 930 - 936
Prions are lethal mammalian pathogens composed of aggregated conformational isomers of a host-encoded glycoprotein and which appear to lack nucleic acids.... 
Nervous system diseases | Disease transmission | Inbred strains | Neurodegenerative diseases | Prions | Humans | Prion diseases | Mice | Infections | Review | Genetic mutation | FATAL FAMILIAL INSOMNIA | TRANSMISSIBLE MINK ENCEPHALOPATHY | BOVINE SPONGIFORM ENCEPHALOPATHY | MULTIDISCIPLINARY SCIENCES | CREUTZFELDT-JAKOB-DISEASE | VARIANT CJD | PROTEIN GENE | MOLECULAR-BASIS | BSE AGENT | TRANSGENIC MICE | SPECIES-BARRIER | Prions - pathogenicity | Species Specificity | Recombinant Proteins - chemistry | Prions - chemistry | PrPSc Proteins - isolation & purification | PrPC Proteins - chemistry | PrPSc Proteins - chemistry | Protein Folding | PrPC Proteins - isolation & purification | PrPSc Proteins - metabolism | Animals | Prion Diseases - transmission | Models, Biological | Prions - isolation & purification | Protein Conformation | Brain Chemistry | PrPC Proteins - metabolism | PrPSc Proteins - pathogenicity | Prion Diseases - metabolism | Neurosciences | Models | Biochemistry | Molecular biology | Public health | Risk factors
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5. Full Text Prions hijack tunnelling nanotubes for intercellular spread
by Marijanovic, Zrinka and Caputo, Anna and Zurzolo, Chiara and Männel, Daniela and Martino, Angelo and Olivo-Marin, Jean-Christophe and Gousset, Karine and Enninga, Jost and Langevin, Christelle and Browman, Duncan T and Chenouard, Nicolas and Schiff, Edwin and de Chaumont, Fabrice
Nature Cell Biology, ISSN 1465-7392, 03/2009, Volume 11, Issue 3, pp. 328 - 336
In variant Creutzfeldt-Jakob disease, prions (PrPSc) enter the body with contaminated foodstuffs and can spread from the intestinal entry site to the central... 
MEMBRANE NANOTUBES | SCRAPIE | IMMUNE CELLS | IMAGINAL DISCS | PEYERS-PATCHES | IN-VIVO | FOLLICULAR DENDRITIC CELLS | NEURONAL CELLS | T-CELLS | CUTTING EDGE | CELL BIOLOGY | Cell Line | Green Fluorescent Proteins - metabolism | Neurons - pathology | Prions - metabolism | Movement | Cell Communication | Amines - metabolism | Recombinant Fusion Proteins - metabolism | Protein Transport | PrPSc Proteins - metabolism | Extracellular Space - metabolism | Animals | Cytoplasmic Vesicles - metabolism | Brain - pathology | Mice | Neurons - metabolism | Bone Marrow Cells - metabolism | Dendritic Cells - metabolism | Physiological aspects | Cell interaction | Research | Biological transport | Prions | Life Sciences | Microbiology and Parasitology
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6. Full Text Cells Release Prions in Association with Exosomes
by Benoit Fevrier and Didier Vilette and Fabienne Archer and Damarys Loew and Wolfgang Faigle and Michel Vidal and Hubert Laude and Graça Raposo and Pietro V. De Camilli
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
Prion diseases are infectious neurodegenerative disorders linked to the accumulation in the central nervous system of the abnormally folded prion protein (PrP)... 
Cell culture techniques | Biological Sciences | Dendritic cells | B lymphocytes | Epithelial cells | Prions | Centrifugation | Cultured cells | Cell membranes | Exosomes | P branes | LOCALIZATION | PROTEIN | MULTIVESICULAR BODIES | TRANSFERRIN RECEPTOR | VESICLES | MULTIDISCIPLINARY SCIENCES | SURFACE | MICROVESICLES | RETICULOCYTES | TUMOR-DERIVED EXOSOMES | SHEEP SCRAPIE | Prion Proteins | PrPSc Proteins - secretion | Culture Media, Conditioned - chemistry | Secretory Vesicles - metabolism | Culture Media, Conditioned - pharmacology | Exocytosis | Endosomes - metabolism | Prions - secretion | Brain - metabolism | PrPSc Proteins - metabolism | Extracellular Space - metabolism | Prion Diseases - transmission | Amyloid - metabolism | Gene Deletion | Mass Spectrometry | Biological Assay | Cell Membrane - metabolism | Amyloid - deficiency | Amyloid - genetics | Cell Line | Prions - metabolism | Protein Precursors - genetics | Mice, Transgenic | Blotting, Western | Protein Precursors - metabolism | Brain - drug effects | Protein Precursors - deficiency | Animals | Cell Extracts | Sheep | Mice | Intracellular Membranes - metabolism | Prion Diseases - metabolism | Culture Media, Conditioned - metabolism | Scrapie | Prion diseases | Research
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7. Full Text Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
by Sandberg, Malin K and Al-Doujaily, Huda and Sharps, Bernadette and Clarke, Anthony R and Collinge, John
Nature, ISSN 0028-0836, 02/2011, Volume 470, Issue 7335, pp. 540 - 542
Mammalian prions cause fatal neurodegenerative conditions including Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy in... 
PATHOGENESIS | STRAINS | RESISTANT | PROTEIN | REPLICATION | MULTIDISCIPLINARY SCIENCES | DISEASE | INFECTIVITY | MICE | MOUSE SCRAPIE | PRP | PrPC Proteins - analysis | Prion Diseases - physiopathology | Gene Expression | Biocatalysis | Mice, Transgenic | PrPSc Proteins - biosynthesis | Survival Rate | Prion Diseases - pathology | PrPSc Proteins - metabolism | Animals | Prion Diseases - transmission | Time Factors | Models, Biological | Biological Assay | Mice | Kinetics | PrPC Proteins - metabolism | PrPSc Proteins - pathogenicity | PrPSc Proteins - toxicity | PrPC Proteins - biosynthesis | PrPC Proteins - genetics | Toxicity Tests | Prion Diseases - metabolism | Disease Models, Animal | Physiological aspects | Prions | Chemical properties | Brain | Neurotoxicity | Propagation | Biological assays | Rodents
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8. Full Text Prions disturb post-Golgi trafficking of membrane proteins
by Uchiyama, Keiji and Muramatsu, Naomi and Yano, Masashi and Usui, Takeshi and Miyata, Hironori and Sakaguchi, Suehiro
Nature Communications, ISSN 2041-1723, 2013, Volume 4, Issue 1, p. 1846
Conformational conversion of normal cellular prion protein PrPC into pathogenic PrPSc is central to the pathogenesis of prion diseases. However, the pathogenic... 
INSULIN | NERVOUS-SYSTEM | TRANSPORT | PRP GENE | MULTIDISCIPLINARY SCIENCES | NEURODEGENERATION | MICE | ENDOPLASMIC-RETICULUM STRESS | APPARATUS | TRANSMEMBRANE FORM | CELL-DEATH | Humans | Male | Endosomes - metabolism | Brain - metabolism | PrPSc Proteins - metabolism | Endocytosis | Biotin - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | PrPC Proteins - metabolism | Cell Line | Prions - metabolism | Cricetinae | Signal Transduction | Subcellular Fractions - metabolism | Blotting, Western | Protein Transport | Insulin - metabolism | Animals | Models, Biological | Brain - pathology | Golgi Apparatus - metabolism | Receptor, Insulin - metabolism | Mice | Antibodies, Monoclonal - metabolism
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9. Full Text Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein
by David R. Taylor and Edward T. Parkin and Sarah L. Cocklin and James R. Ault and Alison E. Ashcroft and Anthony J. Turner and Nigel M. Hooper
Journal of Biological Chemistry, ISSN 0021-9258, 08/2009, Volume 284, Issue 34, pp. 22590 - 22600
The cellular prion protein (PrP C ) is essential for the pathogenesis and transmission of prion diseases. PrP C is bound to the plasma membrane via a... 
METALLOPROTEASE | SOLUBLE FORM | DISINTEGRIN | HUMAN CEREBROSPINAL-FLUID | CELLULAR PRION | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIPID RAFTS | AMYLOID PRECURSOR PROTEIN | CULTURED-CELLS | ANGIOTENSIN-CONVERTING ENZYME | TRUNCATED FORMS | ADAM17 Protein | Amyloid Precursor Protein Secretases - genetics | Humans | Immunoblotting | Aspartic Acid Endopeptidases - genetics | PrPSc Proteins - metabolism | Mass Spectrometry | Membrane Proteins - metabolism | PrPC Proteins - metabolism | PrPC Proteins - genetics | Recombinant Proteins - metabolism | Cell Line | Membrane Proteins - genetics | ADAM10 Protein | Recombinant Proteins - genetics | Reverse Transcriptase Polymerase Chain Reaction | PrPSc Proteins - genetics | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Aspartic Acid Endopeptidases - metabolism | Cell Line, Tumor | Mice | RNA, Small Interfering | ADAM Proteins - genetics | DNA, Complementary | Protein Synthesis, Post-Translational Modification, and Degradation
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10. Full Text Molecular Cross Talk between Misfolded Proteins in Animal Models of Alzheimer's and Prion Diseases
by Morales, Rodrigo and Estrada, Lisbell D and Diaz-Espinoza, Rodrigo and Morales-Scheihing, Diego and Jara, Maria C and Castilla, Joaquin and Soto, Claudio
Journal of Neuroscience, ISSN 0270-6474, 03/2010, Volume 30, Issue 13, pp. 4528 - 4535
The central event in protein misfolding disorders (PMDs) is the accumulation of a misfolded form of a naturally expressed protein. Despite the diversity of... 
COEXISTENCE | SCRAPIE | FIBRILS | TYPICAL CLINICAL-FEATURES | A-BETA | AMYLOID PLAQUES | PATIENT | CREUTZFELDT-JAKOB-DISEASE | NEUROPATHOLOGY | STRESS | NEUROSCIENCES | Prions - metabolism | Mice, Inbred C57BL | Mice, Transgenic | Prion Diseases - pathology | Prions - chemistry | PrPSc Proteins - chemistry | Protein Folding | Alzheimer Disease - pathology | Brain - metabolism | PrPSc Proteins - metabolism | Animals | Amyloid - metabolism | Alzheimer Disease - metabolism | Amyloid beta-Peptides - metabolism | Brain - pathology | Mice | Amyloid beta-Peptides - chemistry | Prion Diseases - metabolism
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11. Full Text A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes
by Chu, Nam K and Shabbir, Waheed and Bove-Fenderson, Erin and Araman, Can and Lemmens-Gruber, Rosa and Harris, David A and Becker, Christian F. W
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