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Nature, ISSN 0028-0836, 03/2013, Volume 495, Issue 7442, pp. 467 - 473
Algorithms designed to identify canonical yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with... 
RNA-BINDING PROTEINS | DROSOPHILA MODEL | TDP-43 | MULTIDISCIPLINARY SCIENCES | FRONTOTEMPORAL DEMENTIA | VCP MUTATIONS | DISEASE | AMYOTROPHIC-LATERAL-SCLEROSIS | SACCHAROMYCES-CEREVISIAE | STRESS GRANULES | MULTIPLE ALIGNMENT | Prions - genetics | Humans | Molecular Sequence Data | Osteitis Deformans - metabolism | Male | Drosophila melanogaster - genetics | Osteitis Deformans - genetics | Drosophila melanogaster - metabolism | Frontotemporal Dementia - metabolism | Muscular Dystrophies, Limb-Girdle - genetics | Myositis, Inclusion Body - pathology | Female | Inclusion Bodies - metabolism | Muscular Dystrophies, Limb-Girdle - pathology | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics | Frontotemporal Dementia - pathology | RNA - metabolism | Frontotemporal Dementia - genetics | Amino Acid Sequence | Prions - metabolism | Peptide Termination Factors - genetics | Amyotrophic Lateral Sclerosis - genetics | Drosophila melanogaster - cytology | Mutant Proteins - genetics | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism | Mutant Proteins - metabolism | Protein Structure, Tertiary - genetics | Prions - chemistry | Saccharomyces cerevisiae Proteins - genetics | Mutation - genetics | Myositis, Inclusion Body - genetics | Peptide Termination Factors - metabolism | Amyotrophic Lateral Sclerosis - pathology | Inclusion Bodies - genetics | Osteitis Deformans - pathology | Animals | Heterogeneous-Nuclear Ribonucleoprotein Group A-B - chemistry | Muscular Dystrophies, Limb-Girdle - metabolism | Mutant Proteins - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Inclusion Bodies - pathology | Myositis, Inclusion Body - metabolism | Mice | Peptide Termination Factors - chemistry | HeLa Cells | Saccharomyces cerevisiae Proteins - chemistry | Pathology | Insects | Genomics | Genetics | Software | Genomes | Mutation | Genetic testing | Patients | Index Medicus
Journal Article
Neurobiology of Disease, ISSN 0969-9961, 2006, Volume 23, Issue 3, pp. 669 - 678
Prion (PrP) and amyloid-β (Aβ) peptides are involved in the neuronal loss that occurs in Prion disorders (PrD) and Alzheimer's disease (AD), respectively,... 
Oxidative stress | Prion peptide | Ca 2+ homeostasis | Prion disorders | Amyloid-β peptide | Alzheimer's disease | Endoplasmic reticulum | Apoptosis | homeostasis | prion peptide | peptide | ACTIVATION | CA2+ STORES | prion disorders | ALZHEIMERS-DISEASE | CALCIUM HOMEOSTASIS | ER STRESS | apoptosis | NEUROBLASTOMA-CELLS | NEUROSCIENCES | amyloid-beta | Ca2+ homeostasis | UNFOLDED PROTEIN RESPONSE | A-BETA | endoplasmic reticulum | oxidative stress | CASPASE-12 | Neurons - pathology | Prion Diseases - physiopathology | Reactive Oxygen Species - metabolism | Calcium Channels - metabolism | Rats, Wistar | Apoptosis - drug effects | Calcium - metabolism | Peptide Fragments - toxicity | Calcium Signaling - physiology | Oxidative Stress - physiology | Endoplasmic Reticulum - metabolism | Ryanodine Receptor Calcium Release Channel - metabolism | Cerebral Cortex - metabolism | Cerebral Cortex - physiopathology | Electron Transport Complex IV - metabolism | Caspases - metabolism | Peptides - metabolism | Peptides - toxicity | Endoplasmic Reticulum - drug effects | Amyloid beta-Peptides - metabolism | Inositol 1,4,5-Trisphosphate Receptors | Cerebral Cortex - drug effects | Homeostasis - drug effects | Neurons - drug effects | Calcium Channels - drug effects | Prions - metabolism | Alzheimer Disease - physiopathology | Peptide Fragments - metabolism | Amyloid beta-Peptides - toxicity | Receptors, Cytoplasmic and Nuclear - drug effects | Cells, Cultured | Rats | Neurotoxins - toxicity | Ryanodine Receptor Calcium Release Channel - drug effects | Prions - toxicity | Animals | Calcium Signaling - drug effects | Homeostasis - physiology | Alzheimer Disease - metabolism | Neurotoxins - metabolism | Apoptosis - physiology | Oxidative Stress - drug effects | Prion Diseases - metabolism | Receptors, Cytoplasmic and Nuclear - metabolism | Cytochrome c | Inositol | Neurosciences | Corticosteroids | Synthesis | Peptides | Analysis | Lipids | Target marketing | Index Medicus
Journal Article
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
Nature Communications, ISSN 2041-1723, 04/2015, Volume 6, Issue 1, pp. 6768 - 6768
The brain has a limited capacity to self-protect against protein aggregate-associated pathology, and mounting evidence supports a role for phagocytic glia in... 
MOTOR-NEURONS | CELLS | IN-VITRO | ACTIVATION | ENGULFMENT | MULTIDISCIPLINARY SCIENCES | MUTANT HUNTINGTIN | DISEASE | TAU | PATHOLOGY | PROPAGATION | Protein Aggregates | Neurons - pathology | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Neuroglia - pathology | Humans | Huntington Disease - pathology | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Brain - metabolism | Drosophila melanogaster - metabolism | Molecular Mimicry | Membrane Proteins - metabolism | Neurons - metabolism | Protein Aggregation, Pathological - genetics | Genes, Reporter | Disease Models, Animal | Neuroglia - chemistry | Prions - metabolism | Neurons - chemistry | Signal Transduction | Membrane Proteins - genetics | Bacterial Proteins - genetics | Gene Expression Regulation | Prions - chemistry | Huntington Disease - metabolism | Disease Progression | Huntingtin Protein | Animals | Brain - pathology | Huntington Disease - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Neuroglia - metabolism | Drosophila Proteins - genetics | Mutation | Phagocytosis | Protein Aggregation, Pathological - metabolism | Luminescent Proteins - metabolism | Draper protein | Neuroprotection | Brain | Huntingtin | Neurodegenerative diseases | Pathogenesis | Drosophila | Conversion | Neuronal-glial interactions | Proteins | Neurological diseases | Phagocytes | Signal transduction | Aggregates | Insects | Cytoplasm | Index Medicus
Journal Article
Journal Article
Genetics, ISSN 0016-6731, 02/2017, Volume 205, Issue 2, pp. 633 - 655
Nitrogen catabolite repression (NCR),the ability of Saccharomyces cerevisiae to use good nitrogen sources in preference to poor ones, derives from... 
Bmh1/2 | Gcn2 | Gln3 | Nitrogen catabolite repression | Gat1 | KINASE GCN2 | SIGNALING PATHWAYS | RAPAMYCIN TREATMENT | TOR PROTEINS | EGO COMPLEX | FACTOR RESPONSES | nitrogen catabolite repression | YEAST SACCHAROMYCES-CEREVISIAE | NUCLEAR-LOCALIZATION | GENETICS & HEREDITY | METHIONINE SULFOXIMINE | TRANSCRIPTION ACTIVATOR | Phosphorylation | Basic-Leucine Zipper Transcription Factors - metabolism | Prions - genetics | TOR Serine-Threonine Kinases - metabolism | Saccharomyces cerevisiae - genetics | Multiprotein Complexes - genetics | Mechanistic Target of Rapamycin Complex 1 | Saccharomyces cerevisiae - metabolism | Amino Acids - metabolism | Catabolite Repression | Multiprotein Complexes - metabolism | Cell Nucleus - metabolism | TOR Serine-Threonine Kinases - genetics | GATA Transcription Factors - metabolism | Active Transport, Cell Nucleus | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Glutathione Peroxidase - metabolism | Prions - metabolism | Nitrogen - metabolism | Protein-Serine-Threonine Kinases - genetics | Basic-Leucine Zipper Transcription Factors - genetics | Saccharomyces cerevisiae Proteins - genetics | Transcription Factors - genetics | GATA Transcription Factors - genetics | Glutathione Peroxidase - genetics | 14-3-3 Proteins - metabolism | Transcription Factors - metabolism | Epistasis, Genetic | Saccharomyces cerevisiae Proteins - metabolism | Protein Processing, Post-Translational | Proteins | Cell division | Regulation | Kinases | Phosphatase | Localization | Experiments | Index Medicus | 2 | Bmh1 | Investigations
Journal Article