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Journal of Neuroscience, ISSN 0270-6474, 09/2012, Volume 32, Issue 39, pp. 13454 - 13469
Abnormal deposition and intercellular propagation of alpha-synuclein plays a central role in the pathogenesis of disorders such as Parkinson's Disease (PD) and... 
IMMUNIZATION | PROTEIN | PLASMA | BIOMARKER | ALZHEIMERS-DISEASE | MOUSE MODEL | PATHOLOGY | FC-GAMMA-RIIA | NEUROSCIENCES | NEURODEGENERATIVE DISEASES | PARKINSONS-DISEASE | Synaptic Transmission - physiology | Antibodies - metabolism | Lewy Body Disease - immunology | Humans | alpha-Synuclein - immunology | Extracellular Space - drug effects | Nerve Degeneration - genetics | Cell Communication - physiology | Culture Media, Conditioned - pharmacology | Phosphopyruvate Hydratase - metabolism | Amyloid - ultrastructure | Antigens, CD - metabolism | Neuroglia - drug effects | Brain - metabolism | Lewy Body Disease - genetics | Extracellular Space - metabolism | Amyloid - metabolism | Microfilament Proteins - metabolism | alpha-Synuclein - genetics | Disease Models, Animal | Calcium-Binding Proteins - metabolism | Cell Line | Microscopy, Electron, Transmission | Cytokines - metabolism | Mice, Transgenic | Nerve Degeneration - immunology | Cathepsin D - metabolism | Extracellular Space - immunology | Antibodies - pharmacology | Caveolin 1 - metabolism | Lewy Body Disease - metabolism | Platelet-Derived Growth Factor - metabolism | Animals | Analysis of Variance | Brain - pathology | Immunization, Passive | Neuroglia - metabolism | Mice | Chromatography, Gel | alpha-Synuclein - metabolism | Nerve Degeneration - drug therapy | Astrocytes - metabolism | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2015, Volume 10, Issue 6, pp. e0130624 - e0130624
Neuroinflammation is the local reaction of the brain to infection, trauma, toxic molecules or protein aggregates. The brain resident macrophages, microglia,... 
INTERLEUKIN-1 | ACTIVATION | MOLECULAR PLATFORM | INHIBITION | DISTINCT PATHWAYS | NEUROINFLAMMATION | MULTIDISCIPLINARY SCIENCES | IL-1-BETA | MECHANISMS | RECEPTORS | NALP3 INFLAMMASOME | Microglia - metabolism | Inflammasomes - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein | Peptide Fragments - toxicity | Caspase 1 - metabolism | Interleukin-1alpha - metabolism | alpha-Synuclein - pharmacology | Interleukin-1beta - metabolism | Interleukin-1beta - secretion | Microglia - cytology | Brain - cytology | Interleukin-1beta - analysis | Enzyme-Linked Immunosorbent Assay | Microglia - drug effects | Amyloid beta-Peptides - toxicity | Mice, Inbred C57BL | Cells, Cultured | Mice, Knockout | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Caspase 1 - genetics | Caspase 1 - deficiency | Receptors, Purinergic P2X7 - metabolism | Mice | Interleukin-18 - metabolism | Astrocytes - metabolism | Cytokines | Health aspects | Nervous system diseases | Brain | Cell culture | Traumatic brain injury | Peptides | Aluminum sulfate | Homeostasis | Nervous system | Activation | Macrophages | Synuclein | Proteins | Rodents | Amyloid | Life sciences | Communication | Neurodegenerative diseases | Secretion | Astrocytes | Inflammation | Trauma | Molecular chains | Microglia | Interleukin 18 | Mode of action | Neurological diseases | Immune systems | Nigericin | Brain research | Ligands | Alum | Laboratory animals | Alzheimers disease | Chemokines | Index Medicus
Journal Article
Journal Article
Science, ISSN 0036-8075, 12/2003, Volume 302, Issue 5651, pp. 1772 - 1775
Alpha-synuclein is implicated in several neurodegenerative disorders, such as Parkinson's disease and multiple system atrophy, yet its functions remain... 
Yeasts | Neurons | Plasmids | Ubiquitins | Lipids | Reports | Cell membranes | Physiological regulation | Cytoplasmic inclusions | Genetic screening | Cells | SYSTEM | MEMBRANE INTERACTIONS | PHOSPHOLIPASE-D | PROTEIN AGGREGATION | MULTIDISCIPLINARY SCIENCES | BINDING PROTEINS | NEURODEGENERATION | FATTY-ACIDS | MUTATIONS | OLIGOMERIZATION | PARKINSONS-DISEASE | Saccharomyces cerevisiae - genetics | Ubiquitin - metabolism | Fluorescent Dyes - metabolism | Cytoplasm - metabolism | Recombinant Fusion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Endocytosis | Nerve Tissue Proteins - chemistry | Cell Division | Cell Membrane - metabolism | Inclusion Bodies - metabolism | Saccharomyces cerevisiae - physiology | Lipid Metabolism | Nuclear Proteins - metabolism | Phospholipase D - antagonists & inhibitors | Synucleins | Nerve Tissue Proteins - genetics | Phospholipase D - metabolism | Protein Folding | Nerve Tissue Proteins - metabolism | Point Mutation | Quaternary Ammonium Compounds - metabolism | Vacuoles - metabolism | Pyridinium Compounds - metabolism | Intracellular Membranes - metabolism | Saccharomyces cerevisiae - growth & development | alpha-Synuclein | Cell metabolism | Causes of | Parkinson's disease | Chemical properties | Research | Proteins | Genetics | Yeast | Neurological disorders | Index Medicus
Journal Article
Cell Metabolism, ISSN 1550-4131, 07/2014, Volume 20, Issue 1, pp. 145 - 157
Neurodegenerative diseases represent an increasing burden in our aging society, yet the underlying metabolic factors influencing onset and progression remain... 
LONGEVITY | MUTANTS | CAENORHABDITIS-ELEGANS | PROTEIN | PROTEOTOXICITY | DROSOPHILA LIFE-SPAN | DISEASE | ENDOCRINOLOGY & METABOLISM | ALPHA-SYNUCLEIN | GENE-EXPRESSION CHANGES | C.-ELEGANS | CELL BIOLOGY | Caenorhabditis elegans Proteins - metabolism | Male | Insulin Receptor Substrate Proteins - metabolism | Drosophila Proteins - metabolism | Dopaminergic Neurons - cytology | Glucose-6-Phosphate Isomerase - genetics | RNA Interference | Forkhead Transcription Factors - metabolism | Receptor, Insulin - genetics | Dopaminergic Neurons - metabolism | Aging | Parkinson Disease - metabolism | Insulin Receptor Substrate Proteins - genetics | Cytokines - genetics | Drosophila Proteins - antagonists & inhibitors | Disease Models, Animal | Parkinson Disease - pathology | Caenorhabditis elegans - metabolism | Cytokines - metabolism | Signal Transduction | Cells, Cultured | Transcription Factors - antagonists & inhibitors | Transcription Factors - genetics | Receptor, Insulin - antagonists & inhibitors | alpha-Synuclein - chemistry | Glucose-6-Phosphate Isomerase - metabolism | Transcription Factors - metabolism | Animals | Caenorhabditis elegans Proteins - antagonists & inhibitors | Glucose-6-Phosphate Isomerase - antagonists & inhibitors | Glucose - metabolism | Glycolysis | Receptor, Insulin - metabolism | Mice | Cytokines - antagonists & inhibitors | Drosophila - metabolism | Drosophila Proteins - genetics | Caenorhabditis elegans Proteins - genetics | alpha-Synuclein - metabolism | Insulin-Like Growth Factor I - metabolism | RNA, Small Interfering - metabolism | Glucose metabolism | Enzymes | Medical colleges | Analysis | Physiological aspects | Cystic fibrosis | Glucose | Dextrose | Neurophysiology | Insulin | Index Medicus
Journal Article
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 03/2012, Volume 32, Issue 12, pp. 4240 - 4246
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 03/2010, Volume 30, Issue 9, pp. 3184 - 3198
Increasing evidence suggests that phosphorylation may play an important role in the oligomerization, fibrillogenesis, Lewy body (LB) formation, and... 
BACKBONE DYNAMICS | MULTIPLE SYSTEM ATROPHY | INCLUSION FORMATION | BETA-SHEET | ALZHEIMERS-DISEASE | SERINE 129 | TAU-PHOSPHORYLATION | NEUROSCIENCES | LEWY BODIES | RAT MODEL | PARKINSONS-DISEASE | Phosphorylation | Rats, Wistar | Humans | Male | Brain - metabolism | Lewy Bodies - genetics | Lewy Body Disease - genetics | Protein Isoforms - metabolism | Multiple System Atrophy - metabolism | Cell Membrane - metabolism | Neurons - metabolism | Parkinson Disease - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | Disease Models, Animal | Alzheimer Disease - physiopathology | Rats | Mice, Transgenic | Neurodegenerative Diseases - genetics | Amino Acid Sequence - physiology | Multiple System Atrophy - genetics | Neurodegenerative Diseases - metabolism | Parkinson Disease - genetics | Parkinson Disease - physiopathology | Serine - metabolism | alpha-Synuclein - chemistry | Creatine Kinase - genetics | Lewy Body Disease - metabolism | Animals | Neurodegenerative Diseases - physiopathology | Alzheimer Disease - metabolism | Brain - pathology | Creatine Kinase - metabolism | Mice | Multiple System Atrophy - physiopathology | Alzheimer Disease - genetics | alpha-Synuclein - metabolism | Polymers - metabolism | Lewy Body Disease - physiopathology | Protein Isoforms - genetics | Index Medicus | serine 87 | phosphorylation | synucleinopathies | phosphomimics | Parkinson’s disease | α-synuclein
Journal Article
Journal Article
Journal Article
Neurobiology of Disease, ISSN 0969-9961, 2015, Volume 79, pp. 81 - 99
Abstract α-Synuclein (α-syn), a small protein that has the intrinsic propensity to aggregate, is implicated in several neurodegenerative diseases including... 
Neurology | α-Synuclein | Conformation-specific monoclonal antibodies | Parkinson’s disease | Dementia with Lewy bodies | Parkinson's disease | NEURODEGENERATIVE DISORDERS | ALZHEIMERS-DISEASE | VESICLE DOCKING | BRAIN PATHOLOGY | NEUROSCIENCES | MULTIPLE SYSTEM ATROPHY | MEMBRANE-BINDING | ELEVATED LEVELS | SOLUBLE OLIGOMERS | alpha-Synuclein | LEWY BODIES | PARKINSONS-DISEASE | gamma-Synuclein - immunology | Membrane Glycoproteins - metabolism | Escherichia coli | Protein Multimerization | alpha-Synuclein - immunology | Neoplasm Proteins - immunology | tau Proteins - metabolism | Neoplasm Proteins - metabolism | Brain - metabolism | gamma-Synuclein - metabolism | Amyloid beta-Peptides - metabolism | Parkinson Disease - metabolism | beta-Synuclein - immunology | Antibodies, Monoclonal - immunology | Recombinant Proteins - metabolism | Parkinson Disease - pathology | Peptide Fragments - metabolism | Lewy Body Disease - pathology | Islet Amyloid Polypeptide - metabolism | Recombinant Proteins - chemistry | Antibodies, Monoclonal - isolation & purification | alpha-Synuclein - chemistry | Lewy Body Disease - metabolism | Animals | Recombinant Proteins - immunology | Alzheimer Disease - metabolism | Brain - pathology | Protein Conformation | Mice | Antibodies, Monoclonal - metabolism | beta-Synuclein - metabolism | alpha-Synuclein - metabolism | Index Medicus | Basic Medicine | Neurosciences | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Neurovetenskaper
Journal Article
SCIENCE, ISSN 0036-8075, 09/2017, Volume 357, Issue 6357, pp. 1255 - 1255
Mitochondrial and lysosomal dysfunction have been implicated in substantia nigra dopaminergic neurodegeneration in Parkinson's disease (PD), but how these... 
GLUCOCEREBROSIDASE | PACEMAKING | DJ-1 | ALPHA-SYNUCLEIN | SUBSTANTIA-NIGRA | MULTIDISCIPLINARY SCIENCES | Mitochondria - enzymology | Mesencephalon - metabolism | Humans | Protein Deglycase DJ-1 - genetics | Substantia Nigra - metabolism | Melanins - metabolism | Glucosylceramidase - deficiency | Lysosomes - metabolism | Dopaminergic Neurons - metabolism | Tacrolimus - pharmacology | Parkinson Disease - metabolism | Dopamine - metabolism | Disease Models, Animal | Substantia Nigra - enzymology | Cell Line | Calcineurin Inhibitors - pharmacology | Oxidation-Reduction | Mesencephalon - enzymology | Mitochondria - metabolism | Antioxidants - pharmacology | Mitochondria - drug effects | Parkinson Disease - genetics | Mice, Knockout | Animals | Parkinson Disease - enzymology | Mice | Oxidative Stress - drug effects | alpha-Synuclein - metabolism | Oxidation-reduction reaction | Development and progression | Mitochondria | Dopamine | Parkinson's disease | Health aspects | Brain | Energy metabolism | Animal models | Target recognition | Mesencephalon | Pathogenesis | Substantia nigra | Parkinsons disease | Lysosomes | Synuclein | Accumulation | Pathways | Enzymatic activity | Neurodegeneration | Rodents | Oxidation | Degeneration | Species | Movement disorders | Dopamine receptors | Neurodegenerative diseases | Neurons | Medical treatment | Metabolism | Patients | Glucosylceramidase | Index Medicus
Journal Article
13.