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1. Full Text Neuronal Aggregates: Formation, Clearance, and Spreading
by Lim, Junghyun and Yue, Zhenyu
Developmental Cell, ISSN 1534-5807, 02/2015, Volume 32, Issue 4, pp. 491 - 501
Proteostasis is maintained by multiple cellular pathways, including protein synthesis, quality control, and degradation. An imbalance of neuronal proteostasis,... 
UBIQUITIN-PROTEASOME SYSTEM | UNCONVENTIONAL PROTEIN SECRETION | AMYLOID-BETA | MUTANT HUNTINGTIN | DEVELOPMENTAL BIOLOGY | AUTOPHAGY-DEFICIENT MICE | ALPHA-SYNUCLEIN | TO-CELL TRANSMISSION | INCLUSION-BODY FORMATION | SELECTIVE AUTOPHAGY | NEURODEGENERATIVE DISEASES | CELL BIOLOGY | Animals | Homeostasis - physiology | Humans | Signal Transduction - physiology | Autophagy - physiology | Proteasome Endopeptidase Complex - metabolism | Cell Differentiation - physiology | Protein Aggregation, Pathological - metabolism | Proteins | Physiological aspects | Protein biosynthesis | Neurons
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2. Full Text Inclusion Formation and Neuronal Cell Death through Neuron-to-Neuron Transmission of α-Synuclein
by Paula Desplats and He-Jin Lee and Eun-Jin Bae and Christina Patrick and Edward Rockenstein and Leslie Crews and Brian Spencer and Eliezer Masliah and Seung-Jae Lee and Inder M. Verma
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2009, Volume 106, Issue 31, pp. 13010 - 13015
Neuronal accumulation of α-synuclein and Lewy body formation are characteristic to many neurodegenerative diseases, including Parkinson's disease (PD). This... 
Pathology | Nervous system diseases | Neurons | Synaptic transmission | Transgenic animals | Inclusion bodies | Stem cells | Parkinson disease | Cell aggregates | Tissue grafting | Protein aggregation | Parkinson's disease | Neurodegeneration | Lewy body | CLEARANCE | DEMENTIA | MULTIDISCIPLINARY SCIENCES | neurodegeneration | HOST | PATHOLOGY | MODELS | protein aggregation | ACCUMULATION | LEWY BODIES | PROPAGATION | BRAIN | PARKINSONS-DISEASE | Cell Line | Lewy Bodies - physiology | alpha-Synuclein - toxicity | Humans | Mice, Inbred C57BL | Rats | Mice, Transgenic | Synaptic Transmission | Stem Cell Transplantation | Animals | Biological Transport | Neurons - physiology | Mice | alpha-Synuclein - metabolism | Apoptosis | Index Medicus | Biological Sciences
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3. Full Text New insights in the formation of polyhydroxyalkanoate granules (carbonosomes) and novel functions of poly(3‐hydroxybutyrate)
by Jendrossek, Dieter and Pfeiffer, Daniel
Environmental Microbiology, ISSN 1462-2912, 08/2014, Volume 16, Issue 8, pp. 2357 - 2373
Summary The metabolism of polyhydroxybutyrate (PHB) and related polyhydroxyalkanoates (PHAs) has been investigated by many groups for about three decades, and... 
PHB GRANULES | RALSTONIA-EUTROPHA H16 | IN-VIVO IMMOBILIZATION | POLY-BETA-HYDROXYBUTYRATE | PSEUDOMONAS-PUTIDA | PHAP PHASIN | ESCHERICHIA-COLI | RHODOSPIRILLUM-RUBRUM | MICROBIOLOGY | INTRACELLULAR 3-HYDROXYBUTYRATE-OLIGOMER HYDROLASE | POLYHYDROXYBUTYRATE GRANULES | Cupriavidus necator - chemistry | Hydroxybutyrates - chemistry | Inclusion Bodies - chemistry | Polyhydroxyalkanoates - chemistry | Polyhydroxyalkanoates - metabolism | Cupriavidus necator - metabolism | Polyesters - chemistry | Pseudomonas putida - chemistry | Pseudomonas putida - metabolism | Polyesters - metabolism | Bacterial Proteins - metabolism | Hydroxybutyrates - metabolism | Inclusion Bodies - metabolism | Bacterial Proteins - isolation & purification | Biodegradation | Physiological aspects | Analysis
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4. Full Text C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging
by van Ham, T.J and Thijssen, K.L and Breitling, R and Hofstra, R.M.W and Plasterk, R.H.A and Nollen, E.A.A
PLoS Genetics, ISSN 1553-7404, 2008, Volume 4, Issue 3, p. e1000027
Inclusions in the brain containing alpha-synuclein are the pathological hallmark of Parkinson's disease, but how these inclusions are formed and how this links... 
LIFE-SPAN | CAENORHABDITIS-ELEGANS | DEMENTIA | DROSOPHILA MODEL | GENETICS & HEREDITY | ENVIRONMENTAL RISK-FACTORS | TOXICITY | LEWY BODIES | AGGREGATION | PARKINSONS-DISEASE | G-Protein-Coupled Receptor Kinases - genetics | Fluorescence Recovery After Photobleaching | alpha-Synuclein - antagonists & inhibitors | Humans | Genes, Helminth | DNA Primers - genetics | Recombinant Fusion Proteins - metabolism | Brain - metabolism | Aging - genetics | RNA Interference | Base Sequence | Gene Deletion | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Inclusion Bodies - metabolism | Caenorhabditis elegans - metabolism | G-Protein-Coupled Receptor Kinases - metabolism | Animals, Genetically Modified | Caenorhabditis elegans - genetics | Bacterial Proteins - genetics | Parkinson Disease - genetics | G-Protein-Coupled Receptor Kinases - antagonists & inhibitors | Animals | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Models, Genetic | alpha-Synuclein - metabolism | Aging - metabolism | Luminescent Proteins - metabolism | Parkinson Disease - etiology
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5. Full Text Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative Disorders
by Eliezer Masliah and Edward Rockenstein and Isaac Veinbergs and Margaret Mallory and Makoto Hashimoto and Ayako Takeda and Yutaka Sagara and Abbyann Sisk and Lennart Mucke
Science, ISSN 0036-8075, 2/2000, Volume 287, Issue 5456, pp. 1265 - 1269
To elucidate the role of the synaptic protein α-synuclein in neurodegenerative disorders, transgenic mice expressing wild-type human α-synuclein were... 
Transgenic animals | Neurons | Substantia nigra | Inclusion bodies | Cell lines | Antibodies | Parkinson disease | Reports | Mice | Cytoplasmic inclusions | Lewy bodies | GENE | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | MUTATION | NACP/ALPHA-SYNUCLEIN | AMYLOID PRECURSOR PROTEIN | LEWY BODIES | AGGREGATION | TRANSGENIC MICE | PARKINSONS-DISEASE | BETA | Lewy Bodies - ultrastructure | Tyrosine 3-Monooxygenase - metabolism | Humans | Substantia Nigra - metabolism | Motor Activity | Brain - metabolism | Tyrosine 3-Monooxygenase - immunology | Neurons - ultrastructure | Dopamine - physiology | Brain - ultrastructure | Mice, Inbred DBA | Neurons - metabolism | Inclusion Bodies - metabolism | Ubiquitins - metabolism | Inclusion Bodies - ultrastructure | Neurodegenerative Diseases - pathology | Nerve Tissue Proteins - immunology | Mice, Inbred C57BL | Lewy Body Disease - pathology | Mice, Transgenic | Neurodegenerative Diseases - metabolism | Microscopy, Electron | Synucleins | Nerve Tissue Proteins - genetics | Lewy Body Disease - metabolism | Nerve Tissue Proteins - metabolism | Animals | Substantia Nigra - ultrastructure | alpha-Synuclein | Proteins | Nervous system | Amino acids | Rodents | a-Synuclein | inclusion bodies
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6. Full Text Raised calcium promotes α-synuclein aggregate formation
by Nath, S and Goodwin, J and Engelborghs, Y and Pountney, D.L
Molecular and Cellular Neuroscience, ISSN 1044-7431, 02/2011, Volume 46, Issue 2, pp. 516 - 526
Parkinson's and Parkinson's-plus diseases are associated with abnormal, aggregated forms of the protein, α-synuclein. We have investigated the effects of... 
Protein aggregation | Parkinson's disease | Calcium | Alpha-synuclein | INCLUSIONS | NEUROSCIENCES | OLIGOMERS | FORMS | MUTANTS | CONFORMATIONAL PROPERTIES | BETA-SYNUCLEIN | NEURONS | BINDING | PARKINSONS-DISEASE | Microscopy, Electron, Scanning | Parkinson Disease - pathology | Inclusion Bodies - ultrastructure | Neurons - chemistry | Calcium - metabolism | Inclusion Bodies - chemistry | Humans | Calcium - chemistry | alpha-Synuclein - chemistry | Microscopy, Confocal | Neurons - ultrastructure | Cell Line, Tumor | Neurons - metabolism | Parkinson Disease - metabolism | Inclusion Bodies - metabolism | alpha-Synuclein - metabolism | Microscopy, Fluorescence
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7. Full Text α-Synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
by Feany, Mel B and Chen, Li
Nature Neuroscience, ISSN 1097-6256, 05/2005, Volume 8, Issue 5, pp. 657 - 663
alpha-Synuclein is phosphorylated at serine 129 (Ser129) in intracellular protein aggregates called Lewy bodies. These inclusion bodies are the characteristic... 
HUMAN BRAIN | PROTEIN | GENE | COUPLED RECEPTOR KINASES | NEURODEGENERATION | TAU | MUTATIONS | SUPPRESSION | HUNTINGTIN | NEUROSCIENCES | LESIONS | Neurons - pathology | Phosphorylation | Central Nervous System - metabolism | Nerve Degeneration - physiopathology | Central Nervous System - pathology | Nerve Degeneration - metabolism | Neurons - metabolism | Parkinson Disease - metabolism | Inclusion Bodies - metabolism | Dopamine - metabolism | Disease Models, Animal | Cyclic AMP-Dependent Protein Kinases - metabolism | Drosophila Proteins | G-Protein-Coupled Receptor Kinase 2 | Animals, Genetically Modified | Point Mutation - physiology | Drosophila | Parkinson Disease - genetics | Parkinson Disease - physiopathology | Synucleins | Serine - metabolism | Nerve Degeneration - pathology | Nerve Tissue Proteins - metabolism | Animals | Amino Acid Substitution - physiology | Brain - pathology | Aspartic Acid - metabolism | Central Nervous System - physiopathology | Retina - pathology | alpha-Synuclein | beta-Adrenergic Receptor Kinases
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8. Full Text A novel, high‐efficiency cellular model of fibrillar α‐synuclein inclusions and the examination of mutations that inhibit amyloid formation
by Waxman, Elisa A and Giasson, Benoit I
Journal of Neurochemistry, ISSN 0022-3042, 04/2010, Volume 113, Issue 2, pp. 374 - 388
J. Neurochem. (2010) 113, 374–388. Intracytoplasmic alpha‐synuclein (α‐syn) amyloidogenic inclusions are a major pathological feature of Parkinson’s disease,... 
inhibitors | nucleation | fibrillization | cellular model | α‐synuclein | phosphorylation | Parkinson’s disease | Cellular model | Phosphorylation | Inhibitors | Nucleation | Parkinson's disease | Fibrillization | α-synuclein | SEQUENCE DETERMINANTS | AGGRESOME FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYTOPLASMIC INCLUSIONS | LEWY BODY DISEASE | alpha-synuclein | PATHOLOGICAL INCLUSIONS | CULTURED-CELLS | NEUROSCIENCES | MEDIATED PHOSPHORYLATION | MULTIPLE SYSTEM ATROPHY | IN-VITRO | PARKINSONS-DISEASE | Thiazoles - metabolism | Inclusion Bodies - ultrastructure | Humans | Inclusion Bodies - drug effects | Amyloid - ultrastructure | Point Mutation - genetics | Inclusion Bodies - genetics | Transfection - methods | Amyloid - metabolism | Hydrophobic and Hydrophilic Interactions | alpha-Synuclein - genetics | Inclusion Bodies - metabolism | alpha-Synuclein - metabolism | Calcium Phosphates - pharmacology | Cell Line, Transformed
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9. Full Text Exogenous α-Synuclein Fibrils Seed the Formation of Lewy Body-Like Intracellular Inclusions in Cultured Cells
by Kelvin C. Luk and Cheng Song and Patrick O'Brien and Anna Stieber and Jonathan R. Branch and Kurt R. Brunden and John Q. Trojanowski and Virginia M.-Y. Lee
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2009, Volume 106, Issue 47, pp. 20051 - 20056
Cytoplasmic inclusions containing α-synuclein (α-Syn) fibrils, referred to as Lewy bodies (LBs), are the signature neuropathological hallmarks of Parkinson's... 
Aggregation | Cell culture techniques | Neurons | Inclusion bodies | Cell lines | Parkinson disease | Cultured cells | Solar fibrils | Cytoplasmic inclusions | Cells | Pathology | Parkinson's disease | Protein misfolding | SYSTEM | NEURODEGENERATIVE DISORDERS | pathology | PROTEIN | MULTIDISCIPLINARY SCIENCES | TRANSMISSION | MODELS | protein misfolding | MUTATION | BODIES | MICE | AGGREGATION | PARKINSONS-DISEASE | Recombinant Proteins - metabolism | Neurons - pathology | Lewy Bodies - chemistry | Parkinson Disease - pathology | Inclusion Bodies - ultrastructure | Inclusion Bodies - chemistry | Humans | Cells, Cultured | Neurons - cytology | Recombinant Proteins - genetics | Amyloid - chemistry | alpha-Synuclein - chemistry | Amyloid - metabolism | Inclusion Bodies - pathology | Neurons - metabolism | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Lewy Bodies - metabolism | Inclusion Bodies - metabolism | alpha-Synuclein - metabolism | Biological Sciences
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10. Full Text The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of α‐synuclein aggregates
by Wakabayashi, Koichi and Tanji, Kunikazu and Mori, Fumiaki and Takahashi, Hitoshi
Neuropathology, ISSN 0919-6544, 10/2007, Volume 27, Issue 5, pp. 494 - 506
The histological hallmark of Parkinson's disease (PD) is the presence of fibrillar aggregates called Lewy bodies (LBs). LB formation has been considered to be... 
α‐synucleinopathy | Parkinson's disease | α‐synuclein | pale body | Lewy body | Pale body | α-synuclein | α-synucleinopathy | HUMAN NEURODEGENERATIVE DISEASES | ALZHEIMERS-DISEASE | NEURONAL INCLUSIONS | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | alpha-synuclein | SUBSTANTIA-NIGRA | NEUROSCIENCES | CLINICAL NEUROLOGY | alpha-synucleinopathy | UBIQUITINATED INCLUSION-BODIES | MULTIPLE SYSTEM ATROPHY | GLIAL CYTOPLASMIC INCLUSIONS | CENTRAL-NERVOUS-SYSTEM | CYCLIN-DEPENDENT KINASE-5 | Nerve Tissue Proteins - metabolism | Parkinson Disease - pathology | Brain Stem - pathology | Humans | Brain Stem - metabolism | Cerebral Cortex - pathology | Parkinson Disease - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | alpha-Synuclein - metabolism | Cerebral Cortex - metabolism | Enzymes - metabolism
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11. Aggresome formation and neurodegenerative diseases: Therapeutic implications
by Olzmann, J.A and Li, Lian and Chin, L.S
Current Medicinal Chemistry, ISSN 0929-8673, 01/2008, Volume 15, Issue 1, pp. 47 - 60
Accumulation of misfolded proteins in proteinaceous inclusions is a prominent pathological feature common to many age-related neurodegenerative diseases,... 
Aggresome | Ubiquilin-1 | Protein misfolding | Ataxin-3 | Neurodegenerative diseases | Inclusion body | HDAC6 | Parkin | ataxin-3 | CHEMISTRY, MEDICINAL | UBIQUITIN-PROTEASOME SYSTEM | MARIE-TOOTH-DISEASE | parkin | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AGGREGATE-PRONE PROTEINS | MOTOR-NEURON DISEASE | ALPHA-SYNUCLEIN | ubiquilin-1 | inclusion body | neurodegenerative diseases | protein misfolding | SMALL-MOLECULE INHIBITORS | PHARMACOLOGY & PHARMACY | HISTONE DEACETYLASE INHIBITORS | LEWY-BODY FORMATION | aggresome | PARKINSONS-DISEASE
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12. Full Text Formation of Nuclear Bodies of Arabidopsis CRY2 in Response to Blue Light Is Associated with Its Blue Light-Dependent Degradation
by Xuhong Yu and Ricardo Sayegh and Maskit Maymon and Katherine Warpeha and John Klejnot and Hongyun Yang and Jie Huang and Janet Lee and Lon Kaufman and Chentao Lin
The Plant Cell, ISSN 1040-4651, 1/2009, Volume 21, Issue 1, pp. 118 - 130
Arabidopsis thaliana cryptochrome 2 (CRY2) mediates photoperiodic promotion of floral initiation and blue light inhibition of hypocotyl elongation. It has been... 
Proteins | Phosphorylation | Hypocotyls | Light | Fluorescence | Photoreceptors | Flowering | Plants | Seedlings | Plant cells | LOCALIZATION | CRYPTOCHROME 2 | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | PLANT SCIENCES | CELL BIOLOGY | SIGNAL-TRANSDUCTION | COP1 | THALIANA | PHYTOCHROME-B | GFP FUSION PROTEIN | PHOTORECEPTORS | Flavoproteins - radiation effects | Photoreceptors, Plant - metabolism | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Arabidopsis - radiation effects | Recombinant Fusion Proteins - radiation effects | Gene Expression Regulation, Plant | Green Fluorescent Proteins - metabolism | Arabidopsis Proteins - genetics | Flavoproteins - metabolism | Green Fluorescent Proteins - radiation effects | Flavoproteins - genetics | Arabidopsis - cytology | Models, Molecular | RNA, Plant - genetics | Arabidopsis - metabolism | Arabidopsis Proteins - radiation effects | Arabidopsis - genetics | Cryptochromes | Recombinant Fusion Proteins - genetics | Proteasome Endopeptidase Complex - metabolism | Intranuclear Inclusion Bodies - metabolism | Usage | Monochromatic light | Arabidopsis | Optical properties | Green fluorescent protein | Physiological aspects | Research
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