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1. 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
Aggresome | Ubiquilin-1 | Protein misfolding | Ataxin-3 | Neurodegenerative diseases | Inclusion body | HDAC6 | Parkin | Index Medicus
Journal Article
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2. 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
Life Sciences & Biomedicine | Microbiology | Science & Technology | Fundamental and applied biological sciences. Psychology | Microbial ecology | Biological and medical sciences | General aspects | Animal, plant and microbial ecology | 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 | Index Medicus
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3. 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 (American Association for the Advancement of Science), ISSN 0036-8075, 2/2000, Volume 287, Issue 5456, pp. 1265 - 1269
Transgenic animals | Neurons | Substantia nigra | Inclusion bodies | Cell lines | Antibodies | Parkinson disease | Reports | Mice | Cytoplasmic inclusions | Lewy bodies | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Neurology | Biological and medical sciences | Medical sciences | Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases | 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 | Index Medicus
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4. 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 neurosciences, ISSN 1044-7431, 02/2011, Volume 46, Issue 2, pp. 516 - 526
Protein aggregation | Parkinson's disease | Calcium | Alpha-synuclein | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus
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5. Full Text 14-3-3 and aggresome formation: Implications in neurodegenerative diseases
by Jia, Baohui and Wu, Yuying and Zhou, Yi
Prion, ISSN 1933-6896, 03/2014, Volume 8, Issue 2, pp. 173 - 177
14-3-3 | aggresomes | protein misfolding | protein aggregation | Protein misfolding and aggregation | neurodegeneration | inclusion bodies | chaperones | Protein aggregation | Protein misfolding | Aggresomes | Neurodegeneration | Inclusion bodies | Chaperones | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 14-3-3 Proteins - physiology | Neurodegenerative Diseases - physiopathology | Humans | Protein Folding | Index Medicus | Extra View
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6. Full Text Molecular mechanisms of magnetosome formation
by Komeili, Arash
Annual Review of Biochemistry, ISSN 0066-4154, 2007, Volume 76, Issue 1, pp. 351 - 366
Ma mj | Biomineralization | Magnetosome island | Magnetotactic bacteria | Mamk | Mreb | Genes, Bacterial | Inclusion Bodies - chemistry | Bacterial Proteins - genetics | Ferrosoferric Oxide - metabolism | Magnetics | Intracellular Membranes - chemistry | Cell Movement - physiology | Biological Evolution | Bacterial Proteins - metabolism | Magnetospirillum - cytology | Inclusion Bodies - metabolism | Magnetospirillum - classification | Intracellular Membranes - metabolism | Magnetospirillum - physiology | Bacteria | Biochemistry | Magnetism | Molecular biology | Crystals | Index Medicus
Conference Proceeding
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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
Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus
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8. Full Text Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation
by Kim, Yong Man and Jang, Won Hee and Quezado, Martha M and Oh, Yohan and Chung, Kwang Chul and Junn, Eunsung and Mouradian, M. Maral
Journal of the neurological sciences, ISSN 0022-510X, 2011, Volume 307, Issue 1, pp. 157 - 161
Neurology | α-Synuclein | Protein aggregation | Parkinson's disease | SUMOylation | Dementia with Lewy Bodies | Proteasome | Neurosciences | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Biological and medical sciences | Medical sciences | Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases | Chlorocebus aethiops | Humans | Lewy Bodies - enzymology | Lewy Body Disease - enzymology | Sumoylation - physiology | Inclusion Bodies - enzymology | Parkinson Disease - physiopathology | Proteasome Endopeptidase Complex - physiology | Protein Processing, Post-Translational - physiology | Lewy Body Disease - metabolism | Animals | Parkinson Disease - enzymology | Inclusion Bodies - pathology | Parkinson Disease - metabolism | SUMO-1 Protein - metabolism | Lewy Bodies - metabolism | Inclusion Bodies - metabolism | Proteasome Inhibitors | COS Cells | Lewy Bodies - pathology | alpha-Synuclein - metabolism | Macromolecular Substances - metabolism | Lewy Body Disease - physiopathology | Index Medicus | proteasome | protein aggregation | Parkinson’s disease
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9. Aggresome formation and neurodegenerative diseases: Therapeutic implications
by Olzmann, J. A and Li, L and Chin, L. S
Current medicinal chemistry, ISSN 0929-8673, 01/2008, Volume 15, Issue 1, pp. 47 - 60
Pharmacology & Pharmacy | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Chemistry, Medicinal | Science & Technology | Molecular Chaperones - metabolism | Humans | Proteasome Endopeptidase Complex - chemistry | Inclusion Bodies - drug effects | Molecular Chaperones - chemistry | Neurodegenerative Diseases - metabolism | Neurodegenerative Diseases - drug therapy | Protein Folding | Animals | Models, Biological | Molecular Structure | Proteasome Endopeptidase Complex - metabolism | Inclusion Bodies - metabolism
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10. Full Text Compromised paraspeckle formation as a pathogenic factor in FUSopathies
by Shelkovnikova, Tatyana A and Robinson, Hannah K and Troakes, Claire and Ninkina, Natalia and Buchman, Vladimir L
Human molecular genetics, ISSN 0964-6906, 05/2014, Volume 23, Issue 9, pp. 2298 - 2312
Biochemistry & Molecular Biology | Genetics & Heredity | Life Sciences & Biomedicine | Science & Technology | Cell Line | Animals | Humans | Amyotrophic Lateral Sclerosis - metabolism | Cells, Cultured | Mice, Transgenic | Mice | RNA-Binding Protein FUS - metabolism | In Vitro Techniques | RNA, Long Noncoding - metabolism | Intranuclear Inclusion Bodies - metabolism | Index Medicus
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