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1. 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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2. Full Text Cellular milieu imparts distinct pathological α-synuclein strains in α-synucleinopathies
by Peng, Chao and Gathagan, Ronald J and Covell, Dustin J and Medellin, Coraima and Stieber, Anna and Robinson, John L and Zhang, Bin and Pitkin, Rose M and Olufemi, Modupe F and Luk, Kelvin C and Trojanowski, John Q and Lee, Virginia M.-Y
Nature, ISSN 0028-0836, 05/2018, Volume 557, Issue 7706, pp. 558 - 563
In Lewy body diseases-including Parkinson's disease, without or with dementia, dementia with Lewy bodies, and Alzheimer's disease with Lewy body... 
FIBRILS | MESSENGER-RNA EXPRESSION | LEWY BODY | ALZHEIMERS-DISEASE | MULTIDISCIPLINARY SCIENCES | MOUSE MODEL | NEURONS | PARKINSON-DISEASE | MULTIPLE-SYSTEM ATROPHY | CULTURED-CELLS | OLIGODENDROCYTES | Neurons - pathology | Oligodendroglia - metabolism | alpha-Synuclein - classification | Humans | Cytoplasm - metabolism | Male | Cytoplasm - pathology | Female | Neurons - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | Oligodendroglia - chemistry | Cytoplasm - chemistry | Lewy Bodies - chemistry | Neurons - chemistry | Mice, Inbred C57BL | Lewy Body Disease - pathology | Organ Specificity | Protein Folding | alpha-Synuclein - chemistry | Lewy Body Disease - metabolism | Oligodendroglia - pathology | Animals | Mice | alpha-Synuclein - metabolism | Parkinson's disease | Seeds | Neurodegenerative diseases | Neurons | Lewy body disease | Synuclein | Seeding | Lewy bodies | Atrophy | Pathology | Axons | Hypotheses | Neurodegeneration | Inclusion bodies | Oligodendrocytes | Dementia disorders | Intracellular | Alzheimers disease | Alzheimer's disease | Movement disorders | Dementia
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3. Full Text Lewy body extracts from Parkinson disease brains trigger α‐synuclein pathology and neurodegeneration in mice and monkeys
by Recasens, Ariadna and Dehay, Benjamin and Bové, Jordi and Carballo‐Carbajal, Iria and Dovero, Sandra and Pérez‐Villalba, Ana and Fernagut, Pierre‐Olivier and Blesa, Javier and Parent, Annabelle and Perier, Celine and Fariñas, Isabel and Obeso, José A and Bezard, Erwan and Vila, Miquel
Annals of Neurology, ISSN 0364-5134, 03/2014, Volume 75, Issue 3, pp. 351 - 362
Objective Mounting evidence suggests that α‐synuclein, a major protein component of Lewy bodies (LB), may be responsible for initiating and spreading the... 
TRANSMISSION | PROTEIN | DEMENTIA | INCLUSIONS | AGGREGATE | DISORDER | NEURONAL CELL-DEATH | BODIES | DYSFUNCTION | PREVENTS | NEUROSCIENCES | CLINICAL NEUROLOGY | Tissue Extracts - chemistry | Substantia Nigra - pathology | alpha-Synuclein - administration & dosage | Dopaminergic Neurons - pathology | Humans | Macaca mulatta | Nerve Degeneration - chemically induced | Nerve Degeneration - metabolism | Dopaminergic Neurons - metabolism | Dopaminergic Neurons - drug effects | Female | Parkinson Disease - metabolism | alpha-Synuclein - genetics | Lewy Bodies - metabolism | Corpus Striatum - pathology | Lewy Bodies - pathology | Lewy Bodies - chemistry | Parkinson Disease - pathology | Microinjections | alpha-Synuclein - toxicity | Nerve Degeneration - pathology | Mice, Knockout | alpha-Synuclein - isolation & purification | Substantia Nigra - drug effects | Animals | Corpus Striatum - drug effects | Mice | Tissue Extracts - toxicity | Parkinson Disease - etiology | Life Sciences
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4. Full Text Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
by Bernardi, Rosa and Pandolfi, Pier Paolo
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 12/2007, Volume 8, Issue 12, pp. 1006 - 1016
The promyelocytic leukaemia (PML) tumour suppressor protein epitomizes the PML-nuclear body (PML-NB) and is crucially required for the proper assembly of this... 
INDUCED DNA-DAMAGE | FAS-INDUCED APOPTOSIS | PREMATURE SENESCENCE | PML GROWTH-SUPPRESSOR | MULTIPLE APOPTOTIC PATHWAYS | CLASS-I EXPRESSION | TUMOR-SUPPRESSOR | NEOPLASTIC HUMAN TISSUES | PROTEIN PML | CELLULAR SENESCENCE | CELL BIOLOGY | Transcription Factors - metabolism | Cell Nucleus Structures - chemistry | Intranuclear Inclusion Bodies - chemistry | Tumor Suppressor Proteins - metabolism | Animals | Cell Nucleus Structures - physiology | Humans | Nuclear Proteins - metabolism | Intranuclear Inclusion Bodies - physiology | Neoplasm Proteins - metabolism | Promyelocytic Leukemia Protein | Physiological aspects | Cellular proteins | Tumor suppressor genes | Genetic aspects | Research | Chronic myeloid leukemia
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5. Full Text Bacterial Inclusion Bodies: Discovering Their Better Half
by Rinas, Ursula and Garcia-Fruitós, Elena and Corchero, José Luis and Vázquez, Esther and Seras-Franzoso, Joaquin and Villaverde, Antonio
Trends in Biochemical Sciences, ISSN 0968-0004, 09/2017, Volume 42, Issue 9, pp. 726 - 737
Bacterial inclusion bodies (IBs) are functional, non-toxic amyloids occurring in recombinant bacteria showing analogies with secretory granules of the... 
PROTEIN AGGREGATION | RECOMBINANT PROTEINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | AMYLOID AGGREGATION KINETICS | CELL-PROLIFERATION | FUNCTIONAL AMYLOIDS | BIOLOGICAL ROLE | BODY FORMATION | EXPRESSION SYSTEM | SECRETORY GRANULES | Bacteria - metabolism | Bacteria - chemistry | Inclusion Bodies - metabolism | Inclusion Bodies - chemistry | Molecular biology | Recombinant proteins | Glycoproteins
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6. Full Text Cajal bodies: A long history of discovery
by Cioce, Mario and Lamond, Angus I
Annual Review of Cell and Developmental Biology, ISSN 1081-0706, 2005, Volume 21, Issue 1, pp. 105 - 131
This review surveys what is known about the structure and function of the subnuclear domains called Cajal bodies (CBs). The major focus is on CBs in mammalian... 
Nucleus | Disease | Coilin | snRNP | Stress | stress | disease | S-PHASE ENTRY | SMALL NUCLEAR-RNA | coilin | nucleus | DEVELOPMENTAL BIOLOGY | SMN PROTEIN | SMALL NUCLEOLAR RNA | XENOPUS GERMINAL VESICLE | COILED BODIES | GREEN FLUORESCENT PROTEIN | SPINAL MUSCULAR-ATROPHY | IN-VIVO | CELL-CYCLE | Intranuclear Inclusion Bodies - chemistry | History, 20th Century | Humans | RNA-Binding Proteins - chemistry | Coiled Bodies - chemistry | Forecasting | Animals | Cell Nucleus - metabolism | Models, Biological | Coiled Bodies - metabolism | Cell Nucleus - chemistry | Ribonucleoproteins, Small Nuclear - chemistry | Intranuclear Inclusion Bodies - metabolism | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism
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7. 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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8. Full Text Distinct β-sheet structure in protein aggregates determined by ATR-FTIR spectroscopy
by Shivu, Bhavana and Seshadri, Sangita and Li, Jie and Oberg, Keith A and Uversky, Vladimir N and Fink, Anthony L
Biochemistry, ISSN 0006-2960, 08/2013, Volume 52, Issue 31, pp. 5176 - 5183
Attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) was used to study the conformation of aggregated proteins in vivo and in vitro.... 
POLYPEPTIDE-CHAINS | IN-VITRO | INCLUSION-BODIES | AMYLOID FIBRILS | APOMYOGLOBIN | TRANSFORM INFRARED-SPECTROSCOPY | TRANSTHYRETIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-DIFFRACTION | SECONDARY STRUCTURE | FIBRILLOGENESIS | Amyloid - genetics | Protein Structure, Secondary | Inclusion Bodies - chemistry | Humans | Amyloid - chemistry | Protein Folding | Immunoglobulin Light Chains - metabolism | alpha-Synuclein - chemistry | Immunoglobulin Light Chains - chemistry | Immunoglobulin Light Chains - genetics | Inclusion Bodies - genetics | Insulin - metabolism | Amyloid - metabolism | Escherichia coli - genetics | Insulin - chemistry | Escherichia coli - metabolism | Spectroscopy, Fourier Transform Infrared - methods | alpha-Synuclein - genetics | HeLa Cells | Inclusion Bodies - metabolism | Insulin - genetics | alpha-Synuclein - metabolism
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9. Full Text Protein quality in bacterial inclusion bodies
by Ventura, Salvador and Villaverde, Antonio
Trends in Biotechnology, ISSN 0167-7799, 2006, Volume 24, Issue 4, pp. 179 - 185
A common limitation of recombinant protein production in bacteria is the formation of insoluble protein aggregates known as inclusion bodies. The propensity of... 
PROTEOLYTIC DIGESTION | HEAT-SHOCK PROTEINS | PLUS CHAPERONE CLPB | RECOMBINANT ESCHERICHIA-COLI | BETA-LACTAMASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | MOLECULAR CHAPERONES | IN-VIVO | AGGREGATED PROTEINS | SECONDARY STRUCTURE | BODY FORMATION | Sequence Analysis, Protein | Inclusion Bodies - chemistry | Recombinant Proteins - analysis | Bacterial Proteins - chemistry | Recombinant Proteins - chemistry | Bacterial Proteins - analysis | Protein Folding | Recombinant proteins | Polypeptides | Enzymes | Biomedical research | E coli | Microscopy | Protein folding | Quality control | Proteomics | Heat shock proteins | Growth hormones | Gene expression | Biological activity
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10. Full Text Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
by Hasegawa, Masato and Arai, Tetsuaki and Nonaka, Takashi and Kametani, Fuyuki and Yoshida, Mari and Hashizume, Yoshio and Beach, Thomas G and Buratti, Emanuele and Baralle, Francisco and Morita, Mitsuya and Nakano, Imaharu and Oda, Tatsuro and Tsuchiya, Kuniaki and Akiyama, Haruhiko
Annals of Neurology, ISSN 0364-5134, 07/2008, Volume 64, Issue 1, pp. 60 - 70
Objective TAR DNA‐binding protein of 43kDa (TDP‐43) is deposited as cytoplasmic and intranuclear inclusions in brains of patients with frontotemporal lobar... 
TAU-PROTEIN | DEMENTIA | ALZHEIMERS-DISEASE | INCLUSION-BODY | IN-VIVO | PAIRED HELICAL FILAMENTS | UBIQUITIN IMMUNOHISTOCHEMISTRY | MOTOR-NEURON DISEASE | ALPHA-SYNUCLEIN | NEUROSCIENCES | NEURODEGENERATIVE DISEASES | CLINICAL NEUROLOGY | Antibody Specificity | Phosphorylation | Inclusion Bodies - chemistry | Humans | Middle Aged | Antibodies | Male | Brain - metabolism | DNA-Binding Proteins - metabolism | Epitopes - immunology | Dementia - metabolism | Neurofibrillary Tangles - metabolism | Peptide Fragments - immunology | Aged, 80 and over | Female | Neurofibrillary Tangles - immunology | Neurofibrillary Tangles - pathology | Protein Structure, Tertiary | Inclusion Bodies - immunology | DNA-Binding Proteins - immunology | Dementia - pathology | DNA-Binding Proteins - chemistry | Amyotrophic Lateral Sclerosis - pathology | Peptide Fragments - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Brain - pathology | Inclusion Bodies - pathology | Aged | Casein Kinase I - metabolism | Epitopes - chemistry
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