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1. Full Text Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death
by Volpicelli-Daley, Laura A and Luk, Kelvin C and Patel, Tapan P and Tanik, Selcuk A and Riddle, Dawn M and Stieber, Anna and Meaney, David F and Trojanowski, John Q and Lee, Virginia M.-Y
Neuron, ISSN 0896-6273, 2011, Volume 72, Issue 1, pp. 57 - 71
Inclusions composed of α-synuclein (α-syn), i.e., Lewy bodies (LBs) and Lewy neurites (LNs), define synucleinopathies including Parkinson's disease (PD) and... 
PATHOGENESIS | MULTIPLE SYSTEM ATROPHY | IN-VITRO | TRANSMISSION | INCLUSIONS | BODIES | ENDOCYTOSIS | BLOOD-BRAIN-BARRIER | NEUROSCIENCES | AGGREGATION | SPORADIC PARKINSONS-DISEASE | Neurons - pathology | Humans | Synapses - pathology | Nerve Degeneration - metabolism | Neurons - ultrastructure | Synapses - metabolism | Voltage-Sensitive Dye Imaging - methods | Neurons - physiology | Hippocampus - ultrastructure | Neurons - metabolism | Lewy Bodies - metabolism | Lewy Bodies - pathology | Mice, Inbred C57BL | Axonal Transport - physiology | Hippocampus - pathology | Neurites - metabolism | Nerve Degeneration - pathology | Endocytosis - physiology | Nerve Tissue Proteins - metabolism | Hippocampus - metabolism | Neurites - pathology | Animals | Cell Death - physiology | Mice | Primary Cell Culture | Hippocampus - physiology | alpha-Synuclein - adverse effects | alpha-Synuclein - metabolism
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2. Full Text Dynactin is involved in Lewy body pathology
by Shen, Chang and Honda, Hiroyuki and Suzuki, Satoshi O and Maeda, Norihisa and Shijo, Masahiro and Hamasaki, Hideomi and Sasagasako, Naokazu and Fujii, Naoki and Iwaki, Toru
Neuropathology, ISSN 0919-6544, 12/2018, Volume 38, Issue 6, pp. 583 - 590
Dynactin forms a protein complex with dynein that retrogradely transports cargo along microtubules. Dysfunction of this dynein‐dynactin complex causes several... 
dynein | Parkinson's disease | multiple system atrophy | dynactin | α‐synuclein | α-synuclein | KINASE 1 | AXONAL-TRANSPORT | ALPHA-SYNUCLEIN | CHAMELEON | PATHOLOGY | NEUROSCIENCES | CLINICAL NEUROLOGY | DEGENERATION | synuclein | PROTEINS | BINDING | PARKINSONS-DISEASE | Parkinson Disease - pathology | Multiple System Atrophy - pathology | Humans | Middle Aged | Lewy Body Disease - pathology | Aged, 80 and over | Brain - pathology | Female | Male | Aged | Lewy Bodies - pathology | Dynactin Complex - metabolism | Proteins | Immunohistochemistry | Brain | Nervous system diseases | Neurons | Dynein | Dementia | Dynactin | Neurodegenerative diseases | Brain stem | Cortex | Synuclein | Neuronal-glial interactions | Lewy bodies | Atrophy | Axons | Progressive supranuclear palsy | Microtubules | Inclusion bodies | Dementia disorders | Paralysis | Movement disorders
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3. Full Text Stanley Fahn Lecture 2005: The staging procedure for the inclusion body pathology associated with sporadic Parkinson's disease reconsidered
by Braak, Heiko and Bohl, Jürgen R and Müller, Christian M and Rüb, Udo and de Vos, Rob A.I and Del Tredici, Kelly
Movement Disorders, ISSN 0885-3185, 12/2006, Volume 21, Issue 12, pp. 2042 - 2051
The synucleinopathy known as sporadic Parkinson's disease (PD) is a multisystem disorder that severely damages predisposed nerve cell types in circumscribed... 
aging | Lewy bodies/neurites | α‐synuclein | sporadic Parkinson's disease | staging | pathoarchitectonics | Aging | Pathoarchitectonics | Sporadic Parkinson's disease | Staging | α-synuclein | REGIONAL-DISTRIBUTION | OXIDATIVE STRESS | HUMAN BRAIN | ALZHEIMERS-DISEASE | CORTICAL LEWY BODIES | alpha-synuclein | NEURODEGENERATIVE DISEASES | CLINICAL NEUROLOGY | SLEEP BEHAVIOR DISORDER | MULTIPLE SYSTEM ATROPHY | PRECLINICAL PERIOD | ALPHA-SYNUCLEIN PATHOLOGY | Inclusion Bodies - pathology | Parkinson Disease - pathology | Animals | Parkinson Disease - physiopathology | Humans | Disease Progression
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4. 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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5. Full Text FUS pathology in basophilic inclusion body disease
by Munoz, David G and Neumann, Manuela and Kusaka, Hirofumi and Yokota, Osamu and Ishihara, Kenji and Terada, Seishi and Kuroda, Shigetoshi and MacKenzie, Ian R
Acta Neuropathologica, ISSN 0001-6322, 11/2009, Volume 118, Issue 5, pp. 617 - 627
Basophilic Inclusion Body Disease (BIBD) is a tau-negative form of frontotemporal lobar degeneration (FTLD), characterized by neuronal cytoplasmic inclusions... 
Dendritic mRNA | Pick's disease | TDP-43 | FTD | FTLD | Frontotemporal lobar degeneration | Frontotemporal dementia | PRO-ONCOPROTEIN TLS/FUS | PICKS-DISEASE | CYTOPLASMIC INCLUSIONS | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | PATHOLOGY | NEUROSCIENCES | INTRANEURONAL INCLUSIONS | CLINICAL NEUROLOGY | EXPRESSION PATTERNS | DENDRITIC SPINES | MESSENGER-RNA | Inclusion Bodies - pathology | Frontotemporal Lobar Degeneration - pathology | RNA-Binding Protein FUS - metabolism | Frontotemporal Lobar Degeneration - metabolism | Inclusion Bodies - metabolism | Humans
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6. Full Text Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
by Kim, Hong Joo and Kim, Nam Chul and Wang, Yong-Dong and Scarborough, Emily A and Moore, Jennifer and Diaz, Zamia and MacLea, Kyle S and Freibaum, Brian and Li, Songqing and Molliex, Amandine and Kanagaraj, Anderson P and Carter, Robert and Boylan, Kevin B and Wojtas, Aleksandra M and Rademakers, Rosa and Pinkus, Jack L and Greenberg, Steven A and Trojanowski, John Q and Traynor, Bryan J and Smith, Bradley N and Topp, Simon and Gkazi, Athina-Soragia and Miller, Jack and Shaw, Christopher E and Kottlors, Michael and Kirschner, Janbernd and Pestronk, Alan and Li, Yun R and Ford, Alice Flynn and Gitler, Aaron D and Benatar, Michael and King, Oliver D and Kimonis, Virginia E and Ross, Eric D and Weihl, Conrad C and Shorter, James and Taylor, J. Paul
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
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7. Full Text Cytoplasmic body pathology in severe ACTA1 -related myopathy in the absence of typical nemaline rods
by Donkervoort, Sandra and Chan, Sophelia HS and Hotchkiss, Leslie and Bradley, Nathaniel and Nguyen, David and Leach, Meganne E and Mohassel, Payam and Hu, Ying and Thangarajh, Mathula and Bharucha-Goebel, Diana and Kan, Amanda and Ho, Ronnie SL and Reyes, Christine and Nance, Jessica and Moore, Steven A and Foley, A. Reghan and Bönnemann, Carsten G
Neuromuscular Disorders, ISSN 0960-8966, 2017, Volume 27, Issue 6, pp. 531 - 536
Highlights • ACTA1 -myopathy can present with cytoplasmic bodies in the absence of nemaline rods. • p.Asn94Lys ACTA1 mutation may be linked to this pathology... 
Neurology | ACTA1 | Skeletal muscle α-actin | Congenital myopathies | Cytoplasmic bodies | Myopathies, Nemaline - genetics | Humans | Child, Preschool | Male | Muscular Diseases - pathology | Myopathies, Nemaline - pathology | Actins - genetics | Whole Exome Sequencing | Myopathies, Nemaline - complications | Pedigree | Inclusion Bodies - pathology | Muscular Diseases - complications | Muscle, Skeletal - pathology | Muscular Diseases - genetics | Mutation | Twins | Muscles | Genetic disorders | Muscle proteins | Actin
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8. Full Text Parkinson's disease and parkinsonism: Neuropathology
by Dickson, Dennis W
Cold Spring Harbor Perspectives in Medicine, ISSN 2157-1422, 2012, Volume 2, Issue 8, pp. a009258 - a009258
Parkinsonism, the clinical term for a disorder with prominent bradykinesia and variable associated extrapyramidal signs and symptoms, is accompanied by... 
MEDICINE, RESEARCH & EXPERIMENTAL | MULTIPLE SYSTEM ATROPHY | ALZHEIMERS-DISEASE | CLINICAL-DIAGNOSIS | DEMENTIA COMPLEX | ALPHA-SYNUCLEIN IMMUNOREACTIVITY | MONOCLONAL-ANTIBODIES | AMYGDALA LEWY BODIES | SUBSTANTIA-NIGRA | PROGRESSIVE SUPRANUCLEAR PALSY | CORTICOBASAL DEGENERATION | Diagnosis, Differential | Parkinson Disease - pathology | Head Injuries, Closed - pathology | Supranuclear Palsy, Progressive - pathology | Multiple System Atrophy - pathology | Neuroglia - pathology | Humans | Nerve Degeneration - pathology | Parkinsonian Disorders - pathology | Brain - pathology | Inclusion Bodies - pathology | TDP-43 Proteinopathies - pathology | Lewy Bodies - pathology
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9. Full Text p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS
by Al-Sarraj, Safa and King, Andrew and Troakes, Claire and Smith, Bradley and Maekawa, Satomi and Bodi, Istvan and Rogelj, Boris and Al-Chalabi, Ammar and Hortobágyi, Tibor and Shaw, Christopher E
Acta Neuropathologica, ISSN 0001-6322, 12/2011, Volume 122, Issue 6, pp. 691 - 702
Neuronal cytoplasmic inclusions (NCIs) containing phosphorylated TDP-43 (p-TDP-43) are the pathological hallmarks of motor neuron disease/amyotrophic lateral... 
C9 orf 72 | TDP43 | Pathology | Neurosciences | MND/ALS | Medicine & Public Health | FTLD | p62 | C9orf72 | PROGRANULIN GENE | DEMENTIA | UBIQUITIN | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | FRONTOTEMPORAL LOBAR DEGENERATION | NEUROSCIENCES | CLINICAL NEUROLOGY | DISEASE | FTD | MUTATIONS | HEXANUCLEOTIDE REPEAT | Frontotemporal Lobar Degeneration - pathology | Neurons - pathology | Pyramidal Cells - metabolism | DNA Repeat Expansion - genetics | Sequestosome-1 Protein | Humans | Middle Aged | Male | Case-Control Studies | DNA-Binding Proteins - metabolism | Aged, 80 and over | Adult | Female | C9orf72 Protein | Neurons - metabolism | Inclusion Bodies - metabolism | Purkinje Cells - metabolism | Amyotrophic Lateral Sclerosis - genetics | Cerebellum - metabolism | Hippocampus - pathology | DNA-Binding Proteins - genetics | Mutation - genetics | Cerebellum - pathology | Intranuclear Inclusion Bodies - pathology | DNA - genetics | Proteins - genetics | Hippocampus - metabolism | Amyotrophic Lateral Sclerosis - pathology | Adaptor Proteins, Signal Transducing - genetics | Inclusion Bodies - pathology | Pyramidal Cells - pathology | Aged | Frontotemporal Lobar Degeneration - genetics | Adaptor Proteins, Signal Transducing - metabolism | Purkinje Cells - pathology | Intranuclear Inclusion Bodies - metabolism | Ubiquitin | Brain | School facilities | Neurons | Amyotrophic lateral sclerosis | Universities and colleges | Education parks | Protein binding | Cerebellum | Spinal cord | Motor neuron disease | Polymerase chain reaction | Neurodegeneration | Primers | Purkinje cells | Pyramidal cells | Inclusion bodies | Mutation | Hippocampus
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10. 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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11. Full Text FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
by Neumann, Manuela and Bentmann, Eva and Dormann, Dorothee and Jawaid, Ali and DeJesus-Hernandez, Mariely and Ansorge, Olaf and Roeber, Sigrun and Kretzschmar, Hans A and Munoz, David G and Kusaka, Hirofumi and Yokota, Osamu and Ang, Lee-Cyn and Bilbao, Juan and Rademakers, Rosa and Haass, Christian and Mackenzie, Ian R. A
Brain, ISSN 0006-8950, 9/2011, Volume 134, Issue 9, pp. 2595 - 2609
Accumulation of the DNA/RNA binding protein fused in sarcoma as cytoplasmic inclusions in neurons and glial cells is the pathological hallmark of all patients... 
EWS | frontotemporal dementia | TAF15 | FUS | amyotrophic lateral sclerosis | LOCALIZATION | METHYLATION | SUBTYPES | FRONTOTEMPORAL LOBAR DEGENERATION | IDENTIFICATION | NEUROSCIENCES | CLINICAL NEUROLOGY | HETEROGENEITY | GENE | TDP-43 | FUS/TLS | TLS | Biomarkers - metabolism | Frontotemporal Lobar Degeneration - pathology | TATA-Binding Protein Associated Factors - metabolism | Amyotrophic Lateral Sclerosis - physiopathology | Amyotrophic Lateral Sclerosis - genetics | Humans | RNA-Binding Protein EWS - genetics | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | Frontotemporal Lobar Degeneration - physiopathology | RNA-Binding Protein EWS - metabolism | TATA-Binding Protein Associated Factors - genetics | Amyotrophic Lateral Sclerosis - pathology | Animals | Inclusion Bodies - pathology | Frontotemporal Lobar Degeneration - genetics | HeLa Cells | Mutation | Inclusion Bodies - metabolism | Original
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