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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
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 12/2009, Volume 187, Issue 6, pp. 875 - 888
Mutations in valosin-containing protein (VCP) cause inclusion body myopathy (IBM), Paget's disease of the bone, and frontotemporal dementia (IBMPFD). Patient... 
Proteins | Muscular diseases | Transgenic animals | Inclusion bodies | Cell nucleus | Cell lines | Muscles | Small interfering RNA | Frontotemporal dementia | Skeletal muscle | GENE-MUTATIONS | NEURODEGENERATIVE DISEASE | SKELETAL-MUSCLE | IN-VITRO | AAA ATPASE CDC48/P97 | DEMENTIA | INCLUSION-BODY MYOPATHY | TDP-43 ACCUMULATION | FRONTOTEMPORAL LOBAR DEGENERATION | PAGET-DISEASE | CELL BIOLOGY | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Chloroquine | Humans | Valosin Containing Protein | Ubiquitin - metabolism | Recombinant Fusion Proteins - metabolism | Case-Control Studies | Osteitis Deformans - genetics | Osteitis Deformans - chemically induced | DNA-Binding Proteins - metabolism | Myositis, Inclusion Body - enzymology | Transfection | Quadriceps Muscle - enzymology | RNA Interference | Cell Cycle Proteins - genetics | Myositis, Inclusion Body - pathology | Female | Autophagy - genetics | Quadriceps Muscle - pathology | Disease Models, Animal | Frontotemporal Dementia - pathology | Frontotemporal Dementia - genetics | Cell Line | Heat-Shock Proteins - metabolism | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Mice, Transgenic | Myositis, Inclusion Body - genetics | Osteitis Deformans - enzymology | Osteitis Deformans - pathology | Animals | Biopsy | Frontotemporal Dementia - chemically induced | Frontotemporal Dementia - enzymology | Myositis, Inclusion Body - chemically induced | Adenosine Triphosphatases - genetics | Mice | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Autophagy (Cytology) | Gene mutations | Genetic aspects | Research | Binding proteins | Health aspects | Risk factors | Brain diseases | Index Medicus
Journal Article
Neuron, ISSN 0896-6273, 04/2013, Volume 78, Issue 1, pp. 57 - 64
Valosin-containing protein (VCP) is a highly expressed member of the type II AAA+ ATPase family. mutations are the cause of inclusion body myopathy, Paget’s... 
LIPID-PEROXIDATION | SPINAL-CORD PATHOLOGY | MOUSE MODEL | ALS | AMYOTROPHIC-LATERAL-SCLEROSIS | DYSFUNCTION | BONE | NEUROSCIENCES | PAGET-DISEASE | TRANSGENIC MICE | REVEALS | RNA, Small Interfering - genetics | Humans | Middle Aged | Male | Frontotemporal Dementia - metabolism | Neurons - ultrastructure | Muscular Dystrophies, Limb-Girdle - genetics | Adenosine Triphosphate - metabolism | Membrane Potential, Mitochondrial - genetics | Muscular Dystrophies, Limb-Girdle - pathology | NAD - metabolism | Fibroblasts - metabolism | Animals, Newborn | Frontotemporal Dementia - genetics | Magnesium - metabolism | Mitochondria - pathology | Fibroblasts - pathology | Mutation - genetics | Myositis, Inclusion Body - genetics | Osteitis Deformans - pathology | Muscular Dystrophies, Limb-Girdle - metabolism | Analysis of Variance | Luminescent Proteins - genetics | Adenosine Triphosphatases - genetics | Mice | Lipid Peroxidation - genetics | RNA, Small Interfering - metabolism | Valosin Containing Protein | Osteitis Deformans - metabolism | Family Health | Cerebral Cortex - cytology | Case-Control Studies | Osteitis Deformans - genetics | Transfection | Mitochondria - genetics | Cell Cycle Proteins - genetics | Myositis, Inclusion Body - pathology | Adult | Female | Neuroblastoma - pathology | Frontotemporal Dementia - pathology | Adenosine Triphosphatases - deficiency | Mice, Inbred C57BL | Cells, Cultured | Cell Cycle Proteins - deficiency | Mitochondria - metabolism | Animals | Oxygen Consumption - genetics | Myositis, Inclusion Body - metabolism | Aged | Nervous system diseases | Neurosciences | Genes | Amyotrophic lateral sclerosis | Genetic aspects | Adenosine triphosphatase | Dementia | Proteins | Medical research | Phosphorylation | Biomedical research | Disease | Rodents | Respiration | Experiments | Patients | Report
Journal Article
Journal Article
Nature Reviews Endocrinology, ISSN 1759-5029, 11/2015, Volume 11, Issue 11, pp. 662 - 671
Journal Article
Journal of Neuropathology and Experimental Neurology, ISSN 0022-3069, 02/2007, Volume 66, Issue 2, pp. 152 - 157
Journal Article
Autophagy, ISSN 1554-8627, 02/2010, Volume 6, Issue 2, pp. 217 - 227
VCP (VCP/p97) is a ubiquitously expressed member of the AAA + -ATPase family of chaperone-like proteins that regulates numerous cellular processes including... 
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | ERAD | Ubiquitin | IBMPFD | VCP | Autophagy | p97 | CLEARANCE | COMPLEX | autophagy | ENDOPLASMIC-RETICULUM STRESS | MYOPATHY | ubiquitin | PAGET-DISEASE | HDAC6 | CELL BIOLOGY | AAA-ATPASE | DEGRADATION | PROTEASOME SYSTEM
Journal Article
Journal Article
Journal Article