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1874, Sammlung klinischer Vorträge, Volume Nr. 23, [445]-464. --
Book
Rheumatology, ISSN 1462-0324, 10/2018, Volume 57, Issue suppl_8
Journal Article
1959, Radiodiagnostic et radio-anatomie de précision, 131
Book
The Journal of Clinical Endocrinology & Metabolism, ISSN 0021-972X, 12/2014, Volume 99, Issue 12, pp. 4408 - 4422
Journal Article
Vaccine, ISSN 0264-410X, 06/2018, Volume 36, Issue 28, pp. 4046 - 4053
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 | Pathology | Biochemistry | Adenosine triphosphatase | 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 | Index Medicus | Report
Journal Article
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 | Index Medicus
Journal Article
Journal of Bone and Mineral Research, ISSN 0884-0431, 01/2010, Volume 25, Issue 1, pp. 20 - 31
Journal Article