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PLoS ONE, ISSN 1932-6203, 04/2015, Volume 10, Issue 4, p. e0122888
Mutations in the valosin containing protein (VCP) gene cause hereditary Inclusion body myopathy (hIBM) associated with Paget disease of bone (PD B),... 
MAMMALIAN TARGET | LIFE-SPAN | INCLUSION-BODY MYOPATHY | MULTIDISCIPLINARY SCIENCES | FRONTOTEMPORAL DEMENTIA | VCP MUTATIONS | MOUSE MODEL | MUSCULAR-DYSTROPHY | BONE | PAGET-DISEASE | FAMILY | TOR Serine-Threonine Kinases - metabolism | Apoptosis - drug effects | Humans | Peptides - genetics | Ubiquitin - metabolism | Osteitis Deformans - metabolism | Male | Muscle, Skeletal - metabolism | Autophagy - drug effects | DNA-Binding Proteins - metabolism | Frontotemporal Dementia - metabolism | Chloroquine - pharmacology | Myoblasts - drug effects | Myoblasts - metabolism | Peptides - metabolism | Myoblasts - cytology | Disease Models, Animal | Frontotemporal Dementia - pathology | Cell Line | Sirolimus - pharmacology | Gene Knock-In Techniques | Osteitis Deformans - pathology | Animals | Eye Proteins - metabolism | Signal Transduction - drug effects | Mice | Muscle, Skeletal - pathology | Ubiquitin | Rapamycin | Analysis | Protein binding | TOR protein | Drugs | Chloroquine | Disorders | Lysosomes | Kinases | Accumulation | Defects | Signal transduction | DNA-binding protein | Rodents | Inclusion bodies | Dementia disorders | Heart diseases | Deoxyribonucleic acid--DNA | Cardiac muscle | Muscles | Amyotrophic lateral sclerosis | Substrate inhibition | Pharmacology | Patients | Substrates | Myoblasts | Pathology | Signaling | Inhibitors | Quadriceps muscle | Mutation | Frontotemporal dementia | Vacuoles | Phagocytosis | Myopathy | Deoxyribonucleic acid | DNA
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
Journal Article
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 10, p. e13183
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
Molecular cytogenetics, ISSN 1755-8166, 2014, Volume 7, Issue Suppl 1 Proceedings of the International Conference on Human, p. I34
Journal Article
Molecular cytogenetics, ISSN 1755-8166, 2014, Volume 7, Issue Suppl 1 Proceedings of the International Conference on Human, pp. I39 - I39
Journal Article
PLOS ONE, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, p. e0176919
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, p. e0131995
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2013, Volume 8, Issue 10, p. e76187
Journal Article
Journal Article