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Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 25, pp. 10337 - 10342
Spinal muscular atrophy (SMA), caused by the deletion of the SMN1 gene, is the leading genetic cause of infant mortality. SMN protein is present at high levels... 
Axons | Motor neurons | Growth cones | Neuroscience | Messenger RNA | RNA | Neurons | Antibodies | Gene expression regulation | SMN complex proteins | Neuritin | Local protein synthesis | Embryonic lethal abnormal vision drosophila-like 4 (ELAV-L4) | LOCALIZATION | RIBONUCLEOPROTEIN | MULTIDISCIPLINARY SCIENCES | ACTIVITY-DEPENDENT EXPRESSION | IDENTIFICATION | neuritin | GROWTH CONES | TRANSPORT | DETERMINING GENE-PRODUCT | SPINAL MUSCULAR-ATROPHY | IN-VIVO | ASSOCIATION | embryonic lethal abnormal vision Drosophila-like 4 (ELAV-L4) | local protein synthesis | ELAV-Like Protein 4 | Humans | RNA, Messenger - metabolism | Zebrafish - embryology | Recombinant Fusion Proteins - metabolism | Embryo, Mammalian - anatomy & histology | Motor Neurons - cytology | Survival of Motor Neuron 1 Protein - genetics | Neuropeptides - genetics | Animals, Genetically Modified | RNA, Messenger - genetics | Cells, Cultured | ELAV Proteins - metabolism | Axons - metabolism | Neuropeptides - metabolism | Survival of Motor Neuron 1 Protein - metabolism | Nerve Tissue Proteins - genetics | GPI-Linked Proteins - metabolism | Motor Neurons - metabolism | Nerve Tissue Proteins - metabolism | Embryo, Mammalian - physiology | Animals | Axons - pathology | Recombinant Fusion Proteins - genetics | Zebrafish - physiology | Mice | ELAV Proteins - genetics | GPI-Linked Proteins - genetics | Gene mutations | Physiological aspects | Genetic aspects | Research | Health aspects | Risk factors | Spinal muscular atrophy | Proteins | Genotype & phenotype | Neuromuscular diseases | Zebrafish | Infant mortality | Ribonucleic acid--RNA | Index Medicus | Spinal cord | Translation | Cell survival | Mental disorders | Axonogenesis | Mortality | SMN protein | survival | Mass spectroscopy | Infants | Gene deletion | infant mortality | HuD protein | Pathology | RNA-binding protein | Actin | Neuromuscular junctions | spinal muscular atrophy | Axon guidance | Mass spectrometry | Biological Sciences
Journal Article
Journal Article
Development (Cambridge), ISSN 0950-1991, 2017, Volume 144, Issue 12, pp. 2175 - 2186
The major sperm protein domain (MSPd) has an extracellular signaling function implicated in amyotrophic lateral sclerosis. Secreted MSPds derived from the C.... 
Major sperm protein domain | Mitochondria | VAPA | VAPB | SMA | ALS | Amyotrophic lateral sclerosis | MSP | Striated muscle | SMN-1 | Spinal muscular atrophy | EARLY PATHOGENESIS | NERVOUS-SYSTEM | SOD1(G93A) MOUSE MODEL | DROSOPHILA-MELANOGASTER | DEVELOPMENTAL BIOLOGY | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | CAENORHABDITIS-ELEGANS | SPINAL MUSCULAR-ATROPHY | MAJOR SPERM | PROTEIN VAPB | Caenorhabditis elegans Proteins - chemistry | Humans | Mitochondria, Muscle - metabolism | Genes, Helminth | Caenorhabditis elegans Proteins - metabolism | Male | Actin-Related Protein 2-3 Complex - metabolism | RNA Interference | Larva - growth & development | Protein Domains | Receptor-Like Protein Tyrosine Phosphatases - genetics | Actin-Related Protein 2 - metabolism | Membrane Proteins - metabolism | Germ Cells - metabolism | Sarcolemma - metabolism | SMN Complex Proteins - metabolism | Caenorhabditis elegans - metabolism | Caenorhabditis elegans - growth & development | Signal Transduction | Animals, Genetically Modified | Caenorhabditis elegans - genetics | Membrane Proteins - genetics | Larva - metabolism | Receptor-Like Protein Tyrosine Phosphatases - metabolism | Motor Neurons - metabolism | SMN Complex Proteins - antagonists & inhibitors | Animals | Membrane Proteins - chemistry | Amyotrophic Lateral Sclerosis - metabolism | Muscle, Striated - growth & development | Mutation | Muscle, Striated - metabolism | SMN Complex Proteins - genetics | Caenorhabditis elegans Proteins - genetics | Tyrosine | Body wall | Cell survival | Splicing | Secretion | RNA-mediated interference | Nervous system | mRNA | Skeletal muscle | Sclerosis | Actin | Localization | Protein-tyrosine-phosphatase | Index Medicus | 209
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2008, Volume 283, Issue 9, pp. 5598 - 5610
Journal Article
Brain Research, ISSN 0006-8993, 08/2018, Volume 1693, Issue Pt A, pp. 11 - 23
Many RNA binding proteins, including FUS, contain moderately repetitive, low complexity, intrinsically disordered domains. These sequence motifs have recently... 
Amyotrophic lateral sclerosis | Cation-pi interactions | Frontotemporal dementia | Phase separation | Arginine methylation | RNA binding proteins | PRION-LIKE DOMAINS | NUCLEAR IMPORT RECEPTOR | LIQUID DROPLETS | NEUROSCIENCES | CELL-FREE FORMATION | SARCOMA FUS | LOW-COMPLEXITY DOMAINS | FUS MUTATIONS | STRESS GRANULES | NUCLEOCYTOPLASMIC TRANSPORT | Frontotemporal Dementia - genetics | Neurodegenerative Diseases - pathology | Amyotrophic Lateral Sclerosis - physiopathology | Amyotrophic Lateral Sclerosis - genetics | Humans | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | Frontotemporal Lobar Degeneration - physiopathology | Temporal Lobe - metabolism | DNA-Binding Proteins - metabolism | Cytoplasmic Granules - metabolism | Protein Domains | Protein Processing, Post-Translational | Frontotemporal Lobar Degeneration - genetics | Mutation | Biophysics - methods | RNA-Binding Proteins - metabolism | Post-translational modification | Medical research | Nervous system diseases | Neurosciences | Sarcoma | RNA | Amino acids | Physiological aspects | Medicine, Experimental | Binding proteins | Methylation | Protein binding | Dementia | PTM, post-translational modification | hnRNP, heterogeneous nuclear ribonucleoprotein | EBP homologous protein gene | karyopherin β2 | RGG, arginine glycine glycine repeat motif | TNPO1, transportin 1 | EWS, Ewing sarcoma protein | CHOP, C | QGSY, glutamine glycine serine and tyrosine repeats motif | fALS, familial amyotrophic lateral sclerosis | PY-NLS, proline tyrosine nuclear localisation signal | FUS, fused in sarcoma protein | FTLD, frontotemporal lobar degeneration | DDX4, DEAD box helicase 4 | TAF15, TATA box binding protein 15 | ADMA FUS, asymmetrically di-methylated arginine FUS | RRM, RNA recognition Motif | TDP-43, transactive response DNA binding protein 43 | SMN, survival motor neuron
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 12/2007, Volume 16, Issue 24, pp. 3149 - 3159
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2011, Volume 286, Issue 3, pp. 1976 - 1986
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2008, Volume 105, Issue 29, pp. 10045 - 10050
In vertebrates, assembly of spliceosomal uridine-rich small nuclear ribonucleoproteins (UsnRNPs) is mediated by the SMN complex, a macromolecular entity... 
Proteins | Vertebrates | RNA | Drosophila | Rigor mortis | Cell lines | Evolution | Small nuclear RNA | Small nuclear ribonucleoproteins | SMN complex proteins | Splicing | UsnRNA | Spinal muscular atrophy | SURVIVAL | PROTEIN | MULTIDISCIPLINARY SCIENCES | SNRNPS | CLASS RIBONUCLEOPROTEINS | MOTOR-NEURON | IDENTIFICATION | TRANSLATION | IN-VITRO | SPINAL MUSCULAR-ATROPHY | BIOGENESIS | spinal muscular atrophy | splicing | RNA-Binding Proteins - genetics | Cyclic AMP Response Element-Binding Protein - chemistry | Transcription Factors - chemistry | Histone Chaperones | Multiprotein Complexes | Ribonucleoproteins, Small Nuclear - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Drosophila Proteins - biosynthesis | Cell Cycle Proteins - chemistry | Drosophila melanogaster - metabolism | Spliceosomes - metabolism | Nerve Tissue Proteins - chemistry | RNA Splicing | Cell Cycle Proteins - genetics | Ribonucleoproteins, Small Nuclear - chemistry | Genome, Insect | Intracellular Signaling Peptides and Proteins - genetics | Cell Line | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | SMN Complex Proteins | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | Animals | Ribonucleoproteins, Small Nuclear - biosynthesis | Intracellular Signaling Peptides and Proteins - chemistry | Cyclic AMP Response Element-Binding Protein - metabolism | Models, Genetic | Drosophila Proteins - genetics | RNA-Binding Proteins - metabolism | Evolution, Molecular | Physiological aspects | Genetic aspects | Research | Insects | Ribonucleic acid--RNA | Bioinformatics | Genomics | Index Medicus | Biological Sciences
Journal Article
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 3/2007, Volume 176, Issue 6, pp. 831 - 841
Mutations in human survival motor neurons 1 (SMN1) cause spinal muscular atrophy (SMA) and are associated with defects in assembly of small nuclear... 
Neurons | Alleles | Antibodies | Actins | Muscles | Small nuclear RNA | Small nuclear ribonucleoproteins | Thorax | Myofibrils | Spinal muscular atrophy | SURVIVAL | SKELETAL-MUSCLE | DEFECTS | PROTEIN | WERDNIG-HOFFMANN-DISEASE | DETERMINING GENE | INNERVATION | ALPHA-B-CRYSTALLIN | ACTIN GENES | DIFFERENTIATION | CELL BIOLOGY | RNA-Binding Proteins - genetics | Drosophila melanogaster - physiology | Actins - metabolism | Nerve Tissue Proteins - analysis | Muscle, Skeletal - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Muscular Atrophy, Spinal - genetics | Drosophila Proteins - physiology | Protein Isoforms - metabolism | Cyclic AMP Response Element-Binding Protein - analysis | RNA-Binding Proteins - analysis | Actinin - metabolism | Disease Models, Animal | Muscular Atrophy, Spinal - metabolism | Nerve Tissue Proteins - physiology | Survival of Motor Neuron 1 Protein | RNA-Binding Proteins - physiology | Sarcomeres - metabolism | Drosophila Proteins - analysis | SMN Complex Proteins | Cyclic AMP Response Element-Binding Protein - physiology | Nerve Tissue Proteins - genetics | Cyclic AMP Response Element-Binding Protein - genetics | Phenotype | Animals | Myofibrils - metabolism | Drosophila Proteins - genetics | Mutation | Ribonucleoproteins, Small Nuclear - metabolism | Proteins | Musculoskeletal diseases | Insects | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2007, Volume 2, Issue 9, pp. e921 - e921
Spinal muscular atrophy (SMA) is a motor neuron disease caused by reduced levels of the survival motor neuron (SMN) protein. SMN together with Gemins2-8 and... 
MULTIDISCIPLINARY SCIENCES | RNA-Binding Proteins - genetics | Immunoprecipitation | Spinal Cord - metabolism | Humans | Ribonucleoproteins, Small Nuclear - genetics | Brain - metabolism | Muscular Atrophy, Spinal - genetics | Spliceosomes - metabolism | Kidney - metabolism | Mice, Mutant Strains | Spinal Cord - pathology | Ribonucleoproteins - genetics | DEAD Box Protein 20 | DEAD-box RNA Helicases - metabolism | Nuclear Proteins - genetics | Fibroblasts - metabolism | Cell Line | Muscular Atrophy, Spinal - metabolism | Electrophoresis, Polyacrylamide Gel | Genotype | Nuclear Proteins - metabolism | Ribonucleoproteins - metabolism | SMN Complex Proteins | Muscular Atrophy, Spinal - pathology | Nerve Tissue Proteins - genetics | Blotting, Western | Nerve Tissue Proteins - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | DEAD-box RNA Helicases - genetics | Blotting, Northern | Animals | Cyclic AMP Response Element-Binding Protein - metabolism | Fibroblasts - cytology | Mice | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Proteins | Physiological aspects | Analysis | Spinal muscular atrophy | Spinal cord | Animal models | Ribonucleoproteins (small nuclear) | Syngeneic grafts | Pathogenesis | SMN protein | Motor neuron disease | Impairment | Biochemistry | Biosynthesis | Biology | Machinery | Atrophy | Genotype & phenotype | Rodents | Animal tissues | Assembly | Age | Neurological disorders | Cell survival | Kidneys | Splicing | Introns | Macromolecules | Ribonucleoproteins | Metabolism | Pathology | Index Medicus
Journal Article