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1. Full Text Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins
by Ratti, Antonia and Buratti, Emanuele
Journal of Neurochemistry, ISSN 0022-3042, 08/2016, Volume 138, Issue S1, pp. 95 - 111
The multiple roles played by RNA binding proteins in neurodegeneration have become apparent following the discovery of TAR DNA binding protein 43 kDa (TDP‐43)... 
ALS | FUS/TLS | TDP‐43 | protein aggregation | FTLD | RNA binding proteins | Protein aggregation | TDP-43 | MICROTUBULE-ASSOCIATED-PROTEIN | MOLECULAR-WEIGHT TAU | BIOCHEMISTRY & MOLECULAR BIOLOGY | NEURONAL CELL-DEATH | FRONTOTEMPORAL LOBAR DEGENERATION | MULTIPLE-SYSTEM TAUOPATHY | NEUROSCIENCES | TRANSGENIC ZEBRAFISH MODEL | NEUROFIBRILLARY TANGLE FORMATION | TAU PROMOTES NEURODEGENERATION | PAIRED HELICAL FILAMENT | PROGRESSIVE SUPRANUCLEAR PALSY | Frontotemporal Dementia - genetics | Frontotemporal Dementia - physiopathology | DNA-Binding Proteins - physiology | TDP-43 Proteinopathies - genetics | Amyotrophic Lateral Sclerosis - physiopathology | Frontotemporal Lobar Degeneration - metabolism | Amyotrophic Lateral Sclerosis - genetics | Humans | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - physiology | TDP-43 Proteinopathies - pathology | DNA-Binding Proteins - genetics | Physiological aspects | Genetic transcription | RNA | Binding proteins | Dementia | Protein binding
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2. Full Text Domain Architectures and Characterization of an RNA-binding Protein, TLS
by Yuko Iko and Takashi S. Kodama and Nobuyuki Kasai and Takuji Oyama and Eugene H. Morita and Takanori Muto and Mika Okumura and Ritsuko Fujii and Toru Takumi and Shin-ichi Tate and Kosuke Morikawa
Journal of Biological Chemistry, ISSN 0021-9258, 10/2004, Volume 279, Issue 43, pp. 44834 - 44840
Translocated in liposarcoma (TLS) is an important protein component of the heterogeneous nuclear ribonucleoprotein complex involved in the splicing of pre-mRNA... 
RECOGNITION | STRUCTURAL BASIS | CRYSTAL-STRUCTURE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | SECONDARY STRUCTURE | HNRNP A1 | POLYMERASE-II | ONCOGENIC TRANSFORMATION | SPLICING FACTOR TLS | ZINC-FINGER DOMAIN | Protein Structure, Tertiary | Amino Acid Sequence | Zinc Fingers | Magnetic Resonance Spectroscopy | Glutathione Transferase - metabolism | Models, Molecular | Molecular Sequence Data | Cytoplasm - metabolism | RNA-Binding Protein FUS - metabolism | Cysteine - chemistry | RNA - chemistry | RNA-Binding Protein FUS - chemistry | Sequence Homology, Amino Acid | Spectrophotometry, Atomic | Chymotrypsin - pharmacology | Cell Nucleus - metabolism | Protein Binding | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Proteins - chemistry | Circular Dichroism | DNA, Complementary - metabolism
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3. Full Text The RNA Binding Protein TLS Is Translocated to Dendritic Spines by mGluR5 Activation and Regulates Spine Morphology
by Fujii, Ritsuko and Okabe, Shigeo and Urushido, Tomoe and Inoue, Kiyoshi and Yoshimura, Atsushi and Tachibana, Taro and Nishikawa, Toru and Hicks, Geoffrey G and Takumi, Toru
Current Biology, ISSN 0960-9822, 03/2005, Volume 15, Issue 6, pp. 587 - 593
Neuronal dendrites, together with dendritic spines, exhibit enormously diverse structure [ ]. Selective targeting and local translation of mRNAs in dendritic... 
LOCALIZATION | METABOTROPIC GLUTAMATE-RECEPTOR | TRANSPORT | MESSENGER-RNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE-C | MICE | TRANSLATION | STAUFEN | PLASTICITY | Immunohistochemistry | Green Fluorescent Proteins | Fluorescence Recovery After Photobleaching | Actins - metabolism | Cells, Cultured | Neurons - cytology | Protein Transport - physiology | Dendritic Spines - metabolism | RNA-Binding Protein FUS - metabolism | RNA, Messenger - metabolism | Hippocampus - metabolism | Microscopy, Confocal | Receptors, Kainic Acid - metabolism | Microtubules - metabolism | Animals | Mice | Neurons - metabolism | Messenger RNA | Evolutionary biology | Actin | Neurons | Chemical properties | Universities and colleges | Muscle proteins | Protein binding
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4. Full Text RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells
by Hiroshi Doi and Kazumasa Okamura and Peter O. Bauer and Yoshiaki Furukawa and Hideaki Shimizu and Masaru Kurosawa and Yoko Machida and Haruko Miyazaki and Kenichi Mitsui and Yoshiyuki Kuroiwa and Nobuyuki Nukina
Journal of Biological Chemistry, ISSN 0021-9258, 03/2008, Volume 283, Issue 10, pp. 6489 - 6500
Formation of intracellular aggregates is the hallmark of polyglutamine (polyQ) diseases. We analyzed the components of purified nuclear polyQ aggregates by... 
DENDRITIC SPINES | IN-VITRO | DISEASE TRANSGENIC MICE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE MODEL | STRIATAL SPINY NEURONS | INTRANUCLEAR INCLUSIONS | POLYMERASE-II | N-TERMINAL HUNTINGTIN | CASPASE ACTIVATION | CELLULAR TOXICITY | Immunohistochemistry | Neurons - pathology | Exons | Humans | Huntington Disease - pathology | Neurons - cytology | Brain - metabolism | Peptides - metabolism | Nuclear Proteins - genetics | Disease Models, Animal | Cell Line | Intranuclear Inclusion Bodies - genetics | RNA-Binding Protein FUS - genetics | Mice, Transgenic | Nuclear Proteins - metabolism | RNA-Binding Protein FUS - metabolism | Huntington Disease - metabolism | Nerve Tissue Proteins - genetics | Intranuclear Inclusion Bodies - pathology | Nerve Tissue Proteins - metabolism | Huntingtin Protein | Animals | Brain - pathology | Huntington Disease - genetics | Mice | Intranuclear Inclusion Bodies - metabolism
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5. Full Text Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs
by Lagier-Tourenne, Clotilde and Polymenidou, Magdalini and Hutt, Kasey R and Vu, Anthony Q and Baughn, Michael and Huelga, Stephanie C and Clutario, Kevin M and Ling, Shuo-Chien and Liang, Tiffany Y and Mazur, Curt and Wancewicz, Edward and Kim, Aneeza S and Watt, Andy and Freier, Sue and Hicks, Geoffrey G and Donohue, John Paul and Shiue, Lily and Bennett, C Frank and Ravits, John and Cleveland, Don W and Yeo, Gene W
Nature Neuroscience, ISSN 1097-6256, 11/2012, Volume 15, Issue 11, pp. 1488 - 1497
FUS/TLS (fused in sarcoma/translocated in liposarcoma) and TDP-43 are integrally involved in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia.... 
NEURODEGENERATIVE DISEASE | GENE | AMYOTROPHIC-LATERAL-SCLEROSIS | FAMILY PROTEINS | FUS PATHOLOGY | MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | BINDING | NEUROSCIENCES | BRAIN | NASCENT TRANSCRIPTION | RNA, Small Interfering - genetics | Protein Binding - genetics | Oligonucleotide Array Sequence Analysis | Humans | tau Proteins - metabolism | Gene Expression Profiling | RNA, Messenger - metabolism | Kv Channel-Interacting Proteins - metabolism | Brain - metabolism | Frontotemporal Dementia - metabolism | RNA Splicing - genetics | Frontotemporal Dementia - genetics | RNA-Binding Protein FUS - deficiency | Amyotrophic Lateral Sclerosis - genetics | Cell Cycle Proteins - metabolism | Ubiquitin-Protein Ligases - metabolism | RNA-Binding Protein FUS - genetics | Mice, Knockout | Motor Neurons - metabolism | Amyotrophic Lateral Sclerosis - pathology | Shal Potassium Channels - metabolism | Brain - pathology | Mice | Neurofilament Proteins - metabolism | RNA, Small Interfering - metabolism | Immunoprecipitation | Spinal Cord - metabolism | DNA-Binding Proteins - deficiency | DNA-Binding Proteins - metabolism | tau Proteins - genetics | Cell Cycle Proteins - genetics | Female | RNA Precursors - metabolism | Excitatory Amino Acid Transporter 2 - genetics | Membrane Proteins - metabolism | Frontotemporal Dementia - pathology | Gene Expression Regulation - genetics | Mice, Inbred C57BL | RNA, Messenger - genetics | RNA Precursors - genetics | Protein Structure, Tertiary - genetics | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | Excitatory Amino Acid Transporter 2 - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Histone-Lysine N-Methyltransferase - metabolism | Amyotrophic Lateral Sclerosis - metabolism | Neural Cell Adhesion Molecules - metabolism | Neural Stem Cells - metabolism | Cell Line, Transformed | Amyotrophic lateral sclerosis | Development and progression | Genetic aspects | Messenger RNA | Health aspects
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6. Full Text Acceleration of TDP43 and FUS/TLS protein expressions in the preconditioned hippocampus following repeated transient ischemia
by Sun, Miao and Yamashita, Toru and Shang, Jingwei and Liu, Ning and Deguchi, Kentaro and Liu, Wentao and Ikeda, Yoshio and Feng, Juan and Abe, Koji
Journal of Neuroscience Research, ISSN 0360-4012, 01/2014, Volume 92, Issue 1, pp. 54 - 63
The 43‐kDa transactivation response DNA binding protein (TDP43), fused in sarcoma/translocated in liposarcoma (FUS/TLS), heat shock protein 70 (HSP70), and... 
TDP43 | ischemic preconditioning | FUS/TLS | HSP70 | neuroprotection | Neuroprotection | Ischemic preconditioning | PRO-ONCOPROTEIN TLS/FUS | GERBIL HIPPOCAMPUS | FUS | AMYOTROPHIC-LATERAL-SCLEROSIS | FRONTOTEMPORAL LOBAR DEGENERATION | NEUROSCIENCES | DELAYED NEURONAL DEATH | RNA-BINDING PROTEIN | MESSENGER-RNA | RAT HEAT-SHOCK-PROTEIN-70 | TLS | CENTRAL-NERVOUS-SYSTEM | CEREBRAL-ISCHEMIA | Neurons - pathology | Ischemic Preconditioning | Male | HSP72 Heat-Shock Proteins - metabolism | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - metabolism | CA1 Region, Hippocampal - pathology | Animals | Gerbillinae | Time Factors | CA1 Region, Hippocampal - metabolism | Neurons - metabolism | Ischemic Attack, Transient - metabolism | Ischemic Attack, Transient - pathology | Heat shock proteins | Brain | Ischemia | Amyloid beta-protein | Protein binding | Alzheimer's disease
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7. Full Text Regulation of Telomere Length by G-Quadruplex Telomere DNA- and TERRA-Binding Protein TLS/FUS
by Takahama, Kentaro and Takada, Asami and Tada, Shota and Shimizu, Mai and Sayama, Kazutoshi and Kurokawa, Riki and Oyoshi, Takanori
Chemistry & Biology, ISSN 1074-5521, 03/2013, Volume 20, Issue 3, pp. 341 - 350
Mammalian telomeres comprise noncoding TTAGGG repeats in double-stranded regions with a single-stranded TTAGGG repeat 3′ overhang and are bound by a... 
EWINGS-SARCOMA | COMPLEX | REPEAT-CONTAINING RNA | MAMMALIAN TELOMERES | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | HETEROCHROMATIN | TLS | INTRAMOLECULAR G-QUADRUPLEX | PROMOTER | K+ SOLUTION | Protein Structure, Tertiary | Amino Acid Sequence | Humans | Molecular Sequence Data | RNA-Binding Protein FUS - metabolism | DNA - metabolism | RNA - genetics | RNA-Binding Protein FUS - chemistry | DNA - chemistry | Telomere Shortening | Repetitive Sequences, Nucleic Acid | G-Quadruplexes | HeLa Cells | Histones - metabolism | Methylation | RNA - metabolism | Telomere - genetics | Genetic research | Antisense RNA | Glycine | DNA | Protein binding
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8. Full Text Molecular determinants and genetic modifiers of aggregation and toxicity for the als disease protein fus/tls
by Sun, Zhihui and Diaz, Zamia and Fang, Xiaodong and Hart, Michael P and Chesi, Alessandra and Shorter, James and Gitler, Aaron D
PLoS Biology, ISSN 1544-9173, 04/2011, Volume 9, Issue 4, p. e1000614
TDP-43 and FUS are RNA-binding proteins that form cytoplasmic inclusions in some forms of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar... 
NEURODEGENERATIVE DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOLOGY | TARDBP MUTATIONS | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | ALPHA-SYNUCLEIN | FUS MUTATIONS | FRONTOTEMPORAL LOBAR DEGENERATION | SACCHAROMYCES-CEREVISIAE | STRESS GRANULES | RNA-BINDING PROTEIN | Frontotemporal Lobar Degeneration - pathology | Neurons - pathology | Gene Expression | Saccharomyces cerevisiae - genetics | Amyotrophic Lateral Sclerosis - genetics | DNA-Binding Proteins - toxicity | Humans | Computational Biology | RNA-Binding Protein FUS - genetics | Cytoplasm - metabolism | Chromosome Mapping | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Amyotrophic Lateral Sclerosis - pathology | Transfection | Base Sequence | Gene Deletion | RNA-Binding Protein FUS - toxicity | HEK293 Cells | Frontotemporal Lobar Degeneration - genetics | Proteins | Amyotrophic lateral sclerosis | Toxicity | Genes
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9. Full Text A protein–protein interaction of stress‐responsive myosin VI endowed to inhibit neural progenitor self‐replication with RNA binding protein, TLS, in murine hippocampus
by Takarada, Takeshi and Tamaki, Keisuke and Takumi, Toru and Ogura, Masato and Ito, Yuma and Nakamichi, Noritaka and Yoneda, Yukio
Journal of Neurochemistry, ISSN 0022-3042, 09/2009, Volume 110, Issue 5, pp. 1457 - 1468
We have shown preferential expression of both mRNA and corresponding protein for myosin VI (Myo6) in the murine hippocampus within 24 h after the extreme... 
neural progenitors | translocated in liposarcoma | myosin VI | hippocampus | P19 cells | post‐traumatic stress disorder | Myosin VI | Translocated in liposarcoma | Neural progenitors | Hippocampus | Post-traumatic stress disorder | CELLS | post-traumatic stress disorder | BIOCHEMISTRY & MOLECULAR BIOLOGY | D-ASPARTATE RECEPTORS | AMYOTROPHIC-LATERAL-SCLEROSIS | NEUROSCIENCES | DENDRITIC SPINES | MOUSE HIPPOCAMPUS | MEDIATED ENDOCYTOSIS | NEURONS | GAMMA-AMINOBUTYRIC-ACID | DENTATE GYRUS | TRAUMATIC STRESS | Stress, Physiological - physiology | Rats, Wistar | Protein Interaction Domains and Motifs - physiology | Cells, Cultured | Rats | Mice, Transgenic | Neurons - cytology | Stem Cells - cytology | Hippocampus - cytology | Stem Cells - metabolism | Myosin Heavy Chains - metabolism | Hippocampus - metabolism | Animals | Neurogenesis - physiology | Myosin Heavy Chains - physiology | Cell Line, Tumor | Growth Inhibitors - physiology | RNA-Binding Protein FUS - physiology | Mice | Neurons - metabolism | Cell Differentiation - physiology | Brain | Messenger RNA | Neurons | Analysis | Myosin | Biological apparatus and supplies | Universities and colleges | Chemical properties | Muscle proteins | Protein binding | Proteins | Neurology | Biochemistry | Ribonucleic acid--RNA | Binding sites
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