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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 | Index Medicus
Journal Article
Neuron, ISSN 0896-6273, 2005, Volume 47, Issue 6, pp. 817 - 831
The molecular mechanisms controlling the differentiation of neural progenitors into distinct subtypes of neurons during neocortical development are unknown.... 
AREA IDENTITY | NEOCORTICAL NEURONS | CELL FATE SPECIFICATION | CEREBRAL CORTICAL DEVELOPMENT | LAYER NEURONS | CENTRAL-NERVOUS-SYSTEM | SUBCORTICAL TARGETS | ZINC-FINGER GENE | SUBVENTRICULAR ZONE | NEUROSCIENCES | ZEBRAFISH FOREBRAIN | Membrane Glycoproteins - metabolism | Embryo, Mammalian | Homeodomain Proteins - metabolism | Nerve Tissue Proteins - deficiency | S100 Proteins - genetics | POU Domain Factors - genetics | Forkhead Transcription Factors - metabolism | In Situ Hybridization - methods | Repressor Proteins - metabolism | Gene Expression Regulation, Developmental - physiology | POU Domain Factors - metabolism | Animals, Newborn | DNA-Binding Proteins - physiology | Motor Neurons - physiology | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cell Cycle Proteins - metabolism | S100 Proteins - metabolism | In Situ Nick-End Labeling - methods | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Immunohistochemistry - methods | Annexin A2 - genetics | Cell Death - physiology | Green Fluorescent Proteins - biosynthesis | Mice | Annexin A2 - metabolism | Age Factors | Phosphopyruvate Hydratase - metabolism | Cell Movement - physiology | DNA-Binding Proteins - deficiency | DNA-Binding Proteins - metabolism | Amino Acids - metabolism | Motor Neurons - cytology | Tumor Suppressor Proteins - genetics | Cell Cycle Proteins - genetics | Membrane Proteins - metabolism | Bromodeoxyuridine - metabolism | Cell Differentiation - physiology | Pyramidal Tracts - physiology | Nerve Tissue Proteins - physiology | Neocortex - growth & development | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Dopamine and cAMP-Regulated Phosphoprotein 32 - metabolism | Nerve Tissue Proteins - genetics | Homeodomain Proteins - genetics | Membrane Glycoproteins - genetics | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Cell Count - methods | Neocortex - cytology | Receptors, Antigen, T-Cell, alpha-beta - metabolism | Neurosciences | Neurons | Developmental biology | Stem cells | Studies | Brain | Ultrasonic imaging | Transcription factors | Hybridization | Neurogenesis | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 04/2010, Volume 38, Issue 1, pp. 89 - 100
Heat shock proteins 70 (Hsp70) represent a ubiquitous and conserved family of molecular chaperones involved in a plethora of cellular processes. The dynamics... 
PROTEINS | ALLOSTERIC REGULATION | INTERDOMAIN COMMUNICATION | PRECURSOR PROTEINS | SUBSTRATE-BINDING | STRUCTURAL BASIS | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROBABILITY-DISTRIBUTION ANALYSIS | RESONANCE ENERGY-TRANSFER | PROTEIN IMPORT MOTOR | SACCHAROMYCES-CEREVISIAE | CELL BIOLOGY | Calcium-Transporting ATPases - chemistry | Molecular Chaperones - metabolism | Humans | Bacterial Proteins - chemistry | Adenosine Diphosphate - chemistry | Molecular Chaperones - chemistry | Adenosine Triphosphate - metabolism | Fluorescence Resonance Energy Transfer | Calcium-Transporting ATPases - metabolism | HSP70 Heat-Shock Proteins - chemistry | Membrane Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - metabolism | Bacterial Proteins - genetics | Models, Molecular | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Mitochondria - metabolism | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Membrane Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Protein Conformation | Adenosine Diphosphate - metabolism | Adenosine Triphosphate - chemistry | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Hydrolysis | Analysis | Physiological aspects | Fluorescence | Heat shock proteins | Nucleotides | Index Medicus
Journal Article
eLife, ISSN 2050-084X, 08/2014, Volume 3, Issue 2014, pp. 1 - 17
The Cdc45/Mcm2-7/GINS ( CMG) helicase separates DNA strands during replication in eukaryotes. How the CMG is assembled and engages DNA substrates remains... 
replication fork | DNA replication | helicase | motor proteins | AAA+ ATPase | Mcm2-7 | MCM2-7 HELICASE | HEXAMERIC HELICASE | MINICHROMOSOME MAINTENANCE PROTEIN | ARCHAEAL MCM | BUDDING YEAST | STRUCTURAL BASIS | BIOLOGY | REPLICATIVE HELICASE | ELECTRON-MICROSCOPY | 26S PROTEASOME | CRYO-EM STRUCTURE | Minichromosome Maintenance Proteins - metabolism | Protein Multimerization | Eukaryotic Cells - metabolism | Drosophila Proteins - metabolism | Minichromosome Maintenance Proteins - chemistry | Protein Subunits - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Drosophila melanogaster - metabolism | Multiprotein Complexes - metabolism | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Repressor Proteins - metabolism | Protein Structure, Tertiary | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | DNA, Single-Stranded - metabolism | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | RNA Splicing Factors | Adenosine Triphosphatases - metabolism | Models, Molecular | DNA Replication | DNA - metabolism | Drosophila Proteins - chemistry | Microscopy, Electron | DNA-Binding Proteins - chemistry | Adenosine Triphosphate - analogs & derivatives | DNA, Single-Stranded - chemistry | Multiprotein Complexes - ultrastructure | DNA - chemistry | Multiprotein Complexes - chemistry | Animals | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Subunits - chemistry | Adenosine Triphosphate - chemistry | Chromosomal Proteins, Non-Histone - chemistry | RNA-Binding Proteins - metabolism | Medical research | Single-stranded DNA | Hexamers | Electron microscopy | DNA biosynthesis | DNA helicase | Handedness | Microscopy | Insects | Cdc45 protein | Cell cycle | Polarity | Dimerization | Deoxyribonucleic acid--DNA | Adenosine triphosphatase | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2015, Volume 290, Issue 28, pp. 17367 - 17379
The microtubule-associated protein, TPX2, regulates the activity of the mitotic kinesin, Eg5, but the mechanism of regulation is not established. Using total... 
LOCALIZATION | PROTEIN | DYNEIN | KINESIN MOTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | AURORA-A ACTIVATION | MITOTIC SPINDLE | DIRECTIONAL MOTILITY | MAMMALIAN-CELLS | CROSS-LINKS | PROMOTES | Microtubule-Associated Proteins - chemistry | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Green Fluorescent Proteins - genetics | Molecular Motor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Cell Cycle Proteins - chemistry | LLC-PK1 Cells | Microtubules - metabolism | Swine | Protein Structure, Quaternary | Cell Cycle Proteins - genetics | Kinesin - genetics | Molecular Motor Proteins - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Peptide Fragments - genetics | Green Fluorescent Proteins - metabolism | Peptide Fragments - metabolism | Cell Cycle Proteins - metabolism | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Molecular Motor Proteins - chemistry | Nuclear Proteins - chemistry | Kinesin - chemistry | Kinesin - metabolism | Peptide Fragments - chemistry | Animals | Models, Biological | Protein Binding | Recombinant Fusion Proteins - genetics | Microscopy, Fluorescence | Index Medicus | microtubule | microtubule-associated protein (MAP) | TPX2 | Eg5 | kinesin | mitosis | spindle | Cell Biology | mitotic spindle
Journal Article
The EMBO Journal, ISSN 0261-4189, 03/2013, Volume 32, Issue 6, pp. 886 - 898
The mitochondrial presequence translocase interacts with presequence‐containing precursors at the intermembrane space (IMS) side of the inner membrane to... 
import | mitochondria | presequence | TIM23 complex | CONTACT SITES | MATRIX | INNER MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | PREPROTEIN TRANSLOCASES | MITOCHONDRIAL TIM23 COMPLEX | CELL BIOLOGY | TIM50 | STRUCTURAL BASIS | MOLECULAR MACHINES | MOTOR | Protein Sorting Signals - physiology | Protein Interaction Domains and Motifs - physiology | Saccharomyces cerevisiae - genetics | Substrate Specificity | Membrane Transport Proteins - physiology | Mitochondrial Membrane Transport Proteins - genetics | Saccharomyces cerevisiae - metabolism | Mitochondrial Membrane Transport Proteins - physiology | Membrane Transport Proteins - genetics | Protein Interaction Domains and Motifs - genetics | Membrane Transport Proteins - metabolism | Membrane Proteins - metabolism | Binding Sites | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Protein Structure, Secondary | Membrane Proteins - genetics | Models, Molecular | Saccharomyces cerevisiae Proteins - genetics | Protein Transport - genetics | Membrane Transport Proteins - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Membrane Proteins - chemistry | Protein Sorting Signals - genetics | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae Proteins - physiology | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Signal transduction | Membranes | Index Medicus
Journal Article
Science, ISSN 0036-8075, 9/2001, Volume 293, Issue 5536, pp. 1829 - 1832
Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is... 
T lymphocytes | Messenger RNA | HEK293 cells | Spleen cells | CDNA libraries | Cell lines | Cellulose nitrate | Antibodies | Reports | Family members | Apoptosis | APOPTOSIS | DYNEIN | INTEGRINS | MULTIDISCIPLINARY SCIENCES | LIGHT-CHAIN | BIM | PURIFICATION | BCL-2 FAMILY | CELL-DEATH | MEMBER | Humans | Molecular Sequence Data | RNA, Messenger - analysis | Gene Expression Profiling | Neoplasm Proteins - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Transfection | Bcl-2-Like Protein 11 | Carrier Proteins - chemistry | Molecular Motor Proteins - metabolism | Proto-Oncogene Proteins c-bcl-2 - chemistry | Proto-Oncogene Proteins | Neoplasm Proteins - genetics | Dyneins | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Drosophila Proteins | RNA, Messenger - genetics | Calmodulin-Binding Proteins - metabolism | Myosin Type V | Protein Transport | Membrane Proteins | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Two-Hybrid System Techniques | Adaptor Proteins, Signal Transducing | Animals | Apoptosis Regulatory Proteins | Carrier Proteins - metabolism | Myeloid Cell Leukemia Sequence 1 Protein | Cytoskeleton - metabolism | Protein Binding | Anoikis | Mice | Mutation | Proto-Oncogene Proteins c-bcl-2 - genetics | Proteins | Genetic research | Genetic aspects | Analysis | Cellular biology | Cells | Index Medicus
Journal Article
Acta Neuropathologica, ISSN 0001-6322, 11/2012, Volume 124, Issue 5, pp. 733 - 747
While the pathogenesis of amyotrophic lateral sclerosis (ALS) remains to be clearly delineated, there is mounting evidence that altered RNA metabolism is a... 
Pathology | Neurosciences | Ubiquitination | Medicine & Public Health | Amyotrophic lateral sclerosis | Superoxide dismutase | RGNEF | C9orf72 | RNA binding proteins | HEXANUCLEOTIDE REPEAT EXPANSION | GENE-MUTATIONS | INCLUSIONS | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | FRONTOTEMPORAL LOBAR DEGENERATION | LENGTH POLYGLUTAMINE EXPANSIONS | NEUROSCIENCES | CLINICAL NEUROLOGY | MESSENGER-RNA | PATHOLOGICAL TDP-43 | EXPRESSION | SOD1 MUTATIONS | Superoxide Dismutase - genetics | Immunoprecipitation | Membrane Glycoproteins - metabolism | Organic Chemicals | Sequestosome-1 Protein | Humans | Male | Transcription Factor TFIIIA - metabolism | DNA-Binding Proteins - metabolism | Guanine Nucleotide Exchange Factors - metabolism | Spinal Cord - pathology | Female | C9orf72 Protein | Superoxide Dismutase - metabolism | Peripherins | Gene Expression Regulation - genetics | Amyotrophic Lateral Sclerosis - genetics | RNA-Binding Protein FUS - genetics | RNA-Binding Protein FUS - metabolism | DNA-Binding Proteins - genetics | Mutation - genetics | Motor Neurons - metabolism | Nerve Tissue Proteins - metabolism | Proteins - genetics | Microscopy, Confocal | Amyotrophic Lateral Sclerosis - pathology | Proteins - metabolism | Amyotrophic Lateral Sclerosis - classification | Superoxide Dismutase-1 | Adaptor Proteins, Signal Transducing - metabolism | Neurofilament Proteins - metabolism | Intermediate Filament Proteins - metabolism | RNA-Binding Proteins - metabolism | Immunohistochemistry | Ubiquitin | RNA | Neurons | Chemical properties | Binding proteins | Intermediate filament proteins | Protein binding | Index Medicus | Motor neurons | Antibodies | Colorimetry | Nucleotides | Metabolism | FUS protein | RNA-binding protein | Inclusion bodies | Neurofilaments | Peripherin | Mutation
Journal Article
Journal of Cell Science, ISSN 0021-9533, 02/2012, Volume 125, Issue 3, pp. 614 - 624
The Drosophila melanogaster MICAL protein is essential for the neuronal growth cone machinery that functions through plexin- and semaphorin-mediated axonal... 
Actin-rich protrusions | MICAL2 | Reactive oxygen species | Actin | Microfilaments | MICAL1 | CYTOSKELETON | AXON GUIDANCE | FLAVOPROTEIN MONOOXYGENASES | DROSOPHILA | SEMAPHORINS | CELL BIOLOGY | MOTOR | RHO | EXPRESSION | Adaptor Proteins, Signal Transducing - chemistry | Oxidoreductases - antagonists & inhibitors | RNA, Small Interfering - genetics | Reactive Oxygen Species - metabolism | Cytoskeletal Proteins - antagonists & inhibitors | Cytoskeletal Proteins - genetics | Humans | Actin Cytoskeleton - chemistry | DNA Primers - genetics | LIM Domain Proteins - metabolism | Oxidoreductases - chemistry | DNA-Binding Proteins - metabolism | Adaptor Proteins, Signal Transducing - antagonists & inhibitors | Base Sequence | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Protein Interaction Domains and Motifs | Microfilament Proteins - genetics | LIM Domain Proteins - chemistry | Cell Line | Microfilament Proteins - chemistry | Actin Cytoskeleton - metabolism | Oxidoreductases - metabolism | Signal Transduction | Oxidoreductases - genetics | LIM Domain Proteins - antagonists & inhibitors | Axons - metabolism | Semaphorins - metabolism | Cytoskeletal Proteins - chemistry | Cell Adhesion Molecules - metabolism | Nerve Tissue Proteins - metabolism | Animals | Microfilament Proteins - antagonists & inhibitors | Adaptor Proteins, Signal Transducing - genetics | LIM Domain Proteins - genetics | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Index Medicus
Journal Article
PLoS Genetics, ISSN 1553-7390, 12/2016, Volume 12, Issue 12, pp. e1006531 - e1006531
Safeguarding the proteome is central to the health of the cell. In multi-cellular organisms, the composition of the proteome, and by extension, protein-folding... 
MYOD HOMOLOG HLH-1 | PROTEIN-QUALITY CONTROL | BODY-WALL MUSCLE | GENETICS & HEREDITY | MOLECULAR CHAPERONE | MUSCULAR-DYSTROPHY | C-ELEGANS | MISFOLDED PROTEINS | UNC-45 CHAPERONE | J-DOMAIN PROTEIN | FUNCTIONAL SPECIFICITY | Molecular Chaperones - metabolism | Caenorhabditis elegans Proteins - metabolism | Heat-Shock Proteins - biosynthesis | DNA-Binding Proteins - metabolism | Cell Differentiation - genetics | Heat-Shock Proteins - genetics | Gene Expression Regulation, Developmental | HSP90 Heat-Shock Proteins - genetics | Binding Sites | Molecular Chaperones - biosynthesis | Promoter Regions, Genetic | HSP40 Heat-Shock Proteins - metabolism | Caenorhabditis elegans - growth & development | HSP40 Heat-Shock Proteins - genetics | Myogenic Regulatory Factors - genetics | Caenorhabditis elegans - genetics | Embryonic Development - genetics | Molecular Chaperones - genetics | Muscle Cells - metabolism | Myogenic Regulatory Factors - metabolism | DNA-Binding Proteins - genetics | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Animals | HSP90 Heat-Shock Proteins - metabolism | Muscle Development - genetics | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans Proteins - biosynthesis | Biotechnology | Immunoglobulins | Transcription factors | Young adults | Funding | Genes | Colleges & universities | Experiments | Embryos | Proteins | Life sciences | Bioinformatics | Age | Index Medicus
Journal Article