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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
Journal Article
Neuron (Cambridge, Mass.), ISSN 0896-6273, 2012, Volume 75, Issue 4, pp. 618 - 632
.... We have previously demonstrated that stabilization of actin by tau is critical for neurotoxicity of the protein... 
ALZHEIMERS-DISEASE BRAIN | DOMINANT OPTIC ATROPHY | MITOCHONDRIAL-FUNCTION | MOUSE MODEL | LIGHT-CHAIN | FRONTOTEMPORAL DEMENTIA | AXONAL-TRANSPORT | NEUROSCIENCES | DYNAMIN-RELATED PROTEIN | PHOSPHORYLATION SITES | TRANSGENIC MICE | Neurons - pathology | Microtubule-Associated Proteins - genetics | Tauopathies - genetics | Cytoskeletal Proteins - genetics | Gelsolin - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Actins - metabolism | Tauopathies - pathology | Cytoplasm - metabolism | MicroRNAs - metabolism | Green Fluorescent Proteins - genetics | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | GTP-Binding Proteins - genetics | Nerve Degeneration - metabolism | Neurons - ultrastructure | tau Proteins - genetics | Cell Death - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | ATP Synthetase Complexes - metabolism | Cell Cycle Proteins - genetics | Tauopathies - complications | Cytoskeletal Proteins - metabolism | Myosins - metabolism | Cytoplasm - genetics | RNA Interference - physiology | Disease Models, Animal | In Situ Nick-End Labeling | Green Fluorescent Proteins - metabolism | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | Cell Cycle Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Mutation - genetics | Animals | GTP Phosphohydrolases - metabolism | Analysis of Variance | GTP Phosphohydrolases - genetics | Gelsolin - genetics | Mice | Drosophila Proteins - genetics | Nerve Degeneration - etiology | Voltage-Dependent Anion Channels - metabolism | GTP-Binding Proteins - metabolism | Nervous system diseases | Actin | Neurons | Utrophin | Myosin | Mitochondrial DNA | Alzheimer's disease | Proteins | Phosphorylation | Mitochondria | Neurotoxicity | Insects | Microscopy | Neurodegeneration | Pathogenesis | Morphology | Mutation | Defects | Neurodegenerative diseases | Tau protein | Cell death | Elongation
Journal Article
Journal Article
PLoS genetics, ISSN 1553-7404, 2012, Volume 8, Issue 1, p. e1002456
..., apoptosis, oxidative stress and accumulation of protein inclusions have been implicated in the etiology of the disease, mitochondrial dysfunction appears to play... 
LIFE-SPAN | OXIDATIVE STRESS | DROSOPHILA-PARKIN MUTANTS | ALTERNATIVE OXIDASE | QUINONE OXIDOREDUCTASE | NDI1 GENE | HUMAN-CELLS | INCREASED SENSITIVITY | GENETICS & HEREDITY | MITOCHONDRIAL-DYSFUNCTION | RESERVE POOL | Electron Transport Complex III - genetics | Electron Transport Complex III - metabolism | Cytoskeletal Proteins - genetics | Saccharomyces cerevisiae - genetics | Humans | Male | Drosophila Proteins - metabolism | Ciona intestinalis - genetics | Drosophila melanogaster - genetics | Electron Transport Complex I - metabolism | GTP-Binding Proteins - genetics | Electron Transport Complex IV - metabolism | Drosophila melanogaster - metabolism | Mitochondria - genetics | Electron Transport Complex I - genetics | Mitochondrial Proteins - metabolism | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Plant Proteins - metabolism | Protein-Serine-Threonine Kinases - metabolism | Oxidoreductases - metabolism | Membrane Proteins - genetics | Gene Expression Regulation | Protein-Serine-Threonine Kinases - genetics | Ubiquitin-Protein Ligases - metabolism | Mitochondria - metabolism | Electron Transport Complex IV - genetics | Parkinson Disease - genetics | Saccharomyces cerevisiae Proteins - genetics | Animals, Genetically Modified - metabolism | Animals | Animals, Genetically Modified - genetics | Saccharomyces cerevisiae Proteins - metabolism | Drosophila Proteins - genetics | Mutation | Ubiquitin-Protein Ligases - genetics | GTP-Binding Proteins - metabolism | Parkinson's disease | Physiological aspects | NADH dehydrogenase | Genetic aspects | Mitochondrial DNA | Research | Electron transport | Risk factors | Enzymes | Mitochondria | Yeast | Insects | Parkinsons disease | Genetic engineering | Grants | Experiments | Evacuations & rescues | Deoxyribonucleic acid--DNA | Defects | Deoxyribonucleic acid | DNA
Journal Article
Neuron, ISSN 0896-6273, 04/2013, Volume 78, Issue 1, pp. 65 - 80
...  Introduction Mutations in valosin-containing protein (VCP) cause a dominantly inherited, multisystem degenerative disease that affects muscle, bone... 
PATHOGENESIS | PARKIN | VALOSIN-CONTAINING-PROTEIN | INCLUSION-BODY MYOPATHY | DROSOPHILA MODEL | FRONTOTEMPORAL DEMENTIA | PAGETS-DISEASE | BONE | NEUROSCIENCES | P97 | DEGENERATION | Embryo, Mammalian | Humans | Ganglia, Spinal - cytology | Drosophila Proteins - metabolism | HSP72 Heat-Shock Proteins - genetics | Protein Tyrosine Phosphatases - genetics | Neurons - ultrastructure | Time Factors | Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology | Neuromuscular Junction - genetics | Neurons - metabolism | Protein-Serine-Threonine Kinases - metabolism | Mitochondrial Membrane Transport Proteins - metabolism | Cell Cycle Proteins - metabolism | Enzyme Inhibitors - pharmacology | Ubiquitin-Protein Ligases - metabolism | Adenosine Triphosphatases - metabolism | Mutation - genetics | Leupeptins - pharmacology | GTP Phosphohydrolases - metabolism | Luminescent Proteins - genetics | Adenosine Triphosphatases - genetics | Ubiquitin-Protein Ligases - genetics | RNA, Small Interfering - metabolism | Immunoprecipitation | Neuromuscular Junction - metabolism | Valosin Containing Protein | Mitochondria - ultrastructure | Transfection | Mitochondria - genetics | Proton Ionophores - pharmacology | Cell Cycle Proteins - genetics | Microscopy, Electron, Transmission | Animals, Genetically Modified | Gene Expression Regulation - genetics | Drosophila | RNA, Small Interfering - pharmacology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Nuclear Proteins - metabolism | Mitochondria - metabolism | Mitochondria - drug effects | Transcription Factors - genetics | Transcription Factors - metabolism | Animals | Proteins - metabolism | Drosophila Proteins - genetics | In Vitro Techniques | Ubiquitination - genetics | Luminescent Proteins - metabolism | Ubiquitin | Analysis | Genomics | Quality control | Amyotrophic lateral sclerosis | Genetic aspects | Mitochondrial DNA | Dementia | Neurons | Parkinsons disease | Biosynthesis | Digital cameras | Kinases | DNA repair | Proteins | Mitochondria | Brain research | Insects | Microscopy | Morphology | Mutation
Journal Article
EMBO reports, ISSN 1469-221X, 11/2017, Volume 18, Issue 11, pp. 2051 - 2066
Endocytic processes are facilitated by both curvature‐generating BAR‐domain proteins and the coordinated polymerization of actin filaments... 
tau | N‐BAR protein Bin1 | Alzheimer's disease | actin binding | genetic risk factor | N-BAR protein Bin1 | PROTEIN | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CROSS-LINKING | FILAMENT TURNOVER | TAU PATHOLOGY | CELL BIOLOGY | SKELETAL-MUSCLE | STRUCTURAL BASIS | SYNAPTIC VESICLE ENDOCYTOSIS | MEMBRANE CURVATURE | SH3 DOMAIN | Tauopathies - genetics | Humans | Actins - metabolism | Tauopathies - pathology | tau Proteins - metabolism | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Actins - genetics | Drosophila melanogaster - metabolism | Protein Isoforms - metabolism | tau Proteins - genetics | Tumor Suppressor Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Binding Sites | Actin Cytoskeleton - genetics | Disease Models, Animal | Recombinant Proteins - metabolism | Gene Expression | Tumor Suppressor Proteins - metabolism | Actin Cytoskeleton - metabolism | Genetic Vectors - chemistry | Gene Expression Regulation | Genetic Vectors - metabolism | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Transcription Factors - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Tauopathies - metabolism | Animals | Carrier Proteins - metabolism | Escherichia coli - genetics | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Protein Isoforms - genetics | Membranes | Neurodegenerative diseases | Drosophila | Health risks | Polymerization | Rods | Bundles | Risk factors | Membrane proteins | Bundling | Proteins | Depolymerization | Insects | Tau protein | Filaments | Neurodegeneration | Actin | Isoforms | BAR protein | Cytoskeleton | Alzheimers disease | Curvature | Neuroscience | Cell Adhesion, Polarity & Cytoskeleton
Journal Article
Current biology, ISSN 0960-9822, 2010, Volume 20, Issue 7, pp. 573 - 581
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2009, Volume 4, Issue 5, pp. e5622 - e5622
Background: The INK4/ARF locus encodes three tumor suppressor genes (p15(Ink4b), Arf and p16(Ink4a)) and is frequently inactivated in a large number of human... 
INACTIVATION | MAMMALIAN TRITHORAX | DELAYED REPLICATION | METHYLATION | DOMAIN | GROUP GENE | MULTIDISCIPLINARY SCIENCES | METHYLTRANSFERASE ACTIVITY | MLL | CELLULAR SENESCENCE | HISTONE | NIH 3T3 Cells | Myeloid-Lymphoid Leukemia Protein - metabolism | Cellular Senescence | Repressor Proteins - metabolism | Fibroblasts - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Cycle Proteins - metabolism | Gene Silencing | Cyclin-Dependent Kinase Inhibitor p16 - genetics | Nuclear Proteins - metabolism | Polycomb-Group Proteins | Enhancer of Zeste Homolog 2 Protein | Polycomb Repressive Complex 2 | Animals | Cyclin-Dependent Kinase Inhibitor p16 - chemistry | Polycomb Repressive Complex 1 | Histone-Lysine N-Methyltransferase - metabolism | Embryo, Mammalian - cytology | Models, Biological | Cyclin-Dependent Kinase Inhibitor p16 - metabolism | Protein Binding | DNA Replication Timing | Fibroblasts - cytology | Mice | Histones - metabolism | Methylation | Proteins | Epigenetic inheritance | DNA replication | Senescence | Chromatin | Genes | INK4a protein | Genomes | Recruitment | Cell growth | Transcription activation | Cell cycle | Fibroblasts | Cyclin-dependent kinase inhibitors | Dissociation | Deoxyribonucleic acid--DNA | p16 Protein | INK4 protein | Embryo fibroblasts | Gene expression | Embryos | Loci | DNA biosynthesis | Polycomb group proteins | Replication origins | Pilot projects | Insects | Stem cells | Epigenetics | Tumor suppressor genes | Replication | Embryo, Mammalian | Histone-Lysine N-Methyltransferase | Repressor Proteins | Cell Aging | Nuclear Proteins | Cyclin-Dependent Kinase Inhibitor p16 | Life Sciences | Immunology | Histones | Myeloid-Lymphoid Leukemia Protein | Proto-Oncogene Proteins | Cell Cycle Proteins | Deoxyribonucleic acid | DNA
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2002, Volume 298, Issue 5595, pp. 1039 - 1043
Journal Article