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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
Molecular cell, ISSN 1097-2765, 2009, Volume 36, Issue 1, pp. 39 - 50
In the largest E3 ligase subfamily, Cul3 binds a BTB domain, and an associated protein-interaction domain such as MATH recruits substrates for ubiquitination... 
PROTEINS | ACTIVATION | PROTEIN | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | KEAP1 | DIMERIZATION | BTB DOMAIN | HEDGEHOG | CELL BIOLOGY | Transcription Factors - chemistry | Humans | Crystallography, X-Ray | Drosophila Proteins - metabolism | Mutation - physiology | Protein Multimerization - physiology | Protein Structure, Quaternary - physiology | Ubiquitination - physiology | Peptide Fragments - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Nuclear Proteins - chemistry | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Cullin Proteins - chemistry | Peptide Fragments - chemistry | Phosphoprotein Phosphatases - genetics | Consensus Sequence - physiology | Recombinant Fusion Proteins - genetics | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Drosophila melanogaster | Phosphoprotein Phosphatases - chemistry | Protein Binding - physiology | Adaptor Proteins, Signal Transducing - chemistry | Histones - chemistry | Protein Interaction Domains and Motifs - physiology | Phosphoprotein Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | DNA-Binding Proteins - metabolism | Cullin Proteins - metabolism | Nuclear Proteins - genetics | Peptide Fragments - metabolism | Repressor Proteins - chemistry | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Cullin Proteins - genetics | Transcription Factors - metabolism | Animals | Histones - genetics | Adaptor Proteins, Signal Transducing - genetics | Drosophila Proteins - genetics | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin | Chromatin | Phosphatases | Ligases | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERS | PHOSPHATASES
Journal Article
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
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2012, Volume 337, Issue 6090, pp. 96 - 100
Pyruvate constitutes a critical branch point in cellular carbon metabolism. We have identified two proteins, Mpc1 and Mpc2, as essential for mitochondrial pyruvate transport in yeast, , and humans... 
Yeasts | Mitochondria | Diet | Plasmids | Drosophila | REPORTS | Amino acids | Oxidation | Respiration | Sugars | Medical schools | RAT-LIVER | TRANSPORT | COMPLEX | MECHANISM | IDENTIFICATION | MULTIDISCIPLINARY SCIENCES | Metabolomics | Humans | Molecular Sequence Data | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Anion Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - genetics | Drosophila melanogaster - metabolism | Saccharomyces cerevisiae - metabolism | Amino Acids - metabolism | Biological Transport | Mitochondrial Proteins - metabolism | Pyruvic Acid - metabolism | Amino Acid Sequence | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Oxidation-Reduction | Carbohydrate Metabolism | Mitochondria - metabolism | Drosophila Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Anion Transport Proteins - metabolism | Citric Acid Cycle | Mitochondrial Membranes - metabolism | Point Mutation | Animals | Drosophila melanogaster - chemistry | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Drosophila Proteins - genetics | Anion Transport Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Cell metabolism | Pyruvates | Chemical properties | Research | Molecular biology | Proteins | Yeast | Metabolism | Carriers | Human | Bacteria | Transport | Transporter
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
Nature cell biology, ISSN 1476-4679, 2014, Volume 17, Issue 1, pp. 68 - 80
.... We show that FAM40A negatively regulates the MST3 and MST4 kinases, which promote the co-localization of the contractile actomyosin machinery with the Ezrin/Radixin/Moesin family proteins... 
ACTIVATION | INVASION | COMPLEX | KINASE | PP2A | PROTEIN PHOSPHATASE 2A | MYOSIN PHOSPHATASE | MICROARRAY DATA | SUBUNIT | FAMILY | CELL BIOLOGY | Phosphorylation | Autoantigens - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Autoantigens - genetics | Cell Movement - genetics | Neoplasm Metastasis | RNA Interference | rho-Associated Kinases - metabolism | Apoptosis Regulatory Proteins - genetics | Cytoskeletal Proteins - metabolism | Female | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Calmodulin-Binding Proteins - genetics | Actin Cytoskeleton - metabolism | Signal Transduction | Membrane Proteins - genetics | Computational Biology | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Calmodulin-Binding Proteins - metabolism | Actomyosin - metabolism | Protein-Serine-Threonine Kinases - biosynthesis | Carrier Proteins - genetics | Protein Phosphatase 1 - metabolism | Animals | Breast Neoplasms - genetics | Carrier Proteins - metabolism | Breast Neoplasms - pathology | Protein Phosphatase 2 - metabolism | Cell Line, Tumor | RNA, Small Interfering | Drosophila melanogaster | Metastasis | Muscle proteins | Health aspects | Phosphotransferases | Analysis | Cancer cells | Cytoskeletal Proteins | Medical and Health Sciences | Medicin och hälsovetenskap | Protein-Serine-Threonine Kinases | Breast Neoplasms | Klinisk medicin | Calmodulin-Binding Proteins | Journal Article | rho-Associated Kinases | Proto-Oncogene Proteins | Protein Phosphatase 2 | Protein Phosphatase 1 | Carrier Proteins | Phosphoprotein Phosphatases | Actin Cytoskeleton | Actomyosin | Autoantigens | Membrane Proteins | Clinical Medicine | Apoptosis Regulatory Proteins | Microfilament Proteins | Research Support, Non-U.S. Gov't | Cancer and Oncology | Cell Movement | Cancer och onkologi
Journal Article
Nature (London), ISSN 1476-4687, 2004, Volume 431, Issue 7010, pp. 873 - 878
.... The complex, termed hPRC1L (human Polycomb repressive complex 1-like), is composed of several Polycomb-group proteins including Ring1, Ring2, Bmi1 and HPH2... 
CORE | RECRUITMENT | TRANSCRIPTIONAL ACTIVATION | COMPLEX | LIGASE ACTIVITY | MULTIDISCIPLINARY SCIENCES | RAD6 | H3 LYSINE-27 METHYLATION | UBIQUITYLATION | RING FINGER PROTEINS | DROSOPHILA | Nuclear Proteins - isolation & purification | Nucleosomes - chemistry | Humans | Multiprotein Complexes | Ubiquitin - metabolism | Molecular Sequence Data | Drosophila melanogaster - genetics | Promoter Regions, Genetic - genetics | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Protein Subunits - isolation & purification | Repressor Proteins - isolation & purification | Response Elements - genetics | Nuclear Proteins - genetics | Proto-Oncogene Proteins - isolation & purification | Repressor Proteins - metabolism | Protein Subunits - genetics | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Cell Line | Catalytic Domain | Repressor Proteins - chemistry | Gene Silencing | Ubiquitin-Protein Ligases - metabolism | Nucleosomes - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Proto-Oncogene Proteins - genetics | Polycomb-Group Proteins | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - isolation & purification | Ubiquitin-Protein Ligases - chemistry | DNA-Binding Proteins - chemistry | Homeodomain Proteins - genetics | Transcription Factors - metabolism | Polycomb Repressive Complex 2 | Animals | Polycomb Repressive Complex 1 | Transcription Factors - isolation & purification | Ubiquitin-Protein Ligases - isolation & purification | Protein Subunits - chemistry | Drosophila Proteins - genetics | HeLa Cells | Histones - metabolism | Ubiquitin-Protein Ligases - genetics | Proteins | Enzymes | Cell culture | Chromatin | Biochemistry
Journal Article