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Molecular and Cellular Biology, ISSN 0270-7306, 04/2008, Volume 28, Issue 7, pp. 2426 - 2436
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
INACTIVATION | APOPTOSIS | PROTEIN | SIGNALING PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | YAP | SIZE-CONTROL | DIFFERENTIATION | DROSOPHILA | TUMOR-SUPPRESSOR PATHWAY | CELL BIOLOGY | 14-3-3 Proteins - physiology | Phosphorylation | Transferases (Other Substituted Phosphate Groups) - genetics | Humans | Receptor Protein-Tyrosine Kinases - physiology | Recombinant Fusion Proteins - physiology | Transferases (Other Substituted Phosphate Groups) - physiology | Mesoderm - cytology | Drosophila Proteins - physiology | Cell Transdifferentiation - physiology | Membrane Proteins - physiology | Cell Division | c-Mer Tyrosine Kinase | Cell Cycle Proteins - genetics | Conserved Sequence | Transcription, Genetic | Epithelial Cells - cytology | Proteins - physiology | Nerve Tissue Proteins - physiology | Transcription Factors - physiology | Membrane Proteins - genetics | Protein-Serine-Threonine Kinases - physiology | Protein-Serine-Threonine Kinases - genetics | Proto-Oncogene Proteins - genetics | Transcription Factors - genetics | Nerve Tissue Proteins - genetics | Protein Processing, Post-Translational - physiology | Amino Acid Motifs | Proteins - genetics | Receptor Protein-Tyrosine Kinases - genetics | Cell Transformation, Neoplastic | Proto-Oncogene Proteins - physiology | Cell Line, Tumor | Nuclear Proteins - physiology | Drosophila Proteins - genetics | Cell Cycle Proteins - physiology | Cell Movement | Index Medicus
Journal Article
PLoS Computational Biology, ISSN 1553-734X, 2006, Volume 2, Issue 8, pp. 0890 - 0901
Recent proteome-wide screening approaches have provided a wealth of information about interacting proteins in various organisms. To test for a potential... 
UNSTRUCTURED PROTEINS | DATABASE | RECOGNITION | PROTEOME | BIOCHEMICAL RESEARCH METHODS | MATHEMATICAL & COMPUTATIONAL BIOLOGY | INTERACTION MAP | PREDICTIONS | INTERACTION NETWORKS | GENE ONTOLOGY | SACCHAROMYCES-CEREVISIAE | BINDING | Caenorhabditis elegans - chemistry | ELAV-Like Protein 2 | Drosophila Proteins - classification | Saccharomyces cerevisiae - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | Ligases - genetics | Amino Acids - chemistry | Caenorhabditis elegans Proteins - metabolism | ELAV Proteins - classification | Ligases - chemistry | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Saccharomyces cerevisiae - metabolism | Ligases - classification | Carrier Proteins - chemistry | ELAV Proteins - chemistry | Carrier Proteins - classification | Protein Structure, Tertiary | Saccharomyces cerevisiae Proteins - classification | Caenorhabditis elegans - metabolism | Caenorhabditis elegans - genetics | Computational Biology | ELAV Proteins - metabolism | Ligases - metabolism | Models, Molecular | Drosophila Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Carrier Proteins - genetics | Caenorhabditis elegans Proteins - classification | Animals | Carrier Proteins - metabolism | Drosophila melanogaster - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Drosophila Proteins - genetics | Caenorhabditis elegans Proteins - genetics | ELAV Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Eukaryotes | Genetic aspects | Brewer's yeast | Analysis | Drosophila | Index Medicus | Caenorhabditis | Bioinformatics - Computational Biology | Saccharomyces | Homo (Human) | Molecular Biology - Structural Biology | Proteins | Confidence intervals | Genetics | Hypotheses | Organisms | Network hubs
Journal Article
Developmental Cell, ISSN 1534-5807, 02/2010, Volume 18, Issue 2, pp. 300 - 308
The Salvador (Sav)/Warts (Wts)/Hippo (Hpo) (SWH) network controls tissue growth by inhibiting cell proliferation and promoting apoptosis. The core of the... 
CELLBIO | DEVBIO | SIGNALING | APOPTOSIS | WARTS-HIPPO PATHWAY | DROSOPHILA-MELANOGASTER | GROWTH | PROTEIN-PROTEIN INTERACTIONS | CELL-PROLIFERATION | DEVELOPMENTAL BIOLOGY | DIFFERENTIATION | SPLIT-TEV | PROMOTES | AXIS SPECIFICATION | CELL BIOLOGY | Neurofibromin 2 - genetics | Protein Kinases - genetics | Cell Proliferation | Tumor Suppressor Proteins - antagonists & inhibitors | Humans | Drosophila - physiology | Drosophila Proteins - physiology | RNA Interference | Gene Expression Regulation, Developmental | Membrane Proteins - physiology | Base Sequence | Tumor Suppressor Proteins - genetics | Ovarian Follicle - physiology | Cell Cycle Proteins - genetics | Female | Ovarian Follicle - cytology | Drosophila Proteins - antagonists & inhibitors | Intracellular Signaling Peptides and Proteins - genetics | Drosophila - genetics | Signal Transduction | Animals, Genetically Modified | Membrane Proteins - genetics | Protein-Serine-Threonine Kinases - physiology | Protein-Serine-Threonine Kinases - genetics | Neurofibromin 2 - physiology | Tumor Suppressor Proteins - physiology | Phenotype | Animals | Epistasis, Genetic | Protein Kinases - physiology | Drosophila - growth & development | Drosophila Proteins - genetics | Intracellular Signaling Peptides and Proteins - physiology | Cell Cycle Proteins - physiology | Apoptosis | Proteins | Research | Oncology, Experimental | Cancer | Index Medicus | Short
Journal Article
Science, ISSN 0036-8075, 7/2012, 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... 
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 | Index Medicus | Carriers | Human | Bacteria | Transport | Transporter
Journal Article
Science, ISSN 0036-8075, 1/2004, Volume 303, Issue 5657, pp. 495 - 499
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved... 
Proteins | String theory | Drosophila | Liver | Lipids | Cell membranes | Dimers | Liposomes | Curvature | Research Article | P branes | CLATHRIN-MEDIATED ENDOCYTOSIS | ADP-RIBOSYLATION FACTORS | LYSOPHOSPHATIDIC ACID | TERMINAL DOMAIN | DROSOPHILA AMPHIPHYSIN | SYNAPTIC VESICLE ENDOCYTOSIS | MULTIDISCIPLINARY SCIENCES | ACTIN CYTOSKELETON | GTPASE-ACTIVATING PROTEIN | BINDING | SH3 DOMAIN | Cytoskeletal Proteins | Coated Vesicles - metabolism | Drosophila - chemistry | Molecular Sequence Data | Crystallography, X-Ray | GTPase-Activating Proteins - metabolism | Drosophila Proteins - metabolism | Phosphoproteins - metabolism | Clathrin-Coated Vesicles - metabolism | Phosphoproteins - chemistry | Cell Membrane - chemistry | Coated Vesicles - chemistry | Nerve Tissue Proteins - chemistry | Carrier Proteins - chemistry | Cell Membrane - metabolism | ADP-Ribosylation Factors - metabolism | ADP-Ribosylation Factors - genetics | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | COP-Coated Vesicles - metabolism | Models, Molecular | Nuclear Proteins - metabolism | Drosophila Proteins - chemistry | GTPase-Activating Proteins - chemistry | Nuclear Proteins - chemistry | Nerve Tissue Proteins - genetics | Clathrin - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | ADP-Ribosylation Factors - chemistry | Adaptor Proteins, Signal Transducing | Liposomes - chemistry | Animals | Carrier Proteins - metabolism | Protein Binding | Liposomes - metabolism | Mutation | Synapses | Chemical properties | Membranes | Yeast | Cellular biology | Cells | BAR domains | amphiphysin | endophilins | nadrins | Index Medicus
Journal Article
Developmental Cell, ISSN 1534-5807, 2009, Volume 16, Issue 3, pp. 411 - 420
The Hippo kinase pathway plays a central role in growth regulation and tumor suppression from flies to man. The Hippo/Mst kinase phosphorylates and activates... 
SIGNALING | ORGAN SIZE CONTROL | SIGNALING PATHWAY | GROWTH | CONTACT INHIBITION | PROLIFERATION | DEVELOPMENTAL BIOLOGY | CELL-CYCLE EXIT | TEAD/TEF FAMILY | DROSOPHILA | TUMOR-SUPPRESSOR PATHWAY | PROMOTES APOPTOSIS | CELL BIOLOGY | Protein Kinases - metabolism | Sequence Deletion | Protein Kinases - genetics | Cytoplasm - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Drosophila Proteins - metabolism | Transfection | Trans-Activators - genetics | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Drosophila - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Cell Line | Signal Transduction | Animals, Genetically Modified | Membrane Proteins - genetics | Protein-Serine-Threonine Kinases - genetics | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Recombinant Proteins - genetics | Drosophila Proteins - chemistry | Amino Acid Motifs | Animals | Membrane Proteins - chemistry | Models, Biological | Protein Binding | Trans-Activators - metabolism | Drosophila - metabolism | Drosophila Proteins - genetics | Genetic aspects | Genetic transcription | Binding proteins | Mass spectrometry | Cells | Chromatography | Protein binding | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2009, 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 | E3 LIGASE | OXIDATIVE STRESS | PROTEIN SPOP | NRF2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCF | ADAPTER | DEGRADATION | BTB DOMAIN | F-BOX | TRANSCRIPTION FACTOR | 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 | Index Medicus | CHROMATIN | BASIC BIOLOGICAL SCIENCES | SUBSTRATES | FLEXIBILITY | GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE | LIGASES | DIMERIZATION | DIMERS | PHOSPHATASES
Journal Article
Cell, ISSN 0092-8674, 03/2007, Volume 128, Issue 6, pp. 1063 - 1076
Methylation of histones has been regarded as a stable modification defining the epigenetic program of the cell, which regulates chromatin structure and... 
DOMAIN-CONTAINING PROTEINS | METHYLATION | CAENORHABDITIS-ELEGANS | METHYLTRANSFERASE | GENE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCAPES X-INACTIVATION | TRITHORAX | RETINOBLASTOMA-BINDING PROTEIN-2 | TRANSCRIPTIONAL REGULATION | CELL BIOLOGY | Caenorhabditis elegans Proteins - chemistry | Humans | Intracellular Signaling Peptides and Proteins - metabolism | Phylogeny | Gene Deletion | Tumor Suppressor Proteins - chemistry | Oxidoreductases, N-Demethylating - metabolism | Intracellular Signaling Peptides and Proteins - genetics | Repressor Proteins - metabolism | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Repressor Proteins - genetics | Caenorhabditis elegans - embryology | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Histone Demethylases | Lysine | Drosophila melanogaster - enzymology | Schizosaccharomyces - enzymology | Mice | Histones - metabolism | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Embryonic Stem Cells - metabolism | Oxidoreductases, N-Demethylating - genetics | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | DNA-Binding Proteins - metabolism | Tumor Suppressor Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | Genes, Homeobox | Protein Structure, Tertiary | Repressor Proteins - chemistry | Embryonic Stem Cells - enzymology | Nuclear Proteins - metabolism | DNA-Binding Proteins - genetics | Oxidoreductases, N-Demethylating - chemistry | Proteins - genetics | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Retinoblastoma-Binding Protein 2 | Proteins - chemistry | Methylation | Jumonji Domain-Containing Histone Demethylases | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 10/2004, Volume 431, Issue 7010, pp. 873 - 878
Covalent modification of histones is important in regulating chromatin dynamics and transcription. One example of such modification is ubiquitination, which... 
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 | Index Medicus
Journal Article
Neuron, ISSN 0896-6273, 08/2012, Volume 75, Issue 4, pp. 618 - 632
Mitochondrial abnormalities have been documented in Alzheimer’s disease and related neurodegenerative disorders, but the causal relationship between... 
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 | Index Medicus | Neurodegenerative diseases | Tau protein | Cell death | Elongation
Journal Article