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Journal Article
Molecular Cell, ISSN 1097-2765, 2005, Volume 17, Issue 3, pp. 393 - 403
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove... 
CYTOCHROME-C | COMPLEX | SURVIVAL FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | BIM | RELEASE | PEPTIDE | CELL-DEATH | FAMILY | MEMBER | CELL BIOLOGY | Humans | Molecular Sequence Data | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | Genetic Complementation Test | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Carrier Proteins - chemistry | Proto-Oncogene Proteins c-bcl-2 - chemistry | Membrane Proteins - metabolism | Neoplasm Proteins - genetics | Peptide Fragments - genetics | Cell Survival - physiology | Binding, Competitive | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | bcl-X Protein | Peptide Fragments - metabolism | Membrane Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Proteins - genetics | Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Apoptosis Regulatory Proteins | Carrier Proteins - metabolism | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Biosensing Techniques | Ligands | Mice | Apoptosis - physiology | Proteins - chemistry | In Vitro Techniques | Proto-Oncogene Proteins c-bcl-2 - genetics | Index Medicus
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
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
BBA - Biomembranes, ISSN 0005-2736, 11/2016, Volume 1858, Issue 11, pp. 2709 - 2716
Phosphatidic acid (PA) is a crucial membrane phospholipid involved in de novo lipid synthesis and numerous intracellular signaling cascades. The signaling... 
PA target proteins | Epsin-like clathrin adaptor (ECA) | Membrane curvature stress | Type I and type II lipids | PA-binding | Phosphatidic acid | Liposome binding assays | TARGET | DIACYLGLYCEROL | PHOSPHOLIPASE-D | LIPID POLYMORPHISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | BIOPHYSICS | LYSOPHOSPHATIDIC ACID | ARABIDOPSIS | IONIZATION | HYDROGEN BOND SWITCH | MODULATION | Qb-SNARE Proteins - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - chemistry | Humans | Qb-SNARE Proteins - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Cell Membrane - chemistry | Qc-SNARE Proteins - metabolism | Proto-Oncogene Proteins c-raf - chemistry | Biological Assay | Carrier Proteins - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Cell Membrane - metabolism | Cell Membrane - drug effects | Repressor Proteins - metabolism | Lysophosphatidylcholines - pharmacology | Repressor Proteins - chemistry | Arabidopsis - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - metabolism | Recombinant Fusion Proteins - chemistry | Proto-Oncogene Proteins c-raf - metabolism | Saccharomyces cerevisiae - chemistry | Liposomes - chemistry | Carrier Proteins - metabolism | Arabidopsis Proteins - chemistry | Phosphatidic Acids - chemistry | Qc-SNARE Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Liposomes - metabolism | Phosphatidic Acids - metabolism | Phosphatidylethanolamines - metabolism | Phosphatidylethanolamines - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Arabidopsis thaliana | Chemical properties | Binding proteins | Membrane proteins | Protein binding | Plant physiology | Analysis | Phospholipids
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
The EMBO Journal, ISSN 0261-4189, 06/2011, Volume 30, Issue 12, pp. 2325 - 2335
The Hippo tumour suppressor pathway is a conserved signalling pathway that controls organ size. The core of the Hpo pathway is a kinase cascade, which in... 
hippo signalling | F‐actin | growth regulation | F-actin | TISSUE-GROWTH | BIOCHEMISTRY & MOLECULAR BIOLOGY | YORKIE PHOSPHORYLATION | TEAD/TEF FAMILY | CELL BIOLOGY | REGULATE CELL-PROLIFERATION | SIGNALING PATHWAY | GENE-EXPRESSION | CONTACT INHIBITION | SIZE-CONTROL | TUMOR-SUPPRESSOR PATHWAY | PROMOTES APOPTOSIS | Wings, Animal - cytology | Cell Proliferation | Humans | Drosophila melanogaster - genetics | Actins - genetics | Drosophila Proteins - biosynthesis | Organ Specificity - genetics | Wings, Animal - growth & development | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Actins - chemistry | RNA Caps - antagonists & inhibitors | RNA Caps - chemistry | Intracellular Signaling Peptides and Proteins - genetics | Cytoskeleton - chemistry | RNA Caps - genetics | Actins - biosynthesis | Carrier Proteins - biosynthesis | Cells, Cultured | Cytoskeleton - genetics | Drosophila melanogaster - cytology | Protein-Serine-Threonine Kinases - genetics | Signal Transduction - genetics | Drosophila Proteins - chemistry | Carrier Proteins - genetics | Phenotype | Animals | Drosophila melanogaster - chemistry | Intracellular Signaling Peptides and Proteins - chemistry | Wings, Animal - chemistry | Protein-Serine-Threonine Kinases - chemistry | Drosophila Proteins - genetics | HeLa Cells | Proteins | Signal transduction | Tumors | 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
Journal of Biological Chemistry, ISSN 0021-9258, 07/2007, Volume 282, Issue 27, pp. 20036 - 20044
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2007, Volume 104, Issue 7, pp. 2050 - 2055
Due to their small size, nanoparticles have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing... 
Nanoparticles | Exchange rates | Elution | Albumins<