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Nature, ISSN 0028-0836, 03/2012, Volume 483, Issue 7389, pp. 336 - 340
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
EMBO reports, ISSN 1469-221X, 01/2010, Volume 11, Issue 1, pp. 45 - 51
Autophagy is the cellular homeostatic pathway that delivers large cytosolic materials for degradation in the lysosome. Recent evidence indicates that autophagy... 
mitophagy | Nix | LC3 | GABARAP | selective autophagy | Selective autophagy | Mitophagy | APOPTOSIS | PROTEIN | RETICULOCYTE MATURATION | UBIQUITIN | BNIP3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-DEATH | CELL BIOLOGY | STRUCTURAL BASIS | DEGRADATION | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Molecular Sequence Data | Substrate Specificity | Autophagy - physiology | Mitochondrial Proteins - genetics | Proto-Oncogene Proteins - chemistry | Mitochondrial Proteins - metabolism | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Membrane Proteins - metabolism | Binding Sites | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Blotting, Western | Amino Acid Motifs | Autophagy-Related Protein 8 Family | Animals | Membrane Proteins - chemistry | Reticulocytes - cytology | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Mice | Receptors, GABA-A - metabolism | COS Cells | Proteins | Mitochondria | Cellular biology | Cytoplasm | Index Medicus | Scientific Report
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
Cell, ISSN 0092-8674, 04/2016, Volume 165, Issue 3, pp. 643 - 655
Oncogenic activation of genes via point mutations occurs in 20%–30% of human cancers. The development of effective RAS inhibitors has been challenging,... 
rigosertib | RAS-binding domain | PI3K | MAPK | RAS | RAF | POINT MUTATIONS | BLADDER-CARCINOMA ONCOGENE | MUTANT | SELECTIVE INHIBITOR | ACTIVATION | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | KINASE | BINDING | TRANSFORMING PROPERTIES | CELL BIOLOGY | Glycine - analogs & derivatives | Phosphorylation | Humans | Molecular Sequence Data | ras Proteins - metabolism | Crystallography, X-Ray | Proto-Oncogene Proteins - chemistry | Sulfones - pharmacology | MAP Kinase Signaling System | Cell Cycle Proteins - chemistry | Pancreatic Neoplasms - drug therapy | Glycine - chemistry | Sulfones - chemistry | Nuclear Magnetic Resonance, Biomolecular | Dimerization | Glycine - administration & dosage | Protein-Serine-Threonine Kinases - metabolism | Proto-Oncogene Proteins B-raf - metabolism | Proto-Oncogene Proteins B-raf - chemistry | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | RNA-Binding Proteins - chemistry | Cell Cycle Proteins - metabolism | Models, Molecular | Sequence Alignment | Animals | Glycine - pharmacology | Signal Transduction - drug effects | Mice, Nude | Mice | Protein-Serine-Threonine Kinases - chemistry | Cell Transformation, Neoplastic - drug effects | RNA-Binding Proteins - metabolism | Sulfones - administration & dosage | Proteins | Medical colleges | Gene mutations | Protein binding | Jewish schools | Phosphotransferases | Index Medicus
Journal Article
Science, ISSN 0036-8075, 01/2014, Volume 343, Issue 6173, pp. 885 - 888
Journal Article
Science, ISSN 0036-8075, 9/2012, Volume 337, Issue 6099, pp. 1231 - 1235
The brain tumor glioblastoma multiforme (GBM) is among the most lethal forms of human cancer. Here, we report that a small subset of GBMs (3.1%; 3 of 97 tumors... 
Exons | Neurons | Genes | REPORTS | Stem cells | Aneuploidy | Chromosomes | Cells | Tumors | Daughter cells | Cancer | ANEUPLOIDY | SELECTIVE INHIBITOR | POTENT | MULTIDISCIPLINARY SCIENCES | CANCER | RECEPTOR TYROSINE KINASE | DISCOVERY | CHROMOSOMAL INSTABILITY | FAMILY | Microtubule-Associated Proteins - chemistry | Neoplasm Transplantation | Translocation, Genetic | Oncogene Proteins, Fusion - metabolism | Receptor, Fibroblast Growth Factor, Type 3 - chemistry | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Mitosis | Humans | Receptor, Fibroblast Growth Factor, Type 1 - metabolism | Receptor, Fibroblast Growth Factor, Type 3 - antagonists & inhibitors | Fetal Proteins - metabolism | Receptor, Fibroblast Growth Factor, Type 1 - genetics | Receptor, Fibroblast Growth Factor, Type 3 - metabolism | Brain Neoplasms - metabolism | Oncogene Proteins, Fusion - chemistry | Spindle Apparatus - metabolism | Glioblastoma - genetics | Oncogene Fusion | Glioblastoma - metabolism | Antineoplastic Agents - pharmacology | Benzamides - pharmacology | Nuclear Proteins - genetics | Chromosomal Instability | Pyrazoles - pharmacology | Protein Structure, Tertiary | Receptor, Fibroblast Growth Factor, Type 3 - genetics | Enzyme Inhibitors - pharmacology | Brain Neoplasms - genetics | Nuclear Proteins - metabolism | Pyrimidines - pharmacology | Nuclear Proteins - chemistry | Piperazines - pharmacology | Receptor, Fibroblast Growth Factor, Type 1 - antagonists & inhibitors | Xenograft Model Antitumor Assays | Animals | Cell Transformation, Neoplastic | Oncogene Proteins, Fusion - genetics | Fetal Proteins - genetics | Mice | Receptor, Fibroblast Growth Factor, Type 1 - chemistry | Fetal Proteins - chemistry | Physiological aspects | Development and progression | Fibroblast growth factors | Genetic aspects | Research | Health aspects | Glioblastoma multiforme | Proteins | Kinases | Brain cancer | Genomics | Pharmaceutical sciences | Index Medicus
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 307 - 319
SF3b is a heptameric protein complex of the U2 small nuclear ribonucleoprotein (snRNP) that is essential for pre-mRNA splicing. Mutations in the largest SF3b... 
crystal structure | U2AF65 | SF3b | SF3B1 | cancer-related mutations | pre-mRNA splicing | DNA-DAMAGE RECOGNITION | U2 SNRNP PROTEINS | BRANCH-SITE | UBIQUITIN LIGASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SPLICEOSOMAL COMPLEX | POLYPYRIMIDINE TRACT | BINDING | SPLICING FACTOR | PRE-MESSENGER-RNA | CELL BIOLOGY | Oncogene Proteins - genetics | Spliceosomes - chemistry | Baculoviridae - metabolism | Humans | Baculoviridae - genetics | Crystallography, X-Ray | RNA Splicing Factors - chemistry | Moths | Neoplasm Proteins - metabolism | Phosphoproteins - metabolism | Phosphoproteins - chemistry | Protein Subunits - metabolism | RNA Splicing Factors - metabolism | Spliceosomes - metabolism | RNA Splicing | Cloning, Molecular | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Binding Sites | Genes, Tumor Suppressor | Protein Subunits - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Oncogene Proteins - chemistry | Oncogene Proteins - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Recombinant Proteins - genetics | Spliceosomes - ultrastructure | Phosphoproteins - genetics | RNA Splicing Factors - genetics | Splicing Factor U2AF - genetics | Animals | Protein Conformation, beta-Strand | Protein Binding | Splicing Factor U2AF - chemistry | Protein Subunits - chemistry | HeLa Cells | Mutation | Splicing Factor U2AF - metabolism | Crosslinked polymers | RNA | Crystals | Genetic aspects | Structure | Binding proteins | Mass spectrometry | Cancer | Protein binding | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 01/2016, Volume 529, Issue 7587, pp. 541 - 545
Journal Article