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Molecular Cell, ISSN 1097-2765, 09/2016, Volume 63, Issue 5, pp. 781 - 795
Mutations in the human autophagy gene cause the multisystem disorder Vici syndrome. Here we demonstrated that EPG5 is a Rab7 effector that determines the... 
RAB effector | LC3 | autophagosome maturation | epg-5 | SNARE | MEMBRANE-FUSION | LYSOSOME FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MACHINERY | MECHANISMS | SYNTAXIN 17 | MATURATION | VESICLE | C. ELEGANS | HOPS COMPLEX | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cataract - pathology | Qb-SNARE Proteins - metabolism | R-SNARE Proteins - metabolism | Caenorhabditis elegans Proteins - metabolism | Qb-SNARE Proteins - genetics | rab GTP-Binding Proteins - genetics | Endosomes - metabolism | Lysosomes - metabolism | Qc-SNARE Proteins - metabolism | Agenesis of Corpus Callosum - genetics | Endosomes - ultrastructure | Qa-SNARE Proteins - genetics | Autophagy - genetics | Synaptosomal-Associated Protein 25 - genetics | rab GTP-Binding Proteins - metabolism | Agenesis of Corpus Callosum - metabolism | Amino Acid Sequence | Caenorhabditis elegans - metabolism | Membrane Fusion | Signal Transduction | Caenorhabditis elegans - genetics | R-SNARE Proteins - genetics | Gene Expression Regulation | Autophagosomes - metabolism | Cataract - metabolism | Agenesis of Corpus Callosum - pathology | Autophagosomes - ultrastructure | Lysosomes - ultrastructure | Proteins - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Proteins - metabolism | Qa-SNARE Proteins - metabolism | Protein Binding | Qc-SNARE Proteins - genetics | Cataract - genetics | Synaptosomal-Associated Protein 25 - metabolism | HeLa Cells | Caenorhabditis elegans Proteins - genetics | Yuan (China) | Index Medicus
Journal Article
The EMBO Journal, ISSN 0261-4189, 01/2010, Volume 29, Issue 1, pp. 41 - 54
Journal Article
Molecular Cell, ISSN 1097-2765, 2009, Volume 35, Issue 5, pp. 563 - 573
The target of rapamycin complex 1 (TORC1) is a central regulator of eukaryotic cell growth that is activated by a variety of hormones (e.g., insulin) and... 
CELLBIO | PROTEINS | SIGNALING | YEAST SACCHAROMYCES-CEREVISIAE | CELL-GROWTH CONTROL | SIGNALING PATHWAYS | FUNCTIONAL HOMOLOG | RAG GTPASES | VACUOLE FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMINO-ACID PERMEASE | COMPONENT | GTP-BINDING PROTEINS | GAP1 PERMEASE | CELL BIOLOGY | Vacuoles - enzymology | Intracellular Membranes - enzymology | Saccharomyces cerevisiae - genetics | Multiprotein Complexes | Adaptor Proteins, Vesicular Transport - genetics | Saccharomyces cerevisiae - drug effects | Guanosine Triphosphate - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Vacuoles - drug effects | DNA-Binding Proteins - metabolism | Amino Acids - metabolism | Time Factors | Guanine Nucleotide Exchange Factors - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Guanosine Diphosphate - metabolism | Protein Synthesis Inhibitors - pharmacology | Protein-Serine-Threonine Kinases - metabolism | Guanine Nucleotide Exchange Factors - genetics | Signal Transduction | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Monomeric GTP-Binding Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Amino Acid Transport Systems - metabolism | Sirolimus - pharmacology | Cycloheximide - pharmacology | Protein Transport | Transcription Factors - metabolism | Monomeric GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Endosomes - enzymology | Intracellular Membranes - drug effects | Mutation | Saccharomyces cerevisiae - growth & development | Proteins | Purines | Amino acids | Gross domestic product | Guanosine | Index Medicus
Journal Article
Nature Medicine, ISSN 1078-8956, 09/2017, Volume 23, Issue 9, pp. 1055 - 1062
Bromodomain and extraterminal domain (BET) protein inhibitors are emerging as promising anticancer therapies. The gene encoding the E3 ubiquitin ligase... 
SELECTIVE-INHIBITION | TARGET | MEDICINE, RESEARCH & EXPERIMENTAL | ANDROGEN RECEPTOR | STEM-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACUTE MYELOID-LEUKEMIA | ENHANCERS | CELL BIOLOGY | RNA-SEQ | BROMODOMAIN INHIBITION | MUTATIONS | BRD4 | Prostatic Neoplasms - metabolism | Immunoprecipitation | TOR Serine-Threonine Kinases - metabolism | Humans | Drug Resistance, Neoplasm | Male | Gene Expression Profiling | Molecular Targeted Therapy | Mechanistic Target of Rapamycin Complex 1 | Transcription Factors - drug effects | Multiprotein Complexes - metabolism | Prostatic Neoplasms - genetics | Proteasome Endopeptidase Complex - drug effects | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Nuclear Proteins - drug effects | Nuclear Proteins - genetics | Proto-Oncogene Proteins c-akt - metabolism | TOR Serine-Threonine Kinases - drug effects | Multiprotein Complexes - drug effects | Prostatic Neoplasms - drug therapy | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | RNA-Binding Proteins - antagonists & inhibitors | Triazoles - therapeutic use | Cell Survival | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Azepines - therapeutic use | RNA-Binding Proteins - drug effects | Azepines - pharmacology | Transcription Factors - metabolism | Triazoles - pharmacology | Nuclear Proteins - antagonists & inhibitors | Protein-Serine-Threonine Kinases - drug effects | Cell Line, Tumor | Cell Proliferation - drug effects | Mutation | RNA-Binding Proteins - metabolism | rac1 GTP-Binding Protein - metabolism | Proto-Oncogene Proteins c-akt - drug effects | rac1 GTP-Binding Protein - genetics | Gene mutations | Physiological aspects | Genetic aspects | Research | Drug resistance | Drug therapy | Prostate cancer | Ubiquitin | Inhibitor drugs | Stabilization | AKT protein | Activation | Biosynthesis | Degradation | Proteins | Ubiquitination | Transcription activation | Bioindicators | Ubiquitin-protein ligase | Binding | Rac1 protein | Tumor cell lines | Gene expression | Cholesterol | Mutants | Inhibitors | Proteasomes | Biomarkers | Bet protein | Prostate | Cancer | Guanosinetriphosphatase | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 03/2017, Volume 543, Issue 7645, pp. 438 - 442
The mechanistic target of rapamycin complex 1 (mTORC1) is a central regulator of cell growth that responds to diverse environmental signals and is deregulated... 
ENCEPHALOPATHY | COMPLEX | SZT2 | RAG GTPASES | GENE | SIGNALING PATHWAY | AMINO-ACIDS | MULTIDISCIPLINARY SCIENCES | TUMOR-SUPPRESSOR | MUTATIONS | FOCAL EPILEPSIES | Lysosomes | Physiological aspects | Protein research | Research | Biological control systems | Protein-protein interactions | Proteins | Amino acids | Phosphorylation | Mutation | Glucose | Molecular weight | Index Medicus
Journal Article
2004, Molecular biology intelligence unit, ISBN 9780306479922, 235
Book
eLife, ISSN 2050-084X, 2014, Volume 3, pp. e01612 - e01612
Damaged mitochondria can be selectively eliminated by mitophagy. Although two gene products mutated in Parkinson's disease, PINK1, and Parkin have been found... 
Fis1 | rab7 | autophagy | TBC1D15 | Drp1 | Parkin | PARKIN | FIS1 | RECRUITMENT | GTPASE-ACTIVATING PROTEINS | MEMBRANE | PEROXISOMAL FISSION | P62/SQSTM1 | BIOLOGY | DEGRADATION | MAMMALIAN-CELLS | SELECTIVE AUTOPHAGY | Mitochondria - enzymology | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Protein Multimerization | rab GTP-Binding Proteins - genetics | Mitochondrial Proteins - genetics | GTPase-Activating Proteins - metabolism | Autophagy | Microtubules - metabolism | Ubiquitination | Lysosomes - metabolism | Transfection | Time Factors | Mitochondrial Proteins - metabolism | HEK293 Cells | Lysosomes - pathology | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Microfilament Proteins - genetics | rab GTP-Binding Proteins - metabolism | Signal Transduction | Membrane Proteins - genetics | HCT116 Cells | Ubiquitin-Protein Ligases - metabolism | Mitochondria - pathology | Mitochondrial Degradation | Autophagy-Related Protein 8 Family | Adaptor Proteins, Signal Transducing - genetics | Protein Binding | GTPase-Activating Proteins - genetics | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin-Protein Ligases - genetics | Membranes | Yeast | Cloning | Glycerol | Mammals | Morphogenesis | Proteins | Mitochondria | GTPase-activating protein | Microscopy | PTEN-induced putative kinase | Morphology | Parkin protein | GABARAP protein | Guanosinetriphosphatase | 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
Science, ISSN 0036-8075, 1/2009, Volume 323, Issue 5911, pp. 269 - 272
The Vibrio parahaemolyticus type III effector VopS is implicated in cell rounding and the collapse of the actin cytoskeleton by inhibiting Rho guanosine... 
Proteins | Phosphates | Enzymes | HeLa cells | Amino acids | Ions | Mass spectroscopy | Reports | Infections | Biochemistry | Post translational modification | ACTIVATION | PROTEIN | PARAHAEMOLYTICUS | MULTIDISCIPLINARY SCIENCES | III SECRETION SYSTEM | Phosphorylation | Threonine - chemistry | rho GTP-Binding Proteins - antagonists & inhibitors | Humans | Bacterial Proteins - chemistry | Molecular Sequence Data | rac GTP-Binding Proteins - metabolism | Vibrio parahaemolyticus - metabolism | cdc42 GTP-Binding Protein - metabolism | Threonine - metabolism | Recombinant Fusion Proteins - metabolism | rac GTP-Binding Proteins - antagonists & inhibitors | Cell Shape | cdc42 GTP-Binding Protein - antagonists & inhibitors | rho GTP-Binding Proteins - chemistry | Binding Sites | Protein Structure, Tertiary | Amino Acid Sequence | Signal Transduction | Adenosine Monophosphate - metabolism | Bacterial Proteins - genetics | Mutant Proteins - metabolism | Vibrio parahaemolyticus - pathogenicity | Amino Acid Motifs | Mutant Proteins - chemistry | rho GTP-Binding Proteins - metabolism | rac GTP-Binding Proteins - chemistry | Bacterial Proteins - metabolism | cdc42 GTP-Binding Protein - chemistry | Protein Processing, Post-Translational | HeLa Cells | Genetic aspects | Chemical properties | Guanosine triphosphatase | Vibrio | Signal transduction | Eukaryotes | Cellular biology | Molecular biology | Binding sites | Index Medicus
Journal Article
2000, Receptor biochemistry and methodology, ISBN 0471252697, xii, 301
Book
2005, 1. Aufl., Contemporary clinical neuroscience, ISBN 1588293653, xv, 412 p., [4] p. of plates
A comprehensive survey of the many recent advances in the field of G protein-coupled receptors (GPCR). The authors describe the current knowledge of GPCR... 
Medicine | G proteins | Handbooks, manuals, etc | Receptors | Neurosciences | Biomedicine
Book
Nature Cell Biology, ISSN 1465-7392, 03/2012, Volume 14, Issue 3, pp. 311 - 317
Mitotic spindle positioning by cortical pulling forces(1) defines the cell division axis and location(2), which is critical for proper cell division and... 
ACTIVATION | PROTEIN | MECHANISM | KINETOCHORE | IMPORTIN-BETA | MITOTIC SPINDLE | SEGREGATION | ASYMMETRIC CELL-DIVISION | GRADIENT | RAN | CELL BIOLOGY | NIH 3T3 Cells | ran GTP-Binding Protein - genetics | Microtubule-Associated Proteins - genetics | Antigens, Nuclear - metabolism | Microtubule-Associated Proteins - metabolism | Humans | Molecular Sequence Data | Green Fluorescent Proteins - genetics | Intracellular Signaling Peptides and Proteins - metabolism | Centrioles - physiology | Spindle Apparatus - metabolism | RNA Interference | Cell Cycle Proteins - genetics | Chromosome Segregation - physiology | Spindle Apparatus - physiology | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Cytoplasmic Dyneins - metabolism | Dyneins - metabolism | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Green Fluorescent Proteins - metabolism | Cell Cycle Proteins - metabolism | Cytoplasmic Dyneins - genetics | Protein-Serine-Threonine Kinases - genetics | Dynactin Complex | Nuclear Matrix-Associated Proteins - metabolism | Proto-Oncogene Proteins - genetics | ran GTP-Binding Protein - metabolism | Blotting, Western | Animals | Antigens, Nuclear - genetics | Mitosis - physiology | Nuclear Matrix-Associated Proteins - genetics | Models, Biological | Protein Binding | Signal Transduction - physiology | Mice | Centrioles - metabolism | Dyneins - genetics | HeLa Cells | Microscopy, Fluorescence | Spindle (Cell division) | Physiological aspects | Cell division | Research | Chromosomes | Dynein | Index Medicus
Journal Article