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Nature Biotechnology, ISSN 1087-0156, 06/2002, Volume 20, Issue 6, pp. 619 - 622
Journal Article
American Journal of Physiology - Cell Physiology, ISSN 0363-6143, 06/2009, Volume 296, Issue 6, pp. 1258 - 1270
Myostatin is a negative regulator of skeletal muscle size, previously shown to inhibit muscle cell differentiation. Myostatin requires both Smad2 and Smad3... 
MAFbx | Mammalian target of rapamycin complex signaling | MuRF1 | S6 kinase | Smad signaling | Human skeletal muscle cells | Transducer of regulated Ca | responsive element-binding protein activity | MuRF-1 | Atrogin | Transforming growth factor-β-like molecules | IGF-I | PHYSIOLOGY | ATROPHY | RAPID DISUSE | human skeletal muscle cells | transforming growth factor-beta-like molecules | SKELETAL-MUSCLE HYPERTROPHY | FOXO TRANSCRIPTION FACTORS | UBIQUITIN LIGASES | transducer of regulated Ca2+-responsive element-binding protein activity | CELL BIOLOGY | atrogin | PATHWAY | GROWTH | GENE-EXPRESSION | mammalian target of rapamycin complex signaling | CONDITIONAL ACTIVATION | Activin Receptors, Type I - antagonists & inhibitors | Protein Kinases - metabolism | Phosphorylation | Protein Kinases - genetics | Humans | Smad3 Protein - metabolism | Muscle Fibers, Skeletal - drug effects | Tripartite Motif Proteins | Smad3 Protein - genetics | Transfection | RNA Interference | Myoblasts, Skeletal - pathology | Smad2 Protein - genetics | Muscle Proteins - metabolism | Dioxoles - pharmacology | Regulatory-Associated Protein of mTOR | Benzamides - pharmacology | Myostatin - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Rapamycin-Insensitive Companion of mTOR Protein | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Signal Transduction | Cell Size - drug effects | Cells, Cultured | Smad2 Protein - metabolism | Ubiquitin-Protein Ligases - metabolism | Organ Size | Activin Receptors, Type I - metabolism | Myoblasts, Skeletal - enzymology | SKP Cullin F-Box Protein Ligases - metabolism | Mice, SCID | Myostatin - antagonists & inhibitors | Adaptor Proteins, Signal Transducing | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Cell Differentiation - drug effects | Follistatin - pharmacology | Muscle Fibers, Skeletal - pathology | Creatine Kinase - metabolism | Mice | Protein Kinase Inhibitors - pharmacology | TOR Serine-Threonine Kinases | Myoblasts, Skeletal - drug effects | Insulin-Like Growth Factor I - metabolism | Muscle Fibers, Skeletal - enzymology | RNA, Small Interfering - metabolism | Abdominal surgery | Musculoskeletal system | Signal transduction | Cell growth | Kinases | Gene expression | Cells | Index Medicus
Journal Article
PLoS ONE, ISSN 1932-6203, 2010, Volume 5, Issue 11, pp. e15394 - e15394
Autophagy is a highly orchestrated intracellular bulk degradation process that is activated by various environmental stresses. The serine/threonine kinase... 
COMPLEX | ACTIVATED PROTEIN-KINASE | METABOLISM | PHOSPHORYLATION | MACHINERY | BIOLOGY | INHIBITS CELL-GROWTH | INDUCTION | SACCHAROMYCES-CEREVISIAE | ATG13 | DEGENERATION | AMP-Activated Protein Kinases - metabolism | Phosphorylation | Immunoprecipitation | Humans | Multiprotein Complexes | Immunoblotting | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | Protein Subunits - metabolism | Autophagy-Related Protein-1 Homolog | Mechanistic Target of Rapamycin Complex 1 | Transfection | RNA Interference | HEK293 Cells | Regulatory-Associated Protein of mTOR | Binding Sites | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Protein Subunits - genetics | Cell Line | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Mice, Knockout | 14-3-3 Proteins - metabolism | Proteins - genetics | Animals | Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Cell Line, Tumor | Protein Binding | Mice | TOR Serine-Threonine Kinases | Mutation | Adaptor Proteins, Signal Transducing - metabolism | AMP-Activated Protein Kinases - genetics | Microscopy, Fluorescence | TOR protein | Yeast | Homology | Kinases | Inactivation | Proteins | Cell growth | Cell cycle | Binding | Biodegradation | Deactivation | Threonine | Pharmacology | Metabolism | Mammals | Environmental stress | Medicine | TSC2 protein | 14-3-3 protein | Insects | Environmental degradation | Protein-serine/threonine kinase | Regulation | Phagocytosis | Cancer | Apoptosis | 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
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 8, pp. e23367 - e23367
Background: Recent studies have demonstrated that activation of autophagy increases the lifespan of organisms from yeast to flies. In contrast to the lifespan... 
LIFE-SPAN EXTENSION | PATHOGENESIS | OXIDATIVE STRESS | INHIBITION | DISRUPTION | MULTIDISCIPLINARY SCIENCES | GENES | RESISTANCE | MITOCHONDRIAL DYSFUNCTION | SUPPRESSION | CELL BIOLOGY | Reactive Oxygen Species - metabolism | TOR Serine-Threonine Kinases - metabolism | Sequestosome-1 Protein | Humans | Cellular Senescence - drug effects | Male | Autophagy - physiology | Phosphoproteins - metabolism | Fibroblasts - ultrastructure | Tumor Suppressor Protein p53 - genetics | Small Ubiquitin-Related Modifier Proteins - genetics | Toluene - analogs & derivatives | RNA Interference | Time Factors | beta-Galactosidase - metabolism | Autophagy - genetics | Toluene - pharmacology | Child | Fibroblasts - metabolism | Autophagy-Related Protein 12 | Cellular Senescence - genetics | Ubiquitin-Activating Enzymes - genetics | Lysosome-Associated Membrane Glycoproteins - metabolism | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Benzothiazoles - pharmacology | Small Ubiquitin-Related Modifier Proteins - metabolism | Cells, Cultured | Tumor Suppressor Protein p53 - metabolism | Cellular Senescence - physiology | Signal Transduction - genetics | Microscopy, Electron | Ubiquitin-Activating Enzymes - metabolism | Blotting, Western | Autophagy-Related Protein 7 | Acetylcysteine - pharmacology | Lysosome-Associated Membrane Glycoproteins - genetics | Signal Transduction - physiology | Fibroblasts - cytology | Primary Cell Culture | Adaptor Proteins, Signal Transducing - metabolism | Lysosomal-Associated Membrane Protein 2 | Acetylcysteine | Tumor proteins | Genetic translation | Cells | Protein binding | TOR protein | Huntingtons disease | Senescence | Phosphorylation | Yeast | p53 Protein | Impairment | Galactosidase | Viruses | Homology | Activation | Biochemistry | Autophagy | Fibroblasts | Aging | Cytokines | LAMP-2 protein | Translation initiation | Rapamycin | Ribosomal protein S6 | siRNA | Mammals | Membrane proteins | Medicine | Life span | Morphology | Initiation factor eIF-4E | Molecular biology | Alzheimers disease | Phagocytosis | Apoptosis | Index Medicus
Journal Article
PloS one, ISSN 1932-6203, 2012, Volume 7, Issue 6, pp. e39679 - e39679
The target of rapamycin (TOR) is a high molecular weight protein kinase that regulates many processes in cells in response to mitogens and variations in... 
CELLS | TRANSCRIPTIONAL ACTIVATION | DNA-BINDING | PHOSPHOPROTEOMIC ANALYSIS | FACTOR-1 | PHOSPHORYLATION | MULTIDISCIPLINARY SCIENCES | KINASE | AUTOPHAGY | BINDING PROTEIN | THERMOTOLERANCE | Phosphotransferases - metabolism | Phosphorylation | Protein Biosynthesis | Transcription Factors - chemistry | TOR Serine-Threonine Kinases - metabolism | Humans | Stress, Physiological | Heat-Shock Proteins - biosynthesis | Molecular Sequence Data | Substrate Specificity | Promoter Regions, Genetic - genetics | Heat Shock Transcription Factors | DNA-Binding Proteins - metabolism | Heat-Shock Proteins - genetics | Peptides - metabolism | Transcription, Genetic | Amino Acid Sequence | Peptides - chemistry | Heat-Shock Proteins - metabolism | Gene Expression Regulation | Gene Silencing | HSP70 Heat-Shock Proteins - genetics | Phosphoserine - metabolism | DNA-Binding Proteins - chemistry | Transcription Factors - metabolism | Heat-Shock Response | HeLa Cells | RNA | Genes | Heat shock proteins | Protein biosynthesis | Amino acids | Genetic transcription | Protein kinases | Mitogens | Cell culture | Tissue culture | Proteins | Signal transduction | Life sciences | Sodium arsenite | Stress response | Chemical synthesis | Deoxyribonucleic acid--DNA | Stresses | Medical research | RNA-mediated interference | Rapamycin | Hsp70 protein | Gene expression | Heat | Sodium | Protein synthesis | Adapter proteins | Hyperthermia | TOR protein | Hsp90 protein | Serine | Gene regulation | Oncology | Activation | Kinases | Autophagy | Molecular weight | Heat shock factors | Reduction | Transcription activation | HSF1 protein | Alanine | Ribonucleic acid--RNA | Fever | Proteasome inhibitors | Stress | Protein kinase | Plasmids | Nutrient availability | Protein expression | Arsenite | Heat shock | Apoptosis | Index Medicus | Ribonucleic acids | Shock | Deoxyribonucleic acid | DNA
Journal Article
Biochemical Journal, ISSN 0264-6021, 07/2009, Volume 421, Issue 1, pp. 29 - 42
mTOR (mammalian target of rapamycin) stimulates cell growth by phosphorylating and promoting activation of AGC (protein kinase A/protein kinase G/protein... 
Phosphoinositide 3-kinase (PI3K) | Akt/protein kinase B (PKB) | Serum and glucocorticoid protein kinase (SGK) | P70 ribosomal S6 kinase (S6K) | Kinase inhibitor | Cancer | IN-VIVO ROLE | PROTEIN-KINASE B/AKT | BINDING PARTNER | RAG GTPASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | P70 S6 KINASE | kinase inhibitor | phosphoinositide 3-kinase (PI3K) | p70 ribosomal S6 kinase (S6K) | SUBSTRATE-SPECIFICITY | HYDROPHOBIC MOTIF PHOSPHORYLATION | cancer | serum and glucocorticoid protein kinase (SGK) | COMPLEX 2 | PDK1 | Cell Line | Humans | Multiprotein Complexes | Morpholines - pharmacology | Transcription Factors - antagonists & inhibitors | Gene Expression Profiling | G1 Phase - drug effects | Pyrimidines - pharmacology | Morpholines - chemistry | Pyrimidines - chemistry | Mechanistic Target of Rapamycin Complex 1 | Gene Expression Regulation - drug effects | Proteins | Transcription Factors - metabolism | Animals | Fibroblasts - drug effects | Cell Proliferation - drug effects | Mice | TOR Serine-Threonine Kinases | Fibroblasts - metabolism | Index Medicus | PI3K, phosphoinositide 3-kinase | PDK, 3-phosphoinositide-dependent protein kinase | AMPK, AMP-activated protein kinase | mTORC, mTOR complex | DTT, dithiothreitol | SPHK, sphingosine kinase | ERK, extracellular-signal-regulated kinase | RSK, ribosomal S6 kinase | PH domain, pleckstrin homology domain | protein kinase B (PKB) | protein kinase G | NDRG1, N-Myc downstream-regulated gene-1 | IGF, insulin-like growth factor | mTOR, mammalian target of rapamycin | GST, glutathione transferase | SGK, serum and glucocorticoid protein kinase | PKC, protein kinase C | S6K, p70 ribosomal S6 kinase | eIF4E, eukaryotic initiation factor 4E | 4E-BP1, eIF4E-binding protein 1 | protein kinase C family | Akt | PRAS40, proline-rich Akt substrate of 40 kDa | HEK-293 cell, human embryonic kidney 293 cell | MEF, mouse embryonic fibroblast | AGC family, protein kinase A | MAPK, mitogen-activated protein kinase
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 5/2008, Volume 181, Issue 3, pp. 497 - 510
Autophagy is a membrane-mediated intracellular degradation system. The serine/threonine kinase Atg1 plays an essential role in autophagosome formation.... 
Yeasts | Starvation | NIH 3T3 cells | Microscopy | Neurons | Cell lines | Antibodies | Cultured cells | Focal adhesions | Gene expression regulation | COMPLEX | MOLECULAR MACHINERY | FOCAL ADHESION | GENE | C-ELEGANS | AXONAL ELONGATION | HUMAN BREAST-CANCER | SACCHAROMYCES-CEREVISIAE | SERINE/THREONINE KINASE | SELF-DIGESTION | CELL BIOLOGY | Protein Kinases - metabolism | Protein Kinases - genetics | Microtubule-Associated Proteins - genetics | Fibroblasts - physiology | Microtubule-Associated Proteins - metabolism | Protein-Tyrosine Kinases - metabolism | Humans | Autophagy - physiology | Recombinant Fusion Proteins - metabolism | Autophagy-Related Protein-1 Homolog | Intracellular Membranes - ultrastructure | Protein-Tyrosine Kinases - genetics | Protein-Serine-Threonine Kinases - metabolism | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Phagosomes - metabolism | Protein-Serine-Threonine Kinases - genetics | Fungal Proteins - genetics | Mice, Knockout | Focal Adhesion Protein-Tyrosine Kinases - genetics | Animals | Autophagy-Related Protein 5 | Recombinant Fusion Proteins - genetics | Fibroblasts - cytology | Mice | TOR Serine-Threonine Kinases | Intracellular Membranes - metabolism | Fungal Proteins - metabolism | Allelomorphism | Muridae | Physiological aspects | Cell physiology | Research | Properties | Binding proteins | Identification and classification | Phosphotransferases | Proteins | Biochemistry | Mammals | Kinases | Rodents | Cells | Index Medicus
Journal Article
Biogerontology, ISSN 1389-5729, 2013, Volume 14, Issue 3, pp. 303 - 323
During ageing skeletal muscles undergo a process of structural and functional remodelling that leads to sarcopenia, a syndrome characterized by loss of muscle... 
Life Sciences | Sarcopenia | FoxO | Geriatrics/Gerontology | Ageing | mTOR | IGF1 | Akt | Developmental Biology | Cell Biology | LIFE-SPAN | IGF-I | ALPHA-V-BETA-3 INTEGRIN | PLASMINOGEN-ACTIVATOR INHIBITOR-1 | GERIATRICS & GERONTOLOGY | GROWTH-HORMONE | MESSENGER-RNA | GENETIC-DETERMINANTS | FAST-TWITCH | CELL-CYCLE | S6 KINASE | Microtubule-Associated Proteins - genetics | SKP Cullin F-Box Protein Ligases - genetics | Humans | SKP Cullin F-Box Protein Ligases - physiology | Male | Forkhead Transcription Factors - physiology | Ubiquitin-Protein Ligases - physiology | Tripartite Motif Proteins | Young Adult | Aged, 80 and over | Adult | Female | Mice, Inbred DBA | Models, Animal | TOR Serine-Threonine Kinases - physiology | Muscle Proteins - physiology | Serpin E2 - physiology | Mice, Inbred C57BL | Mice, Transgenic | Proto-Oncogene Proteins c-akt - physiology | Muscle, Skeletal - physiology | Mice, Knockout | Microtubule-Associated Proteins - physiology | Muscle Proteins - genetics | Autophagy-Related Protein 7 | Sarcopenia - physiopathology | Serpin E2 - genetics | Animals | Aging - physiology | Insulin-Like Growth Factor I - physiology | Adolescent | Signal Transduction - physiology | Aged | Forkhead Box Protein O1 | Mice | Ubiquitin-Protein Ligases - genetics | Ubiquitin | Muscles | Ligases | Proteolysis | Analysis | Index Medicus | SKP Cullin F-Box Protein Ligases | Muscle Proteins | Aging | Serpin E2 | Signal Transduction | Biochemistry, Molecular Biology | Microtubule-Associated Proteins | Insulin-Like Growth Factor I | Proto-Oncogene Proteins c-akt | Ubiquitin-Protein Ligases | TOR Serine-Threonine Kinases | Muscle, Skeletal | Forkhead Transcription Factors | Clinical Medicine | Neurology | Neurologi | Medical and Health Sciences | Medicin och hälsovetenskap | Clinical Neurophysiology | Klinisk neurofysiologi | Klinisk medicin
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