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Circulation Research, ISSN 0009-7330, 02/2007, Volume 100, Issue 3, pp. 328 - 341
The AMP-activated protein kinase (AMPK) system acts as a sensor of cellular energy status that is conserved in all eukaryotic cells. It is activated by... 
Calcium signaling | Signaling pathways | Diabetes | Metabolism | Insulin | RAT-LIVER | CARDIAC & CARDIOVASCULAR SYSTEMS | insulin | 5-AMINOIMIDAZOLE-4-CARBOXAMIDE RIBONUCLEOSIDE | STIMULATED GLUCOSE-TRANSPORT | calcium signaling | N-TERMINAL KINASE | ACETYL-COA CARBOXYLASE | VEIN ENDOTHELIAL-CELLS | COENZYME-A CARBOXYLASE | HUMAN SKELETAL-MUSCLE | signaling pathways | FATTY-ACID OXIDATION | PANCREATIC BETA-CELLS | PERIPHERAL VASCULAR DISEASE | metabolism | HEMATOLOGY | diabetes | Consensus Sequence | Protein Subunits | Protein-Serine-Threonine Kinases - deficiency | Insulin - physiology | Obesity - drug therapy | Humans | Muscle Cells - drug effects | Adipocytes - drug effects | AMP-Activated Protein Kinases | Aminoimidazole Carboxamide - pharmacology | Multienzyme Complexes - deficiency | Calcium - physiology | Adenosine Triphosphate - metabolism | Energy Metabolism - physiology | Binding Sites | Peptide Hormones - physiology | Hypoglycemic Agents - therapeutic use | Amino Acid Sequence | Diabetes Mellitus - drug therapy | Models, Molecular | Rats | Hypoglycemic Agents - pharmacology | Mice, Knockout | Calcium-Calmodulin-Dependent Protein Kinase Kinase | Carbohydrate Metabolism - physiology | Aminoimidazole Carboxamide - analogs & derivatives | Diabetes Mellitus - therapy | Protein-Serine-Threonine Kinases - drug effects | Mice | Protein-Serine-Threonine Kinases - chemistry | Cell Cycle - drug effects | Energy Metabolism - drug effects | Lipid Metabolism - physiology | Multienzyme Complexes - drug effects | Carbohydrate Metabolism - drug effects | Phosphorylation | Metformin - therapeutic use | Molecular Sequence Data | Hepatocytes - metabolism | Ribonucleotides - pharmacology | Hepatocytes - drug effects | Adenosine Monophosphate - metabolism | Protein-Serine-Threonine Kinases - physiology | Metformin - pharmacology | Muscle Cells - metabolism | Protein-Serine-Threonine Kinases - genetics | Diabetes Mellitus - metabolism | Neoplasms - enzymology | Multienzyme Complexes - genetics | Enzyme Activation - drug effects | Protein Processing, Post-Translational - physiology | Multienzyme Complexes - chemistry | Obesity - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Oxygen Consumption - drug effects | Adipocytes - metabolism | Multienzyme Complexes - physiology | Lipid Metabolism - drug effects | Cell Cycle - physiology | Neoplasms - pathology
Journal Article
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
Journal Article
Cardiovascular Diabetology, ISSN 1475-2840, 11/2013, Volume 12, Issue 1, pp. 158 - 158
Background: Endoplasmic reticulum (ER) stress is considered one of the mechanisms contributing to reactive oxygen species (ROS)-mediated cell apoptosis. In... 
Diabetic cardiomyopathy | Oxidative stress | Apoptosis | Endoplasmic reticulum stress | MITOCHONDRIAL OXIDATIVE STRESS | CARDIAC & CARDIOVASCULAR SYSTEMS | ER STRESS | PREVENTION | SUPPRESSION | RAT MODEL | MYOCARDIAL APOPTOSIS | CELL-DEATH | HEART | ENDOCRINOLOGY & METABOLISM | MICE | CONTRIBUTES | Free Radical Scavengers - pharmacology | Diabetic Cardiomyopathies - metabolism | Reactive Oxygen Species - metabolism | Apoptosis - drug effects | eIF-2 Kinase - metabolism | eIF-2 Kinase - drug effects | Activating Transcription Factor 6 - genetics | Activating Transcription Factor 6 - drug effects | Gene Knockdown Techniques | Membrane Proteins - metabolism | Diabetes Mellitus, Experimental - metabolism | Protein-Serine-Threonine Kinases - metabolism | Disease Models, Animal | Endoplasmic Reticulum Stress - drug effects | Membrane Proteins - genetics | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Rats | Rats, Sprague-Dawley | Activating Transcription Factor 6 - metabolism | Animals | Myocytes, Cardiac - drug effects | Signal Transduction - drug effects | Acetylcysteine - pharmacology | Protein-Serine-Threonine Kinases - drug effects | Glucose - metabolism | Membrane Proteins - drug effects | Myocytes, Cardiac - metabolism | Signal Transduction - physiology | Apoptosis - physiology | Endoplasmic Reticulum Stress - physiology | Studies | Kinases | Rodents | Animal models
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 4/2003, Volume 161, Issue 2, pp. 281 - 294
The proper segregation of sister chromatids in mitosis depends on bipolar attachment of all chromosomes to the mitotic spindle. We have identified the small... 
Mitosis | Kinetochores | Chromatids | Microtubules | HeLa cells | Cellular immunity | Chromosomes | Anaphase | Cells | Mitotic spindle apparatus | Chemical biology | Spindle assembly checkpoint | Chromosome segregation | KINASE-ACTIVITY | MAD2 | BUDDING YEAST | spindle assembly checkpoint | TENSION | G/M TRANSITION | mitosis | HISTONE H3 PHOSPHORYLATION | MAMMALIAN-CELLS | CELL BIOLOGY | kinetochores | chromosome segregation | chemical biology | VERTEBRATE SOMATIC-CELLS | Cell Cycle Proteins - drug effects | Protein Kinases - metabolism | RNA, Small Interfering - genetics | Paclitaxel - pharmacology | Humans | Nocodazole - pharmacology | Chromosome Segregation - drug effects | Mitosis - genetics | Aurora Kinase B | Microtubules - drug effects | Spindle Apparatus - genetics | Cell Cycle Proteins - genetics | Genes, cdc - physiology | Indoles - pharmacology | Kinetochores - enzymology | Protein-Serine-Threonine Kinases - metabolism | Aneugens - pharmacology | Eukaryotic Cells - enzymology | Polyploidy | Protein Kinases - drug effects | Separase | Protein-Serine-Threonine Kinases - genetics | Genes, cdc - drug effects | Aurora Kinases | Pyrimidines - pharmacology | Sulfonamides - pharmacology | Anaphase - drug effects | Phenotype | Anaphase - genetics | Animals | Eukaryotic Cells - drug effects | Mitosis - drug effects | Microtubules - genetics | Microtubules - enzymology | Protein-Serine-Threonine Kinases - drug effects | Eukaryotic Cells - cytology | Kinetochores - drug effects | Spindle Apparatus - drug effects | HeLa Cells | Thiones - pharmacology | Endopeptidases | Chromosome Segregation - genetics | Spindle Apparatus - enzymology | Research | mitosis; chromosome segregation; kinetochores; spindle assembly checkpoint; chemical biology
Journal Article
Stroke, ISSN 0039-2499, 11/2007, Volume 38, Issue 11, pp. 2992 - 2999
Background and Purpose - 5' adenosine monophosphate-dependent protein kinase ( AMPK) acts as a metabolic sensor. AMPK is elevated under ischemic conditions,... 
Animal model | Neuroprotection | Stroke | AMP-activated protein kinase | PROTECTION | FOOD-INTAKE | ISOFORM | stroke | METABOLIC SENSOR | CLINICAL NEUROLOGY | CELL-DEATH | neuroprotection | NITRIC-OXIDE | AMPK | PERIPHERAL VASCULAR DISEASE | FATTY-ACID SYNTHASE | animal model | CEREBRAL-ISCHEMIA | EXPRESSION | Brain Chemistry - drug effects | Neuroprotective Agents - therapeutic use | Brain Ischemia - genetics | Brain - enzymology | Male | AMP-Activated Protein Kinases | Stroke - genetics | Brain Ischemia - enzymology | Dose-Response Relationship, Drug | Neuroprotective Agents - pharmacology | Cell Death - genetics | Gene Deletion | Cytoprotection - drug effects | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Cell Death - drug effects | Protein-Serine-Threonine Kinases - metabolism | Brain Chemistry - genetics | Disease Models, Animal | Protein Subunits - genetics | Drug Administration Schedule | Mice, Inbred C57BL | Enzyme Inhibitors - pharmacology | Protein-Serine-Threonine Kinases - genetics | Treatment Outcome | Multienzyme Complexes - genetics | Stroke - drug therapy | Enzyme Activation - drug effects | Multienzyme Complexes - antagonists & inhibitors | Enzyme Inhibitors - therapeutic use | Mice, Knockout | Stroke - enzymology | Brain - drug effects | Animals | Brain Ischemia - drug therapy | Protein-Serine-Threonine Kinases - drug effects | Brain - pathology | Cytoprotection - genetics | Mice | Enzyme Activation - genetics
Journal Article
Diabetes, ISSN 0012-1797, 10/2010, Volume 59, Issue 10, pp. 2426 - 2434
OBJECTIVE Branched-chain amino acids, such as leucine and glucose, stimulate protein synthesis and increase the phosphorylation and activity of the mammalian... 
MAMMALIAN TARGET | ENERGY | AMINO-ACID METABOLISM | MALONYL-COA | ENDOCRINOLOGY & METABOLISM | STARVATION | ACETYL-COA CARBOXYLASE | VEIN ENDOTHELIAL-CELLS | KINASE ACTIVATION | SIRT1 | EXERCISE | AMP-Activated Protein Kinases - metabolism | Leucine - pharmacology | Phosphoproteins - drug effects | Phosphorylation | Intracellular Signaling Peptides and Proteins - drug effects | Intracellular Signaling Peptides and Proteins - metabolism | Ribosomal Protein S6 Kinases, 70-kDa - drug effects | Carrier Proteins - drug effects | Phosphoproteins - metabolism | Dose-Response Relationship, Drug | Insulin Resistance - physiology | Adenylate Kinase - metabolism | Muscle, Skeletal - drug effects | Aminoimidazole Carboxamide - metabolism | Protein-Serine-Threonine Kinases - metabolism | Pyruvates - metabolism | Muscle, Skeletal - enzymology | Ribonucleotides - metabolism | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Rats | Glucose - pharmacology | Down-Regulation - drug effects | Animals | Carrier Proteins - metabolism | Lactates - metabolism | Aminoimidazole Carboxamide - analogs & derivatives | Protein-Serine-Threonine Kinases - drug effects | TOR Serine-Threonine Kinases | Kinetics | Branched chain amino acids | Analysis | Physiological aspects | Insulin resistance | Protein biosynthesis | Research | Diabetes | Protein kinases | Metabolism
Journal Article