EMBO reports, ISSN 1469-221X, 02/2012, Volume 13, Issue 2, pp. 150 - 156
Sqstm1/p62 functions in the non‐canonical activation of nuclear factor (erythroid‐derived 2)‐like 2 (Nrf2). However, its physiological relevance is not...
nrf2 | p62 | mammalian longevity | mitochondria | nqo1 | LIFE-SPAN | OXIDATIVE STRESS | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | P62/SQSTM1 | DROSOPHILA | CELL BIOLOGY | INACTIVATION | TRANSCRIPTION FACTOR NRF2 | RESISTANCE | MICE | Oxidation-Reduction | Signal Transduction | Sequestosome-1 Protein | Heat-Shock Proteins - metabolism | Male | Mitochondria - metabolism | Autophagy | Heat-Shock Proteins - deficiency | Animals | Adaptor Proteins, Signal Transducing - deficiency | NF-E2-Related Factor 2 - metabolism | Mammals - physiology | NAD(P)H Dehydrogenase (Quinone) - metabolism | Cytoskeletal Proteins - metabolism | Female | Mice | Adaptor Proteins, Signal Transducing - metabolism | Kelch-Like ECH-Associated Protein 1 | Longevity - physiology | Genotype & phenotype | Mitochondria | Life expectancy | Rodents | Aging | Molecular biology | Gene expression | Scientific Reports
nrf2 | p62 | mammalian longevity | mitochondria | nqo1 | LIFE-SPAN | OXIDATIVE STRESS | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | P62/SQSTM1 | DROSOPHILA | CELL BIOLOGY | INACTIVATION | TRANSCRIPTION FACTOR NRF2 | RESISTANCE | MICE | Oxidation-Reduction | Signal Transduction | Sequestosome-1 Protein | Heat-Shock Proteins - metabolism | Male | Mitochondria - metabolism | Autophagy | Heat-Shock Proteins - deficiency | Animals | Adaptor Proteins, Signal Transducing - deficiency | NF-E2-Related Factor 2 - metabolism | Mammals - physiology | NAD(P)H Dehydrogenase (Quinone) - metabolism | Cytoskeletal Proteins - metabolism | Female | Mice | Adaptor Proteins, Signal Transducing - metabolism | Kelch-Like ECH-Associated Protein 1 | Longevity - physiology | Genotype & phenotype | Mitochondria | Life expectancy | Rodents | Aging | Molecular biology | Gene expression | Scientific Reports
Journal Article
Molecular Neurobiology, ISSN 0893-7648, 12/2016, Volume 53, Issue 10, pp. 6620 - 6634
Huntington’s disease (HD) is a devastating neurodegenerative disorder, which is caused by the expression and aggregation of polyQ-expanded mutant huntingtin...
Aggregation | Neurology | Neurosciences | Biomedicine | Neurobiology | ENC1 | ER stress | p62/SQSTM1 | Huntington’s disease | Autophagy | Cell Biology | PHOSPHORYLATION | NEURONAL CELL-DEATH | ENDOPLASMIC-RETICULUM STRESS | Huntington's disease | SELECTIVE AUTOPHAGY | NEUROSCIENCES | NEURODEGENERATIVE DISEASES | NRP/B | NUCLEAR-MATRIX PROTEIN | INHIBITION | NRF2 | PATHWAY | Protein Aggregates | Neurons - pathology | Phosphorylation | Humans | JNK Mitogen-Activated Protein Kinases - metabolism | Proteolysis | Protein Binding - drug effects | HEK293 Cells | Mutant Proteins - toxicity | Microfilament Proteins - metabolism | Neurons - metabolism | Sequestosome-1 Protein - metabolism | Protein-Serine-Threonine Kinases - metabolism | Endoribonucleases - metabolism | TNF Receptor-Associated Factor 2 - metabolism | Neuropeptides - metabolism | Neurotoxins - toxicity | Nuclear Proteins - metabolism | Animals | Huntingtin Protein - toxicity | Endoplasmic Reticulum Stress | Cell Line, Tumor | Mice | Proteasome Endopeptidase Complex - metabolism | Enzymes | Medical colleges | Nervous system diseases | Detergents, Synthetic | Stress (Physiology) | Cells | Huntingtons disease | Pathogenesis | Stress
Aggregation | Neurology | Neurosciences | Biomedicine | Neurobiology | ENC1 | ER stress | p62/SQSTM1 | Huntington’s disease | Autophagy | Cell Biology | PHOSPHORYLATION | NEURONAL CELL-DEATH | ENDOPLASMIC-RETICULUM STRESS | Huntington's disease | SELECTIVE AUTOPHAGY | NEUROSCIENCES | NEURODEGENERATIVE DISEASES | NRP/B | NUCLEAR-MATRIX PROTEIN | INHIBITION | NRF2 | PATHWAY | Protein Aggregates | Neurons - pathology | Phosphorylation | Humans | JNK Mitogen-Activated Protein Kinases - metabolism | Proteolysis | Protein Binding - drug effects | HEK293 Cells | Mutant Proteins - toxicity | Microfilament Proteins - metabolism | Neurons - metabolism | Sequestosome-1 Protein - metabolism | Protein-Serine-Threonine Kinases - metabolism | Endoribonucleases - metabolism | TNF Receptor-Associated Factor 2 - metabolism | Neuropeptides - metabolism | Neurotoxins - toxicity | Nuclear Proteins - metabolism | Animals | Huntingtin Protein - toxicity | Endoplasmic Reticulum Stress | Cell Line, Tumor | Mice | Proteasome Endopeptidase Complex - metabolism | Enzymes | Medical colleges | Nervous system diseases | Detergents, Synthetic | Stress (Physiology) | Cells | Huntingtons disease | Pathogenesis | Stress
Journal Article
BIOMED RESEARCH INTERNATIONAL, ISSN 2314-6133, 07/2019, Volume 2019, pp. 5815604 - 11
Background. Sasa quelpaertensis Nakai extract (SQE) or dwarf bamboo has been extensively investigated for its antioxidant and anti-inflammatory effects;...
MEDICINE, RESEARCH & EXPERIMENTAL | DEPRESSION | PROTEIN-KINASE-C | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | HIGH-FAT DIET | LOCUS-COERULEUS | DOPAMINE | SEROTONIN | STRESS | P-COUMARIC ACID | MENOPAUSAL TRANSITION | EXTRACT | Povidone | Brain | Antidepressants | Menopause | Tryptophan | Aprotinin | Protein kinases | Enzyme-linked immunosorbent assay | Immunohistochemistry | Temperature | Neurosciences | Protein kinase C | Antibodies | Immobilization | Hormones | Mental depression | Hypothalamus | Kinases | Density | Experiments | Proteins | Antioxidants | Locus coeruleus | Medical research | Cortex (prefrontal) | Dopamine | Serotonin | Ovariectomy | Body temperature | Hydroxylase | Inflammation | Stress | Tryptophan hydroxylase | Studies | Neurotransmitters | Womens health | Bamboo
MEDICINE, RESEARCH & EXPERIMENTAL | DEPRESSION | PROTEIN-KINASE-C | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | HIGH-FAT DIET | LOCUS-COERULEUS | DOPAMINE | SEROTONIN | STRESS | P-COUMARIC ACID | MENOPAUSAL TRANSITION | EXTRACT | Povidone | Brain | Antidepressants | Menopause | Tryptophan | Aprotinin | Protein kinases | Enzyme-linked immunosorbent assay | Immunohistochemistry | Temperature | Neurosciences | Protein kinase C | Antibodies | Immobilization | Hormones | Mental depression | Hypothalamus | Kinases | Density | Experiments | Proteins | Antioxidants | Locus coeruleus | Medical research | Cortex (prefrontal) | Dopamine | Serotonin | Ovariectomy | Body temperature | Hydroxylase | Inflammation | Stress | Tryptophan hydroxylase | Studies | Neurotransmitters | Womens health | Bamboo
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 2011, Volume 413, Issue 1, pp. 122 - 127
► The mitochondrion contains its own protein quality control system. ► p62 localizes within the mitochondria and forms mega-dalton sized complexes. ► p62...
Mitochondria | Oxidation | Electron transport | p62 | Chaperone | P62 | RESPIRATORY-CHAIN | MECHANISM | GLUTATHIONYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | P62/SQSTM1 | AUTOPHAGY | INACTIVATION | TRANSCRIPTION FACTOR NRF2 | BIOPHYSICS | COMPLEX-II | DEGRADATION | STRESS | Adaptor Proteins, Signal Transducing - chemistry | Oxidation-Reduction | Sequestosome-1 Protein | Heat-Shock Proteins - metabolism | Mitochondria - metabolism | Brain - metabolism | Animals | Mice, Mutant Strains | Mitochondrial Proteins - metabolism | Mitochondrial Proteins - chemistry | Mice | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Adaptor Proteins, Signal Transducing - metabolism | Heat-Shock Proteins - chemistry | Proteins | Control systems | Mitochondrial DNA | OXIDATION | TIME-OF-FLIGHT METHOD | ENZYMES | IN VITRO | MITOCHONDRIA | QUALITY CONTROL | MASS SPECTROSCOPY | 60 APPLIED LIFE SCIENCES | BIOLOGICAL STRESS | DAMAGE
Mitochondria | Oxidation | Electron transport | p62 | Chaperone | P62 | RESPIRATORY-CHAIN | MECHANISM | GLUTATHIONYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | P62/SQSTM1 | AUTOPHAGY | INACTIVATION | TRANSCRIPTION FACTOR NRF2 | BIOPHYSICS | COMPLEX-II | DEGRADATION | STRESS | Adaptor Proteins, Signal Transducing - chemistry | Oxidation-Reduction | Sequestosome-1 Protein | Heat-Shock Proteins - metabolism | Mitochondria - metabolism | Brain - metabolism | Animals | Mice, Mutant Strains | Mitochondrial Proteins - metabolism | Mitochondrial Proteins - chemistry | Mice | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Adaptor Proteins, Signal Transducing - metabolism | Heat-Shock Proteins - chemistry | Proteins | Control systems | Mitochondrial DNA | OXIDATION | TIME-OF-FLIGHT METHOD | ENZYMES | IN VITRO | MITOCHONDRIA | QUALITY CONTROL | MASS SPECTROSCOPY | 60 APPLIED LIFE SCIENCES | BIOLOGICAL STRESS | DAMAGE
Journal Article
Cell Metabolism, ISSN 1550-4131, 2008, Volume 8, Issue 4, pp. 318 - 324
Autophagy is a cellular degradation-recycling system for aggregated proteins and damaged organelles. Although dysregulated autophagy is implicated in various...
PROTEINS | HUMDISEASE | DIABETES-MELLITUS | SURVIVAL | APOPTOSIS | GLUCOSE-HOMEOSTASIS | NOD MICE | RAT HEPATOCYTES | PATHWAY | ER STRESS | ENDOCRINOLOGY & METABOLISM | DEATH | ENDOPLASMIC-RETICULUM STRESS | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Ubiquitin - metabolism | Autophagy - physiology | Diabetes Mellitus, Type 2 - metabolism | Mice, Knockout | Hyperglycemia - metabolism | Insulin-Secreting Cells - ultrastructure | Autophagy-Related Protein 7 | Insulin - metabolism | Insulin-Secreting Cells - metabolism | Animals | Diabetes Mellitus, Type 2 - physiopathology | Hyperglycemia - pathology | Glucose - metabolism | Mice | Diabetes Mellitus, Type 2 - pathology | Insulin-Secreting Cells - pathology
PROTEINS | HUMDISEASE | DIABETES-MELLITUS | SURVIVAL | APOPTOSIS | GLUCOSE-HOMEOSTASIS | NOD MICE | RAT HEPATOCYTES | PATHWAY | ER STRESS | ENDOCRINOLOGY & METABOLISM | DEATH | ENDOPLASMIC-RETICULUM STRESS | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Ubiquitin - metabolism | Autophagy - physiology | Diabetes Mellitus, Type 2 - metabolism | Mice, Knockout | Hyperglycemia - metabolism | Insulin-Secreting Cells - ultrastructure | Autophagy-Related Protein 7 | Insulin - metabolism | Insulin-Secreting Cells - metabolism | Animals | Diabetes Mellitus, Type 2 - physiopathology | Hyperglycemia - pathology | Glucose - metabolism | Mice | Diabetes Mellitus, Type 2 - pathology | Insulin-Secreting Cells - pathology
Journal Article
Archives of Pharmacal Research, ISSN 0253-6269, 1998, Volume 21, Issue 6, pp. 629 - 633
In addition to selecting proteins for degradation by the 26S proteasome, ubiqitination appears to serve other regulatory functions, including for...
Protein metabolism | Ubiqitination | P62 | Sequestosome | CHEMISTRY, MEDICINAL | protein metabolism | KINASE | P56(LCK) | MULTIUBIQUITIN CHAINS | SH2 DOMAIN | PHOSPHOTYROSINE-INDEPENDENT LIGAND | sequestosome | ubiqitination | BINDING PROTEINS | PROTEASOME | SEQUENCE | GROWTH | PHARMACOLOGY & PHARMACY | COMPONENT | Protein Kinases - metabolism | Humans | Adenosine Triphosphatases - metabolism | Multienzyme Complexes - metabolism | Proteasome Endopeptidase Complex | Proto-Oncogene Proteins c-myc - metabolism | Proto-Oncogene Proteins c-myc - physiology | Animals | Cysteine Endopeptidases - metabolism | Proteins - metabolism | Protein Binding | Proto-Oncogene Proteins c-myc - genetics | Ubiquitins - metabolism
Protein metabolism | Ubiqitination | P62 | Sequestosome | CHEMISTRY, MEDICINAL | protein metabolism | KINASE | P56(LCK) | MULTIUBIQUITIN CHAINS | SH2 DOMAIN | PHOSPHOTYROSINE-INDEPENDENT LIGAND | sequestosome | ubiqitination | BINDING PROTEINS | PROTEASOME | SEQUENCE | GROWTH | PHARMACOLOGY & PHARMACY | COMPONENT | Protein Kinases - metabolism | Humans | Adenosine Triphosphatases - metabolism | Multienzyme Complexes - metabolism | Proteasome Endopeptidase Complex | Proto-Oncogene Proteins c-myc - metabolism | Proto-Oncogene Proteins c-myc - physiology | Animals | Cysteine Endopeptidases - metabolism | Proteins - metabolism | Protein Binding | Proto-Oncogene Proteins c-myc - genetics | Ubiquitins - metabolism
Journal Article
Autophagy, ISSN 1554-8627, 08/2016, Volume 12, Issue 8, pp. 1272 - 1291
Proper regulation of mitophagy for mitochondrial homeostasis is important in various inflammatory diseases. However, the precise mechanisms by which mitophagy...
mitochondrial priming | mitophagy | autophagy | NLRP3 inflammasome | sepsis | SESN2 | REGULATE AUTOPHAGY | RETICULOCYTE MATURATION | PHOSPHORYLATION | INFLAMMASOME ACTIVATION | AUTOPHAGIC DEGRADATION | P62/SQSTM1 | MITOCHONDRIAL QUALITY-CONTROL | CELL BIOLOGY | PINK1/PARKIN-MEDIATED MITOPHAGY | SESTRIN2 | PROMOTES | Inflammasomes - metabolism | Reactive Oxygen Species - metabolism | Humans | Caspase 1 - metabolism | Male | Monocytes - metabolism | Autophagy-Related Protein-1 Homolog - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | Shock, Septic - metabolism | Interleukin-1beta - blood | Interleukin-18 - blood | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Mice, Inbred C57BL | Nuclear Proteins - metabolism | Inflammation | Mitochondria - metabolism | Mitochondrial Degradation | Macrophages - metabolism | Animals | Leukocytes, Mononuclear - cytology | Mice | Enzyme Activation | Lysine - chemistry | Nitric Oxide - metabolism | Nitric Oxide Synthase Type II - metabolism
mitochondrial priming | mitophagy | autophagy | NLRP3 inflammasome | sepsis | SESN2 | REGULATE AUTOPHAGY | RETICULOCYTE MATURATION | PHOSPHORYLATION | INFLAMMASOME ACTIVATION | AUTOPHAGIC DEGRADATION | P62/SQSTM1 | MITOCHONDRIAL QUALITY-CONTROL | CELL BIOLOGY | PINK1/PARKIN-MEDIATED MITOPHAGY | SESTRIN2 | PROMOTES | Inflammasomes - metabolism | Reactive Oxygen Species - metabolism | Humans | Caspase 1 - metabolism | Male | Monocytes - metabolism | Autophagy-Related Protein-1 Homolog - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Autophagy | Shock, Septic - metabolism | Interleukin-1beta - blood | Interleukin-18 - blood | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Mice, Inbred C57BL | Nuclear Proteins - metabolism | Inflammation | Mitochondria - metabolism | Mitochondrial Degradation | Macrophages - metabolism | Animals | Leukocytes, Mononuclear - cytology | Mice | Enzyme Activation | Lysine - chemistry | Nitric Oxide - metabolism | Nitric Oxide Synthase Type II - metabolism
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 09/2011, Volume 413, Issue 2, pp. 376 - 382
► Berberine inhibits adipogenesis by down-regulating C/EBPα and PPARγ. ► Berberine up-regulates two different C/EBP inhibitors, CHOP and DEC2. ► CHOP was...
Berberine | C/EBP inhibitors | Unfolded protein response | Adipogenesis | ACTIVATED PROTEIN-KINASE | MECHANISM | 3T3-L1 ADIPOCYTE DIFFERENTIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOPLASMIC-RETICULUM STRESS | INDUCTION | SUPPRESSION | BIOPHYSICS | CHOP/GADD153 | GENE-TRANSCRIPTION | Berberine - pharmacology | Up-Regulation | Animals | Adipocytes - metabolism | Adipogenesis - drug effects | CCAAT-Enhancer-Binding Proteins - antagonists & inhibitors | Male | Transcription Factors - biosynthesis | Mice | Adipocytes - drug effects | Transcription Factor CHOP - biosynthesis | 3T3-L1 Cells | Dexamethasone | Dimethyl sulfoxide
Berberine | C/EBP inhibitors | Unfolded protein response | Adipogenesis | ACTIVATED PROTEIN-KINASE | MECHANISM | 3T3-L1 ADIPOCYTE DIFFERENTIATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ENDOPLASMIC-RETICULUM STRESS | INDUCTION | SUPPRESSION | BIOPHYSICS | CHOP/GADD153 | GENE-TRANSCRIPTION | Berberine - pharmacology | Up-Regulation | Animals | Adipocytes - metabolism | Adipogenesis - drug effects | CCAAT-Enhancer-Binding Proteins - antagonists & inhibitors | Male | Transcription Factors - biosynthesis | Mice | Adipocytes - drug effects | Transcription Factor CHOP - biosynthesis | 3T3-L1 Cells | Dexamethasone | Dimethyl sulfoxide
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 08/2011, Volume 412, Issue 2, pp. 347 - 352
► Upon prolonged mitosis, cells undergo p53-dependent mitotic catastrophe. ► p62-deficient cells were resistant to mitotic catastrophe. ► p53 stabilization was...
Mitotic catastrophe | Aneuploidy | Noq1 | Nrf2 | p62 | p53 | P62 | P53 | BIOCHEMISTRY & MOLECULAR BIOLOGY | P62/SQSTM1 | AUTOPHAGY | ANTIOXIDANT RESPONSE ELEMENT | TRANSCRIPTION FACTOR NRF2 | DISRUPTION | BIOPHYSICS | GENE | DEGRADATION | POSTMITOTIC CHECKPOINT | SPINDLE-ASSEMBLY CHECKPOINT | Mitosis | Sequestosome-1 Protein | Tubulin Modulators - pharmacology | HCT116 Cells | Humans | Nocodazole - pharmacology | Tumor Suppressor Protein p53 - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | NAD(P)H Dehydrogenase (Quinone) - biosynthesis | NF-E2-Related Factor 2 - metabolism | Adaptor Proteins, Signal Transducing - genetics | Proteasome Endopeptidase Complex - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Kelch-Like ECH-Associated Protein 1 | Tumor proteins
Mitotic catastrophe | Aneuploidy | Noq1 | Nrf2 | p62 | p53 | P62 | P53 | BIOCHEMISTRY & MOLECULAR BIOLOGY | P62/SQSTM1 | AUTOPHAGY | ANTIOXIDANT RESPONSE ELEMENT | TRANSCRIPTION FACTOR NRF2 | DISRUPTION | BIOPHYSICS | GENE | DEGRADATION | POSTMITOTIC CHECKPOINT | SPINDLE-ASSEMBLY CHECKPOINT | Mitosis | Sequestosome-1 Protein | Tubulin Modulators - pharmacology | HCT116 Cells | Humans | Nocodazole - pharmacology | Tumor Suppressor Protein p53 - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Tumor Suppressor Protein p53 - genetics | NAD(P)H Dehydrogenase (Quinone) - biosynthesis | NF-E2-Related Factor 2 - metabolism | Adaptor Proteins, Signal Transducing - genetics | Proteasome Endopeptidase Complex - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Kelch-Like ECH-Associated Protein 1 | Tumor proteins
Journal Article
Cellular Microbiology, ISSN 1462-5814, 01/2008, Volume 10, Issue 1, pp. 165 - 176
Summary The capsid protein of the West Nile virus (WNV) functions as an apoptotic agonist via the induction of mitochondrial dysfunction and the activation of...
P19(ARF) | PATHWAY | CYTOPLASMIC LOCALIZATION | STABILITY | MDM2 | DEGRADATION | MICROBIOLOGY | INFECTION | EXPRESSION | ASSOCIATION | TUMOR-SUPPRESSOR P53 | CELL BIOLOGY | Fibroblasts - virology | Cell Line | West Nile virus - physiology | Capsid Proteins - metabolism | Humans | Cell Nucleolus - chemistry | Cells, Cultured | Tumor Suppressor Protein p53 - metabolism | Cercopithecus aethiops | bcl-2-Associated X Protein - biosynthesis | Animals | Protein Binding | Mice | Proto-Oncogene Proteins c-mdm2 - metabolism | Apoptosis | West Nile fever | Tumor proteins
P19(ARF) | PATHWAY | CYTOPLASMIC LOCALIZATION | STABILITY | MDM2 | DEGRADATION | MICROBIOLOGY | INFECTION | EXPRESSION | ASSOCIATION | TUMOR-SUPPRESSOR P53 | CELL BIOLOGY | Fibroblasts - virology | Cell Line | West Nile virus - physiology | Capsid Proteins - metabolism | Humans | Cell Nucleolus - chemistry | Cells, Cultured | Tumor Suppressor Protein p53 - metabolism | Cercopithecus aethiops | bcl-2-Associated X Protein - biosynthesis | Animals | Protein Binding | Mice | Proto-Oncogene Proteins c-mdm2 - metabolism | Apoptosis | West Nile fever | Tumor proteins
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2010, Volume 285, Issue 10, pp. 7271 - 7280
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2004, Volume 279, Issue 49, pp. 50930 - 50941
PELP1 (proline-, glutamic acid-, and leucine-rich protein 1) has been recognized as a coactivator of estrogen receptor (ER)-recruiting p300/CREB-binding...
ACTIVATION | RETINOBLASTOMA PROTEIN | INTERACTING PROTEIN | CHROMATIN-STRUCTURE | REPRESSION | ACETYLATION | DEACETYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | STEROID-RECEPTOR COACTIVATOR-1 | ESTROGEN-RECEPTOR | Chromatin - metabolism | NIH 3T3 Cells | Receptors, Estrogen - metabolism | Cell Proliferation | Histones - chemistry | Humans | Immunoblotting | Cell Nucleus - metabolism | Transfection | Chromatin Immunoprecipitation | Time Factors | Gene Deletion | Transcription, Genetic | Genes, Reporter | Repressor Proteins - metabolism | Fibroblasts - metabolism | RNA - metabolism | Protein Structure, Tertiary | Cell Line | Promoter Regions, Genetic | Enzyme Inhibitors - pharmacology | Proto-Oncogene Proteins c-fos - metabolism | Glutathione Transferase - metabolism | Nucleosomes - metabolism | Histone Deacetylase 2 | Histone Deacetylases - metabolism | Plasmids - metabolism | Mice, Inbred C3H | Animals | Cell Line, Tumor | Protein Binding | Trans-Activators - metabolism | Mice | Models, Genetic | Transcription Factors | HeLa Cells | Histones - metabolism | Co-Repressor Proteins | COS Cells | DNA, Complementary - metabolism
ACTIVATION | RETINOBLASTOMA PROTEIN | INTERACTING PROTEIN | CHROMATIN-STRUCTURE | REPRESSION | ACETYLATION | DEACETYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | STEROID-RECEPTOR COACTIVATOR-1 | ESTROGEN-RECEPTOR | Chromatin - metabolism | NIH 3T3 Cells | Receptors, Estrogen - metabolism | Cell Proliferation | Histones - chemistry | Humans | Immunoblotting | Cell Nucleus - metabolism | Transfection | Chromatin Immunoprecipitation | Time Factors | Gene Deletion | Transcription, Genetic | Genes, Reporter | Repressor Proteins - metabolism | Fibroblasts - metabolism | RNA - metabolism | Protein Structure, Tertiary | Cell Line | Promoter Regions, Genetic | Enzyme Inhibitors - pharmacology | Proto-Oncogene Proteins c-fos - metabolism | Glutathione Transferase - metabolism | Nucleosomes - metabolism | Histone Deacetylase 2 | Histone Deacetylases - metabolism | Plasmids - metabolism | Mice, Inbred C3H | Animals | Cell Line, Tumor | Protein Binding | Trans-Activators - metabolism | Mice | Models, Genetic | Transcription Factors | HeLa Cells | Histones - metabolism | Co-Repressor Proteins | COS Cells | DNA, Complementary - metabolism
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2010, Volume 285, Issue 10, pp. 7271 - 7280
The T cell-specific tyrosine kinase, p56 lck , plays crucial roles in T cell receptor (TCR)-mediated T cell activation. Here, we report that SOCS-6 ( s...
Interleukin-2 - metabolism | Promoter Regions, Genetic | T-Lymphocytes - physiology | Receptors, Antigen, T-Cell - metabolism | Jurkat Cells | Lymphocyte Activation | Humans | Suppressor of Cytokine Signaling Proteins - genetics | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism | Immunological Synapses - metabolism | Interleukin-2 - genetics | Two-Hybrid System Techniques | Animals | T-Lymphocytes - cytology | Protein Binding | Mice | Receptors, Antigen, T-Cell - genetics | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - genetics | Proteasome Endopeptidase Complex - metabolism | Suppressor of Cytokine Signaling Proteins - metabolism | Binding Sites | Receptors | Immunology | Signal Transduction | Cellular Response | T Cell Receptor | Protein | Tyrosine Kinase | Processing | Protein-Protein Interactions
Interleukin-2 - metabolism | Promoter Regions, Genetic | T-Lymphocytes - physiology | Receptors, Antigen, T-Cell - metabolism | Jurkat Cells | Lymphocyte Activation | Humans | Suppressor of Cytokine Signaling Proteins - genetics | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism | Immunological Synapses - metabolism | Interleukin-2 - genetics | Two-Hybrid System Techniques | Animals | T-Lymphocytes - cytology | Protein Binding | Mice | Receptors, Antigen, T-Cell - genetics | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - genetics | Proteasome Endopeptidase Complex - metabolism | Suppressor of Cytokine Signaling Proteins - metabolism | Binding Sites | Receptors | Immunology | Signal Transduction | Cellular Response | T Cell Receptor | Protein | Tyrosine Kinase | Processing | Protein-Protein Interactions
Journal Article
Journal of Leukocyte Biology, ISSN 0741-5400, 11/2018, Volume 104, Issue 5, pp. 1003 - 1012
Endotoxin tolerance develops in the late phase of sepsis to protect cells from an early hyperinflammatory response. Nonetheless, because it induces an...
ER stress | GSK‐3β | endotoxin tolerance | CLP | TUDCA | GSK-3β | CLEARANCE | LUNG | ACTIVATION | INFECTIONS | MACROPHAGES | GSK-3 | MECHANISMS | SEPSIS | IMMUNOLOGY | CELL BIOLOGY | IMMUNOSUPPRESSION | HEMATOLOGY | EXPRESSION | INNATE IMMUNITY
ER stress | GSK‐3β | endotoxin tolerance | CLP | TUDCA | GSK-3β | CLEARANCE | LUNG | ACTIVATION | INFECTIONS | MACROPHAGES | GSK-3 | MECHANISMS | SEPSIS | IMMUNOLOGY | CELL BIOLOGY | IMMUNOSUPPRESSION | HEMATOLOGY | EXPRESSION | INNATE IMMUNITY
Journal Article
Immune Network, ISSN 1598-2629, 2019, Volume 19, Issue 3, pp. 19 - 32
Journal Article
Blood, ISSN 0006-4971, 2009, Volume 113, Issue 20, pp. 4894 - 4902
Adhesive interactions between multiple myeloma ( MM) cells and marrow stromal cells activate multiple signaling pathways including nuclear factor kappa B...
PROGENITOR CELLS | ADHESION | IN-VITRO | BONE MICROENVIRONMENT | RECEPTOR ACTIVATOR | DRUG-RESISTANCE | PAGETS-DISEASE | STROMAL CELLS | HEMATOLOGY | HUMAN MULTIPLE-MYELOMA | KAPPA-B LIGAND | Cell Proliferation | Sequestosome-1 Protein | Stromal Cells - pathology | Humans | Middle Aged | Male | Bone Marrow - physiology | Heat-Shock Proteins - genetics | Bone Marrow - metabolism | Up-Regulation - physiology | Aged, 80 and over | Female | Osteoclasts - physiology | Heat-Shock Proteins - metabolism | Mice, Inbred C57BL | Stromal Cells - metabolism | Cells, Cultured | Mice, Transgenic | Up-Regulation - genetics | Signal Transduction - genetics | Multiple Myeloma - metabolism | Osteoclasts - metabolism | Adaptor Proteins, Signal Transducing - physiology | Multiple Myeloma - pathology | Animals | Bone Marrow - pathology | Adaptor Proteins, Signal Transducing - genetics | Environment | Signal Transduction - physiology | Aged | Mice | Adaptor Proteins, Signal Transducing - metabolism | Heat-Shock Proteins - physiology | Multiple Myeloma - genetics | Stromal Cells - cytology | Lymphoid Neoplasia
PROGENITOR CELLS | ADHESION | IN-VITRO | BONE MICROENVIRONMENT | RECEPTOR ACTIVATOR | DRUG-RESISTANCE | PAGETS-DISEASE | STROMAL CELLS | HEMATOLOGY | HUMAN MULTIPLE-MYELOMA | KAPPA-B LIGAND | Cell Proliferation | Sequestosome-1 Protein | Stromal Cells - pathology | Humans | Middle Aged | Male | Bone Marrow - physiology | Heat-Shock Proteins - genetics | Bone Marrow - metabolism | Up-Regulation - physiology | Aged, 80 and over | Female | Osteoclasts - physiology | Heat-Shock Proteins - metabolism | Mice, Inbred C57BL | Stromal Cells - metabolism | Cells, Cultured | Mice, Transgenic | Up-Regulation - genetics | Signal Transduction - genetics | Multiple Myeloma - metabolism | Osteoclasts - metabolism | Adaptor Proteins, Signal Transducing - physiology | Multiple Myeloma - pathology | Animals | Bone Marrow - pathology | Adaptor Proteins, Signal Transducing - genetics | Environment | Signal Transduction - physiology | Aged | Mice | Adaptor Proteins, Signal Transducing - metabolism | Heat-Shock Proteins - physiology | Multiple Myeloma - genetics | Stromal Cells - cytology | Lymphoid Neoplasia
Journal Article
FEBS Letters, ISSN 0014-5793, 2002, Volume 510, Issue 1, pp. 57 - 61
It has been reported that prostate apoptosis response‐4 (PAR‐4) binds to and inhibits protein kinase Cζ (PKCζ) which phosphorylates IκB kinase β (IKKβ) for...
Protein kinase Cζ | Prostate apoptosis response-4 | Ternary complex | p62 | Nuclear factor κB | Apoptosis | NFκB, nuclear factor κB | TNF, tumor necrosis factor | PKC, protein kinase C | TRAF, tumor necrosis factor receptor associated factor | PAR-4, prostate apoptosis response-4 | RIP, receptor interacting protein | IKKβ, IκB kinase β
Protein kinase Cζ | Prostate apoptosis response-4 | Ternary complex | p62 | Nuclear factor κB | Apoptosis | NFκB, nuclear factor κB | TNF, tumor necrosis factor | PKC, protein kinase C | TRAF, tumor necrosis factor receptor associated factor | PAR-4, prostate apoptosis response-4 | RIP, receptor interacting protein | IKKβ, IκB kinase β
Journal Article