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Free radical biology & medicine, ISSN 0891-5849, 2015, Volume 88, Issue Pt B, pp. 417 - 426
.... The subsequent AMPK-mediated enhancement of the Nrf2/HO-1 response... 
Xanthohumol | Nrf2 | ER stress | AMPK | HO-1 | PERK | LKB1 | MEF | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | MECHANISMS | ENERGY SENSOR | CELL DEFENSE PATHWAY | ENDOTHELIAL-CELLS | ENDOCRINOLOGY & METABOLISM | NRF2-MEDIATED INDUCTION | HEME OXYGENASE-1 | STRESS | AMP-Activated Protein Kinases - metabolism | Heme Oxygenase-1 - metabolism | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Oxidative Stress - physiology | Propiophenones - pharmacology | Mitochondria - metabolism | Mitochondria - drug effects | Receptor Cross-Talk - physiology | Blotting, Western | Animals | Flow Cytometry | Fibroblasts - drug effects | NF-E2-Related Factor 2 - metabolism | Signal Transduction - physiology | Flavonoids - pharmacology | Membrane Proteins - metabolism | Mice | Real-Time Polymerase Chain Reaction | Unfolded Protein Response - physiology | Fibroblasts - metabolism | RNA | Glycogen | Synthesis | ACC, acetyl-CoA carboxylase | CHO, Chinese hamster ovary | GSH, glutathione (reduced) | OCR, oxygen consumption rate | HO-1, heme oxygenase 1 | CaMKK, calcium calmodulin-dependent kinase kinase | Maf, small musculoaponeurotic fibrosarcoma | PERK, protein kinase RNA-like endoplasmic reticulum kinase | Xn, xanthohumol | Hrd1, synoviolin | TAK, transforming growth factor β-activated kinase | UPR, unfolded protein response | Hrd1 (HMG-CoA reductase degradation)-ubiquitin ligase | MEF, mouse embryonic fibroblasts | βTrcP1, β-transducin-repeat containing protein 1 | mTOR, mammalian target of rapamycin | ROS, reactive oxygen species | LKB1, liver kinase B1 | Keap1, Kelch-like ECH-associated protein | GSSG, oxidized glutathione | ARE, antioxidant response element | WT, wild type | GSK3β, glycogen synthase kinase 3β | Nrf2, nuclear factor E2-related factor 2 | AMPK, AMP-activated kinase | DCF, dichlorofluorescein | NADPH, nicotinamide adenine dinucleotide phosphate | DMSO, dimethyl sulfoxide | ER, endoplasmic reticulum | FCS, fetal calf serum
Journal Article
Current biology, ISSN 0960-9822, 2012, Volume 22, Issue 16, pp. R622 - R626
Journal Article
PloS one, ISSN 1932-6203, 2012, Volume 7, Issue 6, p. e39586
...), pro-apoptotic BH3 domain-only, BCL2 family members, have previously been shown to regulate ER stress-induced cell death, but the upstream signaling pathways that regulate this response in neuronal... 
MITOCHONDRIAL APOPTOSIS | TRANSCRIPTION FACTOR CHOP | UNFOLDED PROTEIN RESPONSE | INDUCED APOPTOSIS | KINASE | BIOLOGY | GENE-EXPRESSION | SYMPATHETIC NEURONS | DEATH | ENDOPLASMIC-RETICULUM STRESS | BH3-ONLY PROTEINS | Transcription Factor CHOP - genetics | Apoptosis - drug effects | Neurons - cytology | Bcl-2-Like Protein 11 | Forkhead Transcription Factors - metabolism | Telencephalon - drug effects | Tumor Suppressor Proteins - genetics | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | Neurons - metabolism | Neurons - drug effects | Proto-Oncogene Proteins c-akt - metabolism | Cell Survival - physiology | Proto-Oncogene Proteins - metabolism | Cell Survival - drug effects | Tumor Suppressor Proteins - metabolism | Telencephalon - metabolism | Telencephalon - cytology | Membrane Proteins - genetics | Proto-Oncogene Proteins - genetics | Forkhead Transcription Factors - genetics | Apoptosis Regulatory Proteins - metabolism | Animals | Signal Transduction - drug effects | Tunicamycin - pharmacology | Signal Transduction - physiology | Mice | Apoptosis - physiology | Forkhead Box Protein O3 | Transcription Factor CHOP - metabolism | Endoplasmic Reticulum Stress - physiology | Nervous system diseases | Parkinson's disease | Huntington's chorea | Neurons | Tumor proteins | Protein kinases | Apoptosis | Phosphorylation | Transcription factors | Transcription | p53 Protein | Tunicamycin | Homology | AKT protein | CCAAT/enhancer-binding protein | Kinases | Proteins | Signal transduction | Mitochondria | Cell activation | Cell growth | Cascades | Rodents | Forkhead protein | Alzheimer's disease | Movement disorders | Deoxyribonucleic acid--DNA | FOXO3 protein | Stresses | Neurodegenerative diseases | Mortality | Gene expression | Stress | Neurological diseases | Pathology | Signaling | Cell death | Endoplasmic reticulum | CHOP protein | BIM protein | Deoxyribonucleic acid | DNA
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 333, Issue 6051, pp. 1891 - 1894
The unfolded protein response (UPR) detects the accumulation of unfolded proteins in the endoplasmic reticulum (ER... 
Yeasts | Messenger RNA | Ungulates | REPORTS | Amino acids | Ligands | Dimers | Coefficients | Goods and services tax | Monomers | Unfolded protein response | IRE1P | MESSENGER-RNA | SPECIFICITY | MECHANISM | PATHWAY | MULTIDISCIPLINARY SCIENCES | BIP | ENDOPLASMIC-RETICULUM | TRANSCRIPTION FACTOR | BINDING | REVEALS | Fungal Proteins - chemistry | Membrane Glycoproteins - metabolism | Membrane Glycoproteins - chemistry | Protein Multimerization | Stress, Physiological | Endoplasmic Reticulum - metabolism | Cathepsin A - chemistry | Cathepsin A - metabolism | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Glutathione Transferase - metabolism | Mutant Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Unfolded Protein Response | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Mutant Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Conformation | Protein-Serine-Threonine Kinases - chemistry | Fluorescence Polarization | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Research | Properties | Endoplasmic reticulum | Ligands (Biochemistry) | Protein binding | Signal transduction | Membranes | Cellular biology | Kinases | Protein folding
Journal Article
Nature cell biology, ISSN 1476-4679, 2015, Volume 17, Issue 7, pp. 829 - 838
Journal Article
Antioxidants & redox signaling, ISSN 1557-7716, 2017, Volume 26, Issue 6, pp. 247 - 261
...), alters structure/function characteristics of certain targeted proteins. Our goal is to characterize how S-glutathionylation of proteins within the endoplasmic reticulum (ER... 
Forum Original Research Communications | unfolded protein response | dendritic cells | protein disulfide isomerase | endoplasmic reticulum | S-glutathionylation | glutathione S-transferases | OXIDATIVE STRESS | INDUCED APOPTOSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEPLETION | SULFIREDOXIN | REGULATOR | ENDOCRINOLOGY & METABOLISM | REDOX | MICE | TRANSCRIPTION FACTOR | EXPRESSION | Cell Line | Unfolded Protein Response - drug effects | Reactive Oxygen Species - metabolism | Endoplasmic Reticulum Stress - drug effects | Unfolded Protein Response - genetics | Calcium - metabolism | Glutathione - metabolism | Liver - metabolism | Endoplasmic Reticulum - metabolism | Glutathione Transferase - metabolism | Drug Discovery | Mice, Knockout | Protein Interaction Mapping | Protein S - metabolism | Protein Transport | Gene Expression Regulation - drug effects | Animals | Glutathione Transferase - genetics | Liver - drug effects | Protein Processing, Post-Translational - drug effects | Models, Biological | Protein Binding | Mice | Research | Protein folding | Endoplasmic reticulum | Transferases | Analysis | Glutathione | Drugs | Reactive oxygen species | Complex formation | Liver | Tunicamycin | Innovations | Cytotoxicity | Ca2+-transporting ATPase | Proteins | Thapsigargin | Calreticulin | Glutathione transferase | Bone marrow | Fibroblasts | Catalysis | Stresses | Isoenzymes | Embryo fibroblasts | Calnexin | Embryos | Stress | Sensitivity | Hepatocytes | Protein disulfide-isomerase | Protein S | Adenosine triphosphatase | Calcium (reticular) | Calcium ions | Cancer | Structure-function relationships
Journal Article