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The FASEB journal, ISSN 0892-6638, 11/2005, Volume 19, Issue 13, pp. 1890 - 1892
ABSTRACTWe investigated a possible beneficial role for bilirubin, one of the products of heme degradation by the cytoprotective enzyme heme oxygenase‐1 in... 
nitric oxide | oxygen free radicals | OXIDATIVE STRESS | SUPEROXIDE | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDUCTION | BILIVERDIN | CELL BIOLOGY | SYNTHASE EXPRESSION | ANTIOXIDANT | IN-VIVO | BIOLOGY | HEME OXYGENASE-1 | SERUM BILIRUBIN | Nitric Oxide Synthase Type II - biosynthesis | Bilirubin - metabolism | Antioxidants - metabolism | Kidney - enzymology | Malondialdehyde - chemistry | NADPH Oxidases - metabolism | Male | Aorta - metabolism | Kidney - metabolism | Time Factors | Myocardium - metabolism | p38 Mitogen-Activated Protein Kinases - metabolism | Interleukin-6 - metabolism | Glutathione Peroxidase - metabolism | Free Radicals | Down-Regulation | NADPH Oxidases - antagonists & inhibitors | Enzyme Inhibitors - pharmacology | Rats | Rats, Sprague-Dawley | Blotting, Western | Nitrates - metabolism | Macrophages - metabolism | Rats, Gunn | Models, Biological | Lipopolysaccharides - chemistry | Mice | Nitric Oxide Synthase - metabolism | Blood Pressure | Jaundice - pathology | Tumor Necrosis Factor-alpha - metabolism | Nitric Oxide Synthase Type II - chemistry | Nitrites - metabolism | Shock, Septic - prevention & control | Oxygen - metabolism | Shock, Septic - metabolism | Heme - chemistry | Escherichia coli - metabolism | Shock, Septic - drug therapy | Interleukin-10 - metabolism | Aorta - enzymology | Superoxide Dismutase - metabolism | Cell Line | Bilirubin - chemistry | Models, Statistical | Homozygote | Myocardium - enzymology | Animals | Nitric Oxide - metabolism
Journal Article
Glia, ISSN 0894-1491, 2010, Volume 58, Issue 5, pp. 588 - 598
Neural injury leads to inflammation and activation of microglia that in turn may participate in progression of neurodegeneration. The mechanisms involved in... 
neurodegenerative diseases | heme oxygenase‐1 | innate immune system | Neurodegenerative diseases | Innate immune system | Heme oxygenase-1 | OXIDATIVE STRESS | ACTIVATION | ALPHA | DJ-1 | heme oxygenase-1 | NEUROSCIENCES | CELL-DEATH | TRANSCRIPTION FACTOR NRF2 | INFLAMMATION | MOUSE MODEL | THERAPEUTIC TARGET | ENHANCES SUSCEPTIBILITY | Dopamine Plasma Membrane Transport Proteins - metabolism | Tyrosine 3-Monooxygenase - metabolism | Flow Cytometry - methods | Leukocyte Common Antigens - metabolism | Reactive Oxygen Species - metabolism | Culture Media, Conditioned - pharmacology | Male | Glial Fibrillary Acidic Protein - metabolism | Brain - metabolism | MPTP Poisoning - complications | Inflammation - metabolism | Microglia - physiology | MPTP Poisoning - pathology | Antigens, Differentiation - metabolism | Neurons - metabolism | Neurons - drug effects | Dopamine - metabolism | Gliosis - etiology | Disease Models, Animal | Calcium-Binding Proteins - metabolism | Cytokines - metabolism | Neurons - chemistry | Mice, Inbred C57BL | Gene Expression Regulation - physiology | NF-E2-Related Factor 2 - deficiency | Inflammation - etiology | Mice, Knockout | Gene Expression Regulation - drug effects | Animals | Analysis of Variance | Microfilament Proteins | NF-E2-Related Factor 2 - metabolism | Cyclooxygenase 2 - metabolism | Brain - pathology | Mice | CD11b Antigen - metabolism | Cell Line, Transformed | Nitric Oxide Synthase Type II - metabolism
Journal Article
Immunity (Cambridge, Mass.), ISSN 1074-7613, 2016, Volume 44, Issue 3, pp. 492 - 504
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 0027-8424, 9/2009, Volume 106, Issue 38, pp. 16381 - 16386
We used the muscle creatine kinase (MCK) conditional frataxin knockout mouse to elucidate how frataxin deficiency alters iron metabolism... 
Up regulation | Molecules | Mitochondria | Energy metabolism | Messenger RNA | Reverse transcriptase polymerase chain reaction | Lead | Iron | Friedreich ataxia | Down regulation | Frataxin | Iron transferrin | Heme synthesis | heme synthesis | FRATAXIN EXPRESSION | HEME-SYNTHESIS | MULTIDISCIPLINARY SCIENCES | transferrin | HOMOLOG | INTERLEUKIN-6 | MATURATION | DEFICIENCY | frataxin | CLUSTER SYNTHESIS | METABOLISM | iron | MICE | PROTEINS | Heme - metabolism | Oligonucleotide Array Sequence Analysis | Friedreich Ataxia - pathology | Humans | Gene Expression Profiling | Antimicrobial Cationic Peptides - metabolism | Iron-Binding Proteins - metabolism | Friedreich Ataxia - genetics | Kidney - metabolism | Carbon-Sulfur Lyases - genetics | Hepcidins | Myocardium - metabolism | Antimicrobial Cationic Peptides - genetics | Disease Models, Animal | Friedreich Ataxia - metabolism | Liver - metabolism | Uroporphyrinogen III Synthetase - genetics | Uroporphyrinogen III Synthetase - metabolism | Mitochondria - metabolism | Coproporphyrinogen Oxidase - genetics | Reverse Transcriptase Polymerase Chain Reaction | Carbon-Sulfur Lyases - metabolism | Iron - metabolism | Blotting, Western | Mice, Knockout | Myocardium - cytology | Animals | Spleen - metabolism | Ferrochelatase - metabolism | Ferrochelatase - genetics | Iron-Binding Proteins - genetics | Mice | Coproporphyrinogen Oxidase - metabolism | Biological Sciences
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 31, pp. 12764 - 12771
Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors.... 
metalloprotein | HUMAN BOLA2 | HEME-BIOSYNTHESIS | DEOXYHYPUSINE HYDROXYLASE | BolA2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | glutaredoxin | SACCHAROMYCES-CEREVISIAE | iron metabolism | molecular chaperone | PHP4 FUNCTION | FERRITIN DEGRADATION | poly C-binding protein | IN-VIVO | GENE-EXPRESSION | iron | iron-sulfur protein | SULFUR CLUSTER | MONOTHIOL GLUTAREDOXIN | Molecular Chaperones - metabolism | Humans | Protein Multimerization | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Nuclear Receptor Coactivators - chemistry | Autophagy | Apoferritins - metabolism | Ferritins - metabolism | Cation Transport Proteins - metabolism | Apoenzymes - metabolism | Carrier Proteins - chemistry | Dimerization | Nuclear Receptor Coactivators - metabolism | Erythroid Precursor Cells - cytology | RNA-Binding Proteins - chemistry | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Models, Molecular | Apoferritins - chemistry | Iron - metabolism | Protein Transport | Animals | Carrier Proteins - metabolism | Proteins - metabolism | Models, Biological | Heterogeneous-Nuclear Ribonucleoproteins - chemistry | Apoenzymes - chemistry | Erythroid Precursor Cells - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Proteins - chemistry | Cation Transport Proteins - chemistry | Ferritins - chemistry | RNA-Binding Proteins - metabolism | iron–sulfur protein | Minireviews
Journal Article
Nature (London), ISSN 1476-4687, 2011, Volume 477, Issue 7363, pp. 225 - 228
Journal Article
Biochemical journal, ISSN 1470-8728, 2011, Volume 434, Issue 3, pp. 365 - 381
.... Iron metabolism is controlled at different... 
Ferroportin | Iron-sulfur cluster (ISC) | Transferrin receptor (TfR) | Iron-regulatory protein 2 (IRP2) | Ferritin | Iron-regulatory protein 1 (IRP1) | ferritin | iron-sulfur cluster (ISC) | transferrin receptor (TfR) | OXIDATIVE STRESS | MAMMALIAN IRON | MITOCHONDRIAL IRON | iron-regulatory protein 2 (IRP2) | HEME-SYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | iron-regulatory protein 1 (IRP1) | ferroportin | AMYLOID PRECURSOR PROTEIN | RESPONSIVE ELEMENT | TRANSFERRIN-BOUND IRON | RNA-BINDING | H-FERRITIN | HEPCIDIN EXPRESSION | Neoplasms - metabolism | Oxidation-Reduction | Response Elements | Humans | RNA, Messenger - genetics | RNA, Messenger - physiology | Mitochondria - metabolism | Iron - metabolism | Iron-Regulatory Proteins - genetics | Animals | Ferritins - metabolism | Biological Transport | Iron-Regulatory Proteins - physiology | Transferrin - metabolism | DHBA, dihydroxybenzoic acid | IRP, iron-regulatory protein | UTR, untranslated region | SLC, solute carrier | iron–sulfur cluster (ISC) | MRCKα, myotonic dystrophy kinase-related Cdc42 (cell division cycle 42)-binding kinase α | LIP, labile iron pool | Lcn2, lipocalin 2 | FLVCR, feline leukaemia virus, subgroup C, receptor | CIA, cytosolic ISC assembly | Cfd1, cytosolic Fe–S cluster-deficient protein 1 | BMP, bone morphogenetic protein | PCBP1, poly(rC)-binding protein 1 | Abcb, ATP-binding cassette, subfamily B | STAT3, signal transducer and activator of transcription 3 | SDH, succinate dehydrogenase | TfR, Tf receptor | c-aconitase, cytosolic aconitase | HIF, hypoxia-inducible factor | HO-1, haem oxygenase 1 | IRIDA, iron-refractory iron deficiency anaemia | ISC, iron–sulfur cluster | m-aconitase, mitochondrial aconitase | DMT1, divalent metal transporter 1 | Review | EBPα, CCAAT | IRE, iron-responsive element | IOP1, iron-only hydrogenase-like protein 1 | Nbp35, nucleotide-binding protein 35 | Skp1, S-phase kinase-associated protein 1 | Nfs, nitrogen fixation homologue | FBXL5, F-box and leucine-rich repeat protein 5 | ROS, reactive oxygen species | Tf, transferrin | enhancer-binding protein α | H, heavy | Isu, iron–sulfur cluster scaffold homologue | Rbx1, Ring-box 1 | β-APP, β-amyloid precursor protein | Dcytb, duodenal cytochrome b | Nar1, nuclear architecture-related protein 1 | ALAS, ALA synthase | NTBI, non-transferrin-bound iron | ALA, 5-aminolevulinic acid | Hpx, haemopexin | Cul1, Cullin 1 | Grx, glutaredoxin | ER, endoplasmic reticulum | L, light
Journal Article