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Antioxidants and Redox Signaling, ISSN 1523-0864, 07/2005, Volume 7, Issue 7-8, pp. 919 - 929
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 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
Biochemical Journal, ISSN 0264-6021, 03/2011, Volume 434, Issue 3, pp. 365 - 381
Iron is an essential but potentially hazardous biometal. Mammalian cells require sufficient amounts of iron to satisfy metabolic needs or to accomplish... 
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
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 12/2016, Volume 101, pp. 334 - 347
AMPK dysregulation contributes to the onset and development of type 2 diabetes (T2DM). AMPK is known to be activated by reactive oxygen species (ROS) and... 
Type 2 diabetes | Glucose metabolism | AMPK | Glutathionylation | Glutaredoxins | ROS | OXIDATIVE STRESS | RAT | MECHANISM | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PREVENTS | INHIBITION | OXIDASE | IN-VIVO | ENDOCRINOLOGY & METABOLISM | RESISTANCE | ENERGY-METABOLISM | AMP-Activated Protein Kinases - metabolism | Liver - pathology | Epithelial Cells - metabolism | Reactive Oxygen Species - metabolism | Streptozocin | Humans | Diet, High-Fat - adverse effects | Male | Diabetes Mellitus, Type 2 - metabolism | Hepatocytes - metabolism | Protein Subunits - metabolism | Reactive Oxygen Species - agonists | Hepatocytes - cytology | Diabetes Mellitus, Experimental - prevention & control | Glycogen - metabolism | HEK293 Cells | Glutaredoxins - genetics | Diabetes Mellitus, Experimental - metabolism | Epithelial Cells - cytology | Protein Subunits - genetics | Cell Line | Glutaredoxins - metabolism | Oxidation-Reduction | Signal Transduction | Liver - metabolism | Gene Expression Regulation | Rats | Rats, Sprague-Dawley | Reactive Oxygen Species - antagonists & inhibitors | Animals | Diabetes Mellitus, Experimental - etiology | Diabetes Mellitus, Experimental - pathology | Glucose - metabolism | Diabetes Mellitus, Type 2 - pathology | AMP-Activated Protein Kinases - genetics | Antioxidants | Synthesis | Glycogen | Physiological aspects | Development and progression | Hypoglycemic agents | Glucose | Dextrose | Oxidases | Cysteine | Isoenzymes | Transmission electron microscopes | Superoxide | Glucose tolerance tests | Hyperglycemia | High performance liquid chromatography
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12754 - 12763
The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular... 
4FE-4S CLUSTERS | acyl carrier protein (ACP) | cysteine desulfurase | fatty acid metabolism | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOTHIOL GLUTAREDOXINS FUNCTION | FUNCTIONAL-CHARACTERIZATION | glutaredoxin | mitochondrial disease | frataxin | ACYL CARRIER PROTEIN | ferredoxin | metal biology | chaperone | INTERACTING PROTEIN | ASSEMBLY MACHINERY | AZOTOBACTER-VINELANDII (NIF)ISCA | FE-S PROTEINS | SCAFFOLD PROTEIN | lipoic acid | Mitochondria - enzymology | Adrenodoxin - genetics | Species Specificity | Humans | Protein Multimerization | Adrenodoxin - metabolism | Iron-Sulfur Proteins - genetics | Iron-Binding Proteins - chemistry | Mitochondrial Proteins - genetics | Iron-Sulfur Proteins - chemistry | Iron-Binding Proteins - metabolism | Mitochondrial Proteins - metabolism | Apoenzymes - metabolism | Sulfurtransferases - chemistry | Acyl Carrier Protein - metabolism | Models, Molecular | Sulfurtransferases - genetics | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Protein Folding | Protein Transport | Gene Expression Regulation, Enzymologic | Acyl Carrier Protein - chemistry | Animals | Models, Biological | Acyl Carrier Protein - genetics | Apoenzymes - genetics | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Apoenzymes - chemistry | Adrenodoxin - chemistry | Iron-Binding Proteins - genetics | Protein Conformation | Iron-Sulfur Proteins - metabolism | Sulfurtransferases - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Minireviews
Journal Article
Journal Article
European Journal of Pharmacology, ISSN 0014-2999, 03/2006, Volume 533, Issue 1-3, pp. 222 - 239
Journal Article