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The Journal of biological chemistry, ISSN 1083-351X, 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 functions, including genome maintenance, protein translation, energy conversion... 
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
Nature (London), ISSN 1476-4687, 2010, Volume 468, Issue 7325, pp. 790 - 795
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2017, Volume 292, Issue 31, pp. 12764 - 12771
.... Iron cofactors include heme, iron-sulfur clusters, and simple iron ions. Poly(rC)-binding proteins are multifunctional adaptors that serve as iron ion chaperones... 
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 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
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 33, pp. 13879 - 13889
Viperin (RSAD2) is an interferon-stimulated antiviral protein that belongs to the radical S-adenosylmethionine (SAM) enzyme family... 
REPLICATION | HEPATITIS-C VIRUS | BIOGENESIS | DNA METABOLISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | WEST NILE VIRUS | MMS19 | IDENTIFICATION | MATURATION | AMPHIPATHIC ALPHA-HELIX | INHIBIT | Apoproteins - chemistry | Immunoprecipitation | Transcription Factors - chemistry | Humans | Iron-Sulfur Proteins - genetics | Iron-Sulfur Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Metallochaperones - chemistry | RNA Interference | HEK293 Cells | Carrier Proteins - chemistry | Protein Interaction Domains and Motifs | Metallochaperones - antagonists & inhibitors | Nuclear Proteins - genetics | Peptide Fragments - genetics | Apoproteins - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Iron - chemistry | Carrier Proteins - antagonists & inhibitors | Recombinant Proteins - chemistry | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Recombinant Fusion Proteins - chemistry | Transcription Factors - genetics | Nuclear Proteins - chemistry | Iron - metabolism | Metallochaperones - genetics | Proteins - genetics | Transcription Factors - metabolism | Carrier Proteins - genetics | Iron Radioisotopes | Peptide Fragments - chemistry | Carrier Proteins - metabolism | Proteins - metabolism | Models, Biological | Nuclear Proteins - antagonists & inhibitors | Apoproteins - genetics | Iron-Sulfur Proteins - metabolism | Metallochaperones - metabolism | Mutation | Proteins - chemistry | Amino Acid Substitution | iron–sulfur protein | molecular cell biology | metal biology | iron | sulfur | Cia targeting complex | viperin | biogenesis | interferon | Cell Biology
Journal Article
FEBS Letters, ISSN 0014-5793, 12/2016, Volume 590, Issue 24, pp. 4531 - 4540
.... The mechanism of Fe–S cluster biogenesis involves multiple proteins in a complex pathway. Cluster biosynthesis primarily occurs in the mitochondria, but key Fe... 
[2Fe‐2S] cluster transfer | iron–sulfur cluster | Nfu | glutaredoxin | IscU | [2Fe-2S] cluster transfer | HUMAN NFU | iron-sulfur cluster | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN BIOGENESIS | MATURATION | SACCHAROMYCES-CEREVISIAE | 4FE-4S CLUSTER | CELL BIOLOGY | MONOTHIOL GLUTAREDOXINS | BIOPHYSICS | BIOSYNTHESIS | 2FE-2S CLUSTER | SCAFFOLD PROTEIN | Apoproteins - chemistry | Humans | Bacterial Proteins - chemistry | Iron-Sulfur Proteins - genetics | Iron-Sulfur Proteins - chemistry | Oxidoreductases - chemistry | Saccharomyces cerevisiae - metabolism | Biological Transport | Escherichia coli - metabolism | Carrier Proteins - chemistry | Thermotoga maritima - chemistry | Thermotoga maritima - metabolism | Apoproteins - metabolism | Sulfur - chemistry | Recombinant Proteins - metabolism | Sulfur - metabolism | Gene Expression | Oxidoreductases - metabolism | Oxidoreductases - genetics | Iron - chemistry | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Iron - metabolism | Saccharomyces cerevisiae - chemistry | Cytosol - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Apoproteins - genetics | Bacterial Proteins - metabolism | Cytosol - metabolism | Iron-Sulfur Proteins - metabolism | Kinetics | Saccharomyces cerevisiae Proteins - chemistry
Journal Article
Nature chemical biology, ISSN 1552-4469, 2010, Volume 6, Issue 10, pp. 758 - 765
Journal Article
Nature (London), ISSN 1476-4687, 2012, Volume 482, Issue 7386, pp. 501 - 506
Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling... 
THERMOCOCCUS-KODAKARAENSIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | NO-GO DECAY | X-RAY-STRUCTURE | FREE PROTEIN-SYNTHESIS | ELECTRON-MICROSCOPY | MESSENGER-RNA DECAY | TRANSLATION TERMINATION | ATP-BINDING | 80S RIBOSOME | Endoribonucleases - chemistry | Pyrococcus furiosus - chemistry | Pyrococcus furiosus - metabolism | Ribosomes - metabolism | Iron-Sulfur Proteins - chemistry | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Multiprotein Complexes - metabolism | ATP-Binding Cassette Transporters - chemistry | ATP-Binding Cassette Transporters - metabolism | Protein Stability | Protein Structure, Tertiary | Movement | Endoribonucleases - metabolism | Cell Cycle Proteins - metabolism | Ribosomes - chemistry | Models, Molecular | Nuclear Proteins - metabolism | Nuclear Proteins - chemistry | Peptide Termination Factors - metabolism | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | Multiprotein Complexes - chemistry | Ribosomes - ultrastructure | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Iron-Sulfur Proteins - metabolism | Peptide Termination Factors - chemistry | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Eukaryotes | Ribosomes | Physiological aspects | Protein biosynthesis | Research | Structure | Archaeabacteria | Proteins | Ribonucleic acid--RNA | Transfer RNA
Journal Article
Journal Article