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The Journal of biological chemistry, ISSN 1083-351X, 08/2017, Volume 292, Issue 31, pp. 12754 - 12763
..., and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 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 | Index Medicus | acyl carrier protein (ACP) | cysteine desulfurase | ferredoxin | metal biology | chaperone | fatty acid metabolism | Minireviews | lipoic acid | glutaredoxin | mitochondrial disease | frataxin
Journal Article
Biochemistry (Easton), ISSN 0006-2960, 10/2009, Volume 48, Issue 40, pp. 9569 - 9581
...) and the BolA homologue Fra2. However, the interactions between these proteins and the iron-dependent mechanism by which they control Aft1 localization are unclear... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Saccharomyces cerevisiae - genetics | Iron-Sulfur Proteins - genetics | Multiprotein Complexes - genetics | Saccharomyces cerevisiae Proteins - biosynthesis | Histidine - metabolism | Iron-Sulfur Proteins - chemistry | Oxidoreductases - chemistry | Cysteine - genetics | Multiprotein Complexes - biosynthesis | Glutaredoxins - chemistry | Glutaredoxins - genetics | Iron-Sulfur Proteins - biosynthesis | Cysteine - metabolism | Enzyme Stability - genetics | Dimerization | Intracellular Signaling Peptides and Proteins - genetics | Oxidoreductases - biosynthesis | Gene Expression Regulation, Fungal | Mutagenesis, Site-Directed | Oxidoreductases - genetics | Histidine - genetics | Signal Transduction - genetics | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Gene Expression Regulation, Enzymologic | Multiprotein Complexes - chemistry | Glutaredoxins - biosynthesis | Intracellular Signaling Peptides and Proteins - chemistry | Saccharomyces cerevisiae - enzymology | Ligands | Saccharomyces cerevisiae Proteins - chemistry | Escherichia coli | Analysis | Physiological aspects | Oxidation-reduction reaction | Genetic aspects | Iron in the body | Chemical properties | Genetic transcription | Gene expression | Brewer's yeast | Index Medicus
Journal Article
Journal of Bacteriology, ISSN 0021-9193, 03/2009, Volume 191, Issue 5, pp. 1490 - 1497
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
Life Sciences & Biomedicine | Microbiology | Science & Technology | Archaeal Proteins - isolation & purification | Archaeal Proteins - chemistry | Bacterial Proteins - chemistry | Iron-Sulfur Proteins - genetics | Methanococcus - chemistry | Molecular Sequence Data | Iron-Sulfur Proteins - chemistry | GTP-Binding Proteins - genetics | Genetic Complementation Test | Methanococcus - genetics | Sulfolobus - genetics | Archaeal Proteins - genetics | Sulfolobus - metabolism | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | GTP-Binding Proteins - chemistry | Bacterial Proteins - genetics | Adenosine Triphosphatases - metabolism | Iron-Sulfur Proteins - isolation & purification | Saccharomyces cerevisiae Proteins - genetics | Sequence Homology, Amino Acid | Methanococcales - genetics | Sequence Alignment | Sulfolobus - chemistry | Methanococcales - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Methanococcus - metabolism | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Adenosine Triphosphatases - genetics | Iron-Sulfur Proteins - metabolism | Methanococcales - chemistry | Mutation | GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Genetic aspects | Chemical properties | Carrier proteins | Properties | Bacterial proteins | Archaeabacteria | Proteins | Eukaryotes | Bacteria | Iron | Biochemistry | Sulfur | Bacteriology | Index Medicus | Enzymes and Proteins
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 | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Cell Biology | 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 | Index Medicus | iron-sulfur cluster
Journal Article
PloS one, ISSN 1932-6203, 02/2010, Volume 5, Issue 2, pp. e9225 - e9225
The twin-arginine translocation (Tat) pathway is well known for its ability to export fully folded substrate proteins out of the cytoplasm of Gram-negative and Gram-positive bacteria... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Molecular Chaperones - metabolism | Protein Multimerization | Iron-Sulfur Proteins - genetics | Substrate Specificity | Recombinant Fusion Proteins - metabolism | Flow Cytometry | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Membrane Transport Proteins - metabolism | Luminescent Measurements - instrumentation | Oxidoreductases - metabolism | Signal Transduction | Oxidoreductases - genetics | Molecular Chaperones - genetics | Escherichia coli Proteins - metabolism | Binding Sites - genetics | Luminescent Measurements - methods | Blotting, Western | Membrane Transport Proteins - chemistry | Protein Transport | Carrier Proteins - genetics | Carrier Proteins - metabolism | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Luminescent Proteins - genetics | Iron-Sulfur Proteins - metabolism | Mutation | Escherichia coli Proteins - chemistry | Luminescent Proteins - metabolism | International trade | Arginine | Analysis | Escherichia coli | Fluorescence | Protein-protein interactions | Membrane proteins | Peptides | Laboratories | Dimethyl sulfoxide reductase | Genes | Gram-positive bacteria | Translocase | Chaperones | Proteins | E coli | Proofreading | Bacteria | Chimeras | Protein transport | Biomedical engineering | Translocation | Enzymes | Yellow fluorescent protein | Cloning | Molybdenum | Substrates | Exports | Mutagenesis | Integrals | Dimethyl sulfoxide | TATB | Protein interaction | Binding sites | Cytoplasm | Index Medicus
Journal Article
The New England journal of medicine, ISSN 1533-4406, 05/2002, Volume 346, Issue 19, pp. 1459 - 1466
Journal Article
Journal of clinical oncology, ISSN 1527-7755, 12/2005, Volume 23, Issue 34, pp. 8812 - 8818
Journal Article