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1982, ISBN 9780471077381, Volume 4., x, 434
Book
Biochemical Journal, ISSN 0264-6021, 01/2010, Volume 425, Issue 1, pp. 207 - 214
Oxygen-evolving chloroplasts possess their own iron-sulfur cluster assembly proteins including members of the SUF (Sulfur mobilization) and the NFU family.... 
Arabidopsis thaliana | Iron-sulfur cluster assembly | Scaffold protein | High chlorophyll fluorescence 101 (HCF101) | Chloroplast | [4Fe-4S]-cluster-containing P-loop NTPase (FSC-NTPase) | ARABIDOPSIS-THALIANA | IRON-SULFUR-PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | iron-sulfur cluster assembly | chloroplast | GENE-CLUSTER | BIOGENESIS | NBP35 | BACTERIAL APBC | BIOSYNTHESIS | CYSTEINE DESULFURASE CPNIFS | scaffold protein | AZOTOBACTER-VINELANDII | PHOTOSYSTEM-I | high chlorophyll fluorescence 101 (HCF101) | Recombinant Proteins - metabolism | Arabidopsis Proteins - genetics | Arabidopsis - enzymology | Mutagenesis, Site-Directed | Oxidoreductases - metabolism | Oxidoreductases - genetics | Saccharomyces cerevisiae - genetics | Iron-Sulfur Proteins - genetics | Mitochondria - metabolism | Spectrophotometry - methods | Binding Sites - genetics | Electron Spin Resonance Spectroscopy - methods | Chloroplasts - metabolism | Arabidopsis - metabolism | Cysteine - genetics | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Escherichia coli - genetics | Protein Binding | Cysteine - metabolism | Iron-Sulfur Proteins - metabolism | Mutation | Index Medicus | ISC, iron-sulfur cluster | WT, wild-type | APO1, accumulation of Photosystem I 1 | PSI, Photosystem I | NFS1, NifS-like | FSC-NTPase, [4Fe-4S]-cluster-containing P-loop NTPase | DTT, dithiothreitol | SUF, sulfur mobilization | HCF101, high chlorophyll fluorescence 101 | FTR, ferredoxin-thioredoxin reductase | Nbp35, nucleotide-binding protein 35 | IPTG, isopropyl β-D-thiogalactoside | Ind1, iron-sulfur protein required for NADH dehydrogenase 1 | NIF, nitrogen fixation | Cfd1, cytosolic iron-sulfur cluster deficient 1 | S, iron-sulfur | DUF, domain of unknown function
Journal Article
Journal Article
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 2005, Volume 74, Issue 1, pp. 247 - 281
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 04/2013, Volume 587, Issue 8, pp. 1172 - 1179
► IscU is a metamorphic protein that converts between two folds: S and D. ► IscU adopts the D-state when interacting with IscS to pick up sulfur. ► Holo-IscU... 
Protein evolution | Peptidyl–prolyl peptide bond isomerization | Metamorphic protein | Conformational equilibrium | Protein–protein interaction | Iron–sulfur cluster | cysteine desulfurase | DnaK-type chaperone | DnaJ-type co-chaperone | HscB | HscA | ADP | nuclear magnetic resonance | scaffold protein for Fe–S cluster biosynthesis and delivery | NMR | PLP | pyridoxal 5′-phosphate | adenosine diphosphate | adenosine triphosphate | apo-form of the iron–sulfur scaffold protein | IscS | ATP | IscU | Iron-sulfur cluster | Peptidyl-prolyl peptide bond isomerization | Protein-protein interaction | ASSEMBLY PROTEIN | DISORDERED FORM | CRYSTAL-STRUCTURE | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | HSCA | CELL BIOLOGY | THERMOTOGA-MARITIMA ISCU | CYSTEINE DESULFURASE | SUBSTRATE-BINDING | BIOPHYSICS | 2FE-2S CLUSTER | Amino Acid Sequence | Sulfur - metabolism | Iron-Sulfur Proteins - genetics | Models, Molecular | Molecular Sequence Data | Escherichia coli Proteins - metabolism | Iron-Sulfur Proteins - chemistry | Iron - metabolism | Sequence Homology, Amino Acid | Escherichia coli - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Protein Conformation | Iron-Sulfur Proteins - metabolism | Escherichia coli Proteins - chemistry | Hydrogen-Ion Concentration | Cysteine | Iron compounds | Peptides | Isomerization | Physiological aspects | Iron | Muscle proteins | Sulfur | Adenosine triphosphate | Adenosine triphosphatase | Protein binding
Journal Article