HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.
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Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesisThe role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseasesStructure of Human J-type Co-chaperone HscB Reveals a Tetracysteine Metal-binding DomainInteraction of J-Protein Co-Chaperone Jac1 with Fe–S Scaffold Isu Is Indispensable In Vivo and Conserved in EvolutionNew insights into [FeFe] hydrogenase activation and maturase functionA New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscSThe HSP70 chaperone machinery: J proteins as drivers of functional specificityFerredoxin competes with bacterial frataxin in binding to the desulfurase IscS.In silico pathway reconstruction: Iron-sulfur cluster biogenesis in Saccharomyces cerevisiae.Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster proteinGlutaredoxins: roles in iron homeostasisIron-sulfur cluster biosynthesis.Role of IscX in iron-sulfur cluster biogenesis in Escherichia coliThree hydrophobic amino acids in Escherichia coli HscB make the greatest contribution to the stability of the HscB-IscU complexSynthesis of the 2Fe subcluster of the [FeFe]-hydrogenase H cluster on the HydF scaffold.The diabetes drug target MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/iron regulatory protein 1Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold proteinTangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Nfu facilitates the maturation of iron-sulfur proteins and participates in virulence in Staphylococcus aureus.The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes.Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfuraseA bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation.Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis.ErpA, an iron sulfur (Fe S) protein of the A-type essential for respiratory metabolism in Escherichia coli.Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU).Separate FeS scaffold and carrier functions for SufB₂C₂ and SufA during in vitro maturation of [2Fe2S] FdxFluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.The Human Iron-Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor MoleculesFrataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly ComplexSpectroscopic and functional characterization of iron-sulfur cluster-bound forms of Azotobacter vinelandii (Nif)IscA.Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters.Iron binding activity is essential for the function of IscA in iron-sulphur cluster biogenesisMonothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking.In vivo iron-sulfur cluster formation.Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulationSalmonella enterica requires ApbC function for growth on tricarballylate: evidence of functional redundancy between ApbC and IscU[2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin.Bacterial ApbC can bind and effectively transfer iron-sulfur clusters.Escherichia coli FtnA acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stressThe Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions.
P2860
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P2860
HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
HscA and HscB stimulate [2Fe-2 ...... in an ATP-dependent reaction.
@en
type
label
HscA and HscB stimulate [2Fe-2 ...... in an ATP-dependent reaction.
@en
prefLabel
HscA and HscB stimulate [2Fe-2 ...... in an ATP-dependent reaction.
@en
P2860
P356
P1433
P1476
HscA and HscB stimulate [2Fe-2 ...... in an ATP-dependent reaction.
@en
P2093
Kala Chandramouli
Michael K Johnson
P2860
P304
11087-11095
P356
10.1021/BI061237W
P407
P577
2006-09-01T00:00:00Z