Reactome | Rouault, TA

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Rouault, TA Show undefined attributes

created	[InstanceEdit:2395456] May, B, 2012-07-02
dbId	2395478
displayName	Rouault, TA
firstname	Tracey A
initial	TA
publications	[Book:6789145] Rouault, Tracey A 3110308428 Iron-Sulfur Clusters in Chemistry and Biology Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair [LiteratureReference:2520956] Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease [LiteratureReference:1362323] Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells [LiteratureReference:5690879] The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation [LiteratureReference:5690888] Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation [LiteratureReference:9854980] A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III [LiteratureReference:1362362] Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis [LiteratureReference:2520943] Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster [LiteratureReference:2520962] Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes [LiteratureReference:2395461] Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis [LiteratureReference:8878851] Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis [LiteratureReference:5690905] A regulated RNA binding protein also possesses aconitase activity [LiteratureReference:9771687] Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets [LiteratureReference:9854991] Disease-Causing SDHAF1 Mutations Impair Transfer of Fe-S Clusters to SDHB
schemaClass	Person
surname	Rouault

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