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- W2626486519 endingPage "12753" @default.
- W2626486519 startingPage "12744" @default.
- W2626486519 abstract "Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent binding to recipient proteins. In this minireview, we discuss how discovery of the role of the mammalian cytosolic aconitase, known as iron regulatory protein 1 (IRP1), led to the characterization of the function of its Fe-S cluster in sensing and regulating cellular iron homeostasis. Moreover, we present an overview of recent studies that have provided insights into the mechanism of Fe-S cluster transfer to recipient Fe-S proteins." @default.
- W2626486519 created "2017-06-23" @default.
- W2626486519 creator A5017226392 @default.
- W2626486519 creator A5080924706 @default.
- W2626486519 date "2017-08-01" @default.
- W2626486519 modified "2023-10-11" @default.
- W2626486519 title "Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways" @default.
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