Iron−Sulfur Cluster Biosynthesis: Functional Characterization of the N- and C-Terminal Domains of Human NFU
Author:
Affiliation:
1. Evans Laboratory of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi801645z
Reference44 articles.
1. Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures
2. Iron-sulfur proteins: ancient structures, still full of surprises
3. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
4. Transfer of Sulfur from IscS to IscU during Fe/S Cluster Assembly
5. Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly
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1. Iron-sulfur protein maturation in Helicobacter pylori : identifying a Nfu-type cluster carrier protein and its iron-sulfur protein targets;Molecular Microbiology;2018-03-30
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3. Analysis of NFU ‐1 metallocofactor binding‐site substitutions—impacts on iron–sulfur cluster coordination and protein structure and function;The FEBS Journal;2017-10-16
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