Iron−Sulfur Cluster Biosynthesis: Characterization of a Molten Globule Domain in 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/bi9002524
Reference30 articles.
1. Identification of human and mouse HIRA-interacting protein-5 (HIRIP5), two mammalian representatives in a family of phylogenetically conserved proteins with a role in the biogenesis of Fe/S proteins
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3. HIRA, a mammalian homologue of Saccharomyces cerevisiae transcriptional co-repressors, interacts with Pax3
4. The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain
5. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
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3. Regulation of human Nfu activity in Fe‐S cluster delivery—characterization of the interaction between Nfu and theHSPA9/Hsc20 chaperone complex;The FEBS Journal;2017-12-29
4. 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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