The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Iron–sulfur-protein biogenesis in eukaryotes
Open accessAbstract
Iron-sulfur (Fe-S) clusters (ISCs) are versatile, ancient co-factors of proteins that are involved in electron transport, enzyme catalysis and regulation of gene expression. The synthesis of ISCs and their insertion into apoproteins involves the function of complex cellular machineries. In eukaryotes, the mitochondrial ISC-assembly machinery is involved in the maturation of all cellular iron-sulfur proteins. A mitochondrial export machinery and a recently discovered cytosolic assembly system specifically participate in the maturation of cytosolic and nuclear iron-sulfur proteins. Of the approximately 20 assembly components, more than ten are encoded by essential genes, which indicates that the process is indispensable for life. Mutations in two of the assembly components lead to neurological diseases. The essential character of Fe-S-protein biogenesis in eukaryotes and its importance for human disease identifies this evolutionary ancient process as one of the most important biosynthetic pathways of life.
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Cites
Iron-sulfur clusters: nature's modular, multipurpose structures
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Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
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Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae
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Cited by
Function and biogenesis of iron-sulphur proteins
Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167
Self-citationThe role of iron regulatory proteins in mammalian iron homeostasis and disease
Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055
Eukaryotic evolution, changes and challenges
Embley, T. M., & Martin, W. (2006) · Nature · doi:10.1038/nature04546 · Cited by 867
Gould, S. B., Waller, R. F., & McFadden, G. I. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.59.032607.092915 · Cited by 634
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624
Metadata
- Authors
- Lill, R., & Mühlenhoff, U.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2005-03
- Volume
- 30
- Issue
- 3
- Pages
- 133-141
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2006756678
- Cited by
- 333
- References
- 6
- FWCI
- 3.48
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.