Evidence map›Paper›PMID 11060020›Full record

ArticleThe EMBO journal2000

Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells.

W H Tong, T Rouault

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
14.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

87 citing papers in PubMed, 192 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
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  6. Construction of novel π-bridged fluorescent probes for FeAnalytical and bioanalytical chemistry · 2024
    Article
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  17. Review
  18. Article
  19. Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
  20. Fe-S cluster assembly in the supergroup Excavata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

W H TongNational Institute of Child Health and Human Development, Cell Biology and Metabolism Branch, Bethesda, MD 20892, USA. trou@helix.nih.gov
T Rouault
Eunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Regulation Of Intracellular Iron MetabolismZIAHD001602 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ROUAULT, TRACEY A. · 2009 to 2025
$21.8M
REGULATION OF INTRACELLULAR IRON METABOLISMZ01HD001602 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ROUAULT, TRACEY A. · 1985 to 2008
$2.3M
6 · The paper itself

Abstract

Iron-sulfur (Fe-S) clusters are cofactors found in many proteins that have important redox, catalytic or regulatory functions. In mammalian cells, almost all known Fe-S proteins are found in the mitochondria, but at least one is found in the cytosol. Here we report cloning of the human homologs to IscU and NifU, iron-binding proteins that play a critical role in Fe-S cluster assembly in bacteria. In human cells, alternative splicing of a common pre-mRNA results in synthesis of two proteins that differ at the N-terminus and localize either to the cytosol (IscU1) or to the mitochondria (IscU2). Biochemical analyses demonstrate that IscU proteins specifically associate with IscS, a cysteine desulfurase that is proposed to sequester inorganic sulfur for Fe-S cluster assembly. Protein complexes containing IscU and IscS can be found in the mitochondria as well as in the cytosol, implying that Fe-S cluster assembly takes place in multiple subcellular compartments in mammalian cells. The possible roles of the IscU proteins in mammalian cells and the potential implications of compartmentalization of Fe-S cluster assembly are discussed.

Indexed as

Escherichia coli ProteinsAlternative SplicingAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCarbon-Sulfur LyasesCell CompartmentationCloning, MolecularCOS CellsCytosolDNAGene ExpressionHumansIron-Sulfur ProteinsMitochondriaBacterial ProteinsCarbon-Sulfur Lyasescysteine desulfuraseDNAEscherichia coli ProteinsIron-Sulfur ProteinsIscU protein, E coliNifU protein, Bacteria

Identifiers

PMID11060020
PMCPMC305809
OpenAlexW2006178088

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.