Evidence map›Paper›PMID 32337520›Full record

ArticleMetallomics : integrated biometal science2020

Defining the mechanism of the mitochondrial Atm1p [2Fe-2S] cluster exporter.

Stephen A Pearson, Christine Wachnowsky, J A Cowan

Open access · greenAbstract read
In one paragraph

Article in Metallomics : integrated biometal science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  4. Review
  5. Yeast Mitochondria Import Aqueous FeJournal of the American Chemical Society · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)Archives of biochemistry and biophysics · 2021
    Article
  16. Review
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

3 authors at 1 institution in 1 country.

Stephen A PearsonThe Ohio State University Biophysics Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio, USA43210. cowan.2@osu.edu.
Christine WachnowskyThe Ohio State University Biochemistry Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio, USA43210.
J A CowanThe Ohio State University Biophysics Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio, USA43210. cowan.2@osu.edu and The Ohio State University Biochemistry Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio, USA43210 and Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio, USA43210.ORCID 0000-0002-4686-6825
The Ohio State University · US

Funding

Novel Therapeutic Approaches to Pathogen InactivationR21AI072443 · NIAID · OHIO STATE UNIVERSITY · PI COWAN, JAMES A · 2009 to 2010
$398k
NIAID NIH HHS R21 AI072443
6 · The paper itself

Abstract

Iron-sulfur cluster proteins play key roles in a multitude of physiological processes; including gene expression, nitrogen and oxygen sensing, electron transfer, and DNA repair. Biosynthesis of iron-sulfur clusters occurs in mitochondria on iron-sulfur cluster scaffold proteins in the form of [2Fe-2S] cores that are then transferred to apo targets within metabolic or respiratory pathways. The mechanism by which cytosolic Fe-S cluster proteins mature to their holo forms remains controversial. The mitochondrial inner membrane protein Atm1p can transport glutathione-coordinated iron-sulfur clusters, which may connect the mitochondrial and cytosolic iron-sulfur cluster assembly systems. Herein we describe experiments on the yeast Atm1p/ABCB7 exporter that provide additional support for a glutathione-complexed cluster as the natural physiological substrate and a reflection of the endosymbiotic model of mitochondrial evolution. These studies provide insight on the mechanism of cluster transport and the molecular basis of human disease conditions related to ABCB7. Recruitment of MgATP following cluster binding promotes a structural transition from closed to open conformations that is mediated by coupling helices, with MgATP hydrolysis facilitating the return to the closed state.

Indexed as

ATP-Binding Cassette TransportersElectron TransportGlutathioneHumansIron-Sulfur ProteinsLiposomesMitochondriaMutagenesis, Site-DirectedProteolipidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATM1 protein, S cerevisiaeATP-Binding Cassette TransportersGlutathioneIron-Sulfur ProteinsLiposomesProteolipidsproteoliposomesSaccharomyces cerevisiae Proteins

Identifiers

PMID32337520
PMCPMC7369126
OpenAlexW3015721092

What OpenQuestion holds

Textmetadata
LicenceTDM
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.