Evidence map›Paper›PMID 30201724›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins.

Oliver Stehling, Jae-Hun Jeoung, Sven A Freibert, Viktoria D Paul, Sebastian Bänfer, Brigitte Niggemeyer, Ralf Rösser, Holger Dobbek, Roland Lill

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021
    Review
  14. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
  15. Article
  16. Article
  17. Article
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

9 authors.

Oliver StehlingInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany.
Jae-Hun JeoungInstitut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.
Sven A FreibertInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany.ORCID 0000-0002-8521-2963
Viktoria D PaulInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany.
Sebastian BänferInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany.
Brigitte NiggemeyerInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany.
Ralf RösserInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany.
Holger DobbekInstitut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany.ORCID 0000-0002-4122-3898
Roland LillInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, 35033 Marburg, Germany; Lill@staff.uni-marburg.de.ORCID 0000-0002-8345-6518

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maturation of iron-sulfur (Fe-S) proteins in eukaryotes requires complex machineries in mitochondria and cytosol. Initially, Fe-S clusters are assembled on dedicated scaffold proteins and then are trafficked to target apoproteins. Within the cytosolic Fe-S protein assembly (CIA) machinery, the conserved P-loop nucleoside triphosphatase Nbp35 performs a scaffold function. In yeast, Nbp35 cooperates with the related Cfd1, which is evolutionary less conserved and is absent in plants. Here, we investigated the potential scaffold function of human CFD1 (NUBP2) in CFD1-depleted HeLa cells by measuring Fe-S enzyme activities or

Indexed as

Amino Acid MotifsApoproteinsCatalytic DomainChaetomiumCrystallography, X-RayFungal ProteinsGTP-Binding ProteinsHeLa CellsHumansIron Regulatory Protein 1Iron-Sulfur ProteinsApoproteinsFungal ProteinsGTP-Binding ProteinsIron Regulatory Protein 1Iron-Sulfur ProteinsCIA machineryiron homeostasisiron-sulfur proteinNBP35NUBP1-NUBP2

Identifiers

PMID30201724
PMCPMC6166825

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.