Evidence map›Paper›PMID 23798678›Full record

ArticleThe Journal of biological chemistry2013

Interaction with Cfd1 increases the kinetic lability of FeS on the Nbp35 scaffold.

Leif J Pallesen, Natalia Solodovnikova, Anil K Sharma, William E Walden

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. A Chemoproteomic Approach to Monitor Native Iron-Sulfur Cluster Binding.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Review
  4. Article
  5. Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021
    Review
  6. Review
  7. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. The bacterial MrpScientific reports · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Leif J PallesenDepartment of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60612, USA.
Natalia Solodovnikova
Anil K Sharma
William E Walden
University of Illinois Chicago · US

Funding

REGULATION OF IRON METABOLISM GENES IN EUKARYOTESR01DK047281 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI WALDEN, WILLIAM EDWARD · 1995 to 2010
$2.4M
NIDDK NIH HHS DK047281NIDDK NIH HHS R01 DK047281
6 · The paper itself

Abstract

P-loop NTPases of the ApbC/Nbp35 family are involved in FeS protein maturation in nearly all organisms and are proposed to function as scaffolds for initial FeS cluster assembly. In yeast and animals, Cfd1 and Nbp35 are homologous P-loop NTPases that form a heterotetrameric complex essential for FeS protein maturation through the cytosolic FeS cluster assembly (CIA) pathway. Cfd1 is conserved in animals, fungi, and several archaeal species, but in many organisms, only Nbp35 is present, raising the question of the unique roles played by Cfd1 and Nbp35. To begin to investigate this issue, we examined Cfd1 and Nbp35 function in budding yeast. About half of each protein was detected in a heterocomplex in logarithmically growing yeast. Nbp35 readily bound (55)Fe when fed to cells, whereas (55)Fe binding by free Cfd1 could not be detected. Rapid (55)Fe binding to and release from Nbp35 was impaired by Cfd1 deficiency. A Cfd1 mutation that caused a defect in heterocomplex stability supported iron binding to Nbp35 but impaired iron release. Our results suggest a model in which Cfd1-Nbp35 interaction increases the lability of assembled FeS on the Nbp35 scaffold for transfer to target apo-FeS proteins.

Indexed as

Models, BiologicalAdenosine TriphosphatasesGTP-Binding ProteinsIronIron-Sulfur ProteinsMutationProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCfd1 protein, S cerevisiaeGTP-Binding ProteinsIronIron-Sulfur ProteinsNBP35 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsATPasesCfd1CIAIronIron MetabolismIron-Sulfur Cluster AssemblyIron-Sulfur ProteinNbp35P-loop ATPaseYeast

Identifiers

PMID23798678
PMCPMC3743505
OpenAlexW2038315768

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.