Evidence map›Paper›PMID 29349662›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2018

Roles and maturation of iron-sulfur proteins in plastids.

Jonathan Przybyla-Toscano, Mélanie Roland, Frédéric Gaymard, Jérémy Couturier, Nicolas Rouhier

Erratum issuedOpen access · hybridAbstract readReview
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Iron and the Intestinal Microbiome.Advances in experimental medicine and biology · 2025
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. TheeLife · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. ThePlant direct · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Jonathan Przybyla-ToscanoUniversité de Lorraine, Interactions Arbres-Microorganismes, UMR1136, 54500, Vandoeuvre-lès-Nancy, France.
Mélanie RolandUniversité de Lorraine, Interactions Arbres-Microorganismes, UMR1136, 54500, Vandoeuvre-lès-Nancy, France.
Frédéric GaymardBiochimie et Physiologie Moléculaire des Plantes, CNRS/INRA/Université Montpellier 2, SupAgro Campus, 34060, Montpellier, France.
Jérémy CouturierUniversité de Lorraine, Interactions Arbres-Microorganismes, UMR1136, 54500, Vandoeuvre-lès-Nancy, France.
Nicolas RouhierUniversité de Lorraine, Interactions Arbres-Microorganismes, UMR1136, 54500, Vandoeuvre-lès-Nancy, France. nicolas.rouhier@univ-lorraine.fr.
Interactions Arbres-Microorganismes · FRUniversité de Lorraine · FRInstitut des Sciences des Plantes de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One reason why iron is an essential element for most organisms is its presence in prosthetic groups such as hemes or iron-sulfur (Fe-S) clusters, which are notably required for electron transfer reactions. As an organelle with an intense metabolism in plants, chloroplast relies on many Fe-S proteins. This includes those present in the electron transfer chain which will be, in fact, essential for most other metabolic processes occurring in chloroplasts, e.g., carbon fixation, nitrogen and sulfur assimilation, pigment, amino acid, and vitamin biosynthetic pathways to cite only a few examples. The maturation of these Fe-S proteins requires a complex and specific machinery named SUF (sulfur mobilisation). The assembly process can be split in two major steps, (1) the de novo assembly on scaffold proteins which requires ATP, iron and sulfur atoms, electrons, and thus the concerted action of several proteins forming early acting assembly complexes, and (2) the transfer of the preformed Fe-S cluster to client proteins using a set of late-acting maturation factors. Similar machineries, having in common these basic principles, are present in the cytosol and in mitochondria. This review focuses on the currently known molecular details concerning the assembly and roles of Fe-S proteins in plastids.

Indexed as

IronIron-Sulfur ProteinsPlastidsSulfurIronIron-Sulfur ProteinsSulfurBiogenesisElectron transferIron–sulfur proteinsPhotosynthesisPlastids

Identifiers

PMID29349662
PMCPMC6006212
OpenAlexW2788316538

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.