Evidence map›Paper›PMID 22152479›Full record

ArticleMolecular cell2011

Regulation of ribonucleotide reductase in response to iron deficiency.

Nerea Sanvisens, M Carmen Bañó, Mingxia Huang, Sergi Puig

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

53 citing papers in PubMed, 92 citations in OpenAlex.

  1. Trial
  2. Article
  3. Iron-Based Nanoparticles as Delivery Tools.Pharmaceuticals (Basel, Switzerland) · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Iron, Copper, and Selenium: Cancer's Thing for Redox Bling.Cold Spring Harbor perspectives in medicine · 2024
    Review
  18. Review
  19. Iron necessity for chlamydospore germination in Fusarium oxysporum f. sp. cubense TR4.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Nerea SanvisensDepartamento de Biotecnología, Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas, Burjassot, Valencia 46100, Spain.
M Carmen Bañó
Mingxia Huang
Sergi Puig
Consejo Superior de Investigaciones Científicas · ESUniversitat de València · ESUniversity of Colorado Denver · US

Funding

Ribonucleotide Reductase Regulation: Diferric Y* assembly/maintenance and Sml1R01GM081393 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI STUBBE, JOANNE · 2008 to 2016
$3.9M
In Vivo Regulation and Inhibition of Ribonucleotide ReductaseR01CA125574 · NCI · UNIVERSITY OF COLORADO DENVER · PI HUANG, MINGXIA · 2008 to 2012
$1.6M
NCI NIH HHS CA125574NCI NIH HHS R01 CA125574NIGMS NIH HHS GM081393NIGMS NIH HHS R01 GM081393
6 · The paper itself

Abstract

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2-Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the redistribution of the Rnr2-Rnr4 heterodimer to the cytoplasm, where it assembles as an active RNR complex and increases deoxyribonucleoside triphosphate levels. When iron is scarce, yeast selectively optimizes RNR function at the expense of other non-essential iron-dependent processes that are repressed, to allow DNA synthesis and repair.

Indexed as

Iron DeficienciesCell Cycle ProteinsCell NucleusCheckpoint Kinase 2CytoplasmDNA-Binding ProteinsGene Expression Regulation, FungalHumansIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesProtein SubunitsProtein TransportRepressor ProteinsResponse ElementsRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesCell Cycle ProteinsCheckpoint Kinase 2CTH1 protein, S cerevisiaeDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeProtein Serine-Threonine KinasesProtein SubunitsRAD53 protein, S cerevisiaeRepressor ProteinsRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesRNA-Binding ProteinsRNA, FungalRNA, MessengerRNR2 protein, S cerevisiaeRnr4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTIS11 protein, S cerevisiaeTranscription FactorsTristetraprolinWtm1 protein, S cerevisiae

Identifiers

PMID22152479
PMCPMC3240860
OpenAlexW2092038519

What OpenQuestion holds

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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.