Evidence map›Paper›PMID 22487307›Full record

ArticleThe FEBS journal2012

A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2.

Nicolas Soler, Constantin T Craescu, Jacques Gallay, Yves-Michel Frapart, Daniel Mansuy, Bertrand Raynal, Giuseppe Baldacci, Annalisa Pastore, Meng-Er Huang, Laurence Vernis

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. 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
  2. Article
  3. Article
  4. Article
  5. Article
  6. Epigenetic role for the conserved Fe-S cluster biogenesis protein AtDRE2 in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Anamorsin, a novel caspase-3 substrate in neurodegeneration.The Journal of biological chemistry · 2014
    Article
  8. Article
  9. Article
  10. Human anamorsin binds [2Fe-2S] clusters with unique electronic properties.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  11. Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

10 authors at 7 institutions in 1 country.

Nicolas SolerCNRS UMR2027, Centre Universitaire, Orsay, France.
Constantin T Craescu
Jacques Gallay
Yves-Michel Frapart
Daniel Mansuy
Bertrand Raynal
Giuseppe Baldacci
Annalisa Pastore
Meng-Er Huang
Laurence Vernis
Centre National de la Recherche Scientifique · FRInstitut Curie · FRDélégation Paris 5 · FRInserm · FRInstitut de Biochimie et Biophysique Moléculaire et Cellulaire · FRInstitut Pasteur · FRSorbonne Paris Cité · FR

Funding

Medical Research Council MC_U117584256
6 · The paper itself

Abstract

Yeast Dre2 is an essential Fe-S cluster-containing protein that has been implicated in cytosolic Fe-S protein biogenesis and in cell death regulation in response to oxidative stress. Its absence in yeast can be complemented by the human homologous antiapoptotic protein cytokine-induced apoptosis inhibitor 1 (also known as anamorsin), suggesting at least one common function. Using complementary techniques, we have investigated the biochemical and biophysical properties of Dre2. We show that it contains an N-terminal domain whose structure in solution consists of a stable well-structured monomer with an overall typical S-adenosylmethionine methyltransferase fold lacking two α-helices and a β-strand. The highly conserved C-terminus of Dre2, containing two Fe-S clusters, influences the flexibility of the N-terminal domain. We discuss the hypotheses that the activity of the N-terminal domain could be modulated by the redox activity of Fe-S clusters containing the C-terminus domain in vivo.

Indexed as

Amino Acid SequenceIron-Sulfur ProteinsMagnetic Resonance SpectroscopyMolecular Sequence DataProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidDre2 protein, S cerevisiaeIron-Sulfur ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22487307
PMCPMC3440578
OpenAlexW1845547649

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.