Evidence map›Paper›PMID 12853613›Full record

ArticleNucleic acids research2003

Histone deacetylases in fungi: novel members, new facts.

Patrick Trojer, Eva M Brandtner, Gerald Brosch, Peter Loidl, Johannes Galehr, Roland Linzmaier, Hubertus Haas, Karin Mair, Martin Tribus, Stefan Graessle

Open access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

35 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Contributions of a Histone Deacetylase (SirT2/Hst2) toJournal of fungi (Basel, Switzerland) · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Frontiers in cellular and infection microbiology · 2017
    Review
  20. 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

10 authors at 1 institution in 1 country.

Patrick TrojerDepartment of Molecular Biology, University of Innsbruck, Peter-Mayr-Strasse 4b, Innsbruck, A-6020, Austria.
Eva M Brandtner
Gerald Brosch
Peter Loidl
Johannes Galehr
Roland Linzmaier
Hubertus Haas
Karin Mair
Martin Tribus
Stefan Graessle
Universität Innsbruck · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylation is the most prominent modification on core histones that strongly affects nuclear processes such as DNA replication, DNA repair and transcription. Enzymes responsible for the dynamic equilibrium of histone acetylation are histone acetyltransferases (HATs) and histone deacetylases (HDACs). In this paper we describe the identification of novel HDACs from the filamentous fungi Aspergillus nidulans and the maize pathogen Cochliobolus carbonum. Two of the enzymes are homologs of Saccharomyces cerevisiae HOS3, an enzyme that has not been identified outside of the established yeast systems until now. One of these homologs, HosB, showed intrinsic HDAC activity and remarkable resistance against HDAC inhibitors like trichostatin A (TSA) when recombinant expressed in an Escherichia coli host system. Phylo genetic analysis revealed that HosB, together with other fungal HOS3 orthologs, is a member of a separate group within the classical HDACs. Immunological investigations with partially purified HDAC activities of Aspergillus showed that all classical enzymes are part of high molecular weight complexes and that a TSA sensitive class 2 HDAC constitutes the major part of total HDAC activity of the fungus. However, further biochemical analysis also revealed an NAD(+)-dependent activity that could be separated from the other activities by different types of chromatography and obviously represents an enzyme of the sirtuin class.

Indexed as

Amino Acid SequenceAscomycotaAspergillus nidulansDNA, FungalEscherichia coliGene Expression Regulation, EnzymologicGene Expression Regulation, FungalHistone DeacetylasesImmunoblottingIsoenzymesMolecular Sequence DataPhylogenyPrecipitin TestsRecombinant ProteinsSequence AlignmentSequence Analysis, DNADNA, FungalHistone DeacetylasesIsoenzymesRecombinant Proteins

Identifiers

PMID12853613
PMCPMC167634
OpenAlexW2113032400

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.