Evidence map›Paper›PMID 14592982›Full record

ArticleThe EMBO journal2003

A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei.

José A García-Salcedo, Purificación Gijón, Derek P Nolan, Patricia Tebabi, Etienne Pays

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 128 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Role of mono-ADP-ribosylation histone modification (Review).Experimental and therapeutic medicine · 2021
    Review
  5. Review
  6. Chemical Constituents ofMolecules (Basel, Switzerland) · 2019
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The natural history of ADP-ribosyltransferases and the ADP-ribosylation system.Current topics in microbiology and immunology · 2015
    Review
  16. Review
  17. ADP-ribosyltransferases and poly ADP-ribosylation.Current protein & peptide science · 2015
    Review
  18. Article
  19. Article
  20. Structural and functional analysis of human SIRT1.Journal of molecular biology · 2014
    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

5 authors.

José A García-SalcedoInstitute of Molecular Biology and Medicine, Free University of Brussels, 12 rue des Professeurs Jeener et Brachet, B-6041 Gosselies, Belgium. jantonio@dbm.ulb.ac.be
Purificación Gijón
Derek P Nolan
Patricia Tebabi
Etienne Pays

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SIR2-like proteins have been implicated in a wide range of cellular events including chromosome silencing, chromosome segregation, DNA recombination and the determination of life span. We report here the molecular and functional characterization of a SIR2-related protein from the protozoan parasite Trypanosoma brucei, which we termed TbSIR2RP1. This protein is a chromosome-associated NAD-dependent enzyme which, in contrast to other known proteins of this family, catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Under- or overexpression of TbSIR2RP1 decreased or increased, respectively, cellular resistance to DNA damage. Treatment of trypanosomal nuclei with a DNA alkylating agent resulted in a significant increase in the level of histone ADP-ribosylation and a concomitant increase in chromatin sensitivity to micrococcal nuclease. Both of these responses correlated with the level of TbSIR2RP1 expression. We propose that histone modification by TbSIR2RP1 is involved in DNA repair.

Indexed as

Alkylating AgentsAnimalsDNA DamageDNA RepairGenes, ProtozoanHistone DeacetylasesHistonesIn Vitro TechniquesNuclear ProteinsProtozoan ProteinsSirtuinsSubstrate SpecificityTrypanosoma brucei bruceiAlkylating AgentsHistone DeacetylasesHistonesNuclear ProteinsProtozoan ProteinsSirtuins

Identifiers

PMID14592982
PMCPMC275410
OpenAlexW2062765347

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.