Evidence map›Paper›PMID 26636673›Full record

ArticlePloS one2015

Poly(ADP-Ribosyl)ation Affects Histone Acetylation and Transcription.

Loredana Verdone, Marco La Fortezza, Fabio Ciccarone, Paola Caiafa, Michele Zampieri, Micaela Caserta

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Role of NADCellular and molecular neurobiology · 2023
    Review
  7. Article
  8. Article
  9. PARP1-modulated chromatin remodeling is a new target for cancer treatment.Medical oncology (Northwood, London, England) · 2021
    Review
  10. Role of mono-ADP-ribosylation histone modification (Review).Experimental and therapeutic medicine · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Interplay between NADBiochimica et biophysica acta. Molecular basis of disease · 2019
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Semaphorin 5A drives melanoma progression: role of Bcl-2, miR-204 and c-Myb.Journal of experimental & clinical cancer research : CR · 2018
    Article
  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

6 authors at 4 institutions in 2 countries.

Loredana VerdoneIstituto di Biologia e Patologia Molecolari, CNR c/o Dipartimento di Biologia e Biotecnologie, Sapienza Università di Roma, Rome, Italy.
Marco La FortezzaLudwig Maximilians University Munich, Planegg-Martinsried, Germany.
Fabio CiccaroneDipartimento di Biotecnologie Cellulari ed Ematologia, Sapienza Università di Roma, Rome, Italy.
Paola CaiafaDipartimento di Biotecnologie Cellulari ed Ematologia, Sapienza Università di Roma, Rome, Italy.
Michele ZampieriDipartimento di Biotecnologie Cellulari ed Ematologia, Sapienza Università di Roma, Rome, Italy.
Micaela CasertaIstituto di Biologia e Patologia Molecolari, CNR c/o Dipartimento di Biologia e Biotecnologie, Sapienza Università di Roma, Rome, Italy.
Istituto Pasteur · ITSapienza University of Rome · ITInstitute of Molecular Biology and Pathology · ITLudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribosyl)ation (PARylation) is a posttranslational protein modification catalyzed by members of the poly(ADP-ribose) polymerase (PARP) enzyme family. PARylation regulates a wide variety of biological processes in most eukaryotic cells including energy metabolism and cell death, maintenance of genomic stability, chromatin structure and transcription. Inside the nucleus, cross-talk between PARylation and other epigenetic modifications, such as DNA and histone methylation, was already described. In the present work, using PJ34 or ABT888 to inhibit PARP activity or over-expressing poly(ADP-ribose) glycohydrolase (PARG), we show decrease of global histone H3 and H4 acetylation. This effect is accompanied by a reduction of the steady state mRNA level of p300, Pcaf, and Tnfα, but not of Dnmt1. Chromatin immunoprecipitation (ChIP) analyses, performed at the level of the Transcription Start Site (TSS) of these four genes, reveal that changes in histone acetylation are specific for each promoter. Finally, we demonstrate an increase of global deacetylase activity in nuclear extracts from cells treated with PJ34, whereas global acetyltransferase activity is not affected, suggesting a role for PARP in the inhibition of histone deacetylases. Taken together, these results show an important link between PARylation and histone acetylation regulated transcription.

Indexed as

Transcription, GeneticAcetylationAnimalsBenzimidazolesDNA (Cytosine-5-)-Methyltransferase 1DNA (Cytosine-5-)-MethyltransferasesE1A-Associated p300 ProteinGenomic InstabilityHistonesMiceNIH 3T3 Cellsp300-CBP-Associated Factorp300-CBP Transcription FactorsPhenanthrenesPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesBenzimidazolesDNA (Cytosine-5-)-Methyltransferase 1DNA (Cytosine-5-)-MethyltransferasesDnmt1 protein, mouseE1A-Associated p300 ProteinEp300 protein, mouseHistonesN-(oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloridep300-CBP-Associated Factorp300-CBP Transcription FactorsPhenanthrenesPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesTumor Necrosis Factor-alphaveliparib

Identifiers

PMID26636673
PMCPMC4670112
OpenAlexW2186413662

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.