Evidence map›Paper›PMID 22178397›Full record

ArticleMolecular cell2012

Activator-induced spread of poly(ADP-ribose) polymerase promotes nucleosome loss at Hsp70.

Steven J Petesch, John T Lis

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

77 citing papers in PubMed, 116 citations in OpenAlex.

  1. PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Disordered Protein Tail Is Wagging Poly(ADP-ribosyl)ation.International journal of molecular sciences · 2025
    Article
  5. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  6. Review
  7. PARG Protein Regulation Roles inInternational journal of molecular sciences · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The regulation of transcription elongation in embryonic stem cells.Frontiers in cell and developmental biology · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

17 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Steven J PeteschDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
John T Lis
Cornell University · US

Funding

COORDINATE GENE REGULATION IN ANIMAL CELLSR01GM025232 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIS, JOHN T · 1985 to 2020
$8.4M
COORDINATE GENE REGULATION IN ANIMAL CELLSR37GM025232 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIS, JOHN THOMAS · 1995 to 2004
$2.5M
NIGMS NIH HHS GM25232NIGMS NIH HHS R01 GM025232NIGMS NIH HHS R37 GM025232NIGMS NIH HHS T32-GM70723
6 · The paper itself

Abstract

Eukaryotic cells possess many transcriptionally regulated mechanisms to alleviate the nucleosome barrier. Dramatic changes to the chromatin structure of Drosophila melanogaster Hsp70 gene loci are dependent on the transcriptional activator, heat shock factor (HSF), and poly(ADP-ribose) polymerase (PARP). Here, we find that PARP is associated with the 5' end of Hsp70, and its enzymatic activity is rapidly induced by heat shock. This activation causes PARP to redistribute throughout Hsp70 loci and Poly(ADP-ribose) to concurrently accumulate in the wake of PARP's spread. HSF is necessary for both the activation of PARP's enzymatic activity and its redistribution. Upon heat shock, HSF triggers these PARP activities mechanistically by directing Tip60 acetylation of histone H2A lysine 5 at the 5' end of Hsp70, where inactive PARP resides before heat shock. This acetylation is critical for the activation and spread of PARP as well as for the rapid nucleosome loss over the Hsp70 loci.

Indexed as

AcetylationAnimalsDrosophila melanogasterDrosophila ProteinsHeat-Shock ResponseHistone AcetyltransferasesHistone Deacetylase 3Histone DeacetylasesHistonesHSP70 Heat-Shock ProteinsNucleosomesPoly(ADP-ribose) PolymerasesDrosophila ProteinsHistone AcetyltransferasesHistone Deacetylase 3Histone DeacetylasesHistonesHSP70 Heat-Shock ProteinsNucleosomesPoly(ADP-ribose) PolymerasesTip60 protein, Drosophila

Identifiers

PMID22178397
PMCPMC3473076
OpenAlexW2164548007

What OpenQuestion holds

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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.