Evidence map›Paper›PMID 26501335›Full record

ReviewBiomolecules2015

Hsp90: A New Player in DNA Repair?

Rosa Pennisi, Paolo Ascenzi, Alessandra di Masi

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.8field-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

65 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Inhibition ofFrontiers in parasitology · 2026
    Article
  3. Article
  4. Identification of thePlants (Basel, Switzerland) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  9. Polymorphisms of DNA Repair Genes in Thyroid Cancer.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Rosa PennisiDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, Roma I-00146, Italy. rosa.pennisi@uniroma3.it.
Paolo AscenziDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, Roma I-00146, Italy. ascenzi@uniroma3.it.
Alessandra di MasiDepartment of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, Roma I-00146, Italy. alessandra.dimasi@uniroma3.it.
Roma Tre University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein 90 (Hsp90) is an evolutionary conserved molecular chaperone that, together with Hsp70 and co-chaperones makes up the Hsp90 chaperone machinery, stabilizing and activating more than 200 proteins, involved in protein homeostasis (i.e., proteostasis), transcriptional regulation, chromatin remodeling, and DNA repair. Cells respond to DNA damage by activating complex DNA damage response (DDR) pathways that include: (i) cell cycle arrest; (ii) transcriptional and post-translational activation of a subset of genes, including those associated with DNA repair; and (iii) triggering of programmed cell death. The efficacy of the DDR pathways is influenced by the nuclear levels of DNA repair proteins, which are regulated by balancing between protein synthesis and degradation as well as by nuclear import and export. The inability to respond properly to either DNA damage or to DNA repair leads to genetic instability, which in turn may enhance the rate of cancer development. Multiple components of the DNA double strand breaks repair machinery, including BRCA1, BRCA2, CHK1, DNA-PKcs, FANCA, and the MRE11/RAD50/NBN complex, have been described to be client proteins of Hsp90, which acts as a regulator of the diverse DDR pathways. Inhibition of Hsp90 actions leads to the altered localization and stabilization of DDR proteins after DNA damage and may represent a cell-specific and tumor-selective radiosensibilizer. Here, the role of Hsp90-dependent molecular mechanisms involved in cancer onset and in the maintenance of the genome integrity is discussed and highlighted.

Indexed as

DNA Breaks, Double-StrandedDNA DamageDNA RepairHSP90 Heat-Shock ProteinsHumansHSP90 Heat-Shock Proteinsbase excision repairDNA damage responseDNA double strand breakDNA repairHsp90Hsp90 inhibitorsmismatch repairtranslation synthesis

Identifiers

PMID26501335
PMCPMC4693249
OpenAlexW1824210888

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.