Evidence map›Paper›PMID 27723831›Full record

ArticlePloS one2016

The Architectural Chromatin Factor High Mobility Group A1 Enhances DNA Ligase IV Activity Influencing DNA Repair.

Ilenia Pellarin, Laura Arnoldo, Silvia Costantini, Silvia Pegoraro, Gloria Ros, Carlotta Penzo, Gianluca Triolo, Francesca Demarchi, Riccardo Sgarra, Alessandro Vindigni and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 18 citations in OpenAlex.

  1. The role of HMGA1 in genome stability: Implications in human cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. HMGA1 in cancer: Cancer classification by location.Journal of cellular and molecular medicine · 2019
    Review
  15. Article
  16. 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

11 authors at 4 institutions in 2 countries.

Ilenia PellarinDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Laura ArnoldoDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Silvia CostantiniInternational Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy.
Silvia PegoraroDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Gloria RosDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Carlotta PenzoDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Gianluca TrioloInternational Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy.
Francesca DemarchiLaboratorio Nazionale Consorzio Interuniversitario Biotecnologie (LNCIB), AREA Science Park, Trieste, Italy.
Riccardo SgarraDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Alessandro VindigniEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, Missouri, United States of America.
Guidalberto ManfiolettiDepartment of Life Sciences, University of Trieste, Trieste, Italy.
University of Trieste · ITInternational Centre for Genetic Engineering and Biotechnology · ITConsorzio Interuniversitario per le Biotecnologie · ITSaint Louis University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The HMGA1 architectural transcription factor is an oncogene overexpressed in the vast majority of human cancers. HMGA1 is a highly connected node in the nuclear molecular network and the key aspect of HMGA1 involvement in cancer development is that HMGA1 simultaneously confers cells multiple oncogenic hits, ranging from global chromatin structural and gene expression modifications up to the direct functional alterations of key cellular proteins. Interestingly, HMGA1 also modulates DNA damage repair pathways. In this work, we provide evidences linking HMGA1 with Non-Homologous End Joining DNA repair. We show that HMGA1 is in complex with and is a substrate for DNA-PK. HMGA1 enhances Ligase IV activity and it counteracts the repressive histone H1 activity towards DNA ends ligation. Moreover, breast cancer cells overexpressing HMGA1 show a faster recovery upon induction of DNA double-strand breaks, which is associated with a higher survival. These data suggest that resistance to DNA-damaging agents in cancer cells could be partially attributed to HMGA1 overexpression thus highlighting the relevance of considering HMGA1 expression levels in the selection of valuable and effective pharmacological regimens.

Indexed as

DNA RepairCell Line, TumorChromatinChromatography, High Pressure LiquidComet AssayDNA Ligase ATPHistonesHMGA1a ProteinHMGA2 ProteinHumansKu AutoantigenMCF-7 CellsMicroscopy, FluorescencePhosphorylationRecombinant ProteinsSubstrate SpecificityChromatinDNA Ligase ATPHistonesHMGA1a ProteinHMGA2 ProteinKu AutoantigenRecombinant Proteins

Identifiers

PMID27723831
PMCPMC5056749
OpenAlexW2530775908

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.