Evidence map›Paper›PMID 24551219›Full record

ArticlePloS one2014

Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1.

Eva Polanská, Šárka Pospíšilová, Michal Štros

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Structure and Functions of HMGB3 Protein.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Structure and Functions of HMGB2 Protein.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Functional Diversity of Non-Histone Chromosomal Protein HmgB1.International journal of molecular sciences · 2020
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Yeast HMO1: Linker Histone Reinvented.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  15. Review
  16. Review
  17. Two high-mobility group box domains act together to underwind and kink DNA.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  18. Article
  19. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    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

3 authors at 2 institutions in 1 country.

Eva PolanskáLaboratory of Analysis of Chromosomal Proteins, Institute of Biophysics, Academy of Science of the Czech Republic, Brno, Czech Republic.
Šárka PospíšilováCentral European Institute of Technology (CEITEC) - Center of Molecular Medicine, Masaryk University, Brno, Czech Republic.
Michal ŠtrosLaboratory of Analysis of Chromosomal Proteins, Institute of Biophysics, Academy of Science of the Czech Republic, Brno, Czech Republic ; Central European Institute of Technology (CEITEC) - Center of Molecular Medicine, Masaryk University, Brno, Czech Republic.
Central European Institute of Technology · CZCzech Academy of Sciences, Institute of Biophysics · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HMGB1 is an architectural protein in chromatin, acting also as a signaling molecule outside the cell. Recent reports from several laboratories provided evidence that a number of both the intracellular and extracellular functions of HMGB1 may depend on redox-sensitive cysteine residues of the protein. In this study we demonstrate that redox state of HMGB1 can significantly modulate the ability of the protein to bind and bend DNA, as well as to promote DNA end-joining. We also report a high affinity binding of histone H1 to hemicatenated DNA loops and DNA minicircles. Finally, we show that reduced HMGB1 can readily displace histone H1 from DNA, while oxidized HMGB1 has limited capacity for H1 displacement. Our results suggested a novel mechanism for the HMGB1-mediated modulation of histone H1 binding to DNA. Possible biological consequences of linker histones H1 replacement by HMGB1 for the functioning of chromatin are discussed.

Indexed as

AnimalsCattleChromatinDNA, CircularDNA, ConcatenatedGene ExpressionGenetic VectorsHistonesHMGB1 ProteinHumansOxidation-ReductionProtein BindingRatsRecombinant ProteinsChromatinDNA, CircularDNA, ConcatenatedHistonesHMGB1 ProteinRecombinant Proteins

Identifiers

PMID24551219
PMCPMC3923860
OpenAlexW2037947607

What OpenQuestion holds

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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.