Evidence map›Paper›PMID 26058396›Full record

ArticleBMB reports2015

Identification of small molecules that inhibit the histone chaperone Asf1 and its chromatin function.

Ja-Hwan Seol, Tae-Yang Song, Se Eun Oh, Chanhee Jo, Ahreum Choi, Byungho Kim, Jinyoung Park, Suji Hong, Ilrang Song, Kwan Young Jung and 5 more

Open access · goldAbstract read
In one paragraph

Article in BMB reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Cancer discovery · 2020
    Article
  9. Recognition of ASF1 by Using Hydrocarbon-Constrained Peptides.Chembiochem : a European journal of chemical biology · 2019
    Article
  10. Article
  11. 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

15 authors at 2 institutions in 1 country.

Ja-Hwan SeolSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Tae-Yang SongSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Se Eun OhDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon 16419, Korea.
Chanhee JoSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Ahreum ChoiSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Byungho KimSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Jinyoung ParkSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Suji HongSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Ilrang SongSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Kwan Young JungSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Jae-Hyun YangSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Hwangseo ParkDepartment of Bioscience and Biotechnology, Sejong University, Seoul 05006, Korea.
Jin-Hyun AhnDepartment of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon 16419, Korea.
Jeung-Whan HanSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Eun-Jung ChoSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Sungkyunkwan University · KRSejong University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eukaryotic genome is packed into chromatin, which is important for the genomic integrity and gene regulation. Chromatin structures are maintained through assembly and disassembly of nucleosomes catalyzed by histone chaperones. Asf1 (anti-silencing function 1) is a highly conserved histone chaperone that mediates histone transfer on/off DNA and promotes histone H3 lysine 56 acetylation at globular core domain of histone H3. To elucidate the role of Asf1 in the modulation of chromatin structure, we screened and identified small molecules that inhibit Asf1 and H3K56 acetylation without affecting other histone modification. These pyrimidine-2,4,6-trione derivative molecules inhibited the nucleosome assembly mediated by Asf1 in vitro, and reduced the H3K56 acetylation in HeLa cells. Furthermore, production of HSV viral particles was reduced by these compounds. As Asf1 is implicated in genome integrity, cell proliferation, and cancer, current Asf1 inhibitor molecules may offer an opportunity for the therapeutic development for treatment of diseases.

Indexed as

AcetylationCell Cycle ProteinsChromatinChromatin Assembly and DisassemblyHistonesHumansMolecular ChaperonesNucleosomesSmall Molecule LibrariesASF1A protein, humanASF1B protein, humanCell Cycle ProteinsChromatinHistonesMolecular ChaperonesNucleosomesSmall Molecule Libraries

Identifiers

PMID26058396
PMCPMC4791324
OpenAlexW2325261083

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.