Evidence map›Paper›PMID 25611318›Full record

ArticlePloS one2015

Histone chaperone-mediated nucleosome assembly process.

Hsiu-Fang Fan, Zi-Ning Liu, Sih-Yao Chow, Yi-Han Lu, Hsin Li

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Histone turnover and chromatin accessibility: Critical mediators of neurological development, plasticity, and disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    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

5 authors at 1 institution in 1 country.

Hsiu-Fang FanDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan; Biophotonics interdisciplinary research center, National Yang-Ming University, 112, Taipei, Taiwan.
Zi-Ning LiuDepartment of Biotechnology and Laboratory Science in Medicine, National Yang-Ming University, 112, Taipei, Taiwan.
Sih-Yao ChowDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan.
Yi-Han LuDepartment of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan.
Hsin LiDepartment of Biotechnology and Laboratory Science in Medicine, National Yang-Ming University, 112, Taipei, Taiwan.
National Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A huge amount of information is stored in genomic DNA and this stored information resides inside the nucleus with the aid of chromosomal condensation factors. It has been reported that the repeat nucleosome core particle (NCP) consists of 147-bp of DNA and two copies of H2A, H2B, H3 and H4. Regulation of chromosomal structure is important to many processes inside the cell. In vivo, a group of histone chaperones facilitate and regulate nucleosome assembly. How NCPs are constructed with the aid of histone chaperones remains unclear. In this study, the histone chaperone-mediated nucleosome assembly process was investigated using single-molecule tethered particle motion (TPM) experiments. It was found that Asf1 is able to exert more influence than Nap1 and poly glutamate acid (PGA) on the nucleosome formation process, which highlights Asf1's specific role in tetrasome formation. Thermodynamic parameters supported a model whereby energetically favored nucleosomal complexes compete with non-nucleosomal complexes. In addition, our kinetic findings propose the model that histone chaperones mediate nucleosome assembly along a path that leads to enthalpy-favored products with free histones as reaction substrates.

Indexed as

Cell Cycle ProteinsMolecular ChaperonesNucleosome Assembly Protein 1NucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASF1 protein, S cerevisiaeCell Cycle ProteinsMolecular ChaperonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1NucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID25611318
PMCPMC4303269
OpenAlexW2063000346

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.