Evidence map›Paper›PMID 25416387›Full record

ArticleCell stress & chaperones2015

ASF1 and the SWI/SNF complex interact functionally during nucleosome displacement, while FACT is required for nucleosome reassembly at yeast heat shock gene promoters during sustained stress.

Tamara Y Erkina, Alexandre Erkine

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Chromatin Stability as a Target for Cancer Treatment.BioEssays : news and reviews in molecular, cellular and developmental biology · 2019
    Review
  8. Article
  9. Article
  10. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  11. Article
  12. 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

2 authors at 1 institution in 1 country.

Tamara Y ErkinaDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Butler University, Indianapolis, IN, 46208, USA.
Alexandre Erkine
Butler University · US

Funding

Selective Inhibitors of Human HSF2R03MH097538 · NIMH · BUTLER UNIVERSITY · PI ERKINE, ALEXANDRE M. · 2012 to 2013
$59k
NIMH NIH HHS R03 MH097538NIMH NIH HHS R03MH097538
6 · The paper itself

Abstract

Histone chaperones are an integral part of the transcription regulatory machinery. We investigated the involvement of histone chaperones and their functional interactions with ATP-dependent chromatin remodeling complexes in the regulation of yeast heat shock genes. Strong functional interaction between the histone chaperone ASF1 and the ATP-dependent chromatin remodeling complex SWI/SNF is exhibited in synergistic diminishment of nucleosome displacement during heat shock in the ΔASF1/ΔSNF2 strain in comparison to individual ASF1 or SNF2 inactivation. A similar but less pronounced effect was observed for ISW1/ASF1 inactivation but not for ASF1/STH1 (RSC complex) combinatorial inactivation. The depletion of Spt16, which is a major subunit of the FACT histone chaperone complex, leads to a severe growth defect phenotype associated with unusual thermotolerance. The acquired thermotolerance in the Spt16-depleted strain is associated with a defect in the reassembly of nucleosomes at the promoters of heat shock genes during sustained heat stress, leading to increased recruitment of the transcriptional activator HSF and RNA polymerase II. The defect in nucleosome assembly associated with Spt16 depletion also leads to an increased tolerance to stress due to an increased concentration of NaCl.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsChromatin Assembly and DisassemblyChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDoxycyclineGene Expression RegulationHeat-Shock ProteinsHeat-Shock ResponseHigh Mobility Group ProteinsHistonesMolecular ChaperonesMutationNuclear ProteinsNucleosomesSaccharomyces cerevisiaeAdenosine TriphosphatasesASF1 protein, S cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDoxycyclineFACT protein, S cerevisiaeHeat-Shock ProteinsHigh Mobility Group ProteinsHistonesISW1 protein, S cerevisiaeMolecular ChaperonesNuclear ProteinsNucleosomesRSC complex, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeSTH1 protein, S cerevisiaeSWI-SNF-B chromatin-remodeling complexTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID25416387
PMCPMC4326380
OpenAlexW1995579782

What OpenQuestion holds

Textmetadata
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.