CENPs and Sweet Nucleosomes Face the FACT.

Magdalena Murawska, Andreas G Ladurner

Abstract readComment

In one paragraph

Article in Trends in biochemical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it

0cells of the map it votes in

3citing papers in PubMed

–field-weighted citation impact

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

3 citing papers in PubMed.

FACT subunit SUPT16H associates with BRD4 and contributes to silencing of interferon signaling.Nucleic acids research · 2022
Article
FACT subunit SUPT16H associates with BRD4 and contributes to silencing of antiviral interferon signaling.bioRxiv : the preprint server for biology · 2021
Article
Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function.Journal of cancer metastasis and treatment · 2019
Article

4 · The record

Corrections and comments

Comment on
The CENP-T/-W complex is a binding partner of the histone chaperone FACT.2016
Comment on
Synthetic Nucleosomes Reveal that GlcNAcylation Modulates Direct Interaction with the FACT Complex.2016

5 · Who and what money

Authors and funding

2 authors.

Magdalena MurawskaBiomedical Center, Physiological Chemistry, LMU Munich, Großhaderner Street 9, 82152 Planegg-Martinsried, Germany.

Andreas G LadurnerBiomedical Center, Physiological Chemistry, LMU Munich, Großhaderner Street 9, 82152 Planegg-Martinsried, Germany; Center for Integrated Protein Science Munich (CIPSM), 81377 Munich, Germany; Munich Cluster for Systems Neurology (SyNergy), 80336 Munich, Germany. Electronic address: andreas.ladurner@med.lmu.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chaperones mediate vital interactions between histones and DNA during chromatin assembly and reorganization. Two recent studies reveal novel substrates for the essential and conserved histone chaperone FAcilitates Chromatin Transcription (FACT). Prendergast et al. show that FACT helps deposit important histone-fold proteins on centromeres. Raj et al. find that FACT preferentially binds O-GlcNAcylated nucleosomes, suggesting that FACT may contribute to nutrient-regulated cellular programs.

Indexed as

CentromereChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHigh Mobility Group ProteinsHistonesHumansNucleosomesTranscriptional Elongation FactorsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHigh Mobility Group ProteinsHistonesNucleosomesSSRP1 protein, humanTranscriptional Elongation FactorsFACTGlcNAcylation.histone foldkinetochore

Identifiers

PMID27499233

DOI10.1016/j.tibs.2016.07.010

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.