Evidence map›Paper›PMID 28468903›Full record

ArticleGenetics2017

Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding in

Amelia J Hodges, Lisa M Gloss, John J Wyrick

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 21 citations in OpenAlex.

  1. Mapping Allosteric Communication in the Nucleosome with Conditional Activity.Journal of chemical information and modeling · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Specialized RSC: Substrate Specificities for a Conserved Chromatin Remodeler.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Article
  11. Article
  12. Article
  13. Chromatin regulation and dynamics in stem cells.Current topics in developmental biology · 2020
    Review
  14. Article
  15. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  16. Article
  17. Article
  18. 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 1 institution in 1 country.

Amelia J HodgesSchool of Molecular Biosciences, Washington State University, Pullman, Washington 99164.
Lisa M GlossSchool of Molecular Biosciences, Washington State University, Pullman, Washington 99164.
John J WyrickSchool of Molecular Biosciences, Washington State University, Pullman, Washington 99164 jwyrick@vetmed.wsu.edu.
Washington State University · US

Funding

Repair of Carcinogen Damaged DNA in Human ChromatinR37ES002614 · NIEHS · WASHINGTON STATE UNIVERSITY · PI SMERDON, MICHAEL J · 2001 to 2010
$4.0M
REPAIR OF CARCINOGEN-DAMAGED DNA IN HUMAN CHROMATINR01ES002614 · NIEHS · WASHINGTON STATE UNIVERSITY · PI SMERDON, MICHAEL J, WYRICK, JOHN J · 1985 to 2015
$2.5M
NIEHS NIH HHS R01 ES002614NIEHS NIH HHS R37 ES002614
6 · The paper itself

Abstract

The essential histone chaperone FACT plays a critical role in DNA replication, repair, and transcription, primarily by binding to histone H2A-H2B dimers and regulating their assembly into nucleosomes. While FACT histone chaperone activity has been extensively studied, the exact nature of the H2A and H2B residues important for FACT binding remains controversial. In this study, we characterized the functions of residues in the histone H2A and H2B acidic patch, which is important for binding many chromatin-associated factors. We found that mutations in essential acidic patch residues cause a defect in histone occupancy in yeast, even though most of these histone mutants are expressed normally in yeast and form stable nucleosomes

Indexed as

Binding SitesHistonesNucleosome Assembly Protein 1NucleosomesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription FactorsHistonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1NucleosomesPOB3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT16 protein, S cerevisiaeTranscriptional Elongation FactorsTranscription FactorsH2A-H2B dimerNap1nucleosome assemblyPob3Spt16

Identifiers

PMID28468903
PMCPMC5500134
OpenAlexW2611720166

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.