Evidence map›Paper›PMID 21454601›Full record

ReviewThe Journal of biological chemistry2011

The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization.

Duane D Winkler, Karolin Luger

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

137 citing papers in PubMed, 207 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025
    Review
  14. Article
  15. Activation and Evasion of the FEAR Pathway by RNA Viruses.bioRxiv : the preprint server for biology · 2025
    Article
  16. Article
  17. Article
  18. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
  19. Review
  20. Review

77 more citing papers are in PubMed but not listed here.

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.

Duane D WinklerDepartment of Biochemistry and Molecular Biology and the Howard Hughes Medical Institute, Colorado State University, Fort Collins, Colorado 80523-1870, USA.
Karolin Luger
Howard Hughes Medical Institute · US

Funding

project 3P01GM088409 · NIGMS · COLORADO STATE UNIVERSITY · PI NYBORG, JENNIFER K. · 2010 to 2014
$7.3M
Howard Hughes Medical InstituteNIGMS NIH HHS 1P01GM088409-01A1NIGMS NIH HHS P01 GM088409
6 · The paper itself

Abstract

Changes in chromatin architecture induced by epigenetic mechanisms are essential for normal cellular processes such as gene expression, DNA repair, and cellular division. Compact chromatin presents a barrier to these processes and is highly regulated by epigenetic markers binding to components of the nucleosome. Histone modifications directly influence chromatin dynamics and facilitate recruitment of additional factors such as chromatin remodelers and histone chaperones. One member of this last class of factors, FACT (facilitates chromatin transcription), is categorized as a histone chaperone critical for nucleosome reorganization during replication, transcription, and DNA repair. Significant discoveries regarding the role of histone chaperones and specifically FACT have come over the past dozen years from a number of independent laboratories. Here, we review the structural and biophysical basis for FACT-mediated nucleosome reorganization and discuss up-to-date models for FACT function.

Indexed as

Models, BiologicalAnimalsChromatin Assembly and DisassemblyDNA-Binding ProteinsDNA RepairDNA ReplicationHigh Mobility Group ProteinsHistonesHumansMolecular ChaperonesNucleosomesStructure-Activity RelationshipTranscriptional Elongation FactorsTranscription, GeneticDNA-Binding ProteinsHigh Mobility Group ProteinsHistonesMolecular ChaperonesNucleosomesSSRP1 protein, humanTranscriptional Elongation Factors

Identifiers

PMID21454601
PMCPMC3099653
OpenAlexW2064558750

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.