Evidence map›Paper›PMID 33523989›Full record

ArticleScience advances2021

Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies.

Jung-Hoon Lee, Daniel Bollschweiler, Tillman Schäfer, Robert Huber

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. HDAC1: An Essential and Conserved Member of the Diverse ZnInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Class I histone deacetylase complex: Structure and functional correlates.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Using deep-learning predictions of inter-residue distances for model validation.Acta crystallographica. Section D, Structural biology · 2022
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. 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

4 authors at 2 institutions in 2 countries.

Jung-Hoon LeeMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. hlee@biochem.mpg.de huber@biochem.mpg.de.ORCID 0000-0002-3190-6644
Daniel BollschweilerMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Tillman SchäferMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.ORCID 0000-0002-9992-2501
Robert HuberMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. hlee@biochem.mpg.de huber@biochem.mpg.de.ORCID 0000-0002-0133-5334
Max Planck Institute of Biochemistry · DEProterixBio (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chromatin-modifying histone deacetylases (HDACs) remove acetyl groups from acetyl-lysine residues in histone amino-terminal tails, thereby mediating transcriptional repression. Structural makeup and mechanisms by which multisubunit HDAC complexes recognize nucleosomes remain elusive. Our cryo-electron microscopy structures of the yeast class II HDAC ensembles show that the HDAC protomer comprises a triangle-shaped assembly of stoichiometry Hda1

Indexed as

NucleosomesSaccharomyces cerevisiae ProteinsChromatinCryoelectron MicroscopyHistone DeacetylasesHistonesProtein SubunitsSaccharomyces cerevisiaeChromatinHDA1 protein, S cerevisiaeHistone DeacetylasesHistonesNucleosomesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID33523989
PMCPMC7793584
OpenAlexW3120191573

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.