Evidence map›Paper›PMID 25281266›Full record

ArticleFEBS letters2014

Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain.

Mulu Y Lubula, Brian E Eckenroth, Samuel Carlson, Amanda Poplawski, Maksymilian Chruszcz, Karen C Glass

Abstract read
In one paragraph

Article in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Mosaicism inCase reports in genetics · 2023
    Article
  7. Review
  8. Coordination of Di-Acetylated Histone Ligands by the ATAD2 Bromodomain.International journal of molecular sciences · 2021
    Article
  9. Deficiency of Intellectual Disability-Related GeneFrontiers in cell and developmental biology · 2021
    Article
  10. The BRPF1 bromodomain is a molecular reader of di-acetyllysine.Current research in structural biology · 2020
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Unveiling the folding mechanism of the Bromodomains.Biochemistry and biophysics reports · 2017
    Article
  17. Review
  18. Review
  19. Article
  20. Article
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

6 authors.

Mulu Y LubulaDepartment of Pharmaceutical Science, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA.
Brian E EckenrothDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Samuel CarlsonDepartment of Pharmaceutical Science, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA.
Amanda PoplawskiDepartment of Pharmaceutical Science, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA.
Maksymilian ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Karen C GlassDepartment of Pharmaceutical Science, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA. Electronic address: karen.glass@acphs.edu.

Funding

SUBSTRATE SPECIFICITY OF THE BER OXIDATIVE DNA GLYCOSYLASESP01CA098993 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI DOUBLIE, SYLVIE · 2004 to 2021
$25.9M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Processing of Radiation Damage by Translesion DNA SynthesisR01CA052040 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI DOUBLIE, SYLVIE · 1991 to 2017
$4.5M
Mechanisms of chromatin binding and selection by family IV bromodomainsR15GM104865 · NIGMS · ALBANY COLLEGE OF PHARMACY · PI GLASS, KAREN CHAMPAGNE · 2013 to 2016
$910k
NCI NIH HHS P01 CA098993NCI NIH HHS P01CA098993NCI NIH HHS R01 CA052040NCI NIH HHS R01CA52040NIGMS NIH HHS 1R15GM104865NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R15 GM104865
6 · The paper itself

Abstract

Bromodomain-PHD finger protein 1 (BRPF1) is part of the MOZ HAT complex and contains a unique combination of domains typically found in chromatin-associated factors, which include plant homeodomain (PHD) fingers, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. Bromodomains are conserved structural motifs generally known to recognize acetylated histones, and the BRPF1 bromodomain preferentially selects for H2AK5ac, H4K12ac and H3K14ac. We solved the X-ray crystal structures of the BRPF1 bromodomain in complex with the H2AK5ac and H4K12ac histone peptides. Site-directed mutagenesis on residues in the BRPF1 bromodomain-binding pocket was carried out to investigate the contribution of specific amino acids on ligand binding. Our results provide critical insights into the molecular mechanism of ligand binding by the BRPF1 bromodomain, and reveal that ordered water molecules are an essential component driving ligand recognition.

Indexed as

AcetylationAdaptor Proteins, Signal TransducingBromodomain Containing ProteinsDNA-Binding ProteinsHistonesHumansLigandsLysineModels, MolecularMolecular Targeted TherapyNuclear ProteinsProtein BindingProtein Structure, TertiaryAdaptor Proteins, Signal TransducingBromodomain Containing ProteinsBRPF1 protein, humanDNA-Binding ProteinsHistonesLigandsLysineNuclear ProteinsBromodomain-PHD finger protein 1Circular dichroismEpigeneticsIsothermal titration calorimetrySite-directed mutagenesisX-ray crystallography

Identifiers

PMID25281266
PMCPMC4252766

What OpenQuestion holds

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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.