Evidence map›Paper›PMID 28771339›Full record

ArticleBiochemistry2017

Specific Acetylation Patterns of H2A.Z Form Transient Interactions with the BPTF Bromodomain.

Gabriella T Perell, Neeraj K Mishra, Babu Sudhamalla, Peter D Ycas, Kabirul Islam, William C K Pomerantz

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2017. 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
1.3field-weighted citation impact, top 19% 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, 22 citations in OpenAlex.

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  13. SAR by (Protein-Observed)Accounts of chemical research · 2019
    Review
  14. The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019
    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

6 authors at 2 institutions in 1 country.

Gabriella T PerellDepartment of Chemistry, University of Minnesota , 207 Pleasant Street Southeast, Minneapolis, Minnesota 55455, United States.
Neeraj K MishraDepartment of Chemistry, University of Minnesota , 207 Pleasant Street Southeast, Minneapolis, Minnesota 55455, United States.
Babu SudhamallaDepartment of Chemistry, University of Pittsburgh , 1307 Chevron Science Center, 219 Parkman Avenue, Pittsburgh, Pennsylvania 15260, United States.
Peter D YcasDepartment of Chemistry, University of Minnesota , 207 Pleasant Street Southeast, Minneapolis, Minnesota 55455, United States.
Kabirul IslamDepartment of Chemistry, University of Pittsburgh , 1307 Chevron Science Center, 219 Parkman Avenue, Pittsburgh, Pennsylvania 15260, United States.
William C K PomerantzDepartment of Chemistry, University of Minnesota , 207 Pleasant Street Southeast, Minneapolis, Minnesota 55455, United States.ORCID 0000-0002-0163-4078
University of Minnesota · USUniversity of Pittsburgh · US

Funding

Site-Specific Photochemistry on Epigenetic Readers for Interactome ProfilingR01GM123234 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ISLAM, KABIRUL · 2017 to 2021
$1.5M
NIGMS NIH HHS R01 GM123234
6 · The paper itself

Abstract

Post-translational lysine acetylation of histone tails affects both chromatin accessibility and recruitment of multifunctional bromodomain-containing proteins for modulating transcription. The bromodomain- and PHD finger-containing transcription factor (BPTF) regulates transcription but has also been implicated in high gene expression levels in a variety of cancers. In this report, the histone variant H2A.Z, which replaces H2A in chromatin, is evaluated for its affinity for BPTF with a specific recognition pattern of acetylated lysine residues of the N-terminal tail region. Although BPTF immunoprecipitates H2A.Z-containing nucleosomes, a direct interaction with its bromodomain has not been reported. Using protein-observed fluorine nuclear magnetic resonance (PrOF NMR) spectroscopy, we identified a diacetylation of H2A.Z on lysine residues 4 and 11, with the highest affinity for BPTF with a K

Indexed as

AcetylationAmino Acid SequenceBinding SitesEscherichia coliGene Expression RegulationHistonesLigandsModels, MolecularPlasmodium falciparumProtein ConformationProtein Domainshistone H2A.F-ZHistonesLigands

Identifiers

PMID28771339
PMCPMC5779092
OpenAlexW2744691030

What OpenQuestion holds

Textmetadata
LicenceTDM
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.