Evidence map›Paper›PMID 26421618›Full record

ArticlePloS one2015

The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain.

Bas J G E Pieters, Erik Meulenbroeks, Roman Belle, Jasmin Mecinović

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Epigenetic Regulation Via Electrical Forces.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  2. Article
  3. Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020
    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 1 institution in 1 country.

Bas J G E PietersInstitute of Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
Erik MeulenbroeksInstitute of Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
Roman BelleInstitute of Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
Jasmin MecinovićInstitute of Molecules and Materials, Radboud University Nijmegen, Nijmegen, The Netherlands.
Radboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several reader domain proteins that specifically recognize methyllysine-containing histones contain the negatively-charged aspartate or glutamate residues as part of the aromatic cage. Herein, we report thermodynamic analyses for the recognition of histone H3K4me3 and H3K4me2 by the tandem tudor domain of Sgf29 and its recognition site variants. Small uncharged and large aromatic substitutions on the Asp266 site resulted in a significant decrease in binding affinities for both H3K4me3 and H3K4me2, demonstrating the role of the negative charge of Asp266 in the readout process by Sgf29. This study emphasizes the essential contribution of electrostatic interactions to the overall binding affinity, and reveals that the underlying mechanisms for the recognition of Kme2/3 depend on the composition and arrangement of the aromatic cage.

Indexed as

Static ElectricityAcetyltransferasesAspartic AcidHistonesLysineMethylationModels, MolecularProtein BindingProtein Structure, TertiaryThermodynamicsAcetyltransferasesAspartic AcidHistonesLysine

Identifiers

PMID26421618
PMCPMC4589357
OpenAlexW2337308003

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.