Evidence map›Paper›PMID 18086704›Full record

ArticleNucleic acids research2008

Differentiation-dependent lysine 4 acetylation enhances MEF2C binding to DNA in skeletal muscle cells.

Cecilia Angelelli, Alessandro Magli, Daniela Ferrari, Massimo Ganassi, Vittoria Matafora, Flavia Parise, Giorgia Razzini, Angela Bachi, Stefano Ferrari, Susanna Molinari

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. 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
0.7field-weighted citation impact, top 31% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

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  13. Suppression of the GLUT4 adaptive response to exercise in fructose-fed rats.American journal of physiology. Endocrinology and metabolism · 2014
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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

10 authors at 1 institution in 1 country.

Cecilia AngelelliDepartment of Biomedical Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Alessandro Magli
Daniela Ferrari
Massimo Ganassi
Vittoria Matafora
Flavia Parise
Giorgia Razzini
Angela Bachi
Stefano Ferrari
Susanna Molinari
University of Modena and Reggio Emilia · IT

Funding

Telethon GP0210Y01
6 · The paper itself

Abstract

Myocyte enhancer factor 2 (MEF2) proteins play a key role in promoting the expression of muscle-specific genes in differentiated muscle cells. MEF2 activity is regulated by the association with several transcriptional co-factors and by post-translational modifications. In the present report, we provide evidence for a novel regulatory mechanism of MEF2C activity, which occurs at the onset of skeletal muscle differentiation and is based on Lys4 acetylation. This covalent modification results in the enhancement of MEF2C binding to DNA and chromatin. In particular, we report that the kinetic parameters of MEF2/DNA association change substantially upon induction of differentiation to give a more stable complex and that this effect is mediated by Lys4 acetylation. We also show that Lys4 acetylation plays a prominent role in the p300-dependent activation of MEF2C.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceAnimalsBinding SitesCell DifferentiationCell LineChromatinDNAElectrophoretic Mobility Shift AssayFluorescence Recovery After PhotobleachingLysineMEF2 Transcription FactorsMiceMolecular Sequence DataMuscle, SkeletalChromatinDNALysineMef2c protein, mouseMEF2 Transcription FactorsMyogenic Regulatory FactorsMyogeninp300-CBP-Associated Factorp300-CBP Transcription Factors

Identifiers

PMID18086704
PMCPMC2241889
OpenAlexW2139503369

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.