Evidence map›Paper›PMID 23934150›Full record

ArticleNature structural & molecular biology2013

The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.

Nadia Arnaudo, Israel S Fernández, Stephen H McLaughlin, Sew Y Peak-Chew, Daniela Rhodes, Fabrizio Martino

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 85 citations in OpenAlex.

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  16. NAA10 as a New Prognostic Marker for Cancer Progression.International journal of molecular sciences · 2020
    Review
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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

6 authors at 2 institutions in 2 countries.

Nadia ArnaudoStructural Studies Division, Medical Research Council-Laboratory of Molecular Biology, Cambridge, UK.
Israel S Fernández
Stephen H McLaughlin
Sew Y Peak-Chew
Daniela Rhodes
Fabrizio Martino
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC-A025-5PJ80Medical Research Council MC_U105184333
6 · The paper itself

Abstract

The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.

Indexed as

AcetylationCrystallography, X-RayMacromolecular SubstancesModels, MolecularMutagenesis, Site-DirectedNucleosomesProtein ConformationProtein Interaction Domains and MotifsProtein StabilityRecombinant ProteinsSaccharomyces cerevisiaeSilent Information Regulator Proteins, Saccharomyces cerevisiaeStatic ElectricityMacromolecular SubstancesNucleosomesRecombinant ProteinsSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR3 protein, S cerevisiae

Identifiers

PMID23934150
PMCPMC3818696
OpenAlexW2105572826

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.