Evidence map›Paper›PMID 18268010›Full record

ArticleMolecular and cellular biology2008

14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation.

Wendy Walter, David Clynes, Yong Tang, Ronen Marmorstein, Jane Mellor, Shelley L Berger

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 92 citations in OpenAlex.

  1. Phase II Open-Label, Single-Arm Trial to Investigate the Efficacy and Safety of Topical Remetinostat Gel in Patients with Basal Cell Carcinoma.Clinical cancer research : an official journal of the American Association for Cancer Research · 2021
    Trial
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  5. Understanding PTM Cross Talk Through a Visualization Tool, PTMViz.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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  18. Epigenetic regulation of estrogen-dependent memory.Frontiers in neuroendocrinology · 2014
    Review
  19. Review
  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 at 2 institutions in 2 countries.

Wendy WalterDivision of Molecular Genetics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3 QU, United Kingdom.
David Clynes
Yong Tang
Ronen Marmorstein
Jane Mellor
Shelley L Berger
The Wistar Institute · USUniversity of Oxford · GB

Funding

TRAINING PROGRAM IN BASIC CANCER RESEARCHT32CA009171 · NCI · WISTAR INSTITUTE · PI Alessandro Gardini · 1985 to 2026
$15.3M
Chromatin regulatory mechanisms in eukaryotic gametogenesisR01GM055360 · NIGMS · WISTAR INSTITUTE · PI BERGER, SHELLEY L · 1998 to 2015
$5.1M
NCI NIH HHS 5T32 CA09171-28NCI NIH HHS T32 CA009171NIGMS NIH HHS GM55360NIGMS NIH HHS R01 GM055360
6 · The paper itself

Abstract

Histone modifications occur in precise patterns and are proposed to signal the recruitment of effector molecules that profoundly impact chromatin structure, gene regulation, and cell cycle events. The linked modifications serine 10 phosphorylation and lysine 14 acetylation on histone H3 (H3S10phK14ac), modifications conserved from Saccharomyces cerevisiae to humans, are crucial for transcriptional activation of many genes. However, the mechanism of H3S10phK14ac involvement in these processes is unclear. To shed light on the role of this dual modification, we utilized H3 peptide affinity assays to identify H3S10phK14ac-interacting proteins. We found that the interaction of the known phospho-binding 14-3-3 proteins with H3 is dependent on the presence of both of these marks, not just phosphorylation alone. This is true of mammalian 14-3-3 proteins as well as the yeast homologues Bmh1 and Bmh2. The importance of acetylation in this interaction is also seen in vivo, where K14 acetylation is required for optimal Bmh1 recruitment to the GAL1 promoter during transcriptional activation.

Indexed as

14-3-3 ProteinsAcetylationCalorimetryHeLa CellsHistonesHumansPhosphorylationPhosphoserinePromoter Regions, GeneticProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins14-3-3 ProteinsHistonesPhosphoserineSaccharomyces cerevisiae Proteins

Identifiers

PMID18268010
PMCPMC2293105
OpenAlexW2047100301

What OpenQuestion holds

Textmetadata
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.