Evidence map›Paper›PMID 23870121›Full record

ArticleCell2013

SET1 and p300 act synergistically, through coupled histone modifications, in transcriptional activation by p53.

Zhanyun Tang, Wei-Yi Chen, Miho Shimada, Uyen T T Nguyen, Jaehoon Kim, Xiao-Jian Sun, Toru Sengoku, Robert K McGinty, Joseph P Fernandez, Tom W Muir and 1 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

111 citing papers in PubMed, 168 citations in OpenAlex.

  1. Article
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51 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Zhanyun TangLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10065, USA.
Wei-Yi Chen
Miho Shimada
Uyen T T Nguyen
Jaehoon Kim
Xiao-Jian Sun
Toru Sengoku
Robert K McGinty
Joseph P Fernandez
Tom W Muir
Robert G Roeder
Rockefeller University · USPrinceton University · US

Funding

Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
Mechanisms of p53 target gene activation in DNA damage responsesR01CA129325 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2007 to 2011
$4.0M
Development and Applications of 'Designer Chromatin'R01GM107047 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2013 to 2016
$1.2M
NCI NIH HHS CA129325NCI NIH HHS R01 CA129325NIGMS NIH HHS R01 GM107047NIGMS NIH HHS T32 GM007739
6 · The paper itself

Abstract

The H3K4me3 mark in chromatin is closely correlated with actively transcribed genes, although the mechanisms involved in its generation and function are not fully understood. In vitro studies with recombinant chromatin and purified human factors demonstrate a robust SET1 complex (SET1C)-mediated H3K4 trimethylation that is dependent upon p53- and p300-mediated H3 acetylation, a corresponding SET1C-mediated enhancement of p53- and p300-dependent transcription that reflects a primary effect of SET1C through H3K4 trimethylation, and direct SET1C-p53 and SET1C-p300 interactions indicative of a targeted recruitment mechanism. Complementary cell-based assays demonstrate a DNA-damage-induced p53-SET1C interaction, a corresponding enrichment of SET1C and H3K4me3 on a p53 target gene (p21/WAF1), and a corresponding codependency of H3K4 trimethylation and transcription upon p300 and SET1C. These results establish a mechanism in which SET1C and p300 act cooperatively, through direct interactions and coupled histone modifications, to facilitate the function of p53.

Indexed as

Transcriptional ActivationAcetylationAmino Acid SequenceCyclin-Dependent Kinase Inhibitor p21DNA DamageE1A-Associated p300 ProteinHCT116 CellsHistone CodeHistone-Lysine N-MethyltransferaseHistonesHumansMethylationMolecular Sequence DataMultiprotein ComplexesTranscription, GeneticTumor Suppressor Protein p53CDKN1A protein, humanCyclin-Dependent Kinase Inhibitor p21E1A-Associated p300 ProteinEP300 protein, humanHistone-Lysine N-MethyltransferaseHistonesMultiprotein ComplexesSetd1A protein, humanTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID23870121
PMCPMC4023349
OpenAlexW2016148607

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.