Evidence map›Paper›PMID 29170789›Full record

ReviewCellular and molecular life sciences : CMLS2018

CREBBP and p300 lysine acetyl transferases in the DNA damage response.

Ilaria Dutto, Claudia Scalera, Ennio Prosperi

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

61 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. HSP90α lactylation orchestrates PGC1α and LRPGC1 nuclear translocation driving mitochondrial biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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1 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Ilaria DuttoIstituto di Genetica Molecolare del CNR, Via Abbiategrasso 207, 27100, Pavia, Italy.
Claudia ScaleraIstituto di Genetica Molecolare del CNR, Via Abbiategrasso 207, 27100, Pavia, Italy.
Ennio ProsperiIstituto di Genetica Molecolare del CNR, Via Abbiategrasso 207, 27100, Pavia, Italy. prosperi@igm.cnr.it.ORCID 0000-0001-5391-5157
Istituto di Genetica Molecolare · ITInstitute for Research in Biomedicine · ES

Funding

Associazione Italiana per la Ricerca sul Cancro IG 17041
6 · The paper itself

Abstract

The CREB-binding protein (CREBBP, or in short CBP) and p300 are lysine (K) acetyl transferases (KAT) belonging to the KAT3 family of proteins known to modify histones, as well as non-histone proteins, thereby regulating chromatin accessibility and transcription. Previous studies have indicated a tumor suppressor function for these enzymes. Recently, they have been found to acetylate key factors involved in DNA replication, and in different DNA repair processes, such as base excision repair, nucleotide excision repair, and non-homologous end joining. The growing list of CBP/p300 substrates now includes factors involved in DNA damage signaling, and in other pathways of the DNA damage response (DDR). This review will focus on the role of CBP and p300 in the acetylation of DDR proteins, and will discuss how this post-translational modification influences their functions at different levels, including catalytic activity, DNA binding, nuclear localization, and protein turnover. In addition, we will exemplify how these functions may be necessary to efficiently coordinate the spatio-temporal response to DNA damage. CBP and p300 may contribute to genome stability by fine-tuning the functions of DNA damage signaling and DNA repair factors, thereby expanding their role as tumor suppressors.

Indexed as

DNA RepairProtein Processing, Post-TranslationalAcetylationAnimalsChromatinChromatin Assembly and DisassemblyCREB-Binding ProteinDNADNA DamageDNA ReplicationGenomic InstabilityHumansp300-CBP Transcription FactorsProtein BindingTumor Suppressor ProteinsChromatinCREB-Binding ProteinCREBBP protein, humanDNAp300-CBP Transcription FactorsTumor Suppressor ProteinsDNA repairDNA repair enzymesDNA replicationPost-translational modificationProtein acetylation

Identifiers

PMID29170789
PMCPMC11105205
OpenAlexW2770260059

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.