Evidence map›Paper›PMID 18845255›Full record

ReviewCurrent opinion in structural biology2008

Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function.

Ling Wang, Yong Tang, Philip A Cole, Ronen Marmorstein

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
–field-weighted citation impact
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

97 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. CBP/p300, a promising therapeutic target for prostate cancer.Journal of translational medicine · 2025
    Review
  6. Targeting lysine acetylation readers and writers.Nature reviews. Drug discovery · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. DELLA proteins recruit the Mediator complex subunit MED15 to coactivate transcription in land plants.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

37 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

4 authors.

Ling WangDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
Yong Tang
Philip A Cole
Ronen Marmorstein

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Structure/Function of Histone AcetyltransferasesR01GM060293 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2000 to 2016
$5.3M
Mechanisms &Inhibition of Histone AcetyltransferasesR01GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2001 to 2012
$3.8M
NCRR NIH HHS U54 RR020839NIGMS NIH HHS R01 GM060293NIGMS NIH HHS R01 GM062437
6 · The paper itself

Abstract

The recent structure and associated biochemical studies of the metazoan-specific p300/CBP and fungal-specific Rtt109 histone acetyltransferases (HATs) have provided new insights into the ancestral relationship between HATs and their functions. These studies point to a common HAT ancester that has evolved around a common structural framework to form HATs with divergent catalytic and substrate-binding properties. These studies also point to the importance of regulatory loops within HATs and autoacetylation in HAT function. Implications for future studies are discussed.

Indexed as

AcetylationAnimalsBinding SitesCrystallographyEvolution, MolecularHistone AcetyltransferasesHumansp300-CBP Transcription FactorsSaccharomyces cerevisiae ProteinsHistone Acetyltransferasesp300-CBP Transcription FactorsRtt109 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID18845255
PMCPMC2643075

What OpenQuestion holds

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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.