Evidence map›Paper›PMID 24984779›Full record

ReviewCold Spring Harbor perspectives in biology2014

Writers and readers of histone acetylation: structure, mechanism, and inhibition.

Ronen Marmorstein, Ming-Ming Zhou

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 345 papers.

0numbers the graph read from it
0cells of the map it votes in
345citing 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

345 citing papers in PubMed, 627 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Current Challenges of Transcription Compartmentalization Research.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Post-Translational Regulation of CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  14. Review
  15. Review
  16. Article
  17. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  18. Article
  19. Article
  20. Review

285 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

2 authors at 2 institutions in 1 country.

Ronen MarmorsteinProgram in Gene Expression and Regulation, Wistar Institute, and Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, 19104.
Ming-Ming ZhouDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York 10065.
Icahn School of Medicine at Mount Sinai · USThe Wistar Institute · US

Funding

STRUCTURAL BASIS FOR EPIGENETICS IN AGING AND LONGEVITYP01AG031862 · NIA · WISTAR INSTITUTE · PI GARCIA, BENJAMIN A · 2008 to 2022
$28.3M
PW1--A mediator of cell survival by NFKB and cell death by p53P01CA080058 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI AARONSON, STUART A · 2000 to 2016
$20.2M
Chemical Genomics Paradigm for Epigentic RegulationR01HG004508 · NHGRI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI ZHOU, MING-MING · 2008 to 2014
$6.7M
Structure/Function of Histone AcetyltransferasesR01GM060293 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2000 to 2016
$5.3M
STRUCTURE OF PROTEIN MODULES IN CHROMATIN REMODELINGR01CA087658 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI ZHOU, MING-MING · 2000 to 2016
$4.8M
Development of an HTS assay for ySas2/hMOF histone acetyltransferase inhibitorsR01GM098910 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2011 to 2013
$949k
NCI NIH HHS CA87658NCI NIH HHS P01 CA080058NCI NIH HHS R01 CA087658NHGRI NIH HHS HG004508NHGRI NIH HHS R01 HG004508NIA NIH HHS AG031862NIA NIH HHS P01 AG031862NIGMS NIH HHS GM060293NIGMS NIH HHS GM098910NIGMS NIH HHS R01 GM060293NIGMS NIH HHS R01 GM098910
6 · The paper itself

Abstract

Histone acetylation marks are written by histone acetyltransferases (HATs) and read by bromodomains (BrDs), and less commonly by other protein modules. These proteins regulate many transcription-mediated biological processes, and their aberrant activities are correlated with several human diseases. Consequently, small molecule HAT and BrD inhibitors with therapeutic potential have been developed. Structural and biochemical studies of HATs and BrDs have revealed that HATs fall into distinct subfamilies containing a structurally related core for cofactor binding, but divergent flanking regions for substrate-specific binding, catalysis, and autoregulation. BrDs adopt a conserved left-handed four-helix bundle to recognize acetyllysine; divergent loop residues contribute to substrate-specific acetyllysine recognition.

Indexed as

Models, MolecularAcetylationBinding SitesChromatinDrug DiscoveryEnzyme InhibitorsHistone AcetyltransferasesHistonesProtein Processing, Post-TranslationalProtein Structure, TertiaryChromatinEnzyme InhibitorsHistone AcetyltransferasesHistones

Identifiers

PMID24984779
PMCPMC4067988
OpenAlexW2143277424

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.