Evidence map›Paper›PMID 32498971›Full record

ReviewTrends in biochemical sciences2020

Nothing Is Yet Set in (Hi)stone: Novel Post-Translational Modifications Regulating Chromatin Function.

Jennifer C Chan, Ian Maze

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

66 citing papers in PubMed, 122 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
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  6. Quinone reductase 2bioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Review
  9. Review
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  11. Article
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  15. The role of epigenetics in cancer: From pathways to the clinic.Journal of family medicine and primary care · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

6 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.

Jennifer C ChanDepartment of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Ian MazeDepartment of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA. Electronic address: ian.maze@mssm.edu.
Allen Institute for Brain Science · USIcahn School of Medicine at Mount Sinai · US

Funding

Molecular studies of neural histone monoaminylation in normal and aberrant brain plasticityR01MH116900 · NIMH · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Ian S. Maze · 2019 to 2026
$4.7M
Aberrant chromatin regulatory mechanisms in Down syndrome brainR01HD097088 · NICHD · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Ian S. Maze · 2019 to 2026
$4.0M
Roles for histone monoaminylation in cocaine-induced transcriptional and behavioral plasticityDP1DA042078 · NIDA · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI MAZE, IAN S. · 2016 to 2021
$3.2M
Application of intein-based chemical methods to directly manipulate neuronal histone modifications in rodent models of addictionR21DA044767 · NIDA · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI DAVID-SHTERNBERG, YAEL E, MAZE, IAN S. · 2018 to 2019
$444k
NICHD NIH HHS R01 HD097088NIDA NIH HHS DP1 DA042078NIDA NIH HHS R21 DA044767NIMH NIH HHS R01 MH116900
6 · The paper itself

Abstract

Histone post-translational modifications (PTMs) have emerged as exciting mechanisms of biological regulation, impacting pathways related to cancer, immunity, brain function, and more. Over the past decade alone, several histone PTMs have been discovered, including acylation, lipidation, monoaminylation, and glycation, many of which appear to have crucial roles in nucleosome stability and transcriptional regulation. In this review, we discuss novel histone PTMs identified within the past 10 years, with an extended focus on enzymatic versus nonenzymatic mechanisms underlying modification and adduction. Furthermore, we consider how these novel histone PTMs might fit within the framework of a so-called 'histone code', emphasizing the physiological relevance of these PTMs in metabolism, development, and disease states.

Indexed as

Protein Processing, Post-TranslationalAcetylationChromatinGene Expression RegulationHistonesHumansChromatinHistonesacylationglycationhistone code hypothesislipidationmonoaminylationnonenzymatic adduction

Identifiers

PMID32498971
PMCPMC7502514
OpenAlexW3032351423

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.