Evidence map›Paper›PMID 37054563›Full record

ReviewCurrent opinion in chemical biology2023

Post-translational modifications of histone proteins by monoamine neurotransmitters.

Amni Al-Kachak, Ian Maze

Open access · hybridAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  8. Quinone reductase 2bioRxiv : the preprint server for biology · 2026
    Article
  9. Review
  10. Epigenetic regulation of brain development, plasticity, and response to early-life stress.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026
    Review
  11. Article
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  20. Beyond the 5-HTThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Review
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.

Amni Al-KachakNash Family Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Ian MazeNash Family Department 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; Howard Hughes Medical Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA. Electronic address: ian.maze@mssm.edu.
Allen Institute for Brain Science · USHoward Hughes Medical Institute · 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
Contributions of aberrant synaptic protein monoaminylation to opiate use disorderR01DA056595 · NIDA · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI DAVID M DIETZ, Ian S. Maze · 2022 to 2026
$3.5M
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
NIDA NIH HHS DP1 DA042078NIDA NIH HHS R01 DA056595NIMH NIH HHS R01 MH116900
6 · The paper itself

Abstract

Protein monoaminylation is a biochemical process through which biogenic monoamines (e.g., serotonin, dopamine, histamine, etc.) are covalently bonded to certain protein substrates via Transglutaminase 2, an enzyme that catalyzes the transamidation of primary amines to the γ-carboxamides of glutamine residues. Since their initial discovery, these unusual post-translational modifications have been implicated in a wide variety of biological processes, ranging from protein coagulation to platelet activation and G-protein signaling. More recently, histone proteins - specifically histone H3 at glutamine 5 (H3Q5) - have been added to the growing list of monoaminyl substrates in vivo, with H3Q5 monoaminylation demonstrated to regulate permissive gene expression in cells. Such phenomena have further been shown to contribute critically to various aspects of (mal)adaptive neuronal plasticity and behavior. In this short review, we examine the evolution of our understanding of protein monoaminylation events, highlighting recent advances in the elucidation of their roles as important chromatin regulators.

Indexed as

GlutamineHistonesBiogenic MonoaminesNeurotransmitter AgentsProtein Processing, Post-TranslationalBiogenic MonoaminesGlutamineHistonesNeurotransmitter Agents

Identifiers

PMID37054563
PMCPMC10225327
OpenAlexW4364369932

What Socratic 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 Socratic graph.