Evidence map›Paper›PMID 30839196›Full record

ReviewChemical research in toxicology2019

(De)Toxifying the Epigenetic Code.

Qingfei Zheng, Nicholas A Prescott, Igor Maksimovic, Yael David

Open access · greenAbstract readReview
In one paragraph

Review in Chemical research in toxicology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Epigenetic meets metabolism: novel vulnerabilities to fight cancer.Cell communication and signaling : CCS · 2023
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. A chemical field guide to histone nonenzymatic modifications.Current opinion in chemical biology · 2021
    Review
  15. Sirtuin 2 Regulates Protein LactoylLys Modifications.Chembiochem : a European journal of chemical biology · 2021
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
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 at 1 institution in 1 country.

Qingfei ZhengChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10044 , New York , United States.ORCID 0000-0002-8397-3507
Nicholas A PrescottChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10044 , New York , United States.
Igor MaksimovicChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10044 , New York , United States.
Yael DavidChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10044 , New York , United States.
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
Tri-Institutional PhD Program in Chemical BiologyT32GM115327 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI TAN, DEREK S · 2015 to 2019
$741k
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
NCI NIH HHS P30 CA008748NIDA NIH HHS R21 DA044767NIGMS NIH HHS T32 GM115327
6 · The paper itself

Abstract

Cells are continuously subjected to an array of reactive/toxic chemical species which are produced both endogenously through metabolic pathways and taken up exogenously by diet and exposure to drugs or toxins. As a result, proteins often undergo non-enzymatic covalent modifications (NECMs) by these species, which can alter protein structure, function, stability, and binding partner affinity. NECMs accumulate over time and are linked to various diseases such as Alzheimer's disease, cancer, and diabetes. In the cellular proteome, histones have some of the longest half-lives, making them prime targets for NECMs. In addition, histones have emerged as key regulators of transcription, a function that is primarily controlled by modification of their tails. These modifications are usually installed or removed enzymatically, but recent evidence suggests that some may also occur non-enzymatically. Despite the vast knowledge detailing the relationship between histone modifications and gene regulation, NECMs on histones remain poorly explored. A major reason for this difference stems from the fact that, unlike their enzymatically installed counterparts, NECMs are difficult to both control and test in vivo. Here, we review advances in our understanding of the effect non-enzymatic covalent modifications (NECMs) have on the epigenetic landscape, cellular fate, and their implications in disease. Cumulatively, this illustrates how the epigenetic code is directly toxified by chemicals and detoxified by corresponding eraser enzymes.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAnimalsEpigenomicsHistone CodeHistonesHumansHistones

Identifiers

PMID30839196
PMCPMC6583786
OpenAlexW2921657004

What OpenQuestion holds

Textmetadata
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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.