Evidence map›Paper›PMID 22777714›Full record

ReviewMedicinal research reviews2012

Chemical and biochemical approaches in the study of histone methylation and demethylation.

Keqin Kathy Li, Cheng Luo, Dongxia Wang, Hualiang Jiang, Y George Zheng

Open access · greenAbstract readReview
In one paragraph

Review in Medicinal research reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. JMJD family proteins in cancer and inflammation.Signal transduction and targeted therapy · 2022
    Review
  6. Review
  7. Article
  8. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mechanisms and Inhibitors of Histone Arginine Methylation.Chemical record (New York, N.Y.) · 2018
    Review
  15. Review
  16. Computer-Aided Drug Design in Epigenetics.Frontiers in chemistry · 2018
    Review
  17. Article
  18. Review
  19. Small Molecule Inhibitors of Protein Arginine Methyltransferases.Expert opinion on investigational drugs · 2016
    Review
  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

5 authors at 4 institutions in 2 countries.

Keqin Kathy LiState Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, Rui Jin Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Cheng Luo
Dongxia Wang
Hualiang Jiang
Y George Zheng
Shanghai Institute of Materia Medica · CNCenters for Disease Control and Prevention · USGeorgia State University · USOFS (United States) · US

Funding

Chemical Approaches to Protein Arginine MethylationR01GM086717 · NIGMS · UNIVERSITY OF GEORGIA · PI ZHENG, Y. GEORGE · 2010 to 2014
$1.2M
NIGMS NIH HHS R01 GM086717
6 · The paper itself

Abstract

Histone methylation represents one of the most critical epigenetic events in DNA function regulation in eukaryotic organisms. Classic molecular biology and genetics tools provide significant knowledge about mechanisms and physiological roles of histone methyltransferases and demethylases in various cellular processes. In addition to this stream line, development and application of chemistry and chemistry-related techniques are increasingly involved in biological study, and offer information otherwise difficult to obtain by standard molecular biology methods. Herein, we review recent achievements and progress in developing and applying chemical and biochemical approaches in the study of histone methylation, including chromatin immunoprecipitation, chemical ligation, mass spectrometry, biochemical methylation and demethylation assays, and inhibitor development. These technological advances allow histone methylation to be studied from genome-wide level to molecular and atomic levels. With ChIP technology, information can be obtained about precise mapping of histone methylation patterns at specific promoters, genes, or other genomic regions. MS is particularly useful in detecting and analyzing methylation marks in histone and nonhistone protein substrates. Chemical approaches that permit site-specific incorporation of methyl groups into histone proteins greatly facilitate the investigation of biological impacts of methylation at individual modification sites. Discovery and design of selective organic inhibitors of histone methyltransferases and demethylases provide chemical probes to interrogate methylation-mediated cellular pathways. Overall, these chemistry-related technological advances have greatly improved our understanding of the biological functions of histone methylation in normal physiology and diseased states, and also are of great potential to translate basic epigenetics research into diagnostic and therapeutic applications in the clinic.

Indexed as

AnimalsEnzyme InhibitorsEpigenomicsGenomeHistone DemethylasesHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansMethylationProtein-Arginine N-MethyltransferasesEnzyme InhibitorsHistone DemethylasesHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesProtein-Arginine N-Methyltransferases

Identifiers

PMID22777714
PMCPMC4129395
OpenAlexW2067685926

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.