Evidence map›Paper›PMID 22220966›Full record

ReviewACS chemical biology2012

Current chemical biology approaches to interrogate protein methyltransferases.

Minkui Luo

Abstract readReview
In one paragraph

Review in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 136 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Detection and Quantification of Histone Methyltransferase Activity In Vitro.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Lysine Ethylation by Histone Lysine Methyltransferases.Chembiochem : a European journal of chemical biology · 2020
    Article
  18. Article
  19. Review
  20. Article

15 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

1 author at 1 institution in 1 country.

Minkui LuoMolecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, United States. luom@mskcc.org
Memorial Sloan Kettering Cancer Center · US

Funding

Profile substrates and inhibitors of protein lysine methyltransferaseR01GM096056 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI LUO, MINKUI · 2011 to 2018
$3.2M
Enzyme-engineering Approaches to Dissect Protein Methylation ProfilesDP2OD007335 · OD · SLOAN-KETTERING INST CAN RESEARCH · PI LUO, MINKUI · 2010 to 2010
$2.9M
Developing High Throughput Assay to Identify Protein Methyltransferase InhibitorsR21NS071520 · NINDS · SLOAN-KETTERING INST CAN RESEARCH · PI LUO, MINKUI · 2010 to 2010
$191k
NIGMS NIH HHS 1R01GM096056-01NIGMS NIH HHS R01 GM096056NIH HHS 1-DP2-OD007335-01NIH HHS DP2 OD007335NINDS NIH HHS 1R21NS071520-01NINDS NIH HHS R21 NS071520
6 · The paper itself

Abstract

Protein methyltransferases (PMTs) play various physiological and pathological roles through methylating histone and nonhistone targets. However, most PMTs including more than 60 human PMTs remain to be fully characterized. The current approaches to elucidate the functions of PMTs have been diversified by many emerging chemical biology technologies. This review focuses on progress in these aspects and is organized into four discussion modules (assays, substrates, cofactors, and inhibitors) that are important to elucidate biological functions of PMTs. These modules are expected to provide general guidance and present emerging methods for researchers to select and combine suitable PMT-activity assays, well-defined substrates, novel SAM surrogates, and PMT inhibitors to interrogate PMTs.

Indexed as

MethyltransferasesAnimalsHumansModels, MolecularMethyltransferases

Identifiers

PMID22220966
PMCPMC3306480
OpenAlexW1986955438

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.