Evidence map›Paper›PMID 23667794›Full record

ArticleCurrent protocols in chemical biology2013

Bioorthogonal profiling of protein methylation (BPPM) using an azido analog of S-adenosyl-L-methionine.

Gil Blum, Kabirul Islam, Minkui Luo

Abstract read
In one paragraph

Article in Current protocols in chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. DNA Labeling Using DNA Methyltransferases.Advances in experimental medicine and biology · 2022
    Article
  4. Article
  5. Article
  6. Lysine methylation signaling of non-histone proteins in the nucleus.Cellular and molecular life sciences : CMLS · 2019
    Review
  7. Review
  8. Methyltransferase-Directed Labeling of Biomolecules and its Applications.Angewandte Chemie (International ed. in English) · 2017
    Review
  9. Review
  10. Review
  11. DNA Labeling Using DNA Methyltransferases.Advances in experimental medicine and biology · 2016
    Review
  12. Article
  13. 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

3 authors.

Gil BlumMolecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Kabirul Islam
Minkui Luo

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 1R01GM096056NIGMS NIH HHS R01 GM096056NIH HHS 1DP2-OD007335NIH HHS DP2 OD007335NINDS NIH HHS R21 NS071520NINDS NIH HHS R21NS071520
6 · The paper itself

Abstract

Protein methyltransferases (PMTs) utilize S-adenosyl-L-methionine (SAM) as a cofactor and transfer its sulfonium methyl moiety to diverse substrates. These methylation events can lead to meaningful biological outcomes, from transcriptional activation/silencing to cell cycle regulation. This article describes recently developed technology based on protein engineering in tandem with SAM analog cofactors and bioorthogonal click chemistry to unambiguously profile the substrates of a specific PMT. The protocols encapsulate the logic and methods of selectively profiling the substrates of a candidate PMT by (1) engineering the selected PMT to accommodate a bulky SAM analog; (2) generating a proteome containing the engineered PMT; (3) visualizing the proteome-wide substrates of the designated PMT via bioorthogonal labeling with a fluorescent tag; and finally (4) pulling down the proteome-wide substrates for mass spectrometric analysis.

Indexed as

Amino Acid SequenceAzidesHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansMass SpectrometryMethylationMolecular Sequence DataMutationProteinsProteomeS-AdenosylmethionineStaining and LabelingAzidesEHMT2 protein, humanHistocompatibility AntigensHistone-Lysine N-MethyltransferaseProteinsProteomeS-Adenosylmethionine

Identifiers

PMID23667794
PMCPMC3647616

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.