Evidence map›Paper›PMID 23788324›Full record

ArticleCurrent protocols in chemical biology2013

Profiling protein methylation with cofactor analog containing terminal alkyne functionality.

Gil Blum, Ian R Bothwell, 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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Biocompatible Chemistry: A Plug-and-Play Toolbox for Chemical Biology Research.Chembiochem : a European journal of chemical biology · 2025
    Review
  2. Review
  3. Chemical proteomics approaches for protein post-translational modification studies.Biochimica et biophysica acta. Proteins and proteomics · 2024
    Review
  4. Functionalised Cofactor Mimics for Interactome Discovery and Beyond.Angewandte Chemie (International ed. in English) · 2022
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Chemical Proteomic Profiling of Human Methyltransferases.Journal of the American Chemical Society · 2016
    Article
  13. Sensing Enzymatic Activity by Exposure and Selection of DNA-Encoded Probes.Angewandte Chemie (International ed. in English) · 2016
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. 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.

Gil BlumMolecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Ian R Bothwell
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

Enzymatic transmethylation from the cofactor S-adenosyl-L-methionine (SAM) to biological molecules has recently garnered increased attention because of the diversity of possible substrates and implications in normal biology and diseases. To reveal the substrates of protein methyltransferases (PMTs), the present article focuses on an alkyne-containing SAM mimic, Se-adenosyl-L-selenomethionine (ProSeAM), and a cleavable azido-azo-biotin probe to profile the targets of endogenous PMTs in cellular contexts. This article describes the stepwise preparation of cell lysates containing active, endogenous PMTs and subsequent target labeling with ProSeAM. The article continues with the enrichment of the ProSeAM-labeled proteins with the azido-azo biotin probe as a pulldown reagent and the subsequent reductive elution with sodium dithionate for proteomic analysis. The protocols provided here were formulated for ProSeAM as a profiling reagent but can be applied to other terminal-alkyne-containing SAM analog cofactors.

Indexed as

AzidesBiotinCell LineChloroformFluorescent DyesHumansMethanolMethylationProtein MethyltransferasesProteinsProteomeSelenomethionineSolventsStaining and LabelingWaterAzidesBiotinChloroformFluorescent DyesMethanolpropargylic Se-adenosyl-L-selenomethionineProtein MethyltransferasesProteinsProteomeSelenomethionineSolventsWaterazido‐azo biotin probeclick chemistryProSeAMSe‐adenosyl‐L‐selenomethionine

Identifiers

PMID23788324
PMCPMC4562793

What OpenQuestion holds

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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.