ArticleEpigenetics2011
MassSQUIRM: An assay for quantitative measurement of lysine demethylase activity.
Article in Epigenetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Discovery of a potent and dual-selective bisubstrate inhibitor for protein arginine methyltransferase 4/5.Acta pharmaceutica Sinica. B · 2021Article
- Chemical and Biochemical Perspectives of Protein Lysine Methylation.Chemical reviews · 2018Review
- LSD1 Histone Demethylase Assays and Inhibition.Methods in enzymology · 2016Review
- A direct, ratiometric, and quantitative MALDI-MS assay for protein methyltransferases and acetyltransferases.Analytical biochemistry · 2015Article
- Design, synthesis, and kinetic analysis of potent protein N-terminal methyltransferase 1 inhibitors.Organic & biomolecular chemistry · 2015Article
- Measurement of lysine-specific demethylase-1 activity in the nuclear extracts by flow-injection based time-of-flight mass spectrometry.Journal of clinical biochemistry and nutrition · 2015Article
- A selective phenelzine analogue inhibitor of histone demethylase LSD1.ACS chemical biology · 2014Article
- Using glycinylation, a chemical derivatization technique, for the quantitation of ubiquitinated proteins.Analytical chemistry · 2013Article
- Comprehending dynamic protein methylation with mass spectrometry.Current opinion in chemical biology · 2013Review
- Application of MassSQUIRM for quantitative measurements of lysine demethylase activity.Journal of visualized experiments : JoVE · 2012Article
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
In eukaryotes, DNA is wrapped around proteins called histones and is condensed into chromatin. Post-translational modification of histones can result in changes in gene expression. One of the most well-studied histone modifications is the methylation of lysine 4 on histone H3 (H3K4). This residue can be mono-, di- or tri-methylated and these varying methylation states have been associated with different levels of gene expression. Understanding exactly what the purpose of these methylation states is, in terms of gene expression, has been a topic of much research in recent years. Enzymes that can add (methyltransferases) and remove (demethylases) these modifications are of particular interest. The first demethylase discovered, LSD1, is the most well-classified and has been implicated in contributing to human cancers and to DNA damage response pathways. Currently, there are limited methods for accurately studying the activity of demethylases in vitro or in vivo. In this work, we present MassSQUIRM (mass spectrometric quantitation using isotopic reductive methylation), a quantitative method for studying the activity of demethylases capable of removing mono- and di-methyl marks from lysine residues. We focus specifically on LSD1 due to its potential as a prime therapeutic target for human disease. This quantitative approach will enable better characterization of the activity of LSD1 and other chromatin modifying enzymes in vitro, in vivo or in response to inhibitors.
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