Evidence map›Paper›PMID 42219643›Full record

ArticleAnalytica chimica acta2026

Ion chromatography-ultra-high-resolution mass spectrometry reveals EZH2-driven reprogramming of nucleic acid and protein methylation.

Mohamed M Y Kaddah, Teresa W-M Fan, Jahid M M Islam, Penghui Lin, Teresa A Cassel, Richard Cunningham, Tom Brown, Richard M Higashi, Andrew N Lane

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Analytica chimica acta, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Mohamed M Y KaddahCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA; Department of Toxicology and Cancer Biology, College of Medicine, University of Kentucky, Lexington, KY, 40536, USA; Pharmaceutical and Fermentation Industries Development Center, City of Scientific Research and Technological Applications, New Borg El-Arab, Alexandria, 21934, Egypt.
Teresa W-M FanCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA; Department of Toxicology and Cancer Biology, College of Medicine, University of Kentucky, Lexington, KY, 40536, USA. Electronic address: Teresa.fan@uky.edu.
Jahid M M IslamCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA.
Penghui LinCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA.
Teresa A CasselCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA.
Richard CunninghamAssemblon Ltd., Atlas Building, Harwell Campus, Didcot, OX11 0QX, England. Electronic address: richard.cunningham@assemblon.co.uk.
Tom BrownDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, 12 Mansfield Road, Oxford, OX1 3TA, United Kingdom.
Richard M HigashiCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA; Department of Toxicology and Cancer Biology, College of Medicine, University of Kentucky, Lexington, KY, 40536, USA.
Andrew N LaneCenter for Environmental and Systems Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, KY, 40536, USA; Department of Toxicology and Cancer Biology, College of Medicine, University of Kentucky, Lexington, KY, 40536, USA. Electronic address: Andrew.lane@uky.edu.

Funding

University of Kentucky Center for Cancer MetabolismP20GM121327 · NIGMS · UNIVERSITY OF KENTUCKY · 2022 to 2025
$10.9M
University of Kentucky Markey Cancer Center – Cancer Center Support GrantP30CA177558 · UNIVERSITY OF KENTUCKY · 2025 to 2025
$2.8M
NCI NIH HHS P30 CA177558NIGMS NIH HHS P20 GM121327
6 · The paper itself

Abstract

enhancer of zestehomolog 2 (EZH2), a histone H3K27 trimethyltransferase, is a key epigenetic regulator frequently dysregulated in cancer. To determine its impact on nucleotide biosynthesis and nucleic acid methylation in intact cells requires highly sensitive, isomer-resolving analytical workflows. We developed a targeted ion chromatography-ultra-high-resolution Fourier transform mass spectrometry (IC-UHR-FTMS) workflow with lower limits of quantification down to 9 fmol on-column to determine changes in methylation of DNA, total RNA, and mRNA in A549 cells following EZH2 knockdown (KD). Using dual stable isotope tracers, l-methionine-(methyl-

Indexed as

Enhancer of Zeste Homolog 2 ProteinDNA MethylationHumansMass SpectrometryMethylationRNA MethylationEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanEZH2Ion chromatography (IC)Isotopologue analysisMethylated nucleotidesRNA methylationStable isotope-resolved metabolomics (SIRM)Ultra-high-resolution mass spectrometry (UHR-MS)

Identifiers

PMID42219643
PMCPMC13245552

What Socratic 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 Socratic graph.