Determining the Substrate Specificity of Lysine Methyltransferases.

Jocelyne N Hanquier, Christine A Berryhill, Evan M Cornett

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. 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

3 authors.

Jocelyne N HanquierDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.

Christine A BerryhillDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.

Evan M CornettDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA. evcorn@iu.edu.

Funding

Regulation of non-histone protein function by lysine methylationR35GM147023 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI Evan Mitchell Cornett · 2022 to 2026

$1.9M

NIGMS NIH HHS R35 GM147023

6 · The paper itself

Abstract

Lysine methyltransferases (KMTs) catalyze mono-, di-, and tri-methylation on histone and non-histone proteins. Determining the substrate specificity of KMTs is a critical task. This chapter outlines a method to perform highly sensitive in vitro methyltransferase assays on peptide substrates. In addition to comparing peptide substrates from histone or non-histone proteins, we also describe the use of a lysine-oriented peptide library (K-OPL) to generate high-resolution substrate specificity profiles for KMTs.

Indexed as

Enzyme AssaysHistone-Lysine N-MethyltransferaseHistonesHumansLysineMethylationPeptide LibraryPeptidesSubstrate SpecificityHistone-Lysine N-MethyltransferaseHistonesLysinePeptide LibraryPeptidesChromatinEpigeneticsHistonesLysine methylationMethyltransferasePeptide librariesPosttranslational modificationsSubstrate specificityWriters

Identifiers

PMID40257566

DOI10.1007/978-1-0716-4486-7_13

PMCPMC13213818

What Socratic holds

Textmetadata

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Registered trials

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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.