Evidence map›Paper›PMID 34592262›Full record

ArticleBiophysical journal2021

Probing multiple enzymatic methylation events in real time with NMR spectroscopy.

Emery T Usher, Kevin E W Namitz, Michael S Cosgrove, Scott A Showalter

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 25% of its field
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

8 citing papers in PubMed, 15 citations in OpenAlex.

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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 at 2 institutions in 1 country.

Emery T UsherCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology.
Kevin E W NamitzDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania.
Michael S CosgroveSUNY Upstate Medical University, Department of Biochemistry and Molecular Biology, Syracuse, New York.
Scott A ShowalterCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology; Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania. Electronic address: sas76@psu.edu.
Pennsylvania State University · USSUNY Upstate Medical University · US

Funding

Molecular Mechanisms for the Assembly and Regulation of the MLL1 Core ComplexR01CA140522 · NCI · UPSTATE MEDICAL UNIVERSITY · PI COSGROVE, MICHAEL S. · 2010 to 2019
$3.6M
Structure and Mechanism of Transcription Factors in Pancreatic Beta CellsR01DK121509 · NIDDK · PENNSYLVANIA STATE UNIVERSITY, THE · PI SHOWALTER, SCOTT A · 2019 to 2021
$1.2M
The molecular mechanisms of Pdx1 destabilization by SPOPF31DK124047 · NIDDK · PENNSYLVANIA STATE UNIVERSITY, THE · PI USHER, EMERY THOMAS · 2019 to 2022
$101k
NCI NIH HHS R01 CA140522NIDDK NIH HHS F31 DK124047NIDDK NIH HHS R01 DK121509
6 · The paper itself

Abstract

Post-translational modification (PTM) of proteins is of critical importance to the regulation of many cellular processes in eukaryotic organisms. One of the most well-studied protein PTMs is methylation, wherein an enzyme catalyzes the transfer of a methyl group from a cofactor to a lysine or arginine side chain. Lysine methylation is especially abundant in the histone tails and is an important marker for denoting active or repressed genes. Given their relevance to transcriptional regulation, the study of methyltransferase function through in vitro experiments is an important stepping stone toward understanding the complex mechanisms of regulated gene expression. To date, most methyltransferase characterization strategies rely on the use of radioactive cofactors, detection of a methyl transfer byproduct, or discontinuous-type assays. Although such methods are suitable for some applications, information about multiple methylation events and kinetic intermediates is often lost. Herein, we describe the use of two-dimensional NMR to monitor mono-, di-, and trimethylation in a single reaction tube. To do so, we incorporated

Indexed as

Histone-Lysine N-MethyltransferaseHistonesMagnetic Resonance SpectroscopyMethylationProtein Processing, Post-TranslationalHistone-Lysine N-MethyltransferaseHistones

Identifiers

PMID34592262
PMCPMC8595733
OpenAlexW3201843501

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.