Evidence map›Paper›PMID 35733021›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Characterization of SET-Domain Histone Lysine Methyltransferase Substrates Using a Cofactor S-Adenosyl-L-Methionine Surrogate.

Alexandre Désert, Karine Guitot, Audrey Michaud, Daniel Holoch, Raphaël Margueron, Fabienne Burlina, Dominique Guianvarc'h

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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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
0.5field-weighted citation impact, top 40% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

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

7 authors at 1 institution in 1 country.

Alexandre DésertSorbonne Université, École normale supérieure, PSL University, CNRS, Laboratoire des Biomolécules, LBM, Paris, France.
Karine GuitotUniversité Paris-Saclay, CNRS, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182, Orsay, France.
Audrey MichaudInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne University, Paris, France.
Daniel HolochInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne University, Paris, France.
Raphaël MargueronInstitut Curie, Paris Sciences et Lettres Research University, Sorbonne University, Paris, France.
Fabienne BurlinaSorbonne Université, École normale supérieure, PSL University, CNRS, Laboratoire des Biomolécules, LBM, Paris, France.
Dominique Guianvarc'hUniversité Paris-Saclay, CNRS, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182, Orsay, France. dominique.guianvarch@universite-paris-saclay.fr.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identification of histone lysine methyltransferase (HKMT) substrates has recently benefited from chemical-biology-based strategies in which artificial S-adenosyl-L-methionine (SAM) cofactors are engineered to allow substrate labeling using either the wild-type target enzyme or designed mutants. Once labeled, substrates can be selectively functionalized with an affinity tag, using a bioorthogonal ligation reaction, to allow their recovery from cell extracts and subsequent identification. In this chapter, we describe steps on how to proceed to set up such an approach to characterize substrates of specific HKMTs of the SET domain superfamily, from the characterization of the HKMT able to accommodate a SAM surrogate containing a bioorthogonal moiety, to the proteomic analysis conducted on a cell extract. We focus in particular on the controls that are necessary to ensure reliable proteomic data analysis. The example of PR-Set7 on which we have implemented this approach is shown.

Indexed as

MethionineS-AdenosylmethionineHistone-Lysine N-MethyltransferaseProteomicsPR-SET DomainsHistone-Lysine N-MethyltransferaseMethionineS-AdenosylmethionineBioorthogonal chemistryHistone lysine methyltransferaseProteomicsS-adenosyl-L-methionine surrogate

Identifiers

PMID35733021
OpenAlexW4285308981

What OpenQuestion holds

Textmetadata
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.