Evidence map›Paper›PMID 42309558›Full record

ArticleJournal of inherited metabolic disease2026

Methionine Synthase Interacts With the Methionine Adenosyl-Transferase MATα2 and the DNA Methyltransferase DNMT3b in the Nucleus.

Manon Jeandel, Jean-Marc Alberto, Okan Baspinar, Aurélie Robert, Natacha Dreumont, Zeinab Alsahly, David Meyre, Jean-Louis Guéant, David Coelho

Abstract read
In one paragraph

Article in Journal of inherited metabolic disease, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Manon JeandelInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
Jean-Marc AlbertoInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
Okan BaspinarInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
Aurélie RobertInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
Natacha DreumontInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.ORCID https://orcid.org/0000-0001-7108-5804
Zeinab AlsahlyInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
David MeyreInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
Jean-Louis GuéantInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.
David CoelhoInserm, UMRS 1256, NGERE-Nutrition, Genetics, and Environmental Risk Exposure, University of Lorraine, Nancy, France.ORCID https://orcid.org/0000-0001-7010-5789

Funding

FHU ARRIMAGEMESRIUniversité de Lorraine
6 · The paper itself

Abstract

Transmethylation reactions, which are crucial for regulating gene expression, require S-adenosyl-L-methionine (SAM) as methyl donor. The substrate for SAM synthesis is methionine, which can be produced by methionine synthase (MS) whose dysfunctions are associated with SAM synthesis alterations despite the presence of methionine in the milieu, suggesting a preferential use of the methionine produced de novo. This highlights the crucial role of MS activity and would imply nuclear import of SAM or MS nuclear localization, allowing protein-protein interactions with the methionine adenosyl-transferases (MAT) responsible for SAM production. Using subcellular fractions of human cells, biochemical and cellular approaches, including incorporation of

Indexed as

5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseCell NucleusDNA (Cytosine-5-)-MethyltransferasesMethionine AdenosyltransferaseDNA Methyltransferase 3BHumansMethionineS-Adenosylmethionine5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseDNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3BMethionineMethionine AdenosyltransferaseS-AdenosylmethioninecompartmentalizationDNA methyltransferasemethionine adenosyl‐transferasemethionine synthaseone‐carbon metabolism

Identifiers

PMID42309558
PMCPMC13275206

What OpenQuestion holds

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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.