Evidence map›Paper›PMID 40943510›Full record

ArticleInternational journal of molecular sciences2025

Phospho-Switch: Regulation of the Activity of SAM-Dependent Methyltransferases Using

Vsevolod L Filonov, Maxim A Khomutov, Alexander Yu Rudenko, Sofia S Mariasina, Ratislav M Ozhiganov, Alexander V Sergeev, Sergei N Kochetkov, Vladimir I Polshakov, Elizaveta S Gromova, Anastasia L Khandazhinskaya and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Frontiers in microbiology · 2026
    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

11 authors.

Vsevolod L FilonovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Maxim A KhomutovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0003-2833-9834
Alexander Yu RudenkoBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-8320-0539
Sofia S MariasinaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-9190-1298
Ratislav M OzhiganovBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia.
Alexander V SergeevFaculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-0479-6910
Sergei N KochetkovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0002-7443-6961
Vladimir I PolshakovFaculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-3216-5737
Elizaveta S GromovaFaculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0001-9086-7238
Anastasia L KhandazhinskayaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0003-1452-0253
Alex R KhomutovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0001-6833-7855

Funding

Russian Science Foundation 22-14-00291Russian Science Foundation 23-64-10018
6 · The paper itself

Abstract

S-Adenosyl-L-methionine (SAM) is a central cofactor in cellular methylation, donating methyl groups to a wide range of biological substrates. SAM analogues are promising tools for selective modulation of methyltransferase activity. Here, we investigated phosphorus-containing analogues of SAM and S-adenosyl-L-homocysteine (SAH), focusing on the

Indexed as

Catechol O-MethyltransferaseDNA (Cytosine-5-)-MethyltransferasesS-AdenosylmethionineCatalytic DomainDNA (Cytosine-5-)-Methyltransferase 1DNA MethylationDNA Methyltransferase 3AHumansS-AdenosylhomocysteineSubstrate SpecificityCatechol O-MethyltransferaseDNA (Cytosine-5-)-Methyltransferase 1DNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3ADNMT1 protein, humanDNMT3A protein, humanS-AdenosylhomocysteineS-AdenosylmethionineCOMTDNA methylationDnmt1Dnmt3aH-phosphinic analogue of SAMmethyltransferasesS-adenosyl-L-methionine

Identifiers

PMID40943510
PMCPMC12428852

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.