Evidence map›Paper›PMID 31970375›Full record

ArticleChemical communications (Cambridge, England)2020

Nucleoside-modified AdoMet analogues for differential methyltransferase targeting.

Nicolas V Cornelissen, Freideriki Michailidou, Fabian Muttach, Kristina Rau, Andrea Rentmeister

Open access · hybridAbstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Histidine Ethylation by Histidine Methyltransferases SETD3 and METTL9.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Article
  4. Article
  5. OrganophosphorusFrontiers in chemistry · 2024
    Article
  6. MePMe-seq: antibody-free simultaneous mNature communications · 2023
    Article
  7. Article
  8. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  9. Article
  10. Article
  11. Analogs ofMolecular biology · 2022
    Article
  12. Article
  13. From Natural Methylation to Versatile Alkylations Using Halide Methyltransferases.Chembiochem : a European journal of chemical biology · 2021
    Review
  14. Review
  15. A bicyclicRSC chemical biology · 2021
    Article
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Nicolas V CornelissenDepartment of Chemistry, Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Straße 2, D-48149 Muenster, Germany. a.rentmeister@uni-muenster.de.ORCID http://orcid.org/0000-0002-3625-7612
Freideriki MichailidouDepartment of Chemistry, Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Straße 2, D-48149 Muenster, Germany. a.rentmeister@uni-muenster.de.
Fabian MuttachDepartment of Chemistry, Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Straße 2, D-48149 Muenster, Germany. a.rentmeister@uni-muenster.de.
Kristina RauDepartment of Chemistry, Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Straße 2, D-48149 Muenster, Germany. a.rentmeister@uni-muenster.de.
Andrea RentmeisterDepartment of Chemistry, Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Straße 2, D-48149 Muenster, Germany. a.rentmeister@uni-muenster.de.ORCID http://orcid.org/0000-0002-3107-4147
University of Münster · DE

Funding

European Research Council 772280NIAID NIH HHS HHSN272201700059C
6 · The paper itself

Abstract

Methyltransferases (MTases) modify a wide range of biomolecules using S-adenosyl-l-methionine (AdoMet) as the cosubstrate. Synthetic AdoMet analogues are powerful tools to site-specifically introduce a variety of functional groups and exhibit potential to be converted only by distinct MTases. Extending the size of the substituent at the sulfur/selenium atom provides selectivity among MTases but is insufficient to discriminate between promiscuous MTases. We present a panel of AdoMet analogues differing in the nucleoside moiety (NM-AdoMets). These NM-AdoMets were efficiently produced by a previously uncharacterized methionine adenosyltransferase (MAT) from methionine and ATP analogues, such as ITP and N

Indexed as

MethyltransferasesMolecular StructureNucleosidesS-AdenosylmethionineMethyltransferasesNucleosidesS-Adenosylmethionine

Identifiers

PMID31970375
PMCPMC7030947
OpenAlexW3002179344

What OpenQuestion holds

Textmetadata
LicenceTDM
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.