Evidence map›Paper›PMID 23835516›Full record

ReviewCurrent opinion in chemical biology2013

Radical SAM-mediated methylation reactions.

Danica Galonić Fujimori

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

30 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Sulfide regulation and catabolism in health and disease.Signal transduction and targeted therapy · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Late-Stage C(Journal of the American Chemical Society · 2023
    Article
  12. Review
  13. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Replacement of the Cobalt Center of Vitamin BAngewandte Chemie (International ed. in English) · 2020
    Article
  18. Article
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Danica Galonić FujimoriDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158-2280, USA. Danica.Fujimori@ucsf.edu
University of California, San Francisco · US

Funding

Radical SAM MethytransferasesR01AI095393 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FUJIMORI, DANICA GALONIC · 2011 to 2015
$1.7M
NIAID NIH HHS R01 AI095393
6 · The paper itself

Abstract

A subset of enzymes that belong to the radical S-adenosylmethionine (SAM) superfamily is able to catalyze methylation reactions. Substrates of these enzymes are distinct from the nucleophilic substrates that undergo methylation by a polar mechanism. Recently, activities of several radical SAM methylating enzymes have been reconstituted in vitro and their mechanisms of catalysis investigated. The RNA modifying enzymes RlmN and Cfr catalyze methylation via a methyl synthase mechanism. These enzymes use SAM in two distinct roles: as a source of a methyl group transferred to a conserved cysteine and as a source of 5'-deoxyadenosyl radical (5'-dA). Hydrogen atom abstraction by this species generates a thiomethylene radical which adds into the RNA substrate, forming an enzyme-substrate covalent adduct. In another recent study, methylation of the indole moiety of tryptophan by the radical SAM and cobalamin-binding domain enzyme TsrM has been reconstituted. Methylcobalamin serves as an intermediate methyl donor in TsrM, and is proposed to transfer the methyl group as a methyl radical. Interestingly, despite the presence of the radical SAM motif, no reductive cleavage of SAM has been observed in this methylation. These important reconstitutions set the stage for further studies on mechanisms of radical methylation.

Indexed as

Free RadicalsMethylationRNAS-AdenosylmethionineSubstrate SpecificityTryptophanFree RadicalsRNAS-AdenosylmethionineTryptophan

Identifiers

PMID23835516
PMCPMC3799849
OpenAlexW2048064762

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.