Evidence map›Paper›PMID 29485151›Full record

ReviewNatural product reports2018

Following the electrons: peculiarities in the catalytic cycles of radical SAM enzymes.

Mark W Ruszczycky, Aoshu Zhong, Hung-Wen Liu

Abstract readReview
In one paragraph

Review in Natural product reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. RadicalJournal of the American Chemical Society · 2025
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Natural product reports · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Activation modes in biocatalytic radical cyclization reactions.Journal of industrial microbiology & biotechnology · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019
    Review
  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

3 authors at 1 institution in 2 countries.

Mark W RuszczyckyDivision of Chemical Biology & Medicinal Chemistry, College of Pharmacy, University of Texas at Austin, USA. mwr8@utexas.edu h.w.liu@mail.utexas.edu.
Aoshu Zhong
Hung-Wen Liu
Medicina · PL

Funding

Three-Membered Ring Metabolites, Inhibition &FormationR01GM040541 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIU, HUNG-WEN · 1989 to 2023
$7.4M
Mechanistic Studies of Deoxy Sugar BiosynthesisR01GM035906 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI LIU, HUNG-WEN · 1986 to 2023
$6.1M
MECHANISMS OF BIOSYNTHETIC FORMATION OF DEOXY SUGARSR37GM035906 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LIU, HUNG-WEN · 1999 to 2008
$3.4M
NIGMS NIH HHS R01 GM035906NIGMS NIH HHS R01 GM040541NIGMS NIH HHS R37 GM035906
6 · The paper itself

Abstract

Radical SAM enzymes use S-adenosyl-l-methionine as an oxidant to initiate radical-mediated transformations that would otherwise not be possible with Lewis acid/base chemistry alone. These reactions are either redox neutral or oxidative leading to certain expectations regarding the role of SAM as either a reusable cofactor or the ultimate electron acceptor during each turnover. However, these expectations are frequently not realized resulting in fundamental questions regarding the redox handling and movement of electrons associated with these biological catalysts. Herein we provide a focused perspective on several of these questions and associated hypotheses with an emphasis on recently discovered radical SAM enzymes.

Indexed as

AlkylationBacterial ProteinsCarbon-Carbon LyasesCarbon-Nitrogen LyasesCatalysisEnzymesOxidation-ReductionS-Adenosylmethionine7-carboxy-7-deazaguanine synthase, Burkholderia multivoransBacterial ProteinsCarbon-Carbon LyasesCarbon-Nitrogen LyasesEnzymesLipA protein, BacteriaS-adenosyl-L-methionine tryptophan lyase, Streptomyces actuosusS-Adenosylmethionine

Identifiers

PMID29485151
PMCPMC6051909
OpenAlexW2794083769

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.