Evidence map›Paper›PMID 19269883›Full record

ReviewCurrent opinion in chemical biology2009

Control of radical chemistry in the AdoMet radical enzymes.

Kaitlin S Duschene, Susan E Veneziano, Sunshine C Silver, Joan B Broderick

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Radical SAM enzymes: surprises along the path to understanding mechanism.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 4-Hydroxyphenylacetate decarboxylase activating enzyme catalyses a classical S-adenosylmethionine reductive cleavage reaction.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  18. Article
  19. Article
  20. Emerging themes in radical SAM chemistry.Current opinion in structural biology · 2012
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Kaitlin S DuscheneDepartment of Chemistry and Biochemistry, Montana State University, Bozeman, 59717, United States.
Susan E Veneziano
Sunshine C Silver
Joan B Broderick
Montana State University · US

Funding

Iron-Sulfur Clusters in Biological Radical GenerationR01GM054608 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI BRODERICK, JOAN B · 2001 to 2018
$4.7M
Generation and Repair of an Unusual UV PhotoproductR01GM067804 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI BRODERICK, JOAN B. · 2003 to 2006
$1.0M
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE LYASE ACTIVASER29GM054608 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BRODERICK, JOAN B. · 1997 to 2000
$102k
SPECTROSCOPIC STUDIES OF PYRUVATE FORMATE-LYASE ACTIVASER55GM054608 · NIGMS · AMHERST COLLEGE · PI BRODERICK, JOAN B. · 1996 to 1996
–
NIGMS NIH HHS GM54608NIGMS NIH HHS GM67804NIGMS NIH HHS R01 GM054608NIGMS NIH HHS R01 GM067804
6 · The paper itself

Abstract

The radical AdoMet superfamily comprises a diverse set of >2800 enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (SAM or AdoMet) to initiate a diverse set of radical-mediated reactions. The intricate control these enzymes exercise over the radical transformations they catalyze is an amazing feat of elegance and sophistication in biochemistry. This review focuses on the accumulating evidence for how these enzymes control this remarkable chemistry, including controlling the reactivity between the iron-sulfur cluster and AdoMet, and controlling the subsequent radical transformations.

Indexed as

EnzymesIronOxidation-ReductionS-AdenosylmethionineSulfurEnzymesIronS-AdenosylmethionineSulfur

Identifiers

PMID19269883
PMCPMC2703739
OpenAlexW2039890551

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.