Evidence map›Paper›PMID 22178611›Full record

ReviewBiochimica et biophysica acta2012

The methylthiolation reaction mediated by the Radical-SAM enzymes.

Mohamed Atta, Simon Arragain, Marc Fontecave, Etienne Mulliez, John F Hunt, Jon D Luff, Farhad Forouhar

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Characterization of LipS1 and LipS2 fromACS bio & med chem Au · 2022
    Article
  3. Review
  4. Progress in the Chemistry of Cytochalasans.Progress in the chemistry of organic natural products · 2021
    Article
  5. Article
  6. First Step in Catalysis of the RadicalJournal of the American Chemical Society · 2020
    Article
  7. Solo act revealed to be duet.Nature chemical biology · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. 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

7 authors.

Mohamed AttaInstitut de Recherches en Technologie et Sciences pour le Vivant IRTSV-LCBM, UMR 5249 CEA/CNRS/UJF, CEA-Grenoble, 17 avenue des Martyrs, 38054, Grenoble Cedex 09, France. mohamed.atta@cea.fr
Simon Arragain
Marc Fontecave
Etienne Mulliez
John F Hunt
Jon D Luff
Farhad Forouhar

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KENNEDY, MICHAEL ALLEN · 2005 to 2009
$56.6M
University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI GOUAUX, JAMES E · 2005 to 2009
$16.8M
NIGMS NIH HHS U54 GM074958NIGMS NIH HHS U54-GM074958NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54 GM094597NIGMS NIH HHS U54-GM094597
6 · The paper itself

Abstract

Over the past 10 years, considerable progress has been made in our understanding of the mechanistic enzymology of the Radical-SAM enzymes. It is now clear that these enzymes appear to be involved in a remarkably wide range of chemically challenging reactions. This review article highlights mechanistic and structural aspects of the methylthiotransferases (MTTases) sub-class of the Radical-SAM enzymes. The mechanism of methylthio insertion, now observed to be performed by three different enzymes is an exciting unsolved problem. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.

Indexed as

Amino Acid SequenceBacterial ProteinsBiocatalysisEscherichia coli ProteinsFree RadicalsHumansIron-Sulfur ProteinsMethyltransferasesModels, MolecularMolecular Sequence DataPhylogenyProtein Structure, TertiaryRibosomal ProteinsS-AdenosylmethionineSulfurtransferasesBacterial ProteinsEscherichia coli ProteinsFree RadicalsIron-Sulfur ProteinsMethyltransferasesRibosomal ProteinsRpsL protein, E coliS-AdenosylmethionineSulfurtransferases

Identifiers

PMID22178611
PMCPMC4150254

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.