Evidence map›Paper›PMID 27934966›Full record

ArticleScientific reports2016

The mechanism of a formaldehyde-sensing transcriptional regulator.

Katie J Denby, Jeffrey Iwig, Claudine Bisson, Jodie Westwood, Matthew D Rolfe, Svetlana E Sedelnikova, Khadine Higgins, Michael J Maroney, Patrick J Baker, Peter T Chivers and 1 more

Open access · goldAbstract readComparative Study
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.7field-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

41 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  7. Modulation of virulence and metabolic profiles inFrontiers in cellular and infection microbiology · 2025
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  10. Genomic insights into the adaptation of Acinetobacter johnsonii RB2-047 to the heavy metal-contaminated subsurface mine environment.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Article
  11. Article
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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

11 authors at 3 institutions in 2 countries.

Katie J DenbyDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Jeffrey IwigDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine in St. Louis, St. Louis, MO, 63110, USA.
Claudine BissonDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Jodie WestwoodDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Matthew D RolfeDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Svetlana E SedelnikovaDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Khadine HigginsDepartment of Chemistry, University of Massachusetts-Amherst, Amherst, MA 01003, USA.
Michael J MaroneyDepartment of Chemistry, University of Massachusetts-Amherst, Amherst, MA 01003, USA.
Patrick J BakerDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
Peter T ChiversDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine in St. Louis, St. Louis, MO, 63110, USA.
Jeffrey GreenDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, S10 2TN, UK.
University of Sheffield · GBUniversity of Massachusetts Amherst · USWashington University in St. Louis · US

Funding

Structural Parameters Involved in Metal RecognitionR01GM069696 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI MARONEY, MICHAEL J · 2004 to 2017
$3.3M
Biotechnology and Biological Sciences Research Council BB/J014443/1Biotechnology and Biological Sciences Research Council BB/L008114/1Biotechnology and Biological Sciences Research Council BB/L013711/1NIGMS NIH HHS R01 GM069696
6 · The paper itself

Abstract

Most organisms are exposed to the genotoxic chemical formaldehyde, either from endogenous or environmental sources. Therefore, biology has evolved systems to perceive and detoxify formaldehyde. The frmRA(B) operon that is present in many bacteria represents one such system. The FrmR protein is a transcriptional repressor that is specifically inactivated in the presence of formaldehyde, permitting expression of the formaldehyde detoxification machinery (FrmA and FrmB, when the latter is present). The X-ray structure of the formaldehyde-treated Escherichia coli FrmR (EcFrmR) protein reveals the formation of methylene bridges that link adjacent Pro2 and Cys35 residues in the EcFrmR tetramer. Methylene bridge formation has profound effects on the pattern of surface charge of EcFrmR and combined with biochemical/biophysical data suggests a mechanistic model for formaldehyde-sensing and derepression of frmRA(B) expression in numerous bacterial species.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceBase SequenceCrystallography, X-RayDNA, BacterialEscherichia coli K12Escherichia coli ProteinsFormaldehydeInactivation, MetabolicInterferometryModels, MolecularOperonPromoter Regions, GeneticProtein ConformationRepressor ProteinsSelenomethionineDNA, BacterialEscherichia coli ProteinsFormaldehydeFrmR protein, E coliRepressor ProteinsSelenomethionine

Identifiers

PMID27934966
PMCPMC5146963
OpenAlexW2560269636

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.