Evidence map›Paper›PMID 29514981›Full record

ArticleThe Journal of biological chemistry2018

Structural basis for the regulatory interaction of the methylglyoxal synthase MgsA with the carbon flux regulator Crh in

Achim Dickmanns, Christopher P Zschiedrich, Johannes Arens, Iwan Parfentev, Jan Gundlach, Romina Hofele, Piotr Neumann, Henning Urlaub, Boris Görke, Ralf Ficner and 1 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 56% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Methylglyoxal Formation-Metabolic Routes and Consequences.Antioxidants (Basel, Switzerland) · 2025
    Review
  2. Article
  3. Why Nature Chose Potassium.Journal of molecular evolution · 2019
    Review
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 2 institutions in 1 country.

Achim DickmannsFrom the Departments of Molecular Structural Biology and adickma@gwdg.de.
Christopher P ZschiedrichGeneral Microbiology, GZMB, Georg-August-University Göttingen, 37077 Göttingen, Germany.
Johannes ArensFrom the Departments of Molecular Structural Biology and.
Iwan Parfentevthe Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany, and.
Jan GundlachGeneral Microbiology, GZMB, Georg-August-University Göttingen, 37077 Göttingen, Germany.
Romina Hofelethe Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany, and.
Piotr NeumannFrom the Departments of Molecular Structural Biology and.
Henning Urlaubthe Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany, and.
Boris GörkeGeneral Microbiology, GZMB, Georg-August-University Göttingen, 37077 Göttingen, Germany.
Ralf FicnerFrom the Departments of Molecular Structural Biology and.
Jörg StülkeGeneral Microbiology, GZMB, Georg-August-University Göttingen, 37077 Göttingen, Germany, jstuelk@gwdg.de.
University of Göttingen · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Utilization of energy-rich carbon sources such as glucose is fundamental to the evolutionary success of bacteria. Glucose can be catabolized via glycolysis for feeding the intermediary metabolism. The methylglyoxal synthase MgsA produces methylglyoxal from the glycolytic intermediate dihydroxyacetone phosphate. Methylglyoxal is toxic, requiring stringent regulation of MgsA activity. In the Gram-positive bacterium

Indexed as

Protein Interaction MapsBacillus subtilisBacterial ProteinsCarbon CycleCarbon-Oxygen LyasesCrystallography, X-RayModels, MolecularPhosphoproteinsProtein ConformationProtein MultimerizationBacterial ProteinsCarbon-Oxygen LyasesCrh protein, Bacillus subtilismethylglyoxal synthasePhosphoproteinsBacillusbacteriabacterial geneticsbacterial metabolismcatabolite regulationCrhcrystal structureglucose catabolismglycolysisHPrmetabolic regulationmethylglyoxal synthasemethylglyoxal toxicityphosphoproteinprokaryotic signal-transductionprotein cross-linkingprotein-protein interactionprotein structure

Identifiers

PMID29514981
PMCPMC5912461
OpenAlexW2792551057

What OpenQuestion holds

Textmetadata
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.