Evidence map›Paper›PMID 30737350›Full record

ArticleApplied and environmental microbiology2019

Artificial Fusion of mCherry Enhances Trehalose Transferase Solubility and Stability.

Luuk Mestrom, Stefan R Marsden, Marit Dieters, Puck Achterberg, Lysanne Stolk, Isabel Bento, Ulf Hanefeld, Peter-Leon Hagedoorn

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 8% 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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. The Disordered Region of ASXL1 Acts as an Auto-Regulator Through Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Two Homologous Enzymes of the GalU Family inInternational journal of molecular sciences · 2019
    Article
  10. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Luuk MestromBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Stefan R MarsdenBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Marit DietersBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Puck AchterbergBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Lysanne StolkBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Isabel BentoEMBL Hamburg, Hamburg, Germany.
Ulf HanefeldBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Peter-Leon HagedoornBiocatalysis, Department of Biotechnology, Delft University of Technology, Delft, The Netherlands P.L.Hagedoorn@tudelft.nl.ORCID 0000-0001-6342-2022
Delft University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LeLoir glycosyltransferases are important biocatalysts for the production of glycosidic bonds in natural products, chiral building blocks, and pharmaceuticals. Trehalose transferase (TreT) is of particular interest since it catalyzes the stereo- and enantioselective α,α-(1→1) coupling of a nucleotide sugar donor and monosaccharide acceptor for the synthesis of disaccharide derivatives. Heterologously expressed thermophilic trehalose transferases were found to be intrinsically aggregation prone and are mainly expressed as catalytically active inclusion bodies in

Indexed as

Enzyme StabilityAdenosine Diphosphate GlucoseAnionsCatalysisCationsEnzyme ActivationEscherichia coliGenetic VectorsGlucoseGlycosyltransferasesKineticsProtein AggregatesPyrobaculumRecombinant Fusion ProteinsSolubilityTransferasesAdenosine Diphosphate GlucoseAnionsCationsGlucoseGlycosyltransferasesProtein AggregatesRecombinant Fusion ProteinsTransferasesTrehaloseUridine Diphosphate Glucoseglycosyltransferaseinclusion bodiesmCherryprotein aggregationprotein solubilitytrehalose transferase

Identifiers

PMID30737350
PMCPMC6450025
OpenAlexW2912370753

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.