Evidence map›Paper›PMID 37655961›Full record

ArticleJournal of agricultural and food chemistry2023

Solvent Engineering for Nonpolar Substrate Glycosylation Catalyzed by the UDP-Glucose-Dependent Glycosyltransferase UGT71E5: Intensification of the Synthesis of 15-Hydroxy Cinmethylin β-d-Glucoside.

Jihye Jung, Hui Liu, Annika J E Borg, Bernd Nidetzky

Open access · hybridAbstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2023. 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
1.1field-weighted citation impact, top 22% 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. HalophyticACS omega · 2025
    Article
  2. Review
  3. Highly Promiscuous Flavonoid Di-Molecules (Basel, Switzerland) · 2024
    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

4 authors at 1 institution in 1 country.

Jihye JungInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, A-8010 Graz, Austria.
Hui LiuInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, A-8010 Graz, Austria.
Annika J E BorgInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, A-8010 Graz, Austria.
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, A-8010 Graz, Austria.ORCID 0000-0002-5030-2643
Graz University of Technology · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sugar nucleotide-dependent glycosyltransferases are powerful catalysts of the glycosylation of natural products and xenobiotics. The low solubility of the aglycone substrate often limits the synthetic efficiency of the transformation catalyzed. Here, we explored different approaches of solvent engineering for reaction intensification of β-glycosylation of 15HCM (a C15-hydroxylated, plant detoxification metabolite of the herbicide cinmethylin) catalyzed by safflower UGT71E5 using UDP-glucose as the donor substrate. Use of a cosolvent (DMSO, ethanol, and acetonitrile; ≤50 vol %) or a water-immiscible solvent (

Indexed as

GlycosyltransferasesUridine Diphosphate GlucoseCatalysisGlucoseGlucosidesGlycosylationSolventsWaterGlucoseGlucosidesGlycosyltransferasesSolventsUridine Diphosphate GlucoseWatercyclodextringlycosylationinclusion complexationLeloir glycosyltransferaseorganic–aqueous biphasic reactionsolubilityxenobiotic metabolite

Identifiers

PMID37655961
PMCPMC10510383
OpenAlexW4386347355

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.