Evidence map›Paper›PMID 32796599›Full record

ArticleInternational journal of molecular sciences2020

Enhanced Heterologous Production of Glycosyltransferase UGT76G1 by Co-Expression of Endogenous

Wenju Shu, Hongchen Zheng, Xiaoping Fu, Jie Zhen, Ming Tan, Jianyong Xu, Xingya Zhao, Shibin Yang, Hui Song, Yanhe Ma

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. The progress on stevia (Frontiers in nutrition · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023
    Review
  11. Article
  12. 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

10 authors at 1 institution in 1 country.

Wenju ShuUniversity of Chinese Academy of Sciences, Beijing 100049, China.ORCID 0000-0001-8053-3277
Hongchen ZhengUniversity of Chinese Academy of Sciences, Beijing 100049, China.ORCID 0000-0001-7780-0784
Xiaoping FuIndustrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Jie ZhenIndustrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Ming TanIndustrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Jianyong XuIndustrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Xingya ZhaoUniversity of Chinese Academy of Sciences, Beijing 100049, China.
Shibin YangUniversity of Chinese Academy of Sciences, Beijing 100049, China.
Hui SongUniversity of Chinese Academy of Sciences, Beijing 100049, China.
Yanhe MaIndustrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Chinese Academy of Sciences · CN

Funding

the National Natural Science Fund of China 31701534the Tianjin outstanding talent training program, the Tianjin Science & Technology Planning Project 16YFZCSY00790 and 15PTCYSY00020Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project TSBICIP-KJGG-006
6 · The paper itself

Abstract

Steviol glycosides (SGs) with zero calories and high-intensity sweetness are the best substitutes of sugar for the human diet. Uridine diphosphate dependent glycosyltransferase (UGT) UGT76G1, as a key enzyme for the biosynthesis of SGs with a low heterologous expression level, hinders its application. In this study, a suitable fusion partner, Smt3, was found to enhance the soluble expression of UGT76G1 by 60%. Additionally, a novel strategy to improve the expression of Smt3-UGT76G1 was performed, which co-expressed endogenous genes

Indexed as

ATP-Binding Cassette TransportersBiocatalysisBioreactorsBiotransformationEscherichia coliEscherichia coli ProteinsFermentationGlycosidesGlycosylationGlycosyltransferasesHydro-LyasesPlasmidsRecombinant Fusion ProteinsRecombination, GeneticSolubilityATP-Binding Cassette TransportersEscherichia coli ProteinsGlycosidesGlycosyltransferasesHydro-LyasesMalK protein, E colimethylcitrate dehydratase, E coliRecombinant Fusion Proteinsco-expressionefficient E. coli expression systemenzymatic biotransformationfusion partnermalKprpDsteviol glycosidesuridine diphosphate dependent glucosyltransferases (UGTs)

Identifiers

PMID32796599
PMCPMC7460871
OpenAlexW3048430053

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.