Evidence map›Paper›PMID 30373312›Full record

ArticleMolecules (Basel, Switzerland)2018

Enzymatic Synthesis of Unnatural Ginsenosides Using a Promiscuous UDP-Glucosyltransferase from Bacillus subtilis.

Ting-Ting Zhang, Ting Gong, Zong-Feng Hu, An-Di Gu, Jin-Ling Yang, Ping Zhu

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. 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

6 authors.

Ting-Ting ZhangState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100050, China. tingtingzhang_pumc@163.com.
Ting GongState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100050, China. gongting@imm.ac.cn.
Zong-Feng HuState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100050, China. huzongfeng@imm.ac.cn.
An-Di GuState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100050, China. gad@imm.ac.cn.
Jin-Ling YangState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100050, China. yangjl@imm.ac.cn.
Ping ZhuState Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100050, China. zhuping@imm.ac.cn.ORCID 0000-0001-8537-2169

Funding

CAMS Innovation Fund for Medical Sciences (CIFMS) 2016-I2M-3-012the Beijing Natural Science Foundation 7122115the Fundamental Research Funds for the Central Universities 2017PT35001the National Natural Science Foundation of China 81673341
6 · The paper itself

Abstract

Glycosylation, which is catalyzed by UDP-glycosyltransferases (UGTs), is an important biological modification for the structural and functional diversity of ginsenosides. In this study, the promiscuous UGT109A1 from

Indexed as

Bacillus subtilisChromatography, High Pressure LiquidEnzyme ActivationEscherichia coliGene ExpressionGinsenosidesGlucosyltransferasesGlycosylationHydrogen-Ion ConcentrationIn Vitro TechniquesIonsMetalsRecombinant ProteinsGinsenosidesGlucosyltransferasesIonsMetalsRecombinant ProteinsBacillus subtilisenzymatic synthesisglycosylationUDP-glycosyltransferaseunnatural ginsenoside

Identifiers

PMID30373312
PMCPMC6278262

What OpenQuestion holds

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Registered trials

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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.