Evidence map›Paper›PMID 31070087›Full record

ArticleBioengineered2019

Expression, characterization, and site-directed mutagenesis of UDP-glycosyltransferase UGT88A1 from Arabidopsis thaliana.

Jingyuan Weng, Liangliang Chen, Yinchu Cheng, Yan Li, Honghua Jia, Hua Zhou, Ping Wei

Open access · goldAbstract read
In one paragraph

Article in Bioengineered, 2019. 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
0.6field-weighted citation impact, top 35% 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

5 citing papers in PubMed, 17 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Jingyuan Wenga College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Liangliang Chena College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Yinchu Chenga College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Yan Lia College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Honghua Jiaa College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Hua Zhoua College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Ping Weia College of Biotechnology and Pharmaceutical Engineering , Nanjing Tech University , Nanjing , China.
Nanjing Tech University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quercetin-4'-O-glucoside is one of the major quercetin derivatives in the mature red onion bulb. It has an adjuvant effect on allergies, asthma, arthritis, and cancer. The present study aimed to use uridine diphosphate glycosyltransferase 88A1 (UGT88A1) from Arabidopsis thaliana to achieve the enzymatic synthesis of quercetin-4'-O-glucoside from quercetin. The results showed that UGT88A1 was most active at pH 9.0. The optimum temperature of UGT88A1 for synthesizing quercetin-4'-O-glucoside was 45°C, which was a little lower than that for synthesizing quercetin-3-O-glucoside (50°C). One mutant, V18R, of UGT88A1 was obtained by site-directed mutation and showed a greater affinity (K

Indexed as

ArabidopsisArabidopsis ProteinsGlycosyltransferasesMutagenesis, Site-DirectedQuercetinUridine DiphosphateArabidopsis ProteinsGlycosyltransferasesQuercetinUridine DiphosphateQuercetinquercetin-4′--glucosidesite-directed mutationuridine diphosphate glycosyltransferase 88A1

Identifiers

PMID31070087
PMCPMC6527070
OpenAlexW2944414382

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.