Evidence map›Paper›PMID 38473971›Full record

ArticleInternational journal of molecular sciences2024

Discovering New Substrates of a UDP-Glycosyltransferase with a High-Throughput Method.

Mary C L Lethe, Dinh Bui, Ming Hu, Xiaoqiang Wang, Rashim Singh, Clement T Y Chan

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

8 citing papers in PubMed, 9 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

6 authors at 2 institutions in 1 country.

Mary C L LetheDepartment of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USA.
Dinh BuiDepartment of Pharmacological and Pharmaceutical Sciences, College of Pharmacy, University of Houston, 4349 Martin Luther King Boulevard, Houston, TX 77204, USA.ORCID 0000-0003-2161-5664
Ming HuDepartment of Pharmacological and Pharmaceutical Sciences, College of Pharmacy, University of Houston, 4349 Martin Luther King Boulevard, Houston, TX 77204, USA.
Xiaoqiang WangDepartment of Biological Sciences, College of Science, University of North Texas, 1155 Union Circle #305220, Denton, TX 76203, USA.
Rashim SinghDepartment of Pharmacological and Pharmaceutical Sciences, College of Pharmacy, University of Houston, 4349 Martin Luther King Boulevard, Houston, TX 77204, USA.
Clement T Y ChanDepartment of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USA.
University of Houston · USUniversity of North Texas · US

Funding

Development of Genetic Sensors and Circuits for Creating Novel Cellular BehaviorsR35GM142421 · NIGMS · UNIVERSITY OF NORTH TEXAS · PI CHAN, TSZ YAN CLEMENT · 2021 to 2025
$1.8M
Development of Drug Detoxifying Bacteria for Chemotherapy Induced Gut InjuryR41CA261292 · NCI · SANARENTERO LLC · PI HU, MING, SINGH, RASHIM · 2021 to 2022
$455k
Genetic Biocontainment Switch to Improve the Safety of Drug Detoxifying Bacteria in Preventing Chemotherapy-induced DiarrheaR41CA275454 · NCI · SANARENTERO LLC · PI CHAN, TSZ YAN CLEMENT, HU, MING · 2023 to 2023
$400k
NCI NIH HHS R41 CA261292NCI NIH HHS R41 CA275454NIGMS NIH HHS R35 GM142421NIH HHS R35GM142421NIH HHS R41CA261292NIH HHS R41CA275454
6 · The paper itself

Abstract

UDP-glycosyltransferases (UGTs) form a large enzyme family that is found in a wide range of organisms. These enzymes are known for accepting a wide variety of substrates, and they derivatize xenobiotics and metabolites for detoxification. However, most UGT homologs have not been well characterized, and their potential for biomedical and environmental applications is underexplored. In this work, we have used a fluorescent assay for screening substrates of a plant UGT homolog by monitoring the formation of UDP. We optimized the assay such that it could be used for high-throughput screening of substrates of the

Indexed as

GlycosyltransferasesTandem Mass SpectrometryChromatography, LiquidPlantsUridine DiphosphateGlycosyltransferasesUridine DiphosphateBPAhigh-throughput screeningSN-38UDP-glycosyltransferasexenobiotics metabolism

Identifiers

PMID38473971
PMCPMC10931590
OpenAlexW4392193205

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.