Evidence map›Paper›PMID 32210023›Full record

ArticleInternational journal of molecular sciences2020

Comparative Analysis of High-Throughput Assays of Family-1 Plant Glycosyltransferases.

Kate McGraphery, Wilfried Schwab

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 30 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

2 authors at 1 institution in 1 country.

Kate McGrapheryBiotechnology of Natural Products, Technische Universität München, 85354 Freising, Germany.
Wilfried SchwabBiotechnology of Natural Products, Technische Universität München, 85354 Freising, Germany.ORCID 0000-0002-9753-3967
Technical University of Munich · DE

Funding

Deutsche Forschungsgemeinschaft DFG-SCHW634/32-1
6 · The paper itself

Abstract

The ability of glycosyltransferases (GTs) to reduce volatility, increase solubility, and thus alter the bioavailability of small molecules through glycosylation has attracted immense attention in pharmaceutical, nutraceutical, and cosmeceutical industries. The lack of GTs known and the scarcity of high-throughput (HTP) available methods, hinders the extrapolation of further novel applications. In this study, the applicability of new GT-assays suitable for HTP screening was tested and compared with regard to harmlessness, robustness, cost-effectiveness and reproducibility. The UDP-Glo GT-assay, Phosphate GT Activity assay, pH-sensitive GT-assay, and UDP

Indexed as

High-Throughput Screening AssaysColorimetryEnzyme ActivationGlycosidesGlycosyltransferasesHydrogen-Ion ConcentrationKineticsMetabolic Networks and PathwaysPhosphatesPlant ProteinsSubstrate SpecificityUridine DiphosphateGlycosidesGlycosyltransferasesPhosphatesPlant ProteinsUridine Diphosphatefamily-1 UGTsglycosyltransferasehigh-throughput assaykineticsphosphate GT assayscreeningUDP-Glo assay

Identifiers

PMID32210023
PMCPMC7139940
OpenAlexW3012746491

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.