Evidence map›Paper›PMID 34684811›Full record

ArticleMolecules (Basel, Switzerland)2021

Utility of Bioluminescent Homogeneous Nucleotide Detection Assays in Measuring Activities of Nucleotide-Sugar Dependent Glycosyltransferases and Studying Their Inhibitors.

Laurie Engel, Juliano Alves, Jacquelyn Hennek, Said A Goueli, Hicham Zegzouti

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. 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
0.4field-weighted citation impact, top 40% 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, 14 citations in OpenAlex.

  1. Article
  2. C-6-Modified 2-F-Fucose Derivatives as Inhibitors of Fucosyltransferases.Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Structure-function and engineering of plant UDP-glycosyltransferase.Computational and structural biotechnology journal · 2023
    Review
  7. Review
  8. 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

5 authors at 2 institutions in 1 country.

Laurie EngelPromega Corporation, R&D Department, 2800 Woods Hollow Road, Madison, WI 53719, USA.
Juliano AlvesPromega Corporation, R&D Department, 2800 Woods Hollow Road, Madison, WI 53719, USA.
Jacquelyn HennekPromega Corporation, R&D Department, 2800 Woods Hollow Road, Madison, WI 53719, USA.
Said A GoueliPromega Corporation, R&D Department, 2800 Woods Hollow Road, Madison, WI 53719, USA.
Hicham ZegzoutiPromega Corporation, R&D Department, 2800 Woods Hollow Road, Madison, WI 53719, USA.ORCID 0000-0002-0989-6195
Promega (United States) · USUniversity of Wisconsin–Madison · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Traditional glycosyltransferase (GT) activity assays are not easily configured for rapid detection nor for high throughput screening because they rely on radioactive product isolation, the use of heterogeneous immunoassays or mass spectrometry. In a typical glycosyltransferase biochemical reaction, two products are generated, a glycosylated product and a nucleotide released from the sugar donor substrate. Therefore, an assay that detects the nucleotide could be universal to monitor the activity of diverse glycosyltransferases in vitro. Here we describe three homogeneous and bioluminescent glycosyltransferase activity assays based on UDP, GDP, CMP, and UMP detection. Each of these assays are performed in a one-step detection that relies on converting the nucleotide product to ATP, then to bioluminescence using firefly luciferase. These assays are highly sensitive, robust and resistant to chemical interference. Various applications of these assays are presented, including studies on the specificity of sugar transfer by diverse GTs and the characterization of acceptor substrate-dependent and independent nucleotide-sugar hydrolysis. Furthermore, their utility in screening for specific GT inhibitors and the study of their mode of action are described. We believe that the broad utility of these nucleotide assays will enable the investigation of a large number of GTs and may have a significant impact on diverse areas of Glycobiology research.

Indexed as

Adenosine TriphosphateAnimalsEnzyme InhibitorsGlycomicsGlycosyltransferasesHigh-Throughput Screening AssaysKineticsLuciferases, FireflyLuminescent MeasurementsNucleotidesSubstrate SpecificityAdenosine TriphosphateEnzyme InhibitorsGlycosyltransferasesLuciferases, FireflyNucleotidesbioluminescencefucosyltransferaseinhibitornucleotide assaysOGTsugar substrate

Identifiers

PMID34684811
PMCPMC8539010
OpenAlexW3205150051

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.