Evidence map›Paper›PMID 32645249›Full record

ArticleThe FEBS journal2021

Mechanistic characterization of UDP-glucuronic acid 4-epimerase.

Annika J E Borg, Alexander Dennig, Hansjörg Weber, Bernd Nidetzky

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  8. Polymers · 2023
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  13. Review
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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

4 authors at 1 institution in 1 country.

Annika J E BorgInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Austria.ORCID 0000-0003-1311-6910
Alexander DennigInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Austria.
Hansjörg WeberInstitute of Organic Chemistry, Graz University of Technology, NAWI Graz, Austria.
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, Austria.ORCID 0000-0002-5030-2643
Graz University of Technology · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UDP-glucuronic acid (UDP-GlcA) is a central precursor in sugar nucleotide biosynthesis and common substrate for C4-epimerases and decarboxylases releasing UDP-galacturonic acid (UDP-GalA) and UDP-pentose products, respectively. Despite the different reactions catalyzed, the enzymes are believed to share mechanistic analogy rooted in their joint membership to the short-chain dehydrogenase/reductase (SDR) protein superfamily: Oxidation at the substrate C4 by enzyme-bound NAD

Indexed as

Bacillus cereusBacterial ProteinsBiocatalysisCarbohydrate SequenceCatalytic DomainChromatography, High Pressure LiquidEscherichia coliHydrogen-Ion ConcentrationKineticsMagnetic Resonance SpectroscopyMolecular Sequence DataMutant ProteinsMutationRacemases and EpimerasesRecombinant ProteinsUridine Diphosphate SugarsBacterial ProteinsMutant ProteinsRacemases and EpimerasesRecombinant ProteinsUDP-galacturonic acidUridine Diphosphate Sugarsdecarboxylaseepimerasekinetic isotope effectshort-chain dehydrogenase/reductaseUDP-glucuronic acid

Identifiers

PMID32645249
PMCPMC7984243
OpenAlexW3040997813

What OpenQuestion holds

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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.