Evidence map›Paper›PMID 38930854›Full record

ArticleMolecules (Basel, Switzerland)2024

Characterization of Two Glycoside Hydrolases of Family GH13 and GH57, Present in a Polysaccharide Utilization Locus (PUL) of

Hilda Hubertha Maria Bax, Edita Jurak

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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.

Hilda Hubertha Maria BaxBioproduct Engineering, Engineering and Technology Institute Groningen, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.ORCID 0000-0001-9036-2096
Edita JurakBioproduct Engineering, Engineering and Technology Institute Groningen, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.ORCID 0000-0003-4253-4556

Funding

Dutch Research Council This research was performed in the public private partnership CarboBased, coordinated by the Carbohydrate Competence Center (CCC) and cofinanced by AVEBE and the "Samenwerkingsverband Noord-Nederland (SNN), Ruimtelijk Economisch Programma".
6 · The paper itself

Abstract

Glycogen, an α-glucan polymer serving as an energy storage compound in microorganisms, is synthesized through distinct pathways (GlgC-GlgA or GlgE pathway). Both pathways involve multiple enzymes, with a shared glycogen branching enzyme (GBE). GBEs play a pivotal role in establishing α-1,6-linkages within the glycogen structure. GBEs are also used for starch modification. Understanding how these enzymes work is interesting for both glycogen synthesis in microorganisms, as well as novel applications for starch modification. This study focuses on a putative enzyme GH13_9 GBE (PoGBE13), present in a polysaccharide utilization locus (PUL) of

Indexed as

Glycoside Hydrolases1,4-alpha-Glucan Branching EnzymeBacterial ProteinsGlycogenPolysaccharidesStarchSubstrate Specificity1,4-alpha-Glucan Branching EnzymeBacterial ProteinsGlycogenGlycoside HydrolasesPolysaccharidesStarchalpha-1,4-transglycosylationglycogen branching enzymeglycogen branching enzymes (EC 2.4.1.18)glycogen synthesismaltooctadecaosepolysaccharide utilization loci

Identifiers

PMID38930854
PMCPMC11206854

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Registered trials

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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.