Evidence map›Paper›PMID 35328813›Full record

ArticleInternational journal of molecular sciences2022

Proteomic Analysis Reveals Enzymes for β-D-Glucan Formation and Degradation in

Julia A Bockwoldt, Chen Meng, Christina Ludwig, Michael Kupetz, Matthias A Ehrmann

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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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

5 authors at 1 institution in 1 country.

Julia A BockwoldtLehrstuhl für Mikrobiologie, Technische Universität München, 85354 Freising, Germany.
Chen MengBayerisches Zentrum für Biomolekulare Massenspektrometrie (BayBioMS), Technische Universität München, 85354 Freising, Germany.
Christina LudwigBayerisches Zentrum für Biomolekulare Massenspektrometrie (BayBioMS), Technische Universität München, 85354 Freising, Germany.ORCID 0000-0002-6131-7322
Michael KupetzLehrstuhl für Brau- und Getränketechnologie, Technische Universität München, 85354 Freising, Germany.
Matthias A EhrmannLehrstuhl für Mikrobiologie, Technische Universität München, 85354 Freising, Germany.ORCID 0000-0003-2004-5751
Technical University of Munich · DE

Funding

German Ministry for Economic Affairs and Energy (BMWi) AiF 20462 BG
6 · The paper itself

Abstract

Bacterial exopolysaccharide (EPS) formation is crucial for biofilm formation, for protection against environmental factors, or as storage compounds. EPSs produced by lactic acid bacteria (LAB) are appropriate for applications in food fermentation or the pharmaceutical industry, yet the dynamics of formation and degradation thereof are poorly described. This study focuses on carbohydrate active enzymes, including glycosyl transferases (GT) and glycoside hydrolases (GH), and their roles in the formation and potential degradation of

Indexed as

beta-GlucansLevilactobacillus brevisCarbohydratesGlucansProteomeProteomicsbeta-GlucansCarbohydratesGlucansProteomeexopolysaccharideglycosyl hydrolaseglycosyltransferaseLevilactobacillus brevis TMW 1.2112moonlighting proteinsproteomesecretomeβ-glucan

Identifiers

PMID35328813
PMCPMC8951740
OpenAlexW4220656312

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.