Evidence map›Paper›PMID 26729713›Full record

ArticleApplied and environmental microbiology2016

Dividing the Large Glycoside Hydrolase Family 43 into Subfamilies: a Motivation for Detailed Enzyme Characterization.

Keith Mewis, Nicolas Lenfant, Vincent Lombard, Bernard Henrissat

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
26.9field-weighted citation impact, top 1% 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

114 citing papers in PubMed, 233 citations in OpenAlex.

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  17. Early-Stage Infection-SpecificInternational journal of molecular sciences · 2024
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  19. A novel glycoside hydrolase 43-like enzyme fromApplied and environmental microbiology · 2024
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  20. Article

54 more citing papers are in PubMed but not listed here.

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 2 institutions in 3 countries.

Keith MewisGenome Science and Technology Program, University of British Columbia, Vancouver, BC, Canada.
Nicolas LenfantArchitecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, Marseille, France.ORCID http://orcid.org/0000-0002-0519-1120
Vincent LombardArchitecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, Marseille, France.
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, Marseille, France Bernard.Henrissat@afmb.univ-mrs.fr.
Centre National de la Recherche Scientifique · FRUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rapid rise in DNA sequencing has led to an expansion in the number of glycoside hydrolase (GH) families. The GH43 family currently contains α-l-arabinofuranosidase, β-d-xylosidase, α-l-arabinanase, and β-d-galactosidase enzymes for the debranching and degradation of hemicellulose and pectin polymers. Many studies have revealed finer details about members of GH43 that necessitate the division of GH43 into subfamilies, as was done previously for the GH5 and GH13 families. The work presented here is a robust subfamily classification that assigns over 91% of all complete GH43 domains into 37 subfamilies that correlate with conserved sequence residues and results of biochemical assays and structural studies. Furthermore, cooccurrence analysis of these subfamilies and other functional modules revealed strong associations between some GH43 subfamilies and CBM6 and CBM13 domains. Cooccurrence analysis also revealed the presence of proteins containing up to three GH43 domains and belonging to different subfamilies, suggesting significant functional differences for each subfamily. Overall, the subfamily analysis suggests that the GH43 enzymes probably display a hitherto underestimated variety of subtle specificity features that are not apparent when the enzymes are assayed with simple synthetic substrates, such as pNP-glycosides.

Indexed as

Glycoside HydrolasesHydrolysisPectinsPolysaccharidesProtein DomainsGlycoside HydrolaseshemicellulosePectinsPolysaccharides

Identifiers

PMID26729713
PMCPMC4784025
OpenAlexW2229013467

What OpenQuestion holds

Textmetadata
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.