Evidence map›Paper›PMID 30814248›Full record

ArticleThe Journal of biological chemistry2019

Structure-function analyses reveal that a glucuronoyl esterase from

Jenny Arnling Bååth, Scott Mazurkewich, Jens-Christian Navarro Poulsen, Lisbeth Olsson, Leila Lo Leggio, Johan Larsbrink

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

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  12. Plastid Transformation: New Challenges in the Circular Economy Era.International journal of molecular sciences · 2022
    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

6 authors at 2 institutions in 2 countries.

Jenny Arnling BååthFrom the Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden and.
Scott MazurkewichFrom the Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden and.ORCID 0000-0002-9238-0615
Jens-Christian Navarro PoulsenDepartment of Chemistry, University of Copenhagen, DK-2100 Copenhagen, Denmark.ORCID 0000-0002-3553-0015
Lisbeth OlssonFrom the Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden and.
Leila Lo LeggioDepartment of Chemistry, University of Copenhagen, DK-2100 Copenhagen, Denmark.ORCID 0000-0002-5135-0882
Johan LarsbrinkFrom the Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden and johan.larsbrink@chalmers.se.ORCID 0000-0001-8386-2914
Wallenberg Wood Science Center · SEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources. However, details on how GEs interact with their natural substrates are sparse, calling for thorough structure-function studies. Presented here is the structure and biochemical characterization of a GE,

Indexed as

Bacterial ProteinsCarbohydratesCrystallography, X-RayEsterasesGammaproteobacteriaHydrocarbons, AromaticMutagenesis, Site-DirectedProtein DomainsStructure-Activity RelationshipUronic AcidsBacterial ProteinsCarbohydratesEsterasesHydrocarbons, AromaticUronic Acidsbiotechnologycarbohydratecarbohydrate-active enzymescarbohydrate esteraseCE15enzyme kineticsenzyme mechanismenzyme mutationenzyme structureglucuronoyl esteraselignin-carbohydrate complexesplant cell wallprotein structureuronic acid

Identifiers

PMID30814248
PMCPMC6484129
OpenAlexW2915907845

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.