Evidence map›Paper›PMID 30877196›Full record

ArticleThe Journal of biological chemistry2019

Structural and functional analyses of glycoside hydrolase 138 enzymes targeting chain A galacturonic acid in the complex pectin rhamnogalacturonan II.

Aurore Labourel, Arnaud Baslé, Jose Munoz-Munoz, Didier Ndeh, Simon Booth, Sergey A Nepogodiev, Robert A Field, Alan Cartmell

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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.0field-weighted citation impact, top 12% 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, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
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

8 authors at 2 institutions in 1 country.

Aurore LabourelFrom the Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and.ORCID 0000-0002-4762-5804
Arnaud BasléFrom the Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and.
Jose Munoz-MunozFrom the Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and.
Didier NdehFrom the Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and.
Simon BoothFrom the Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and.ORCID 0000-0001-5585-022X
Sergey A NepogodievDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Robert A FieldDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Alan CartmellFrom the Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and alan.cartmell2@newcastle.ac.uk.ORCID 0000-0002-5512-249X
Newcastle University · GBJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618
6 · The paper itself

Abstract

The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiome. The selection pressures in this environment have spurred the evolution of a complex reservoir of microbial genes encoding carbohydrate-active enzymes (CAZymes). Previously, we have shown that the human gut bacterium

Indexed as

Bacterial ProteinsBacteroides thetaiotaomicronCatalytic DomainCrystallography, X-RayGlycoside HydrolasesHexuronic AcidsStructure-Activity RelationshipSubstrate SpecificityBacterial Proteinsgalacturonic acidGlycoside HydrolasesHexuronic Acidscarbohydratecarbohydrate-active enzyme (CAZyme)carbohydrate metabolismcomplex glycancrystallographyenzymeenzyme catalysisenzyme kineticsenzyme mechanismglycoside hydrolase (GH)gut microbepectinrhamnogalacturonan II

Identifiers

PMID30877196
PMCPMC6514610
OpenAlexW2921683783

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.