Evidence map›Paper›PMID 38990885›Full record

ArticlePloS one2024

CANDy: Automated analysis of domain architectures in carbohydrate-active enzymes.

Alex Windels, Jorick Franceus, Jürgen Pleiss, Tom Desmet

Abstract read
In one paragraph

Article in PloS one, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

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3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Reverse prediction of carbohydrate esterase polysaccharide targets.Biotechnology for biofuels and bioproducts · 2026
    Article
  3. Mechanisms ofAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2026
    Article
  4. Article
  5. 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

4 authors.

Alex WindelsDepartment of Biotechnology, Centre for Synthetic Biology (CSB), Ghent University, Ghent, Belgium.ORCID 0009-0005-9046-3141
Jorick FranceusDepartment of Biotechnology, Centre for Synthetic Biology (CSB), Ghent University, Ghent, Belgium.ORCID 0000-0003-4377-5933
Jürgen PleissInstitute of Biochemistry and Technical Biochemistry, University of Stuttgart, Stuttgart, Germany.
Tom DesmetDepartment of Biotechnology, Centre for Synthetic Biology (CSB), Ghent University, Ghent, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbohydrate-active enzymes (CAZymes) can be found in all domains of life and play a crucial role in metabolic and physiological processes. CAZymes often possess a modular structure, comprising not only catalytic domains but also associated domains such as carbohydrate-binding modules (CBMs) and linker domains. By exploring the modular diversity of CAZy families, catalysts with novel properties can be discovered and further insight in their biological functions and evolutionary relationships can be obtained. Here we present the carbohydrate-active enzyme domain analysis tool (CANDy), an assembly of several novel scripts, tools and databases that allows users to analyze the domain architecture of all protein sequences in a given CAZy family. CANDy's usability is shown on glycoside hydrolase family 48, a small yet underexplored family containing multi-domain enzymes. Our analysis reveals the existence of 35 distinct domain assemblies, including eight known architectures, with the remaining assemblies awaiting characterization. Moreover, we substantiate the occurrence of horizontal gene transfer from prokaryotes to insect orthologs and provide evidence for the subsequent removal of auxiliary domains, likely through a gene fission event. CANDy is available at https://github.com/PyEED/CANDy.

Indexed as

Protein DomainsAnimalsCarbohydrate MetabolismCarbohydratesCatalytic DomainGlycoside HydrolasesSoftwareCarbohydratesGlycoside Hydrolases

Identifiers

PMID38990885
PMCPMC11238990

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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.