Evidence map›Paper›PMID 27749924›Full record

ArticlePloS one2016

Matching the Diversity of Sulfated Biomolecules: Creation of a Classification Database for Sulfatases Reflecting Their Substrate Specificity.

Tristan Barbeyron, Loraine Brillet-Guéguen, Wilfrid Carré, Cathelène Carrière, Christophe Caron, Mirjam Czjzek, Mark Hoebeke, Gurvan Michel

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
11.9field-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

92 citing papers in PubMed, 173 citations in OpenAlex.

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  11. Arylsulfamates inhibit colonic Bacteroidota growth through a sulfatase-independent mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Hindguts ofmSystems · 2025
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  16. Review
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32 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

8 authors at 1 institution in 1 country.

Tristan BarbeyronSorbonne Universités, UPMC Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Loraine Brillet-GuéguenCNRS FR 2424, Sorbonne Universités, UPMC Univ Paris 06, FR2424, ABiMS platform, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Wilfrid CarréCNRS FR 2424, Sorbonne Universités, UPMC Univ Paris 06, FR2424, ABiMS platform, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Cathelène CarrièreSorbonne Universités, UPMC Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Christophe CaronCNRS FR 2424, Sorbonne Universités, UPMC Univ Paris 06, FR2424, ABiMS platform, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Mirjam CzjzekSorbonne Universités, UPMC Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Mark HoebekeCNRS FR 2424, Sorbonne Universités, UPMC Univ Paris 06, FR2424, ABiMS platform, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Gurvan MichelSorbonne Universités, UPMC Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Station Biologique de Roscoff, CS 90074, Roscoff, Bretagne, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sulfatases cleave sulfate groups from various molecules and constitute a biologically and industrially important group of enzymes. However, the number of sulfatases whose substrate has been characterized is limited in comparison to the huge diversity of sulfated compounds, yielding functional annotations of sulfatases particularly prone to flaws and misinterpretations. In the context of the explosion of genomic data, a classification system allowing a better prediction of substrate specificity and for setting the limit of functional annotations is urgently needed for sulfatases. Here, after an overview on the diversity of sulfated compounds and on the known sulfatases, we propose a classification database, SulfAtlas (http://abims.sb-roscoff.fr/sulfatlas/), based on sequence homology and composed of four families of sulfatases. The formylglycine-dependent sulfatases, which constitute the largest family, are also divided by phylogenetic approach into 73 subfamilies, each subfamily corresponding to either a known specificity or to an uncharacterized substrate. SulfAtlas summarizes information about the different families of sulfatases. Within a family a web page displays the list of its subfamilies (when they exist) and the list of EC numbers. The family or subfamily page shows some descriptors and a table with all the UniProt accession numbers linked to the databases UniProt, ExplorEnz, and PDB.

Indexed as

AnimalsBacteriaBiocatalysisCatalytic DomainDatabases, ProteinHumansInternetPhylogenySubstrate SpecificitySulfatasesSulfatesUser-Computer InterfaceSulfatasesSulfates

Identifiers

PMID27749924
PMCPMC5066984
OpenAlexW2532767550

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.