Evidence map›Paper›PMID 25056938›Full record

ArticleMolecular & cellular proteomics : MCP2014

Broad-range glycosidase activity profiling.

Balakumaran Chandrasekar, Thomas Colby, Asif Emran Khan Emon, Jianbing Jiang, Tram Ngoc Hong, Joji Grace Villamor, Anne Harzen, Herman S Overkleeft, Renier A L van der Hoorn

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 62 citations in OpenAlex.

  1. Pan-Genomic Dissection of GH1 β-Glucosidases inPlants (Basel, Switzerland) · 2026
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  19. Genome-Wide Analysis of Glycoside Hydrolase Family 1 β-glucosidase Genes inInternational journal of molecular sciences · 2019
    Article
  20. Frontiers in bioengineering and biotechnology · 2019
    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

9 authors at 2 institutions in 2 countries.

Balakumaran ChandrasekarFrom the ‡Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom; §Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany;
Thomas Colby‖Gorlaeus Laboratories, Leiden Institute of Chemistry and Netherlands Center for Proteomics, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
Asif Emran Khan Emon§Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany;
Jianbing Jiang‖Gorlaeus Laboratories, Leiden Institute of Chemistry and Netherlands Center for Proteomics, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
Tram Ngoc HongFrom the ‡Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom; §Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany;
Joji Grace Villamor§Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany;
Anne Harzen‖Gorlaeus Laboratories, Leiden Institute of Chemistry and Netherlands Center for Proteomics, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
Herman S Overkleeft‖Gorlaeus Laboratories, Leiden Institute of Chemistry and Netherlands Center for Proteomics, Einsteinweg 55, 2333 CC Leiden, The Netherlands renier.vanderhoorn@plants.ox.ac.uk h.s.overkleeft@chem.leidenuniv.nl.
Renier A L van der HoornFrom the ‡Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom; From the ‡Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom;
Max Planck Society · DEUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants produce hundreds of glycosidases. Despite their importance in cell wall (re)modeling, protein and lipid modification, and metabolite conversion, very little is known of this large class of glycolytic enzymes, partly because of their post-translational regulation and their elusive substrates. Here, we applied activity-based glycosidase profiling using cell-permeable small molecular probes that react covalently with the active site nucleophile of retaining glycosidases in an activity-dependent manner. Using mass spectrometry we detected the active state of dozens of myrosinases, glucosidases, xylosidases, and galactosidases representing seven different retaining glycosidase families. The method is simple and applicable for different organs and different plant species, in living cells and in subproteomes. We display the active state of previously uncharacterized glycosidases, one of which was encoded by a previously declared pseudogene. Interestingly, glycosidase activity profiling also revealed the active state of a diverse range of putative xylosidases, galactosidases, glucanases, and heparanase in the cell wall of Nicotiana benthamiana. Our data illustrate that this powerful approach displays a new and important layer of functional proteomic information on the active state of glycosidases.

Indexed as

ArabidopsisArabidopsis ProteinsAziridinesCatalytic DomainCell WallCyclohexanolsGlycoside HydrolasesMass SpectrometryMolecular ProbesPhylogenyProteomicsArabidopsis ProteinsAziridinesCyclohexanolscyclophellitolGlycoside HydrolasesMolecular Probes

Identifiers

PMID25056938
PMCPMC4189003
OpenAlexW2105346934

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.