Evidence map›Paper›PMID 39213505›Full record

ReviewJournal of the American Chemical Society2024

From Mechanism-Based Retaining Glycosidase Inhibitors to Activity-Based Glycosidase Profiling.

Marta Artola, Johannes M F G Aerts, Gijsbert A van der Marel, Carme Rovira, Jeroen D C Codée, Gideon J Davies, Herman S Overkleeft

Abstract readReview
In one paragraph

Review in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Oseltamivir aziridines are potent influenza neuraminidase inhibitors and imaging agents.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Review
  10. Neutron crystallography of the covalent intermediate of β-glucosidase reveals remodeling of the catalytic center.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Review
  13. Bespoke Activity-Based Probes Reveal that theJournal of the American Chemical Society · 2025
    Article
  14. 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

7 authors.

Marta ArtolaLeiden Institute of Chemistry, Leiden University, 2300 RA, Leiden, The Netherlands.ORCID 0000-0002-3051-3902
Johannes M F G AertsLeiden Institute of Chemistry, Leiden University, 2300 RA, Leiden, The Netherlands.ORCID 0000-0001-8168-2565
Gijsbert A van der MarelLeiden Institute of Chemistry, Leiden University, 2300 RA, Leiden, The Netherlands.
Carme RoviraDepartament de Química Inorgànica I Orgànica & IQTCUB, Universitat de Barcelona, Barcelona 08028, Spain.ORCID 0000-0003-1477-5010
Jeroen D C CodéeLeiden Institute of Chemistry, Leiden University, 2300 RA, Leiden, The Netherlands.ORCID 0000-0003-3531-2138
Gideon J DaviesDepartment of Chemistry, The University York, Heslington, York YO10 5DD, United Kingdom.ORCID 0000-0002-7343-776X
Herman S OverkleeftLeiden Institute of Chemistry, Leiden University, 2300 RA, Leiden, The Netherlands.ORCID 0000-0001-6976-7005

Funding

European Research Council
6 · The paper itself

Abstract

Activity-based protein profiling (ABPP) is an effective technology for the identification and functional annotation of enzymes in complex biological samples. ABP designs are normally directed to an enzyme active site nucleophile, and within the field of Carbohydrate-Active Enzymes (CAZymes), ABPP has been most successful for those enzymes that feature such a residue: retaining glycosidases (GHs). Several mechanism-based covalent and irreversible retaining GH inhibitors have emerged over the past sixty years. ABP designs based on these inhibitor chemistries appeared since the turn of the millennium, and we contributed to the field by designing a suite of retaining GH ABPs modeled on the structure and mode of action of the natural product, cyclophellitol. These ABPs enable the study of both exo- and endo-acting retaining GHs in human health and disease, for instance in genetic metabolic disorders in which retaining GHs are deficient. They are also finding increasing use in the study of GHs in gut microbiota and environmental microorganisms, both in the context of drug (de)toxification in the gut and that of biomass polysaccharide processing for future sustainable energy and chemistries. This account comprises the authors' view on the history of mechanism-based retaining GH inhibitor design and discovery, on how these inhibitors served as blueprints for retaining GH ABP design, and on some current and future developments on how cyclophellitol-based ABPs may drive the discovery of retaining GHs and their inhibitors.

Indexed as

Enzyme InhibitorsGlycoside HydrolasesHumansEnzyme InhibitorsGlycoside Hydrolases

Identifiers

PMID39213505
PMCPMC11403624

What OpenQuestion holds

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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.