Evidence map›Paper›PMID 35268716›Full record

ArticleMolecules (Basel, Switzerland)2022

Detection of Bacterial α-l-Fucosidases with an

Yvette M C A Luijkx, Anniek J Henselijn, Gerlof P Bosman, Dario A T Cramer, Koen C A P Giesbers, Esther M van 't Veld, Geert-Jan Boons, Albert J R Heck, Karli R Reiding, Karin Strijbis and 1 more

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Chemical biology tools to probe bacterial glycans.Current opinion in chemical biology · 2024
    Review
  4. Article
  5. Review
  6. Review
  7. Article
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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

11 authors at 2 institutions in 2 countries.

Yvette M C A LuijkxDepartment Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, Universiteitswg 99, 3584 CG Utrecht, The Netherlands.
Anniek J HenselijnDepartment Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, Universiteitswg 99, 3584 CG Utrecht, The Netherlands.
Gerlof P BosmanDepartment Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, Universiteitswg 99, 3584 CG Utrecht, The Netherlands.
Dario A T CramerDepartment Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands.
Koen C A P GiesbersDepartment Biomolecular Health Sciences, Division Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The Netherlands.
Esther M van 't VeldDepartment Biomolecular Health Sciences, Centre for Cell Imaging, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The Netherlands.
Geert-Jan BoonsDepartment Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, Universiteitswg 99, 3584 CG Utrecht, The Netherlands.
Albert J R HeckDepartment Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands.
Karli R ReidingDepartment Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands.ORCID 0000-0003-3695-5274
Karin StrijbisDepartment Biomolecular Health Sciences, Division Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The Netherlands.
Tom WennekesDepartment Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Bijvoet Center for Biomolecular Research, Utrecht University, Universiteitswg 99, 3584 CG Utrecht, The Netherlands.ORCID 0000-0002-2368-7728
Utrecht University · NLUniversity of Georgia · US

Funding

European Research Council ERC-2019-STG-852452The Netherlands Organization for Scientific Research VIDI grant 723.014.005The Netherlands Organization for Scientific Research VI.Veni.192.058
6 · The paper itself

Abstract

Fucosidases are associated with several pathological conditions and play an important role in the health of the human gut. For example, fucosidases have been shown to be indicators and/or involved in hepatocellular carcinoma, breast cancer, and helicobacter pylori infections. A prerequisite for the detection and profiling of fucosidases is the formation of a specific covalent linkage between the enzyme of interest and the activity-based probe (ABP). The most commonly used fucosidase ABPs are limited to only one of the classes of fucosidases, the retaining fucosidases. New approaches are needed that allow for the detection of the second class of fucosidases, the inverting type. Here, we report an

Indexed as

Helicobacter InfectionsHelicobacter pyloriIndolequinonesalpha-L-FucosidaseHumansalpha-L-FucosidaseIndolequinonesquinone methidebacteriafucoseglycosidaseprobeproteomicsquinone methide

Identifiers

PMID35268716
PMCPMC8911971
OpenAlexW4214577379

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.