Evidence map›Paper›PMID 33497208›Full record

ArticleJournal of the American Chemical Society2021

Activity-Based Protein Profiling of Retaining α-Amylases in Complex Biological Samples.

Yurong Chen, Zachary Armstrong, Marta Artola, Bogdan I Florea, Chi-Lin Kuo, Casper de Boer, Mikkel S Rasmussen, Maher Abou Hachem, Gijsbert A van der Marel, Jeroen D C Codée and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.5field-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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Activity-Based Tracking of Glycan Turnover in Microbiomes.Journal of the American Chemical Society · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Chemical science · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Synthesis of CFrontiers in chemistry · 2022
    Article
  14. Article
  15. Article
  16. Review
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

13 authors at 3 institutions in 3 countries.

Zachary ArmstrongDepartment of Chemistry, York Structural Biology Laboratory, University of York, Heslington, York YO10 5DD, United Kingdom.ORCID 0000-0002-4086-2946
Mikkel S RasmussenDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Søltofts Plad, 2800 Kgs. Lyngby, Denmark.
Maher Abou HachemDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Søltofts Plad, 2800 Kgs. Lyngby, Denmark.ORCID 0000-0001-8250-1842
Gijsbert A van der Marel
Jeroen D C CodéeORCID 0000-0003-3531-2138
Johannes M F G AertsORCID 0000-0001-8168-2565
Gideon J DaviesDepartment of Chemistry, York Structural Biology Laboratory, University of York, Heslington, York YO10 5DD, United Kingdom.ORCID 0000-0002-7343-776X
Herman S OverkleeftORCID 0000-0001-6976-7005
Leiden University · NLTechnical University of Denmark · DKUniversity of York · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amylases are key enzymes in the processing of starch in many kingdoms of life. They are important catalysts in industrial biotechnology where they are applied in, among others, food processing and the production of detergents. In man amylases are the first enzymes in the digestion of starch to glucose and arguably also the preferred target in therapeutic strategies aimed at the treatment of type 2 diabetes patients through down-tuning glucose assimilation. Efficient and sensitive assays that report selectively on retaining amylase activities irrespective of the nature and complexity of the biomaterial studied are of great value both in finding new and effective human amylase inhibitors and in the discovery of new microbial amylases with potentially advantageous features for biotechnological application. Activity-based protein profiling (ABPP) of retaining glycosidases is inherently suited for the development of such an assay format. We here report on the design and synthesis of 1,6-

Indexed as

alpha-AmylasesAnimalsEnzyme AssaysHumansMiceSalivaalpha-Amylases

Identifiers

PMID33497208
PMCPMC7883350
OpenAlexW3121899418

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.