Evidence map›Paper›PMID 35210619›Full record

ArticleNature chemical biology2022

Quantifying lysosomal glycosidase activity within cells using bis-acetal substrates.

Samy Cecioni, Roger A Ashmus, Pierre-André Gilormini, Sha Zhu, Xi Chen, Xiaoyang Shan, Christina Gros, Matthew C Deen, Yang Wang, Robert Britton and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Activity-Based Tracking of Glycan Turnover in Microbiomes.Journal of the American Chemical Society · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. FluorogenicJACS Au · 2023
    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

11 authors.

Samy Cecioni *Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.ORCID http://orcid.org/0000-0003-3169-9646
Roger A Ashmus *Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Pierre-André GilorminiDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Sha ZhuDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.ORCID http://orcid.org/0000-0003-3352-1040
Xi ChenDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Xiaoyang ShanDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Christina GrosDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Matthew C DeenDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Yang WangDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
Robert BrittonDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
David J VocadloDepartment of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada. dvocadlo@sfu.ca.ORCID http://orcid.org/0000-0001-6897-5558

Funding

CIHR
6 · The paper itself

Abstract

Understanding the function and regulation of enzymes within their physiologically relevant milieu requires quality tools that report on their cellular activities. Here we describe a strategy for glycoside hydrolases that overcomes several limitations in the field, enabling quantitative monitoring of their activities within live cells. We detail the design and synthesis of bright and modularly assembled bis-acetal-based (BAB) fluorescence-quenched substrates, illustrating this strategy for sensitive quantitation of disease-relevant human α-galactosidase and α-N-acetylgalactosaminidase activities. We show that these substrates can be used within live patient cells to precisely measure the engagement of target enzymes by inhibitors and the efficiency of pharmacological chaperones, and highlight the importance of quantifying activity within cells using chemical perturbogens of cellular trafficking and lysosomal homeostasis. These BAB substrates should prove widely useful for interrogating the regulation of glycosidases within cells as well as in facilitating the development of therapeutics and diagnostics for this important class of enzymes.

Indexed as

AcetalsLysosomesalpha-GalactosidaseFluorescenceGlycoside HydrolasesHumansAcetalsalpha-GalactosidaseGlycoside Hydrolases

Identifiers

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.