Evidence map›Paper›PMID 39459237›Full record

ArticleMolecules (Basel, Switzerland)2024

Mechanism-Based Allylic Carbasugar Chlorides That Form Covalent Intermediates with α- and β-Galactosidases.

Oluwafemi Akintola, Sandeep Bhosale, Andrew J Bennet

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Oluwafemi AkintolaDepartment of Chemistry, Simon Fraser University, Burnaby, BC V5A 1S6, Canada.
Sandeep BhosaleDepartment of Chemistry, Simon Fraser University, Burnaby, BC V5A 1S6, Canada.ORCID 0000-0002-1850-1271
Andrew J BennetDepartment of Chemistry, Simon Fraser University, Burnaby, BC V5A 1S6, Canada.ORCID 0000-0002-8378-6752

Funding

Natural Sciences and Engineering Research Council 2023-03581
6 · The paper itself

Abstract

Glycoside hydrolases have been implicated in a wide range of human conditions including lysosomal storage diseases. Consequently, many researchers have directed their efforts towards identifying new classes of glycoside hydrolase inhibitors, both synthetic and from natural sources. A large percentage of such inhibitors are reversible competitive inhibitors that bind in the active site often due to them possessing structural features, often a protonatable basic nitrogen atom, that mimic the enzymatic transition state. We report that mechanism-based small molecule

Indexed as

alpha-GalactosidaseAspergillus oryzaebeta-GalactosidaseCarbasugarsCatalytic DomainEnzyme InhibitorsGlycoside Hydrolase InhibitorsKineticsalpha-Galactosidasebeta-GalactosidaseCarbasugarsEnzyme InhibitorsGlycoside Hydrolase Inhibitorscarbasugarcovalent inhibitorgalactosidaseglycoside hydrolasemechanism-basedselectivity

Identifiers

PMID39459237
PMCPMC11510499

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.