Evidence map›Paper›PMID 32575625›Full record

ArticleMolecules (Basel, Switzerland)2020

Strategy for Designing Selective Lysosomal Acid α-Glucosidase Inhibitors: Binding Orientation and Influence on Selectivity.

Atsushi Kato, Izumi Nakagome, Mizuki Hata, Robert J Nash, George W J Fleet, Yoshihiro Natori, Yuichi Yoshimura, Isao Adachi, Shuichi Hirono

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. 1,6-Journal of the American Chemical Society · 2022
    Article
  3. Article
  4. Pharmacological Chaperone Therapy for Pompe Disease.Molecules (Basel, Switzerland) · 2021
    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

9 authors at 5 institutions in 2 countries.

Atsushi KatoDepartment of Hospital Pharmacy, University of Toyama, Toyama 930-0194, Japan.ORCID 0000-0001-8022-196X
Izumi NakagomeSchool of Pharmaceutical Sciences, Kitasato University, Tokyo 108-8641, Japan.
Mizuki HataDepartment of Hospital Pharmacy, University of Toyama, Toyama 930-0194, Japan.
Robert J NashInstitute of Biological, Environmental and Rural Sciences, Plas Gogerddan, Aberystwyth, Ceredigion SY23 3EB, UK.
George W J FleetChemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3TA, UK.ORCID 0000-0003-1903-270X
Yoshihiro NatoriFaculty of Pharmaceutical Sciences, Tohoku Pharmaceutical University, Sendai 981-8558, Japan.
Yuichi YoshimuraFaculty of Pharmaceutical Sciences, Tohoku Pharmaceutical University, Sendai 981-8558, Japan.ORCID 0000-0002-9686-6671
Isao AdachiDepartment of Hospital Pharmacy, University of Toyama, Toyama 930-0194, Japan.
Shuichi HironoSchool of Pharmaceutical Sciences, Kitasato University, Tokyo 108-8641, Japan.
Toyama University Hospital · JPKitasato University · JPTohoku Medical and Pharmaceutical University · JPInstitute of Biological, Environmental and Rural Sciences · GBUniversity of Oxford · GB

Funding

Japanese Society for the Promotion of Science JSPS KAKENHI Grant Number JP17K08362
6 · The paper itself

Abstract

Deoxynojirimycin (DNJ) is the archetypal iminosugar, in which the configuration of the hydroxyl groups in the piperidine ring truly mimic those of d-glucopyranose; DNJ and derivatives have beneficial effects as therapeutic agents, such as anti-diabetic and antiviral agents, and pharmacological chaperones for genetic disorders, because they have been shown to inhibit α-glucosidases from various sources. However, attempts to design a better molecule based solely on structural similarity cannot produce selectivity between α-glucosidases that are localized in multiple organs and tissues, because the differences of each sugar-recognition site are very subtle. In this study, we provide the first example of a design strategy for selective lysosomal acid α-glucosidase (GAA) inhibitors focusing on the alkyl chain storage site. Our design of α-1-

Indexed as

Drug DesignMolecular Docking Simulation1-Deoxynojirimycinalpha-GlucosidasesAntiviral AgentsGlucosamineGlycoside Hydrolase InhibitorsHumansImino Sugars1-Deoxynojirimycinalpha-GlucosidasesAntiviral AgentsdeoxynojirimycineGlucosamineGlycoside Hydrolase InhibitorsImino Sugarsdrug designER α-glucosidase IIglucosidase inhibitoriminosugarsligand dockinglysosomal acid α-glucosidasemolecular dynamics

Identifiers

PMID32575625
PMCPMC7357040
OpenAlexW3036594946

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.