Evidence map›Paper›PMID 29323461›Full record

ArticleChemMedChem2018

N-Benzyl Substitution of Polyhydroxypyrrolidines: The Way to Selective Inhibitors of Golgi α-Mannosidase II.

Sergej Šesták, Maroš Bella, Tomáš Klunda, Soňa Gurská, Petr Džubák, Florian Wöls, Iain B H Wilson, Vladimir Sladek, Marián Hajdúch, Monika Poláková and 1 more

Abstract read
In one paragraph

Article in ChemMedChem, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 25 citations in OpenAlex.

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  8. Crystal structure of 6-azido-6-de-oxy-1,2-Acta crystallographica. Section E, Crystallographic communications · 2020
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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 3 institutions in 3 countries.

Sergej ŠestákInstitute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.
Maroš BellaInstitute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.ORCID 0000-0001-6556-1579
Tomáš KlundaInstitute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.
Soňa GurskáLaboratory of Experimental Medicine, Institute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacky University and University Hospital in Olomouc, Puškinova 6, 775 20, Olomouc, Czech Republic.
Petr DžubákLaboratory of Experimental Medicine, Institute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacky University and University Hospital in Olomouc, Puškinova 6, 775 20, Olomouc, Czech Republic.
Florian WölsDepartment of Chemistry, University of Natural Resources and Life Sciences, 1190, Vienna, Austria.
Iain B H WilsonDepartment of Chemistry, University of Natural Resources and Life Sciences, 1190, Vienna, Austria.ORCID 0000-0001-8996-1518
Vladimir SladekInstitute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.ORCID 0000-0001-5332-7558
Marián HajdúchLaboratory of Experimental Medicine, Institute of Molecular and Translational Medicine, Faculty of Medicine and Dentistry, Palacky University and University Hospital in Olomouc, Puškinova 6, 775 20, Olomouc, Czech Republic.
Monika PolákováInstitute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.ORCID 0000-0002-1125-4482
Juraj KóňaInstitute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.ORCID 0000-0001-5687-9024
Institute of Chemistry of the Slovak Academy of Sciences · SKInstitute of Molecular and Translational Medicine · CZBOKU University · AT

Funding

Austrian Science Fund FWF P 29466
6 · The paper itself

Abstract

Inhibition of the biosynthesis of complex N-glycans in the Golgi apparatus influences progress of tumor growth and metastasis. Golgi α-mannosidase II (GMII) has become a therapeutic target for drugs with anticancer activities. One critical task for successful application of GMII drugs in medical treatments is to decrease their unwanted co-inhibition of lysosomal α-mannosidase (LMan), a weakness of all known potent GMII inhibitors. A series of novel N-substituted polyhydroxypyrrolidines was synthesized and tested with modeled GH38 α-mannosidases from Drosophila melanogaster (GMIIb and LManII). The most potent structures inhibited GMIIb (K

Indexed as

AnimalsAspergillusBinding SitesCatalytic DomainCell LineCell SurvivalDrosophila melanogasterFungal ProteinsGolgi ApparatusHumansInhibitory Concentration 50MannosidasesMolecular Docking SimulationNitrogenPyrrolidinesStructure-Activity RelationshipFungal ProteinsMannosidasesmannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidaseNitrogenPyrrolidinescytotoxicityGolgi α-mannosidase IImolecular modelingpyrrolidinesswainsonine

Identifiers

PMID29323461
PMCPMC6176901
OpenAlexW2885706430

What OpenQuestion holds

Textmetadata
LicenceTDM
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.