Evidence map›Paper›PMID 39595567›Full record

ArticleBiomolecules2024

Efficient Access to New Thienobenzo-1,2,3-Triazolium Salts as Preferred Dual Cholinesterase Inhibitors.

Milena Mlakić, Maja Sviben, Ana Ratković, Anamarija Raspudić, Danijela Barić, Ivana Šagud, Zlata Lasić, Ilijana Odak, Irena Škorić

Abstract read
In one paragraph

Article in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

Milena MlakićDepartment of Organic Chemistry, Faculty of Chemical Engineering and Technology, University of Zagreb, Trg Marka Marulića 19, HR-10 000 Zagreb, Croatia.ORCID 0000-0001-8371-4946
Maja SvibenDepartment of Organic Chemistry, Faculty of Chemical Engineering and Technology, University of Zagreb, Trg Marka Marulića 19, HR-10 000 Zagreb, Croatia.
Ana RatkovićChemistry, Selvita Ltd., Prilaz Baruna Filipovića 29, HR-10 000 Zagreb, Croatia.
Anamarija RaspudićDepartment of Chemistry, Faculty of Science and Education, University of Mostar, Matice hrvatske bb, 88 000 Mostar, Bosnia and Herzegovina.
Danijela BarićGroup for Computational Life Sciences, Division of Physical Chemistry, Ruđer Bošković Institute, Bijenička cesta 54, HR-10 000 Zagreb, Croatia.ORCID 0000-0002-5614-5167
Ivana ŠagudCroatian Agency for Medicinal Products and Medical Devices, Ksaverska cesta 4, HR-10 000 Zagreb, Croatia.ORCID 0000-0003-4410-3602
Zlata LasićTEVA Global R&D, E&L R&D, Pliva Hrvatska d.o.o., Prilaz baruna Filipovića 25, HR-10 000 Zagreb, Croatia.
Ilijana OdakDepartment of Chemistry, Faculty of Science and Education, University of Mostar, Matice hrvatske bb, 88 000 Mostar, Bosnia and Herzegovina.ORCID 0000-0002-6883-8470
Irena ŠkorićDepartment of Organic Chemistry, Faculty of Chemical Engineering and Technology, University of Zagreb, Trg Marka Marulića 19, HR-10 000 Zagreb, Croatia.ORCID 0000-0002-1563-7261

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In previous research, 1,2,3-triazolium salts showed significant biological activity as potential inhibitors of cholinesterase enzymes (ChEs), which are crucial for neurotransmission. In this research, pairs of uncharged thienobenzo-triazoles and their charged salts were prepared in order to further examine the role of the positive charge on the nitrogen of the triazole ring in interactions within the active site of the enzymes, and to compare the selectivity of 1,2,3-triazolium salts in relation to their uncharged analogs obtained by photochemical cyclization. Neutral thienobenzo-triazoles showed very good selective activity toward butyrylcholinesterase (BChE), while their salts showed excellent non-selective inhibition toward both BChE (the most active

Indexed as

AcetylcholinesteraseButyrylcholinesteraseCholinesterase InhibitorsMolecular Docking SimulationTriazolesCatalytic DomainHumansSaltsStructure-Activity RelationshipAcetylcholinesteraseButyrylcholinesteraseCholinesterase InhibitorsSaltsTriazoles1,2,3-triazolium saltscholinesterase inhibitiondockinggenotoxicity

Identifiers

PMID39595567
PMCPMC11591901

What Socratic holds

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LicenceCC BY
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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 Socratic graph.