Evidence map›Paper›PMID 36982951›Full record

ArticleInternational journal of molecular sciences2023

New Thienobenzo/Naphtho-Triazoles as Butyrylcholinesterase Inhibitors: Design, Synthesis and Computational Study.

Milena Mlakić, Ida Selec, Irena Ćaleta, Ilijana Odak, Danijela Barić, Ana Ratković, Krešimir Molčanov, Irena Škorić

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

8 authors at 4 institutions in 2 countries.

Milena MlakićDepartment of Organic Chemistry, Faculty of Chemical Engineering and Technology, University of Zagreb, Marulićev Trg 19, HR-10000 Zagreb, Croatia.
Ida SelecDepartment of Organic Chemistry, Faculty of Chemical Engineering and Technology, University of Zagreb, Marulićev Trg 19, HR-10000 Zagreb, Croatia.
Irena ĆaletaChemistry, Selvita Ltd., Prilaz Baruna Filipovića 29, HR-10000 Zagreb, Croatia.
Ilijana OdakDepartment of Chemistry, Faculty of Science and Education, University of Mostar, Matice hrvatske bb, 88000 Mostar, Bosnia and Herzegovina.ORCID 0000-0002-6883-8470
Danijela BarićGroup for Computational Life Sciences, Division of Physical Chemistry, Ruđer Bošković Institute, Bijenička Cesta 54, HR-10000 Zagreb, Croatia.ORCID 0000-0002-5614-5167
Ana RatkovićChemistry, Selvita Ltd., Prilaz Baruna Filipovića 29, HR-10000 Zagreb, Croatia.
Krešimir MolčanovDivision of Physical Chemistry, Ruđer Bošković Institute, Bijenička Cesta 54, HR-10000 Zagreb, Croatia.ORCID 0000-0002-4328-3181
Irena ŠkorićDepartment of Organic Chemistry, Faculty of Chemical Engineering and Technology, University of Zagreb, Marulićev Trg 19, HR-10000 Zagreb, Croatia.ORCID 0000-0002-1563-7261
University of Zagreb · HRPliva (Croatia) · HRRuđer Bošković Institute · HRUniversity of Mostar · BA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study aims to test the inhibition potency of new thienobenzo/naphtho-triazoles toward cholinesterases, evaluate their inhibition selectivity, and interpret the obtained results by molecular modeling. The synthesis of 19 new thienobenzo/naphtho-triazoles by two different approaches resulted in a large group of molecules with different functionalities in the structure. As predicted, most prepared molecules show better inhibition of the enzyme butyrylcholinesterase (BChE), considering that the new molecules were designed according to the previous results. Interestingly, the binding affinity of BChE for even seven new compounds (

Indexed as

ButyrylcholinesteraseCholinesterase InhibitorsAcetylcholinesteraseMolecular Docking SimulationStructure-Activity RelationshipTriazolesAcetylcholinesteraseButyrylcholinesteraseCholinesterase InhibitorsTriazoles1,2,3-triazolescholinesterasesinhibitionphotochemistrysynthesis

Identifiers

PMID36982951
PMCPMC10059756
OpenAlexW4327952750

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.