Evidence map›Paper›PMID 33588683›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2021

Discovery of new quinolines as potent colchicine binding site inhibitors: design, synthesis, docking studies, and anti-proliferative evaluation.

Mohamed Hagras, Moshira A El Deeb, Heba S A Elzahabi, Eslam B Elkaeed, Ahmed B M Mehany, Ibrahim H Eissa

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 72 citations in OpenAlex.

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  14. PhytoestrogenVaccines · 2023
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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

6 authors at 2 institutions in 2 countries.

Mohamed HagrasDepartment of Pharmaceutical Organic Chemistry, Faculty of Pharmacy (Boys), Al-Azhar University, Cairo, Egypt.
Moshira A El DeebDepartment of Pharmaceutical Organic Chemistry, Faculty of Pharmacy (Girls), Al-Azhar University, Cairo, Egypt.
Heba S A ElzahabiDepartment of Pharmaceutical Medicinal Chemistry & Drug Design, Faculty of Pharmacy (Girls), Al-Azhar University, Cairo, Egypt.
Eslam B ElkaeedDepartment of Pharmaceutical Organic Chemistry, Faculty of Pharmacy (Boys), Al-Azhar University, Cairo, Egypt.
Ahmed B M MehanyDepartment of Zoology, Faculty of Science, Al-Azhar University, Cairo, Egypt.
Ibrahim H EissaDepartment of Pharmaceutical Medicinal Chemistry & Drug Design, Faculty of Pharmacy (Boys), Al-Azhar University, Cairo, Egypt.
Al-Azhar University · EGAlmaarefa University

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Discovering of new anticancer agents with potential activity against tubulin polymerisation is still a promising approach. Colchicine binding site inhibitors are the most relevant anti-tubulin polymerisation agents. Thus, new quinoline derivatives have been designed and synthesised to possess the same essential pharmacophoric features of colchicine binding site inhibitors. The synthesised compounds were tested

Indexed as

Drug DiscoveryMolecular Docking SimulationAntineoplastic AgentsApoptosisBinding SitesCell CycleCell Line, TumorCell ProliferationColchicineDose-Response Relationship, DrugDrug Screening Assays, AntitumorHumansMolecular StructureQuinolinesStructure-Activity RelationshipTubulinAntineoplastic AgentsColchicineQuinolinesTubulinTubulin ModulatorsCancercolchicine binding site inhibitorsdockingquinolinetubulin polymerisation

Identifiers

PMID33588683
PMCPMC7889231
OpenAlexW3133431544

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.