Evidence map›Paper›PMID 38693732›Full record

ArticleCurrent medicinal chemistry2024

Synthesis,

Wurood A Shihab, Ammar A Razzak Kubba, Lubna H Tahtamouni, Khaled M Saleh, Mai F AlSakhen, Sana I Kanaan, Abdulrahman M Saleh, Salem R Yasin

Abstract read
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Article in Current medicinal chemistry, 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
2.5field-weighted citation impact, top 11% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  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

8 authors at 2 institutions in 4 countries.

Wurood A ShihabDepartment of Pharmaceutical Chemistry, College of Pharmacy, University of Baghdad, Bab-Al-Mouadam, Baghdad, 10001, Iraq.
Ammar A Razzak KubbaDepartment of Pharmaceutical Chemistry, College of Pharmacy, University of Baghdad, Bab-Al-Mouadam, Baghdad, 10001, Iraq.
Lubna H TahtamouniDepartment of Biology and Biotechnology, Faculty of Science, The Hashemite University, Zarqa, Jordan.
Khaled M SalehDepartment of Biology and Biotechnology, Faculty of Science, The Hashemite University, Zarqa, Jordan.
Mai F AlSakhenDepartment of Biology and Biotechnology, Faculty of Science, The Hashemite University, Zarqa, Jordan.
Sana I KanaanDepartment of Biology and Biotechnology, Faculty of Science, The Hashemite University, Zarqa, Jordan.
Abdulrahman M SalehPharmaceutical Medicinal Chemistry & Drug Design Department, Faculty of Pharmacy (Boys), Al-Azhar University, Cairo, 11884, Egypt.
Salem R YasinDepartment of Biology and Biotechnology, Faculty of Science, The Hashemite University, Zarqa, Jordan.
Hashemite University · JOUniversity of Baghdad · IQ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionAllosteric inhibition of EGFR tyrosine kinase (TK) is currently among the most attractive approaches for designing and developing anti-cancer drugs to avoid chemoresistance exhibited by clinically approved ATP-competitive inhibitors. The current work aimed to synthesize new biphenyl-containing derivatives that were predicted to act as EGFR TK allosteric site inhibitors based on molecular docking studies.

methodsA new series of 4'-hydroxybiphenyl-4-carboxylic acid derivatives, including hydrazine-1-carbothioamide (S3-S6) and 1,2,4-triazole (S7-S10) derivatives, were synthesized and characterized using IR,

resultsCompound S4 had a relatively high pharmacophore-fit score, indicating that it may have biological activity similar to the EGFR allosteric inhibitor reference, and it scored a relatively low ΔG against EGFR TK allosteric site, indicating a high likelihood of drug-receptor complex formation. Compound S4 was cytotoxic to the three cancer cell lines tested, particularly HCT-116 colorectal cancer cells, with an IC

conclusionCompound S4 is a promising EGFR tyrosine kinase allosteric inhibitor that warrants further research.

Indexed as

Allosteric SiteAntineoplastic AgentsDrug Screening Assays, AntitumorErbB ReceptorsMolecular Docking SimulationProtein Kinase InhibitorsApoptosisBiphenyl CompoundsCarboxylic AcidsCell Line, TumorCell ProliferationHumansMolecular StructureStructure-Activity RelationshipAntineoplastic AgentsBiphenyl CompoundsCarboxylic AcidsEGFR protein, humanErbB ReceptorsProtein Kinase Inhibitorsallosteric site inhibitorsBiphenyl scaffoldcytotoxicityEGFR tyrosine kinasemolecular dockingQSAR.

Identifiers

PMID38693732
OpenAlexW4396591147

What OpenQuestion holds

Textmetadata
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.