Evidence map›Paper›PMID 34770832›Full record

ArticleMolecules (Basel, Switzerland)2021

Icotinib, Almonertinib, and Olmutinib: A 2D Similarity/Docking-Based Study to Predict the Potential Binding Modes and Interactions into EGFR.

Faisal A Almalki, Ahmed M Shawky, Ashraf N Abdalla, Ahmed M Gouda

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. 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. Review
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

4 authors.

Faisal A AlmalkiDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, Umm Al-Qura University, Makkah 21955, Saudi Arabia.ORCID 0000-0003-4048-1526
Ahmed M ShawkyScience and Technology Unit (STU), Umm Al-Qura University, Makkah 21955, Saudi Arabia.ORCID 0000-0002-3035-661X
Ashraf N AbdallaDepartment of Pharmacology and Toxicology, Faculty of Pharmacy, Umm Al-Qura University, Makkah 21955, Saudi Arabia.ORCID 0000-0003-4770-9319
Ahmed M GoudaMedicinal Chemistry Department, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 62514, Egypt.

Funding

Deanship of Scientific Research at Umm Al-Qura University, Mekkah, KSA 19-MED-1-01-0001
6 · The paper itself

Abstract

In the current study, a 2D similarity/docking-based study was used to predict the potential binding modes of icotinib, almonertinib, and olmutinib into EGFR. The similarity search of icotinib, almonertinib, and olmutinib against a database of 154 EGFR ligands revealed the highest similarity scores with erlotinib (0.9333), osimertinib (0.9487), and WZ4003 (0.8421), respectively. In addition, the results of the docking study of the three drugs into EGFR revealed high binding free energies (Δ

Indexed as

Molecular Docking SimulationAcrylamidesBinding SitesCrown EthersErbB ReceptorsHumansIndolesLigandsMolecular StructurePiperazinesProtein Kinase InhibitorsPyrimidinesQuinazolinesAcrylamidesaumolertinibCrown EthersEGFR protein, humanErbB ReceptorsicotinibIndolesLigandsolmutinibPiperazinesProtein Kinase InhibitorsPyrimidinesQuinazolinesalmonertinibdockingicotinibolmutinibsimilarity search

Identifiers

PMID34770832
PMCPMC8588130

What OpenQuestion holds

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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 OpenQuestion graph.