Evidence map›Paper›PMID 35164092›Full record

ReviewMolecules (Basel, Switzerland)2022

Structural Insight and Development of EGFR Tyrosine Kinase Inhibitors.

Tasia Amelia, Rahmana Emran Kartasasmita, Tomohiko Ohwada, Daryono Hadi Tjahjono

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
16.0field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Ferulic andRSC advances · 2026
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Synthesis,RSC advances · 2025
    Article
  15. Article
  16. Article
  17. Design, synthesis, anti-breast cancer andFuture medicinal chemistry · 2025
    Article
  18. Article
  19. Multidrug Resistance: Are We Still Afraid of the Big Bad Wolf.Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  20. 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

4 authors at 2 institutions in 2 countries.

Tasia AmeliaSchool of Pharmacy, Bandung Institute of Technology, Jalan Ganesha 10, Bandung 40132, Indonesia.ORCID 0000-0002-7414-9428
Rahmana Emran KartasasmitaSchool of Pharmacy, Bandung Institute of Technology, Jalan Ganesha 10, Bandung 40132, Indonesia.
Tomohiko OhwadaGraduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.ORCID 0000-0001-5390-0203
Daryono Hadi TjahjonoSchool of Pharmacy, Bandung Institute of Technology, Jalan Ganesha 10, Bandung 40132, Indonesia.ORCID 0000-0002-9675-0134
Bandung Institute of Technology · IDThe University of Tokyo · JP

Funding

P3MI 2020-Bandung Institute of Technology 014/SK/I1.C03/2020
6 · The paper itself

Abstract

Lung cancer has a high prevalence, with a growing number of new cases and mortality every year. Furthermore, the survival rate of patients with non-small-cell lung carcinoma (NSCLC) is still quite low in the majority of cases. Despite the use of conventional therapy such as tyrosine kinase inhibitor for Epidermal Growth Factor Receptor (EGFR), which is highly expressed in most NSCLC cases, there was still no substantial improvement in patient survival. This is due to the drug's ineffectiveness and high rate of resistance among individuals with mutant EGFR. Therefore, the development of new inhibitors is urgently needed. Understanding the EGFR structure, including its kinase domain and other parts of the protein, and its activation mechanism can accelerate the discovery of novel compounds targeting this protein. This study described the structure of the extracellular, transmembrane, and intracellular domains of EGFR. This was carried out along with identifying the binding pose of commercially available inhibitors in the ATP-binding and allosteric sites, thereby clarifying the research gaps that can be filled. The binding mechanism of inhibitors that have been used clinically was also explained, thereby aiding the structure-based development of new drugs.

Indexed as

AnimalsCarcinoma, Non-Small-Cell LungDrug DesignDrug DiscoveryErbB ReceptorsHumansLung NeoplasmsModels, MolecularProtein ConformationProtein Kinase InhibitorsEGFR protein, humanErbB ReceptorsProtein Kinase InhibitorsactivationbindingEGFRinhibitorkinase

Identifiers

PMID35164092
PMCPMC8838133
OpenAlexW4210716527

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.