Evidence map›Paper›PMID 36373202›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2023

Structure-activity exploration of a small-molecule allosteric inhibitor of T790M/L858R double mutant EGFR.

Francesca Foschi, Annachiara Tinivella, Valentina Crippa, Luca Pinzi, Luca Mologni, Daniele Passarella, Giulio Rastelli

Abstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Synthesis,Current medicinal chemistry · 2024
    Article
  3. Strategy toward Kinase-Selective Drug Discovery.Journal of chemical theory and computation · 2023
    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

7 authors.

Francesca FoschiDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Annachiara TinivellaDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Valentina CrippaSchool of Medicine and Surgery, University of Milano-Bicocca, Monza, Italy.
Luca PinziDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Luca MologniSchool of Medicine and Surgery, University of Milano-Bicocca, Monza, Italy.
Daniele PassarellaDepartment of Chemistry, University of Milano, Milano, Italy.
Giulio RastelliDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EGFR is a protein kinase whose aberrant activity is frequently involved in the development of non-small lung cancer (NSCLC) drug resistant forms. The allosteric inhibition of this enzyme is currently one among the most attractive approaches to design and develop anticancer drugs. In a previous study, we reported the identification of a hit compound acting as type III allosteric inhibitor of the L858R/T790M double mutant EGFR. Herein, we report the design, synthesis and

Indexed as

Antineoplastic AgentsCarcinoma, Non-Small-Cell LungLung NeoplasmsCell Line, TumorDrug Resistance, NeoplasmErbB ReceptorsHumansMutationProtein Kinase InhibitorsStructure-Activity RelationshipAntineoplastic AgentsEGFR protein, humanErbB ReceptorsProtein Kinase Inhibitorsallosteric inhibitorsanticancer drugsdrug designEGFR inhibitors

Identifiers

PMID36373202
PMCPMC9665079

What OpenQuestion holds

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LicenceCC BY
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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.