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Structure–Activity Relationships of Inactive‐Conformation Binding EGFR Inhibitors: Linking the ATP and Allosteric Pockets

Archiv der Pharmazie(2025)10.1002/ardp.70027Source: DataRank Database

Structure–Activity Relationships of Inactive‐Conformation Binding EGFR Inhibitors: Linking the ATP and Allosteric Pockets is a research paper published in Archiv der Pharmazie (2025). On theSindex it has a DataRank of 0. It has been cited 5 times.

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Open Access5 citations

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Enrichment:Funding (15 grants)Impact (FWCI 3.76)OA: hybridTopics (45)IDs (PubMed, PMC, OpenAlex)Annotations (1)SDGs (1)

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Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (8)

Florian Wittlinger ORCID,Mareike Möllers ORCID,Tyler J. Hartman,Marcel Günther,Michael J. Eck ORCID

Live enrichment

PubMed:40665765 PMC:PMC12264581 OpenAlex:https://openalex.org/W4412487572

NIGMS NIH HHS

Grant: P30 GM124165

NIGMS NIH HHS

Grant: R35 GM155353

NCI NIH HHS

Grant: R01 CA201049

NCI NIH HHS

Grant: R35 CA242461

NCI NIH HHS

Grant: R01 CA116020

NCATS NIH HHS

Grant: UL1 TR001412

National Institutes of Health

Grant: 5R35CA242461-04

Structure, mechanism, and pharmacology of BRAF and its partners in the RAS/RAF/MAP kinase pathway

National Institutes of Health

Grant: 5R01CA116020-07

Inhibitor-sensitive and -resistant EGFR mutants from lung cancer and glioblastoma

National Institutes of Health

Grant: 3UL1TR001412-08S3

Buffalo Clinical and Translational Research Center

Deutsche Forschungsgemeinschaft

Grant: unidentified

unidentified

National Institutes of Health

Grant: 2R01CA201049-06

Discovery and optimization of novel mutant-selective allosteric inhibitors of EGFR T790M

National Institutes of Health

Grant: 1R35GM155353-01

Improving Drug Development Through Studies of Protein Kinase Inhibitors

National Institutes of Health

Grant: 3P30GM124165-03S1

NE-CAT: A Resource for Advanced Macromolecular Crystallography

National Science Foundation

Grant: 1231306

Biology with X-ray Lasers

This study is funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) (EXC2180-390900677), National Cancer Institute (R01CA201049, R01CA116020, R35CA242461), National Institute of General Medical Sciences (R35GM155353, P30GM124165), and Department of Energy (DE-AC02-06CH11357).

FWCI

3.76

Citation Percentile

0.9%

Citation Trend

2026

hybridLicense: cc-by

journalhttps://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/ardp.70027

publisherhttps://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/ardp.70027

publisherhttps://onlinelibrary.wiley.com/doi/pdf/10.1002/ardp.70027

journalhttps://doi.org/10.1002/ardp.70027

repositoryhttps://pubmed.ncbi.nlm.nih.gov/40665765

Fields of Study

Lung Cancer Treatments and MutationsCancer therapeutics and mechanismsHER2/EGFR in Cancer Research01 natural sciences0104 chemical sciences

MeSH Terms

Adenosine TriphosphateAllosteric SiteAntineoplastic AgentsCarcinoma, Non-Small-Cell LungHumansLung NeoplasmsStructure-Activity RelationshipMolecular StructureProtein Kinase InhibitorsErbB Receptors

Keywords

Allosteric regulationEpidermal growth factor receptorTyrosine kinaseChemistryKinaseBinding siteReceptor tyrosine kinaseEGFR inhibitorsEnzymeBiochemistryCancer researchStereochemistryBiologyReceptorKinase InhibitorsEpidermal Growth Factor Receptor (Egfr)Allosteric InhibitorsNon‐small Cell Lung Cancer (Nsclc)Type I½ InhibitorsErbB ReceptorsStructure-Activity RelationshipAdenosine TriphosphateLung NeoplasmsFull PaperMolecular StructureCarcinoma, Non-Small-Cell LungHumansAntineoplastic AgentsProtein Kinase InhibitorsAllosteric Site

Sustainable Development Goals

SDG 0: Good health and well-being

Structure–Activity Relationships of Inactive‐Conformation Binding EGFR Inhibitors: Linking the ATP and Allosteric Pockets

FAIR Checklist

Authors (8)

Funding (15 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)