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Article

Biophysical and structural characterization of the impacts of MET phosphorylation on tepotinib binding.

The Journal of biological chemistry - 1 Nov 2023

Grädler Ulrich, Schwarz Daniel, Wegener Ansgar, Eichhorn Thomas, Bandeiras Tiago M, Freitas Micael C, Lammens Alfred, Ganichkin Oleg, Augustin Martin, Minguzzi Stefano, Becker Frank, Bomke Jörg

Abstract excerpt

The receptor tyrosine kinase MET is activated by hepatocyte growth factor binding, followed by phosphorylation of the intracellular kinase domain (KD) mainly within the activation loop (A-loop) on Y1234 and Y1235. Dysregulation of MET can lead to both tumor growth and metastatic progression of cancer cells. Tepotinib is a highly selective, potent type Ib MET inhibitor and approved for treatment of non-small cell...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 37806493
DOI: 10.1016/j.jbc.2023.105328
PMCID: PMC10654029

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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