BMC Biophys 2013 Jun 3;6(1). Epub 2013 Jun 3.
Institute of Physical and Theoretical Chemistry, Johann Wolfgang Goethe-University, Max-von-Laue-Str, 7, 60438 Frankfurt, Germany.
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Biochim Biophys Acta 2013 Oct 31;1834(10):2195-204. Epub 2012 Oct 31.
Department of Chemistry and Center for Biotechnology (CeBiTec), Bielefeld University, 33501 Bielefeld, Germany. Electronic address:
The structural basis of ligand-induced dimerization of the receptor tyrosine kinase MET by its natural ligand hepatocyte growth factor/scatter factor (HGF/SF) is not well understood. However, interesting insight into the molecular mechanism of MET dimerization has emerged from crystal structures of MET in complex with a bacterial agonist, the invasion protein internalin B (InlB) from pathogenic Listeria monocytogenes. MET activation by InlB promotes uptake of bacteria into host cells. Read More
Biochim Biophys Acta 2016 Jul 17;1863(7 Pt A):1552-8. Epub 2016 Apr 17.
Karlsruhe Institute of Technology (KIT), Institute of Toxicology and Genetics (ITG), Postfach 3640, 76021 Karlsruhe, Germany. Electronic address:
The canonical model of receptor tyrosine kinase (RTK) activation assumes that ligand-induced dimerization of inactive receptor monomers is a prerequisite for autophosphorylation. For several RTK families, recent results of fluorescence microscopy provided evidence for preformed receptor dimers that may or may not require ligand binding for kinase activity. Here we report, for the first time, the application of advanced quantitative fluorescence microscopy techniques to study changes in the oligomerization state of the RTK Met in response to stimulation by its endogenous ligand hepatocyte growth factor (HGF). Read More
FEBS Open Bio 2017 09 29;7(9):1422-1440. Epub 2017 Aug 29.
Institute of Physical and Theoretical Chemistry Johann Wolfgang Goethe-University Frankfurt Germany.
The human MET receptor tyrosine kinase contributes to vertebrate development and cell proliferation. As a proto-oncogene, it is a target in cancer therapies. MET is also relevant for bacterial infection by and is activated by the bacterial protein internalin B. Read More
J Biol Chem 2009 Jan 6;284(2):774-83. Epub 2008 Nov 6.
Department of Neuroscience and Cell Biology, Sealy Center for Cancer Cell Biology, University of Texas Medical Branch, Galveston, Texas 77555-1074, USA.
Entry of the bacterial pathogen Listeria monocytogenes into host epithelial cells is critical for infection and virulence. One major pathway for Listeria entry involves binding of the bacterial protein Internalin B to the host receptor tyrosine kinase Met (hepatocyte growth factor receptor). Activation of Met and downstream signaling cascades is critical for Listeria entry. Read More