Structural insights into Met receptor activation

Niemann H (2011)
European Journal of Cell Biology 90(11): 972-981.

Journal Article | Published | English

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Abstract
The receptor tyrosine kinase Met plays a pivotal role in vertebrate development and tissue regeneration, its deregulation contributes to cancer. Met is also targeted during the infection by the facultative intracellular bacterium Listeria monocytogenes. The mechanistic basis for Met activation by its natural ligand hepatocyte growth factor/scatter factor (HGF/SF) is only beginning to be understood at a structural level. Crystal structures of Met in complex with L. monocytogenes InlB suggest that Met dimerization by this bacterial invasion protein is mediated by a dimer contact of the ligand. Here, I review the structural basis of Met activation by InlB and highlight parallels and differences to the physiological Met ligand HGF/SF and its splice variant NK1.
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Niemann H. Structural insights into Met receptor activation. European Journal of Cell Biology. 2011;90(11):972-981.
Niemann, H. (2011). Structural insights into Met receptor activation. European Journal of Cell Biology, 90(11), 972-981.
Niemann, H. (2011). Structural insights into Met receptor activation. European Journal of Cell Biology 90, 972-981.
Niemann, H., 2011. Structural insights into Met receptor activation. European Journal of Cell Biology, 90(11), p 972-981.
H. Niemann, “Structural insights into Met receptor activation”, European Journal of Cell Biology, vol. 90, 2011, pp. 972-981.
Niemann, H.: Structural insights into Met receptor activation. European Journal of Cell Biology. 90, 972-981 (2011).
Niemann, Hartmut. “Structural insights into Met receptor activation”. European Journal of Cell Biology 90.11 (2011): 972-981.
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15 Citations in Europe PMC

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Aprile G, Giampieri R, Bonotto M, Bittoni A, Ongaro E, Cardellino GG, Graziano F, Giuliani F, Fasola G, Cascinu S, Scartozzi M., Expert Opin Investig Drugs 23(7), 2014
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Crystal structure of an engineered YopM-InlB hybrid protein.
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Clinical impact of the HGF/MET pathway activation in patients with advanced gastric cancer treated with palliative chemotherapy.
Graziano F, Catalano V, Lorenzini P, Giacomini E, Sarti D, Fiorentini G, De Nictolis M, Magnani M, Ruzzo A., Pharmacogenomics J. 14(5), 2014
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Merchant M, Ma X, Maun HR, Zheng Z, Peng J, Romero M, Huang A, Yang NY, Nishimura M, Greve J, Santell L, Zhang YW, Su Y, Kaufman DW, Billeci KL, Mai E, Moffat B, Lim A, Duenas ET, Phillips HS, Xiang H, Young JC, Vande Woude GF, Dennis MS, Reilly DE, Schwall RH, Starovasnik MA, Lazarus RA, Yansura DG., Proc. Natl. Acad. Sci. U.S.A. 110(32), 2013
PMID: 23882082
Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells.
Dietz MS, Haße D, Ferraris DM, Gohler A, Niemann HH, Heilemann M., BMC Biophys 6(1), 2013
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Lipopolysaccharide-induced phosphorylation of c-Met tyrosine residue 1003 regulates c-Met intracellular trafficking and lung epithelial barrier function.
Zhao Y, Zhao J, Mialki RK, Wei J, Spannhake EW, Salgia R, Natarajan V., Am. J. Physiol. Lung Cell Mol. Physiol. 305(1), 2013
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Decorin: a guardian from the matrix.
Neill T, Schaefer L, Iozzo RV., Am. J. Pathol. 181(2), 2012
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Smith EJ, Corrigan RM, van der Sluis T, Grundling A, Speziale P, Geoghegan JA, Foster TJ., Mol. Microbiol. 83(4), 2012
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