A Peptide Representing the Carboxyl-terminal Tail of the Met Receptor Inhibits Kinase Activity and Invasive Growth (Q57281072)

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31 October 2019

title

A peptide representing the carboxyl-terminal tail of the met receptor inhibits kinase activity and invasive growth (English)

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31 October 2019

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31 October 2019

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31 October 2019

P Longati

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31 October 2019

T A Williams

series ordinal

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31 October 2019

S Benvenuti

series ordinal

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31 October 2019

language of work or name

English

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publication date

1 October 1999

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Journal of Biological Chemistry

31 October 2019

published in

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31 October 2019

volume

274

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31 October 2019

issue

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page(s)

29274-29281

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Identification of the Hepatocyte Growth Factor Receptor As the c- met Proto-Oncogene Product

31 October 2019

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Identification of a fibroblast-derived epithelial morphogen as hepatocyte growth factor

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Purification and characterization of a growth factor from rat platelets for mature parenchymal hepatocytes in primary cultures

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Essential role for the c-met receptor in the migration of myogenic precursor cells into the limb bud

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Germline and somatic mutations in the tyrosine kinase domain of the MET proto-oncogene in papillary renal carcinomas

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Invasiveness and metastasis of NIH 3T3 cells induced by Met-hepatocyte growth factor/scatter factor autocrine stimulation

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A point mutation in the MET oncogene abrogates metastasis without affecting transformation.

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The tyrosine kinase encoded by the MET proto-oncogene is activated by autophosphorylation

21 January 2018

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A novel recognition motif for phosphatidylinositol 3-kinase binding mediates its association with the hepatocyte growth factor/scatter factor receptor

21 January 2018

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A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family

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Induction of epithelial tubules by growth factor HGF depends on the STAT pathway

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Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis

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Gab1 coupling to the HGF/Met receptor multifunctional docking site requires binding of Grb2 and correlates with the transforming potential.

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Specific uncoupling of GRB2 from the Met receptor. Differential effects on transformation and motility

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Mutation of juxtamembrane tyrosine residue 1001 suppresses loss-of-function mutations of the met receptor in epithelial cells.

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.41.29274

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10506185%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

1 reference

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