The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit (Q28287741)

4

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author name string

B H Jhun

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B Rivnay

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D Price

Journal of Biological Chemistry

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language of work or name

English

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publication date

21 April 1995

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published in

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volume

270

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issue

16

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page(s)

9661-6

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cites work

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SH2 domains recognize specific phosphopeptide sequences

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Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach

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A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine

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Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways

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Purification and characterization of a phosphatidylinositol 3-kinase complex from bovine brain by using phosphopeptide affinity columns

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Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme family

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Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product

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The when and how of Src regulation

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Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src

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In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase

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SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors

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Association of Hematopoietic Cell Phosphatase with c-Kit After Stimulation with c-Kit Ligand

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Tec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor binding

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