The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity (Q24290364)

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English	The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity	scientific article

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The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity (English)

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Multiple PDZ domain crumbs cell polarity complex component

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GOA release 2020-03-11

author name string

A Mancini

1

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A Koch

2

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M Stefan

3

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H Niemann

4

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T Tamura

5

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language of work or name

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publication date

29 September 2000

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482

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54-8

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1-2

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The biology of stem cell factor and its receptor C-kit

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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains

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Identification of a point mutation in the catalytic domain of the protooncogene c-kit in peripheral blood mononuclear cells of patients who have mastocytosis with an associated hematologic disorder

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GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors

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Homer: a protein that selectively binds metabotropic glutamate receptors

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Cloning and characterization of MUPP1, a novel PDZ domain protein

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PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands

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PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor

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Identification, sequence, and mapping of the mouse multiple PDZ domain protein gene, Mpdz.

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Mammalian Ras interacts directly with the serine/threonine kinase Raf

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A point mutation at tyrosine-809 in the human colony-stimulating factor 1 receptor impairs mitogenesis without abrogating tyrosine kinase activity, association with phosphatidylinositol 3-kinase, or induction of c-fos and junB genes

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10.1016/S0014-5793(00)02036-6

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