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Matches in Nanopublications for { ?s ?p "A large number of SH2 domain proteins have been shown to bind to PDGF alpha - and beta -receptors (Table 4). Some of these molecules are themselves enzymes, such as phosphatidylinositol 3'-kinase (PI 3-kinase), phospholipase C (PLC)-gamma , the Src family of tyrosine kinases, the tyrosine phosphatase SHP-2, and a GTPase activating protein (GAP) for Ras. Other molecules such as Grb2, Grb7, Nck, Shc, and Crk are devoid of enzymatic activity and have adaptor functions, linking the receptor with downstream catalytic molecules. Also, members of the Stat family bind to the PDGF receptors. They are transcription factors that after phosphorylation on tyrosine dimerize and translocate into the nucleus where they affect the transcription of specific genes. Each SH2 domain molecule that binds to the PDGF receptors initiates a signal transduction pathway. The more important and well-characterized signaling pathways activated by PDGF receptors are described below. For a more comprehensive discussion, see Reference 182." ?g. }

• _8 value "A large number of SH2 domain proteins have been shown to bind to PDGF alpha - and beta -receptors (Table 4). Some of these molecules are themselves enzymes, such as phosphatidylinositol 3'-kinase (PI 3-kinase), phospholipase C (PLC)-gamma , the Src family of tyrosine kinases, the tyrosine phosphatase SHP-2, and a GTPase activating protein (GAP) for Ras. Other molecules such as Grb2, Grb7, Nck, Shc, and Crk are devoid of enzymatic activity and have adaptor functions, linking the receptor with downstream catalytic molecules. Also, members of the Stat family bind to the PDGF receptors. They are transcription factors that after phosphorylation on tyrosine dimerize and translocate into the nucleus where they affect the transcription of specific genes. Each SH2 domain molecule that binds to the PDGF receptors initiates a signal transduction pathway. The more important and well-characterized signaling pathways activated by PDGF receptors are described below. For a more comprehensive discussion, see Reference 182." provenance.
• _8 value "A large number of SH2 domain proteins have been shown to bind to PDGF alpha - and beta -receptors (Table 4). Some of these molecules are themselves enzymes, such as phosphatidylinositol 3'-kinase (PI 3-kinase), phospholipase C (PLC)-gamma , the Src family of tyrosine kinases, the tyrosine phosphatase SHP-2, and a GTPase activating protein (GAP) for Ras. Other molecules such as Grb2, Grb7, Nck, Shc, and Crk are devoid of enzymatic activity and have adaptor functions, linking the receptor with downstream catalytic molecules. Also, members of the Stat family bind to the PDGF receptors. They are transcription factors that after phosphorylation on tyrosine dimerize and translocate into the nucleus where they affect the transcription of specific genes. Each SH2 domain molecule that binds to the PDGF receptors initiates a signal transduction pathway. The more important and well-characterized signaling pathways activated by PDGF receptors are described below. For a more comprehensive discussion, see Reference 182." provenance.
• _8 value "A large number of SH2 domain proteins have been shown to bind to PDGF alpha - and beta -receptors (Table 4). Some of these molecules are themselves enzymes, such as phosphatidylinositol 3'-kinase (PI 3-kinase), phospholipase C (PLC)-gamma , the Src family of tyrosine kinases, the tyrosine phosphatase SHP-2, and a GTPase activating protein (GAP) for Ras. Other molecules such as Grb2, Grb7, Nck, Shc, and Crk are devoid of enzymatic activity and have adaptor functions, linking the receptor with downstream catalytic molecules. Also, members of the Stat family bind to the PDGF receptors. They are transcription factors that after phosphorylation on tyrosine dimerize and translocate into the nucleus where they affect the transcription of specific genes. Each SH2 domain molecule that binds to the PDGF receptors initiates a signal transduction pathway. The more important and well-characterized signaling pathways activated by PDGF receptors are described below. For a more comprehensive discussion, see Reference 182." provenance.
• _8 value "A large number of SH2 domain proteins have been shown to bind to PDGF alpha - and beta -receptors (Table 4). Some of these molecules are themselves enzymes, such as phosphatidylinositol 3'-kinase (PI 3-kinase), phospholipase C (PLC)-gamma , the Src family of tyrosine kinases, the tyrosine phosphatase SHP-2, and a GTPase activating protein (GAP) for Ras. Other molecules such as Grb2, Grb7, Nck, Shc, and Crk are devoid of enzymatic activity and have adaptor functions, linking the receptor with downstream catalytic molecules. Also, members of the Stat family bind to the PDGF receptors. They are transcription factors that after phosphorylation on tyrosine dimerize and translocate into the nucleus where they affect the transcription of specific genes. Each SH2 domain molecule that binds to the PDGF receptors initiates a signal transduction pathway. The more important and well-characterized signaling pathways activated by PDGF receptors are described below. For a more comprehensive discussion, see Reference 182." provenance.