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Journal Abstract Search

240 related items for PubMed ID: 1379698

  • 1. Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis.
    Mohammadi M, Dionne CA, Li W, Li N, Spivak T, Honegger AM, Jaye M, Schlessinger J.
    Nature; 1992 Aug 20; 358(6388):681-4. PubMed ID: 1379698
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  • 2. Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis.
    Peters KG, Marie J, Wilson E, Ives HE, Escobedo J, Del Rosario M, Mirda D, Williams LT.
    Nature; 1992 Aug 20; 358(6388):678-81. PubMed ID: 1379697
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  • 7. Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites.
    Cunningham SA, Arrate MP, Brock TA, Waxham MN.
    Biochem Biophys Res Commun; 1997 Nov 26; 240(3):635-9. PubMed ID: 9398617
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  • 8. Platelet-activating factor stimulation of tyrosine kinase and its relationship to phospholipase C in rabbit platelets: studies with genistein and monoclonal antibody to phosphotyrosine.
    Dhar A, Paul AK, Shukla SD.
    Mol Pharmacol; 1990 Apr 26; 37(4):519-25. PubMed ID: 1691437
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  • 9. FGF-2 facilitates binding of SH3 domain of PLC-gamma1 to vinculin and SH2 domains to FGF receptor in corneal endothelial cells.
    Park SY, Barron E, Suh PG, Ryu SH, Kay EP.
    Mol Vis; 1999 Aug 20; 5():18. PubMed ID: 10459043
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  • 10. Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase.
    Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, Waterfield MD, Campbell ID.
    Nature; 1992 Aug 20; 358(6388):684-7. PubMed ID: 1323062
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  • 11. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1.
    Mohammadi M, Honegger AM, Rotin D, Fischer R, Bellot F, Li W, Dionne CA, Jaye M, Rubinstein M, Schlessinger J.
    Mol Cell Biol; 1991 Oct 20; 11(10):5068-78. PubMed ID: 1656221
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  • 12. Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor beta subunit and are required for binding of phospholipase C gamma and a 64-kilodalton protein, respectively.
    Valius M, Bazenet C, Kazlauskas A.
    Mol Cell Biol; 1993 Jan 20; 13(1):133-43. PubMed ID: 7678051
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  • 16. Protein kinase C inhibits epidermal growth factor-dependent tyrosine phosphorylation of phospholipase C gamma and activation of phosphoinositide hydrolysis.
    Huckle WR, Hepler JR, Rhee SG, Harden TK, Earp HS.
    Endocrinology; 1990 Oct 20; 127(4):1697-705. PubMed ID: 1698145
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  • 17. PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.
    Kim HK, Kim JW, Zilberstein A, Margolis B, Kim JG, Schlessinger J, Rhee SG.
    Cell; 1991 May 03; 65(3):435-41. PubMed ID: 1708307
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  • 18. Demonstration of functionally different interactions between phospholipase C-gamma and the two types of platelet-derived growth factor receptors.
    Eriksson A, Nånberg E, Rönnstrand L, Engström U, Hellman U, Rupp E, Carpenter G, Heldin CH, Claesson-Welsh L.
    J Biol Chem; 1995 Mar 31; 270(13):7773-81. PubMed ID: 7535778
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  • 19. Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase.
    Pleiman CM, Clark MR, Gauen LK, Winitz S, Coggeshall KM, Johnson GL, Shaw AS, Cambier JC.
    Mol Cell Biol; 1993 Sep 31; 13(9):5877-87. PubMed ID: 8395016
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  • 20. Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex.
    Morrison DK, Kaplan DR, Rhee SG, Williams LT.
    Mol Cell Biol; 1990 May 31; 10(5):2359-66. PubMed ID: 1691440
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