Klippel A - Search Results

1

Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells.

Kavanaugh WM, Klippel A, Escobedo JA, Williams LT. Kavanaugh WM, et al. Among authors: klippel a. Mol Cell Biol. 1992 Aug;12(8):3415-24. doi: 10.1128/mcb.12.8.3415-3424.1992. Mol Cell Biol. 1992. PMID: 1321334 Free PMC article.

2

The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor.

Klippel A, Escobedo JA, Fantl WJ, Williams LT. Klippel A, et al. Mol Cell Biol. 1992 Apr;12(4):1451-9. doi: 10.1128/mcb.12.4.1451-1459.1992. Mol Cell Biol. 1992. PMID: 1312663 Free PMC article.

3

Interactions of growth factor receptors with cytoplasmic signaling molecules.

Williams LT, Escobedo JA, Fantl WJ, Turck CW, Klippel A. Williams LT, et al. Among authors: klippel a. Cold Spring Harb Symp Quant Biol. 1991;56:243-50. doi: 10.1101/sqb.1991.056.01.030. Cold Spring Harb Symp Quant Biol. 1991. PMID: 1668083 Review.

4

Tyrosine 508 of the 85-kilodalton subunit of phosphatidylinositol 3-kinase is phosphorylated by the platelet-derived growth factor receptor.

Kavanaugh WM, Turck CW, Klippel A, Williams LT. Kavanaugh WM, et al. Among authors: klippel a. Biochemistry. 1994 Sep 13;33(36):11046-50. doi: 10.1021/bi00202a026. Biochemistry. 1994. PMID: 8086421

5

The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity.

Klippel A, Escobedo JA, Hirano M, Williams LT. Klippel A, et al. Mol Cell Biol. 1994 Apr;14(4):2675-85. doi: 10.1128/mcb.14.4.2675-2685.1994. Mol Cell Biol. 1994. PMID: 8139567 Free PMC article.

6

A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo.

Klippel A, Escobedo JA, Hu Q, Williams LT. Klippel A, et al. Mol Cell Biol. 1993 Sep;13(9):5560-6. doi: 10.1128/mcb.13.9.5560-5566.1993. Mol Cell Biol. 1993. PMID: 8395006 Free PMC article.

7

Phosphatidylinositol 3-kinase activity is important for progesterone-induced Xenopus oocyte maturation.

Muslin AJ, Klippel A, Williams LT. Muslin AJ, et al. Among authors: klippel a. Mol Cell Biol. 1993 Nov;13(11):6661-6. doi: 10.1128/mcb.13.11.6661-6666.1993. Mol Cell Biol. 1993. PMID: 8413262 Free PMC article.

8

Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways.

Klippel A, Reinhard C, Kavanaugh WM, Apell G, Escobedo MA, Williams LT. Klippel A, et al. Mol Cell Biol. 1996 Aug;16(8):4117-27. doi: 10.1128/MCB.16.8.4117. Mol Cell Biol. 1996. PMID: 8754810 Free PMC article.

9

A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through its pleckstrin homology domain.

Klippel A, Kavanaugh WM, Pot D, Williams LT. Klippel A, et al. Mol Cell Biol. 1997 Jan;17(1):338-44. doi: 10.1128/MCB.17.1.338. Mol Cell Biol. 1997. PMID: 8972214 Free PMC article.

10

SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase.

Deuter-Reinhard M, Apell G, Pot D, Klippel A, Williams LT, Kavanaugh WM. Deuter-Reinhard M, et al. Among authors: klippel a. Mol Cell Biol. 1997 May;17(5):2559-65. doi: 10.1128/MCB.17.5.2559. Mol Cell Biol. 1997. PMID: 9111325 Free PMC article.

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