The activation of phosphatidylinositol 3-kinase by Ras (Q28305326)

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R Woscholski

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B Hallberg

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P Rodriguez-Viciana

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P J Parker

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publication date

1 September 1994

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language of work or name

English

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number of pages

9

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Role of SH2-containing proteins in cellular signaling by receptor tyrosine kinases

inferred from page(s)

published in

Current Biology

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volume

4

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issue

9

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page(s)

798-806

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cites work

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New insights into protein-tyrosine kinase receptor signaling complexes

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The assembly of signalling complexes by receptor tyrosine kinases

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Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium

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Epidermal growth factor regulates the exchange rate of guanine nucleotides on p21ras in fibroblasts

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Association between the PDGF receptor and members of the src family of tyrosine kinases

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PDGF beta-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex

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Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6

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Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity

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SH2 domains recognize specific phosphopeptide sequences

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PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.

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An 81 kd protein complexed with middle T antigen and pp60c-src: a possible phosphatidylinositol kinase

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Phosphoinositide kinases

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Phosphoinositide 3-kinase: A new effector in signal transduction?

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

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Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85

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A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits

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Characterization of a phosphatidylinositol-specific phosphoinositide 3-kinase from mammalian cells

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Phospholipase C-gamma 1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal

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Mammalian phosphatidylinositol 3'-kinase induces a lethal phenotype on expression in Schizosaccharomyces pombe; comparison with the VPS34 gene product

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Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit

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Association of p21ras with phosphatidylinositol 3-kinase

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Phosphatidylinositol-3-OH kinase as a direct target of Ras

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Insulin-stimulated GLUT4 translocation is relevant to the phosphorylation of IRS-1 and the activity of PI3-kinase

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Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses.

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Purification of phosphoinositide-specific phospholipase C from a particulate fraction of bovine brain

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Activation of the β1 isozyme of phospholipase C by α subunits of the Gq class of G proteins

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Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane

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Complementation of byrl in fission yeast by mammalian MAP kinase kinase requires coexpression of Raf kinase

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Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression

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Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling

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PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase

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Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils

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Activation of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate

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High-frequency transformation method and library transducing vectors for cloning mammalian cDNAs by trans-complementation of Schizosaccharomyces pombe

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Molecular genetic analysis of fission yeast Schizosaccharomyces pombe

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cdc25+ functions as an inducer in the mitotic control of fission yeast

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

7820549

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Consolidated OpenCitations Corpus – April 2017