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The EMBO Journal, ISSN 0261-4189, 03/2006, Volume 25, Issue 5, pp. 1024 - 1034
The virulence factor IpgD, delivered into nonphagocytic cells by the type III secretion system of the pathogen Shigella flexneri, is a phosphoinositide... 
S. flexneri infection | PtdInsP | Akt | PI 3‐kinase | survival | PI 3-kinase | Survival | CYTOSKELETON | BIOCHEMISTRY & MOLECULAR BIOLOGY | SALMONELLA | PHOSPHOINOSITIDE | MAMMALIAN-CELLS | INSULIN SENSITIVITY | PHOSPHATIDYLINOSITOL 5-PHOSPHATE | CELL BIOLOGY | BACTERIAL PATHOGENS | EPITHELIAL-CELLS | HELA-CELLS | SIGNALING PATHWAY | Phosphates | Pathogens | Bacteria | Infections | Cells
Journal Article
FEBS LETTERS, ISSN 0014-5793, 02/2005, Volume 579, Issue 5, pp. 1301 - 1305
We previously reported that hypertrophy of vascular smooth muscle cells caused by prostaglandin (PG) F-2alpha is mediated by the induction of NOX1, a catalytic... 
TRANSFORMATION | SIGNALING PATHWAYS | ACTIVATION | epidermal growth factor receptor | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANGIOTENSIN-II | PROLIFERATION | CELL BIOLOGY | HYPERTROPHY | NAD(P)H OXIDASE | BIOPHYSICS | prostaglandin F-2 alpha | NADPH oxidase | EPIDERMAL-GROWTH-FACTOR | SMOOTH-MUSCLE-CELLS | EXPRESSION | NOX1 | phosphoinositide 3 kinase
Journal Article
FEBS Letters, ISSN 0014-5793, 02/2005, Volume 579, Issue 5, pp. 1301 - 1305
We previously reported that hypertrophy of vascular smooth muscle cells caused by prostaglandin (PG) F is mediated by the induction of NOX1, a catalytic... 
NADPH oxidase | NOX1 | Epidermal growth factor receptor | Phosphoinositide 3 kinase | Prostaglandin F2α | prostaglandin | EGF | MAPK | mitogen-activated protein kinase | MMP | MEK | MAPK/ERK kinase | PG | matrix metalloproteinase | phosphoinositide 3 | PI3 | epidermal growth factor | extracellular signal-regulated protein kinase | ERK | Prostaglandin F | Receptor, Epidermal Growth Factor - genetics | Up-Regulation | Transcriptional Activation - drug effects | Phosphatidylinositol 3-Kinases - metabolism | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | RNA, Messenger - metabolism | Protein Subunits - metabolism | DNA-Binding Proteins - metabolism | Mitogen-Activated Protein Kinase Kinases - metabolism | Receptor, Epidermal Growth Factor - metabolism | Catalysis | Phosphorylation - drug effects | NADH, NADPH Oxidoreductases - metabolism | Dinoprost - pharmacology | Protein Subunits - genetics | Cell Line | NADH, NADPH Oxidoreductases - genetics | Signal Transduction | RNA, Messenger - genetics | Mitogen-Activated Protein Kinase Kinases - antagonists & inhibitors | Rats | NADPH Oxidase 1 | Transcription Factors - metabolism | Animals | Mitogen-Activated Protein Kinase 3 - metabolism | Activating Transcription Factor 1 | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Protein Kinase Inhibitors - pharmacology | Matrix Metalloproteinases - metabolism | Mitogen-Activated Protein Kinase 1 - metabolism | Oxidases | Prostaglandins | Superoxide | Epidermal growth factor | Wind-pressure | Protein kinases
Journal Article
Journal Article
Journal of Neurochemistry, ISSN 0022-3042, 07/2008, Volume 106, Issue 1, pp. 134 - 146
Axl is a receptor tyrosine kinase implicated in cell survival following growth factor withdrawal and other stressors. The binding of Axl’s ligand, growth... 
growth arrest‐specific protein 6 | Akt signaling | oligodendrocytes | growth factor receptor‐bound protein 2 | Axl receptor tyrosine kinase | p85 subunit of phosphatidylinositol‐3 kinase | Growth factor receptor-bound protein 2 | p85 subunit of phosphatidylinositol-3 kinase | Growth arrest-specific protein 6 | Oligodendrocytes | PROTEIN | PHOSPHATIDYLINOSITOL 3-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | p85 subunit of phosphatidylinositol-3-kinase | DISTINCT ROLES | PHOSPHOINOSITIDE 3-KINASE | NEUROSCIENCES | MONOCLONAL-ANTIBODIES O1 | growth factor receptor-bound protein 2 | SIGNAL-TRANSDUCTION | GENE 6 | CENTRAL-NERVOUS-SYSTEM | growth arrest-specific protein 6 | GROWTH-FACTOR | RECEPTOR TYROSINE KINASE | Oncogene Proteins - genetics | Phosphorylation | Humans | Cercopithecus aethiops | Phosphatidylinositol 3-Kinases - metabolism | Protein Subunits - metabolism | Proto-Oncogene Proteins c-akt - genetics | Brain - metabolism | GRB2 Adaptor Protein - genetics | Binding Sites - physiology | Proto-Oncogene Proteins | Proto-Oncogene Proteins c-akt - metabolism | Binding, Competitive - physiology | Mutagenesis, Site-Directed | Oncogene Proteins - metabolism | Binding Sites - genetics | Receptor Protein-Tyrosine Kinases - metabolism | Phosphatidylinositol 3-Kinases - genetics | Animals | Receptor Protein-Tyrosine Kinases - genetics | Binding, Competitive - genetics | Signal Transduction - physiology | Mice | GRB2 Adaptor Protein - metabolism | COS Cells | Enzyme Activation - physiology | Protein Binding - physiology | Protein Structure, Tertiary - physiology | Protein binding | Neurology | Brain | Signal transduction | Cellular biology | Mutagenesis | Biochemistry | Mutation | Index Medicus
Journal Article
Journal Article
Journal Article
Bioscience Reports, ISSN 0144-8463, 02/2015, Volume 35, Issue 2, pp. 1 - 14
Journal Article