|Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha.
|3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase.
|Phosphorylation and activation of p70s6k by PDK1.
|Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B.
|Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B.
|Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase.
|Regulation of protein kinase C zeta by PI 3-kinase and PDK-1.
|PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2.
|A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans.
|Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo.
|90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1.
|p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1).
|Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role in regulating kinase activity.
|Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B.
|High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site.
|Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3.
|Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates focal adhesions.
|Peroxisomal targeting as a tool for assaying protein-protein interactions in the living cell: cytokine-independent survival kinase (CISK) binds PDK-1 in vivo in a phosphorylation-dependent manner.
|PDK1, the master regulator of AGC kinase signal transduction.
|The adaptor protein Grb14 regulates the localization of 3-phosphoinositide-dependent kinase-1.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|The sequence and analysis of duplication-rich human chromosome 16.
|Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding.
|Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.
|Novel small molecule inhibitors of 3-phosphoinositide-dependent kinase-1.
|3-Phosphoinositide-dependent protein kinase-1-mediated IkappaB kinase beta (IkkB) phosphorylation activates NF-kappaB signaling.
|Regulation of transforming growth factor-beta signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein.
|Tyrosine phosphorylation of phosphoinositide-dependent kinase 1 by the insulin receptor is necessary for insulin metabolic signaling.
|Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity.
|3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins.
|Essential role of PDK1 in regulating endothelial cell migration.
|Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding.
|TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling.
|Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways.
|The C-terminus of PRK2/PKNgamma is required for optimal activation by RhoA in a GTP-dependent manner.
|IGF-I regulated phosphorylation and translocation of PDK-1 in neurons.
|The nuclear localization of 3'-phosphoinositide-dependent kinase-1 is dependent on its association with the protein tyrosine phosphatase SHP-1.
|Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
|Regulation of 3-phosphoinositide-dependent protein kinase 1 activity by homodimerization in live cells.
|Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1.
|PDK1 phosphorylation at Thr354 by murine protein serine/threonine kinase 38 contributes to the negative regulation of PDK1 activity.
|Substrate-selective inhibition of protein kinase PDK1 by small compounds that bind to the PIF-pocket allosteric docking site.
|An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.