PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10834940-6 2000 These effects appeared specifically related to PH domains known to bind to phosphatidylinositol 3,4-bisphosphate [PtdIns(3,4)P(2)] and phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)], indicating involvement of the PI3-K downstream target protein kinase B (PKB/Akt). phosphatidylinositol 3,4-diphosphate 75-112 protein tyrosine kinase 2 beta Homo sapiens 251-267 12822887-1 2003 Growth factor binding events to receptor tyrosine kinases result in activation of phosphatidylinositol 3-kinase (PI3K), and activated PI3K generates the membrane-bound second messengers phosphatidylinositol 3,4-diphosphate [PI(3,4)P2] and PI(3,4,5)P3, which mediate membrane translocation of the phosphoinositide-dependent kinase-1 (PDK1) and protein kinase B (PKB, also known as Akt). phosphatidylinositol 3,4-diphosphate 186-222 protein tyrosine kinase 2 beta Homo sapiens 343-359 12822887-1 2003 Growth factor binding events to receptor tyrosine kinases result in activation of phosphatidylinositol 3-kinase (PI3K), and activated PI3K generates the membrane-bound second messengers phosphatidylinositol 3,4-diphosphate [PI(3,4)P2] and PI(3,4,5)P3, which mediate membrane translocation of the phosphoinositide-dependent kinase-1 (PDK1) and protein kinase B (PKB, also known as Akt). phosphatidylinositol 3,4-diphosphate 186-222 protein tyrosine kinase 2 beta Homo sapiens 361-364 12176338-2 2002 One of the best characterized PtdIns(3,4,5)P3/PtdIns(3,4)P2 effector proteins is protein kinase B (PKB), also known as Akt. phosphatidylinositol 3,4-diphosphate 46-59 protein tyrosine kinase 2 beta Homo sapiens 81-97 12176338-2 2002 One of the best characterized PtdIns(3,4,5)P3/PtdIns(3,4)P2 effector proteins is protein kinase B (PKB), also known as Akt. phosphatidylinositol 3,4-diphosphate 46-59 protein tyrosine kinase 2 beta Homo sapiens 99-102 12176338-4 2002 Following activation of PI 3-kinase, PKB is recruited to the plasma membrane by virtue of its interaction with PtdIns(3,4,5)P3/PtdIns(3,4)P2. phosphatidylinositol 3,4-diphosphate 127-140 protein tyrosine kinase 2 beta Homo sapiens 37-40 12176338-5 2002 PKB is then activated by the 3-phosphoinositide-dependent pro-tein kinase-1 (PDK1), which like PKB, possesses a PtdIns(3,4,5)P3/PtdIns(3,4)P2 binding PH domain. phosphatidylinositol 3,4-diphosphate 128-141 protein tyrosine kinase 2 beta Homo sapiens 0-3 12176338-5 2002 PKB is then activated by the 3-phosphoinositide-dependent pro-tein kinase-1 (PDK1), which like PKB, possesses a PtdIns(3,4,5)P3/PtdIns(3,4)P2 binding PH domain. phosphatidylinositol 3,4-diphosphate 128-141 protein tyrosine kinase 2 beta Homo sapiens 95-98 12176338-8 2002 Mutagenesis of the basic residues that form ionic interactions with the D3 and D4 phosphate groups reduces or abolishes the ability of PKB to interact with PtdIns(3,4,5)P3 and PtdIns(3,4)P2. phosphatidylinositol 3,4-diphosphate 176-189 protein tyrosine kinase 2 beta Homo sapiens 135-138 12176338-9 2002 The D5 phosphate faces the solvent and forms no significant interactions with any residue on the PH domain, and this explains why PKB interacts with similar affinity with both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. phosphatidylinositol 3,4-diphosphate 196-209 protein tyrosine kinase 2 beta Homo sapiens 130-133 10834940-6 2000 These effects appeared specifically related to PH domains known to bind to phosphatidylinositol 3,4-bisphosphate [PtdIns(3,4)P(2)] and phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)], indicating involvement of the PI3-K downstream target protein kinase B (PKB/Akt). phosphatidylinositol 3,4-diphosphate 114-129 protein tyrosine kinase 2 beta Homo sapiens 251-267 10585883-0 1999 The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo. phosphatidylinositol 3,4-diphosphate 169-206 protein tyrosine kinase 2 beta Homo sapiens 35-51 10578066-3 1999 Both PI 3,4-bisphosphate and PI 3,4, 5-trisphosphate increased in H(2)O(2)-treated cells, and the elevation of these phospholipids and activation of PKB were concurrently blocked by wortmannin, a potent inhibitor of PI 3-kinase. phosphatidylinositol 3,4-diphosphate 5-24 protein tyrosine kinase 2 beta Homo sapiens 149-152 10102683-2 1999 PKB is regulated by the lipid products of phosphoinositide 3-kinase (PI 3-kinase), phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2], and phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P3]. phosphatidylinositol 3,4-diphosphate 83-120 protein tyrosine kinase 2 beta Homo sapiens 0-3 22121510-2 2012 In this pathway, PKB is recruited to the plasma membrane by direct interaction of its pleckstrin homology (PH) domain with the inositol phosphate head-group of phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P(3)] or phosphatidylinositol 3,4-bisphosphate [PtdIns(3,4)P(2)]. phosphatidylinositol 3,4-diphosphate 224-261 protein tyrosine kinase 2 beta Homo sapiens 17-20