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1 namide adenine dinucleotide synthetase and 3-phosphoinositide dependent kinase-1.
2 3,4,5-P(3)-dependent serine/threonine kinase phosphoinositide-dependent kinase 1.
3 Balpha/Akt phosphorylation and activation by phosphoinositide-dependent kinase 1.
4 also binds to the Akt kinase mTORC2, but not phosphoinositide-dependent kinase 1.
5 ess effective substrates for upstream kinase phosphoinositide-dependent kinase 1.
6 e plasma membrane where it co-localizes with phosphoinositide-dependent kinase-1.
7 and brain slices by inhibiting its upstream phosphoinositide-dependent kinase-1.
8 requires novel PKC isoform activity and not phosphoinositide-dependent kinase-1.
9 rylation of the activation T-loop of Akt1 by phosphoinositide-dependent kinase-1.
10 activity of PI3K and the phosphorylation of phosphoinositide-dependent kinase 1, Akt, and IkappaB ki
11 hosphorylation of Thr(308) and Ser(473) by 3-phosphoinositide-dependent kinase-1 and 2 (PDK1 and PDK2
12 ion of Akt and its upstream regulators PI3K, phosphoinositide-dependent kinase-1 and integrin-linked
15 e IP-10 promoter, and that the kinases PI3K, phosphoinositide-dependent kinase 1, and Akt act as inte
17 osphorylation of the Akt/PKB upstream kinase phosphoinositide-dependent kinase-1, but also its downst
19 ted similarly to S6K1 by the PI3-K effectors phosphoinositide-dependent kinase 1, Cdc42, Rac, and pro
20 By binding to the PH domains of both Akt and phosphoinositide-dependent kinase-1, D3-phosphorylated p
21 ARE disruption also results in constitutive phosphoinositide-dependent kinase 1 gain of function.
22 xtracellular signal-regulated kinase 1/2 and phosphoinositide-dependent kinase 1 in response to many
24 K (phosphatidylinositol 3-kinase) and PDK-1 (phosphoinositide-dependent kinase-1) kinases along with
27 affecting upstream kinases, such as PI3k or phosphoinositide-dependent kinase-1, or members of other
28 at the plasma membrane (PM), including the 3-phosphoinositide-dependent kinase 1 orthologs Pkh1/Pkh2
29 5 min of training, in which phosphorylated 3-phosphoinositide-dependent kinase-1 (p-PDK1) is increase
30 to be phosphorylated by its upstream kinase phosphoinositide-dependent kinase 1 (PDK-1), 2) the matu
31 protein 90 (Hsp90) from its client protein 3-phosphoinositide-dependent kinase 1 (PDK-1), a major Akt
34 the effect of OSU-03012, a celecoxib-derived phosphoinositide-dependent kinase-1 (PDK-1) inhibitor, o
35 s identified as a novel potent and selective phosphoinositide-dependent kinase-1 (PDK-1) inhibitor.
38 f Akt activation through the inhibition of 3-phosphoinositide-dependent kinase-1 (PDK-1) represents a
40 tion in PC-3 cells through the inhibition of phosphoinositide-dependent kinase-1 (PDK-1) with IC(50)
41 A critical component of this pathway is 3-phosphoinositide-dependent kinase-1 (PDK-1), a PH domain
42 Exendin-4 increased the phosphorylation of 3-phosphoinositide-dependent kinase-1 (PDK-1), AKT, and pr
44 antitumor effects through the inhibition of phosphoinositide-dependent kinase-1 (PDK-1)/Akt signalin
45 his study identifies the recently discovered phosphoinositide-dependent kinase 1, PDK-1, as a regulat
47 se of Cdc37 and concomitant association of 3-phosphoinositide dependent kinase 1 (PDK1) to activate S
49 ) via phosphatidyl inositol-3-kinase (PI3K), phosphoinositide-dependent kinase 1 (PDK1 or PDPK1), and
50 with small interfering RNA (siRNA) targeting phosphoinositide-dependent kinase 1 (PDK1) along with ci
51 tion of Thr308 in the activation loop by the phosphoinositide-dependent kinase 1 (PDK1) and Ser473 wi
52 is AGCVIIIa kinases are substrates for the 3-phosphoinositide-dependent kinase 1 (PDK1) and that tran
56 and eEF2k activity is lost in cells in which phosphoinositide-dependent kinase 1 (PDK1) has been gene
65 the carboxy-terminal kinase domain, and the phosphoinositide-dependent kinase 1 (PDK1) phosphorylate
66 In this study, we show that phosphorylated 3-phosphoinositide-dependent kinase 1 (PDK1) phosphorylate
67 serine and threonine phosphorylation by the phosphoinositide-dependent kinase 1 (PDK1) protein kinas
69 e show that c-Jun regulates transcription of phosphoinositide-dependent kinase 1 (PDK1) with a concom
71 th skeletal muscle-specific deficiency of 3'-phosphoinositide-dependent kinase 1 (PDK1), a key compon
72 the consequences of genetic manipulation of phosphoinositide-dependent kinase 1 (PDK1), a rate-limit
73 robing the phosphorylation of p90-S6 kinase, phosphoinositide-dependent kinase 1 (PDK1), and Akt.
74 dent on phosphoinositide 3-kinase (PI3K) and phosphoinositide-dependent kinase 1 (PDK1), and Dex indu
75 c1 GTPases, and the serine/threonine kinases phosphoinositide-dependent kinase 1 (PDK1), mammalian ta
76 interaction with its upstream kinase, the 3-phosphoinositide-dependent kinase 1 (PDK1), which phosph
77 an allosteric site on the Ser/Thr kinase, 3-phosphoinositide-dependent kinase 1 (PDK1)--the PDK1-int
86 of the kinase domain is phosphorylated by 3-phosphoinositide-dependent kinase-1 (PDK1) and Ser-473 i
87 e translocation and subsequent activation by phosphoinositide-dependent kinase-1 (PDK1) and the mecha
96 (PRK2)-interacting fragment (PIF) pocket of phosphoinositide-dependent kinase-1 (PDK1) was proposed
98 regulation of ROS appeared to be mediated by phosphoinositide-dependent kinase-1 (PDK1), which was hy
103 ivated protein kinase (PAK) 1 on Thr423 (the phosphoinositide-dependent kinase-1 [PDK1] site) was att
104 9-based screen and demonstrated that loss of phosphoinositide-dependent kinase-1 (PDPK1) enhances the
107 target of rapamycin/p70(S6K), independent of phosphoinositide-dependent kinase 1/PKB activation.
108 and that blockade of its upstream kinase, 3'-phosphoinositide-dependent kinase 1, potently inhibits t
109 on of Ala for a Phe of the docking motif for phosphoinositide-dependent kinase-1 prevented activation
110 e signaling components downstream of PI3K, 3-phosphoinositide-dependent kinase 1, protein kinase B (P
111 ctivation of phosphatidylinositol 3'-kinase, phosphoinositide-dependent kinase-1, protein kinase C, s
114 p is well established to be catalyzed by the phosphoinositide-dependent kinase 1, the mechanism of ph
115 weak TCR signals were sufficient to activate phosphoinositide-dependent kinase-1 to phosphorylate AKT
116 so induce conformational changes that permit phosphoinositide-dependent kinase-1 to phosphorylate the
117 n of Akt/PKB, but not its upstream activator phosphoinositide-dependent kinase-1, to the plasma membr
118 ne of the key effectors of this cascade, the phosphoinositide-dependent kinase-1, were found to be de