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1 This elevation depended on activation of p90 ribosomal S6 kinase.
2 ttenuated TPA-induced phosphorylation of ERK/p90 ribosomal S6 kinase.
3 so sufficient to activate both NF-kappaB and p90 ribosomal S6 kinase.
4 eviously we showed that the inactive form of p90 ribosomal S6 kinase 1 (RSK1) interacts with the regu
7 in cultured cells, interacts with mammalian p90 ribosomal S6 kinase 1 (RSK1), and causes a decrease
9 ERK1/2, and its dependent protein, p90RSK-1 (p90 ribosomal S6 kinase 1 or RSK-1), was abolished by me
13 covered a novel regulatory mechanism whereby p90 ribosomal S6 kinase 2 (RSK2) interacts with 5-hydrox
16 ly, we discovered that the ERK/MAPK effector p90 ribosomal S6 kinase 2 (RSK2) phosphorylates the 5-HT
20 nscriptional regulation, in which docking of p90 ribosomal S6 kinase 2 (Rsk2) to the hormone-binding
21 he activity of its downstream substrate, the p90 ribosomal S6 kinase 2 (RSK2), by 1.4-fold, but it ha
23 extracellular signal-regulated kinase 2 and p90 ribosomal S6 kinase 2 but not mitogen- and stress-ac
24 exercise protocol, MAPK phosphorylation and p90 ribosomal S6 kinase 2, MAP kinase kinase 1, and Raf-
28 ctivated protein kinase phosphorylation, and p90 ribosomal S6 kinase activation, but did not affect t
29 nase C (PKC), but not by casein kinase II or p90 ribosomal S6 kinase, also activates PKA (7-fold).
30 mitogen-activated protein kinase (MAPK) and p90 ribosomal S6 kinase and consequent cell proliferatio
31 ing threonine 26 and serine 82, whereas PKC, p90 ribosomal S6 kinase, and casein kinase II, can phosp
32 ivo by isoforms of p70 S6 protein kinase and p90 ribosomal S6 kinase, and there is good evidence that
33 ts support the hypothesis that NF-kappaB and p90 ribosomal S6 kinase are involved in MEK5-ERK5-depend
34 induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of
35 not alter the TPA-induced phosphorylation of p90 ribosomal S6 kinase but caused a approximately 50% d
36 inhibition of the proteasome (by MG-132) or p90 ribosomal S6 kinases (by BI-D1870) is further increa
37 n in B cells was regulated by an ERK1/2- and p90 ribosomal S6 kinase-dependent mechanism, unlike in m
40 e p38 MAPK docking site of MAPKAPK2 converts p90 ribosomal S6 kinase into a stress-activated kinase i
42 ble magnitude of phosphorylation of ERK-1/2, p90 ribosomal S6 kinase-l and Akt, although phosphorylat
43 rminal phosphorylation by p70 S6 kinases and p90 ribosomal S6 kinases on four conserved Ser residues
47 osomal S6 kinase 2 (RSK2) is a member of the p90 ribosomal S6 kinase (p90RSK) family of proteins and
50 ctor receptor (EGFR) that is coupled to MAPK/p90 ribosomal S6 kinase (p90RSK), but not phosphatidylin
52 lly important downstream effector of PKCs is p90 ribosomal S6 kinase (p90RSK), which plays an importa
53 ant downstream effector of Src and ERK1/2 is p90 ribosomal S6 kinase (p90RSK), which plays an importa
55 Here, we report the critical role of the p90 ribosomal S6 kinase (p90RSK)/ERK5 complex in EC dysf
56 PI3K/Akt or mitogen-activated protein kinase/p90 ribosomal S6 kinase pathways and subsequent tuberous
57 ated protein kinase (MAPK)-activated kinase, p90 ribosomal S6 kinase (RSK) 1, was found to interact w
58 iral proteins, ORF45, mediates sustained ERK-p90 ribosomal S6 kinase (RSK) activation during KSHV lyt
59 n CCT as a novel physiological substrate for p90 ribosomal S6 kinase (RSK) and p70 ribosomal S6 kinas
61 ree enzymes that can phosphorylate GMF, only p90 ribosomal S6 kinase (RSK) enhances the inhibitory fu
64 pe I cAMP-dependent protein kinase (PKA) and p90 ribosomal S6 kinase (RSK) in cardiomyocyte apoptosis
65 The present study evaluated the function of p90 ribosomal S6 kinase (RSK) in the Drosophila circadia
69 taining the carboxyl-terminal tails of three p90 ribosomal S6 kinase (RSK) isozymes (RSK1, RSK2, and
70 o regulate signaling through the Raf/MEK/ERK/p90 ribosomal S6 kinase (RSK) kinase cascade and show ho
73 ied extracellular regulated kinase (ERK) and p90 ribosomal S6 kinase (RSK) proteins, we found several
76 tPA induced the phosphorylation of Erk1/2, p90 ribosomal S6 kinase (RSK), and p38 in a temporal ord
77 svirus (KSHV) causes sustained activation of p90 ribosomal S6 kinase (RSK), which is crucial for KSHV
82 gated the role of the MEK kinase (MEKK)1/ERK/p90 ribosomal S6 kinase (RSK)1-dependent C/EBPbeta signa
83 kinase C (PKC), protein kinase B (PKB), p70/p90 ribosomal S6 kinases (RSK and S6K), and the catalyti
84 e demonstrate that DAPK is a novel target of p90 ribosomal S6 kinases (RSK) 1 and 2, downstream effec
86 NTES induced phosphorylation of MEK, ERK1/2, p90 ribosomal S6 kinases (RSK), and cAMP-response elemen
88 ERK leading to increased phosphorylation of p90-ribosomal S6 kinase (RSK) and a concomitant activati
89 lated by ERK via the "alternative" S6 kinase p90-ribosomal S6 kinase (RSK), as evidenced by the site
91 nd IL-15, but not IL-7, rapidly activate the p90 ribosomal S6 kinases, Rsk1 and Rsk2, in human T lymp
92 virus (KSHV), causes sustained activation of p90 ribosomal S6 kinases (RSKs) and extracellular regula
93 arcoma-associated herpesvirus interacts with p90 ribosomal S6 kinases (RSKs) and strongly stimulates
96 The carboxyl-terminal domain (CTD) of the p90 ribosomal S6 kinases (RSKs) is an important regulato
98 ed structure/function analysis of Drosophila p90 ribosomal S6 kinase (S6KII) or its mammalian homolog
100 s after phorbol ester stimulation in the ERK/p90 ribosomal S6 kinase-signaling targets, the tuberous
101 ate its substrates such as p70 S6-kinase and p90 ribosomal S6 kinase that do not interact with phosph
104 , extracellular signal-regulated kinase, and p90 ribosomal s6 kinase was suppressed by CPF or procyan
105 over, replacement of the ERK docking site of p90 ribosomal S6 kinase with the p38 MAPK docking site o
106 cardiac-specific overexpression of wild-type p90 ribosomal S6 kinase (WT-p90RSK-Tg) and a dominant-ne
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