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1 ion via the induction of MAPK phosphatase 3 (MKP-3).
2 d forkhead box O1 (FOXO1) as a substrate for MKP-3.
3 vated protein kinase phosphatase (MKP)-1 and MKP-3.
4 microM and showed selectivity for MKP-1 over MKP-3.
5 h as the dual-specificity kinase/phosphatase MKP-3.
6 ity in MCF10A cells, which had no detectable MKP-3.
7 308 cells, H-ras MCF10A cells highly express MKP-3.
8 in, resulting in the enzymatic activation of MKP-3.
9 nally coupled to the active site residues of MKP-3.
10 ivated protein kinase phosphatases CL100 and MKP-3.
11 however, blocked totally by co-expression of MKP-3.
12 minal sequences of MK-STYX, STYX, MKP-1, and MKP-3.
13 ogs of MK-STYX, MKP (MAPK phosphatase)-1 and MKP-3.
14 oupling is also most similar for MK-STYX and MKP-3.
15                                              MKP-3, a prototypical MKP, achieves substrate specificit
16 nesis in vivo and suggest that inhibition of MKP-3 activity may provide new therapies for T2DM.
17                                              MKP-3 aggregation was reversible and, 1 h after heat sho
18 in unleashes ERK activity by down-regulating MKP-3, an ERK inhibitor, and further suggest that MKP-3
19 ES cells results in the dephosphorylation of MKP-3 and activation of extracellular signal-regulated k
20 hich includes the ERK-specific enzymes DUSP6/MKP-3 and DUSP7/MKP-X.
21                                   Therefore, MKP-3 and MKP-1 appeared to be critical heat-labile phos
22 tively, and showed 5-10-fold selectivity for MKP-3 and MKP-1 over VH-1-related phosphatase, Cdc25B2,
23 tion of MEK1/2 and prevented inactivation of MKP-3 and MKP-1.
24 s exposed to 45 degrees C for 20 min, 90% of MKP-3 became insoluble.
25                      Low level expression of MKP-3 blocks totally epidermal growth factor-stimulated
26 d inactivation of the major ERK phosphatase, MKP-3, by promoting its aggregation, so that in cells ex
27                                 In addition, MKP-3 can activate PEPCK promoter in synergy with dexame
28                        The redistribution of MKP-3 correlated with an increased rate of ERK dephospho
29                        However, unlike DUSP6/MKP-3, DUSP9/MKP-4 also inactivates the p38alpha MAP kin
30                  Therefore, dysregulation of MKP-3 expression and/or function in liver may contribute
31 g a chaperone activity was unable to protect MKP-3 from heat inactivation but interfered with MEK1/2
32                                 We have used MKP-3-green fluorescent protein fusions in conjunction w
33                Palytoxin induced the loss of MKP-3 in a manner that corresponded to increased ERK pho
34               Conversely, shRNA knockdown of MKP-3 in both lean and obese mice resulted in decreased
35 activity and induced a corresponding loss of MKP-3 in H-ras MCF10A cells.
36           Furthermore, ectopic expression of MKP-3 in hepatoma cells by adenoviral infection increase
37 we determined how palytoxin affected ERK and MKP-3 in MCF10A human breast epithelial cells and in H-r
38 only has one, and that MK-STYX is similar to MKP-3 in the evolutionary coupling of the active site an
39 tle is known about the physiological role of MKP-3 in vivo.
40 1alpha) acted downstream of FOXO1 to mediate MKP-3-induced gluconeogenesis.
41 howed that sustained expression of exogenous MKP-3 inhibited palytoxin-stimulated ERK activation.
42  negative ERK2 mutant or a vector expressing MKP-3 inhibited the arginase II promoter activity.
43                     These data indicate that MKP-3 is an important regulator of hepatic gluconeogenes
44    The amino-terminal noncatalytic domain of MKP-3 is both necessary and sufficient for nuclear expor
45       Here, we have shown that expression of MKP-3 is markedly increased in the liver of diet-induced
46 to show that the cytoplasmic localization of MKP-3 is mediated by a chromosome region maintenance-1 (
47 st to M3/6, the dual specificity phosphatase MKP-3 is selective for inactivation of ERK family MAP ki
48                        We used wild-type and MKP-3 knock-out (KO) mice, a paw incision model of acute
49 l p-p38 was expressed mostly in microglia in MKP-3 KO mice, and their selective pharmacological inhib
50 if which abrogate ERK2 binding do not affect MKP-3 localization.
51 sphorylation and inactivation of MAP kinase, MKP-3 may also play a role in determining the subcellula
52 , an ERK inhibitor, and further suggest that MKP-3 may be a vulnerable target in cells that express o
53 ce the idea that regulatory proteins such as MKP-3 may play a key role in the spatio-temporal regulat
54                                              MKP-3-mediated dephosphorylation of FOXO1 at Ser256 prom
55 e (ERK) by the cytoplasmic phosphatase DUSP6/MKP-3 or can regulate more than one MAPK pathway as illu
56 lar basis of the cytoplasmic localization of MKP-3 or its physiological significance is unknown.
57    Consistent with this, adenovirus-mediated MKP-3 overexpression in lean mice promoted gluconeogenes
58 on was reversible and, 1 h after heat shock, MKP-3 partially resolubilized.
59 ERK) 1/2], and increased expression of DUSP6/MKP-3 phosphatase (an inhibitor of phospho-ERK1/2).
60 en together, our data strongly suggests that MKP-3 plays a role in regulating gluconeogenic gene expr
61 sistent mechanical allodynia in mice lacking MKP-3 (postoperative day 21), concurrently with persiste
62 dings strongly suggest that dysregulation of MKP-3 prevents spontaneous resolution of acute postopera
63 Recent studies show that MAPK phosphatase-3 (MKP-3) promotes gluconeogenic gene transcription in hepa
64 Transfection of an inactive ERK phosphatase (MKP-3/Pyst1) that sequesters ERK in the cytoplasm preven
65  of active mammalian MAP kinase phosphatase (MKP-3) resulted in inactivation of MAP kinase in unferti
66    Furthermore, the nuclear translocation of MKP-3 seen in the presence of leptomycin B is mediated b
67  analysis of the ERK2 binding (EB) domain of MKP-3 show that regions that are essential for ERK2 bind
68 diated by an active process, indicating that MKP-3 shuttles between the nucleus and cytoplasm.
69  Finally, we demonstrate that the ability of MKP-3 to cause the cytoplasmic retention of ERK2 require
70 ase in unfertilized eggs, as did addition of MKP-3 to lysates of unfertilized eggs.
71  of the protein also mediates the binding of MKP-3 to MAP kinase, we show that mutations of the kinas
72 ither the binding or phosphatase activity of MKP-3 toward ERK2, indicating that the kinase interactio
73             Selective regulation by M3/6 and MKP-3 was also observed upon chronic MAP kinase activati
74                In this study, we showed that MKP-3 was expressed in insulin-responsive tissues and th
75 al specificity protein kinase phosphatase 3 (MKP-3) was identified as a candidate gene that antagoniz
76 ctivated kinase (MAP) phosphatases MKP-1 and MKP-3 were elevated in neurons.
77 ogen-activated protein kinase phosphatase-3 (MKP-3), which selectively inactivates ERK.