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1 e structure of the catalytic domain of human Cdc25 phosphatase.
2 ologues of the catalytic domain of the human Cdc25 phosphatase.
3 ted by Wee1-related kinases and activated by Cdc25 phosphatase.
4 activities of the Wee1/Myt1 kinases and the Cdc25 phosphatase.
5 ted by Wee1 tyrosine kinase and activated by Cdc25 phosphatase.
6 ical inhibitors of Wee1 and Myt1 kinases and Cdc25 phosphatases.
7 of MPF is regulated by Wee1/Myt1 kinases and Cdc25 phosphatases.
8 ved arginine, which is also present in human Cdc25 phosphatases.
9 idue Cys75 are unchanged with respect to the Cdc25 phosphatases.
10 s driven by downregulation of the activating Cdc25 phosphatases.
11 hat employ Chk1 and Chk2 Ser/Thr kinases and Cdc25 phosphatases.
12 p is not a phosphatase but is a homologue of CDC25 phosphatases.
13 tive, and partially competitive inhibitor of Cdc25 phosphatases.
14 PF through the activating phosphorylation on Cdc25 phosphatases.
15 eracting activities of Wee1/Myt1 kinases and Cdc25 phosphatases.
16 ternal mRNAs, string and twine, which encode Cdc25 phosphatases.
17 ate reductases form, together with the known Cdc25 phosphatases, a well-defined subfamily of the rhod
20 string and twine; and (4) consequent loss of Cdc25 phosphatase activity allows inhibitory phosphoryla
24 ontrolled by Cdk1, which is activated by the Cdc25 phosphatase and inhibited by Wee1 tyrosine kinase,
27 e that triggers G2/M arrest and inhibits the Cdc25 phosphatase, and many compounds that synergize wit
30 with poor prognosis in many diverse cancers, Cdc25 phosphatases are attractive targets for anticancer
33 dual specificity, low-molecular-weight, and Cdc25 phosphatases, are key mediators of a wide variety
36 coding the Drosophila homologue of the yeast CDC25 phosphatase, contributes to the G2 cell cycle dela
37 be useful in further clarifying the role of Cdc25 phosphatase-dependent pathways in checkpoint contr
40 st species, the G(2) checkpoint prevents the Cdc25 phosphatase from removing inhibitory phosphate gro
41 will focus on the role of Plk3 in regulating Cdc25 phosphatase function and its effect on the cell cy
42 s is accomplished in part by maintaining the Cdc25 phosphatase in a phosphorylated form that binds 14
43 s is accomplished in part by maintaining the Cdc25 phosphatase in a phosphorylated form that binds 14
44 Like DA3003-1, JUN1111 selectively inhibited Cdc25 phosphatases in vitro in an irreversible, time-dep
46 phila embryos, zygotic expression of the stg(cdc25) phosphatase in G2 activates cyclin/cdc2 kinases a
50 ng that protein substrate recognition by the Cdc25 phosphatases is an essential and evolutionarily co
51 ession levels, the intracellular activity of Cdc25 phosphatases is determined by their subcellular di
60 Cdk1, a fraction of total cyclin B1, and the Cdc25 phosphatases reside predominantly in the cytoplasm
62 A), regulator of cyclin A1 (rca1) and string/cdc25 phosphatase (stg), and the microtubule destabilizi
66 lated Cys-dependent hydrolases and rhodanese/Cdc25 phosphatases), suggesting that neither secondary s
67 d were abolished in cells overexpressing the Cdc25 phosphatase, suggesting a role for the Cdc2 cyclin
68 s, a well-defined subfamily of the rhodanese/Cdc25 phosphatase superfamily, characterized by a 7-amin
70 uch knowledge of the basic enzymology of the Cdc25 phosphatases that may aid in the development of sp
71 late times, we observed accumulation of the Cdc25 phosphatases that remove the inhibitory phosphates
72 ve-site motif CE[F/Y]SXXR that characterizes Cdc25 phosphatase, the novel CALSQ[Q/V]R motif is also c
73 hosphorylates and suppresses the activity of Cdc25 phosphatase: the resulting failure to remove inhib
75 r gastrulation and require downregulation of Cdc25 phosphatase, which was previously attributed to th
76 rylating activity of Cpd 5, it might inhibit Cdc25 phosphatases, which contain a cysteine in the cata
79 ns are homologous to the catalytic domain of Cdc25 phosphatases, which, in turn, belong to the rhodan
80 structure, specificity, and mechanism of the Cdc25 phosphatases with a special focus on the activity
82 e a valuable reagent to probe the actions of Cdc25 phosphatases within cells and may also be useful s
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