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1 phatase 4 (PP4; also called PPX and PPP4), a serine/threonine phosphatase.
2 ciates with protein phosphatase 2A (PP2A), a serine/threonine phosphatase.
3 38 kDa catalytic subunit of a type 1 protein serine/threonine phosphatase.
4 but not the activity of PP2A, another major serine/threonine phosphatase.
5 ms, controls a serine/threonine kinase and a serine/threonine phosphatase.
6 (PP2A) is a highly conserved and ubiquitous serine/threonine phosphatase.
7 of a novel PKC isozyme and a bFGF-dependent serine/threonine phosphatase.
8 , a cyclosporin-sensitive, calcium-regulated serine/threonine phosphatase.
9 hosphorylated to a p115 form by an activated serine/threonine phosphatase.
10 e structure-function studies of this protein serine/threonine phosphatase.
11 own about the expression and function of the serine-threonine phosphatases.
12 2A (PP2A), an abundantly expressed family of serine-threonine phosphatases.
13 gement during platelet aggregation activates serine/threonine phosphatases.
14 rity to members of the PP2C class of protein serine/threonine phosphatases.
15 associate with members of the PP2A family of serine/threonine phosphatases.
16 ytes with calyculin A, a potent inhibitor of serine/threonine phosphatases.
17 to inhibit acid and alkaline phosphatases or serine/threonine phosphatases.
18 e 2A (PP2A) is a member of the intracellular serine/threonine phosphatases.
19 lls, BAD was rapidly dephosphorylated by the serine-threonine phosphatase 1 alpha, and localized in t
20 orylation of mitotic FAK in vitro by protein serine/threonine phosphatase 1 restores the ability of F
23 ro and in vivo evidence to show that protein serine/threonine phosphatase-1 is a major phosphatase th
24 ctase active site is highly conserved in the serine/threonine phosphatase-1 subfamily, but not in the
25 CCC: PPP2R1A encodes a regulatory subunit of serine/threonine phosphatase 2, and ARID1A encodes adeni
26 toichiometric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in
27 at the protein HOX11 interacted with protein serine-threonine phosphatase 2A catalytic subunit (PP2AC
29 tro mixing experiments indicate that protein serine/threonine phosphatase 2A (PP2A) can dephosphoryla
30 vidence indicates that regulation of protein-serine/threonine phosphatase 2A (PP2A) involves its asso
34 many kinase cascades, heterotrimeric protein serine/threonine phosphatase 2A (PP2A), is composed of c
35 V was shown to stably associate with protein serine/threonine phosphatase 2A (PP2A), which was propos
39 downstream repressor COUP-TFII by inhibiting serine/threonine phosphatase 2A activity, and that decre
40 sein kinase 2 activity and increased protein serine/threonine phosphatase 2A activity, resulting in a
41 chanisms control the activity of the protein serine/threonine phosphatase 2A catalytic subunit (PP2Ac
46 wn that EGCG can negatively regulate protein serine/threonine phosphatase-2A (PP-2A) to positively re
49 lytic and regulatory subunits of the protein serine/threonine phosphatase 4 complex (PP4c/PP4R1).
52 , including purple acid phosphatase, protein serine/threonine phosphatases, 5'-nucleotidase, and DNA
53 noprecipitated c-Fos protein with the type 2 serine/threonine phosphatase A (PP2A) and immunoblotting
54 nd treatment with either protein tyrosine or serine/threonine phosphatases abolished its activity.
57 ediated by KCC2 is completely independent of serine-threonine phosphatase activity, suggesting that t
58 d FIN13 expressed in mammalian cells exhibit serine-threonine phosphatase activity, which requires Mn
59 nuclei-free cell lysates, we find increased serine/threonine phosphatase activity associated with Go
61 ubiquitination of proteins, we examined the serine/threonine phosphatase activity in our CAOV3 cells
62 y has been shown to have modest tyrosine and serine/threonine phosphatase activity, we find that it i
66 ts lacking PP1cgamma, a catalytic subunit of serine/threonine phosphatase, alpha(IIb)beta3 failed to
68 Interestingly, okadaic acid, an inhibitor of serine/threonine phosphatase, also strongly activated tr
70 h repeat protein phosphatase 1) is a protein-serine/threonine phosphatase and a negative regulator of
71 the protein phosphatase 2A (PP2A) family of serine-threonine phosphatases, and this interaction is r
72 ein kinase C (PKC) activation, inhibition of serine/threonine phosphatase, and an active protein tyro
73 in phosphatase-2A (PP2A), a widely expressed serine/threonine phosphatase, and the heterotrimeric G p
74 activating several tyrosine phosphatases and serine/threonine phosphatases, and it suppresses the cel
75 hod is applicable to other DUSPs and protein-serine/threonine phosphatases, and the substrate specifi
79 of the phosphoprotein phosphatase family of serine/threonine phosphatases are thought to exist in di
80 s (PLMs), potent and selective inhibitors of serine threonine phosphatases, are of interest for their
81 tein phosphatase-1 (PP1), a major eukaryotic serine/threonine phosphatase, are defined by the associa
83 thelial cells, we identify PP2A as the first serine/threonine phosphatase associated with the multipr
84 in phosphatase 4 (PP4), a novel PP2A-related serine/threonine phosphatase, at a 50% inhibitory concen
85 we examined the regulatory interactions of a serine/threonine phosphatase (BA-Stp1), serine/threonine
86 gly, has the sequence hallmarks of a phospho-serine/threonine phosphatase belonging to the PPP family
87 cancer cells, it was determined that PP2A, a serine/threonine phosphatase, binds and dephosphorylates
90 nactivation of the Ca2+/calmodulin-dependent serine-threonine phosphatase calcineurin by the drug-imm
91 es a G(1) cell cycle arrest, implicating the serine/threonine phosphatase calcineurin as one Ca(2+)/C
92 (slc4a7) and the Ca(2+)/calmodulin-activated serine/threonine phosphatase calcineurin exist and play
94 ies have revealed that the calcium-dependent serine/threonine phosphatase calcineurin mediates the ef
95 g infection is modulated by Ca(2+)-dependent serine/threonine phosphatase calcineurin, an important t
97 order to explore the redox regulation of the serine/threonine phosphatase calcineurin, we have invest
104 uct was discovered to be an inhibitor of the serine/threonine phosphatase, calcineurin, and its signa
106 idues, and treatment of cRaf-1 with protein (serine/threonine) phosphatases can deactivate it, at lea
107 Treatment of CKIepsilon with any of several serine/threonine phosphatases causes a marked increase i
108 n phosphatase 2A is a heterotrimeric protein serine/threonine phosphatase consisting of a 36-kDa cata
109 ase 2A (PP2A) is a family of multifunctional serine/threonine phosphatases consisting of a catalytic
110 n phosphatase-1, revealed that this class of serine/threonine phosphatases contain in their putative
111 tase 2A (PP2A) is an abundant heterotrimeric serine/threonine phosphatase containing highly conserved
112 a activation and PDZ-mediated formation of a serine/threonine phosphatase-containing complex by synde
113 esting in view of literature suggesting that serine/threonine phosphatases could be subject to redox
114 protein kinase C (PKC)-dependent and protein serine/threonine phosphatase-dependent pathways, respect
117 ole for the dephosphorylation events via the serine/threonine phosphatases during the integrin outsid
119 A) is a ubiquitously expressed member of the serine-threonine phosphatase family that is involved in
120 otein kinases Cdk7 and Cdk9, whereas protein serine/threonine phosphatase FCP1 dephosphorylates CTD.
122 Surprisingly, this structure revealed a serine/threonine phosphatase fold that unexpectedly targ
123 is a homologue of the PPM family of protein-serine/threonine phosphatases found in all eukaryotes as
124 in phosphatase 2A (PP2A) is one of the major serine/threonine phosphatases found in eukaryotic cells.
125 tural gene for a putative PPP family protein-serine/threonine phosphatase from the microcystin-produc
126 frames (ORFs) encoding two potential protein-serine/threonine phosphatases from the cyanobacterium Sy
128 determinant for the targeting of the type 1 serine/threonine phosphatase (Glc7) to the bud neck.
129 protein phosphatase X (PPX)), a PP2A-related serine/threonine phosphatase, has been shown to be invol
134 in Saccharomyces cerevisiae, is an essential serine/threonine phosphatase implicated in the regulatio
135 otein phosphatase 2A (PP2A), one of the main serine-threonine phosphatases in mammalian cells, mainta
136 Protein phosphatase 2A (PP2A), the major serine/threonine phosphatase in eukaryotic cells, is a h
137 ion C (rdgC) gene encodes an unusual protein serine/threonine phosphatase in that it contains at leas
140 ence for the involvement of a type 1 protein serine/threonine phosphatase in the ultraviolet radiatio
141 an involvement of an okadaic-acid-sensitive serine/threonine phosphatase in TNF-alpha-induced blocka
143 h RNA interference (RNAi)-based screening of serine/threonine phosphatases in Drosophila S2 cells, we
144 ed activity of calcineurin, a Ca2+-dependent serine/threonine phosphatase, increases synaptic express
145 ons show that LTD expression is increased by serine/threonine phosphatase inhibition, and negatively
147 e required for iNOS transcription, while the serine-threonine phosphatase inhibitor (OA) had no effec
148 nadate [PV], phenylarsine oxide [PAO]) and a serine-threonine phosphatase inhibitor (okadaic acid [OA
149 inocytes, the tumor promoter okadaic acid, a serine-threonine phosphatase inhibitor, increased bindin
150 ol ester type tumor promoter okadaic acid, a serine-threonine phosphatase inhibitor, on activator pro
152 in, prostaglandin E(2), cAMP-raising agents, serine/threonine phosphatase inhibitor and activation of
154 ate, the Ca(2+) ionophore ionomycin, and the serine/threonine phosphatase inhibitor calyculin A incre
156 hibitors citrate and tartrate or the protein serine/threonine phosphatase inhibitor okadaic acid.
157 stimulated by treatment with calyculin A, a serine/threonine phosphatase inhibitor that elevates MLC
158 protein kinases A and C, and okadaic acid (a serine/threonine phosphatase inhibitor) decreased the cu
159 beta(3)-fibrinogen blocker) or okadaic acid (serine/threonine phosphatase inhibitor) dramatically enh
160 reatment of eosinophils with okadaic acid, a serine/threonine phosphatase inhibitor, at the concentra
161 retion were inhibited by pretreatment with a serine/threonine phosphatase inhibitor, calyculin A.
162 nduction by nickel; however, okadaic acid, a serine/threonine phosphatase inhibitor, induced Cap43 to
163 When cells were lysed in the presence of serine/threonine phosphatase inhibitor, NaF, the PKA-enh
164 Low concentrations (2 nM) of okadaic acid, a serine/threonine phosphatase inhibitor, prevented TNF-al
165 cells were treated with okadaic acid (OA), a serine/threonine phosphatase inhibitor, to induce tau ph
166 cose transport stimulated by okadaic acid, a serine/threonine phosphatase inhibitor, was also 45% low
168 nd ex vivo skin and esophagus cultures, with serine/threonine phosphatase inhibitors causes a dramati
169 nt cell cytosol, is resistant to the classic serine/threonine phosphatase inhibitors okadaic acid and
170 Treatment of cells with the cell-permeable serine/threonine phosphatase inhibitors okadaic acid or
172 , an inhibitor of type 1 and type 2A protein serine/threonine phosphatase, inhibits both receptor-ind
173 nd phosphatases modulate GPCR signaling, how serine/threonine phosphatases integrate with G protein s
174 vel cytoskeletal associated protein, proline serine threonine phosphatase interacting protein (PST PI
175 s resulted in the identification of proline, serine, threonine phosphatase interacting protein (PSTPI
176 quence similarity with the PST PIP (proline, serine, threonine phosphatase interacting protein)/CDC15
177 CD2BP1 and its murine ortholog, proline-serine-threonine phosphatase interacting protein (PSTPIP
178 c15 homology family protein PSTPIP2 (proline-serine-threonine phosphatase interacting protein 2), spo
179 ted an interaction between pyrin and proline serine threonine phosphatase-interacting protein 1 (PSTP
180 ression of the F-BAR domain protein, proline serine threonine phosphatase-interacting protein 2 (PSTP
183 f a cytoskeletal-associated protein, proline-serine-threonine phosphatase-interacting protein (PSTPIP
184 h dominant missense mutations in the proline-serine-threonine phosphatase-interacting protein 1 gene
186 pressions of anti-inflammatory IL37, proline-serine-threonine phosphatase-interacting protein 2 (PSTP
188 The mouse Lupo (I282N) mutation in proline-serine-threonine phosphatase-interacting protein 2 (PSTP
189 in phosphatase 2A (PP2A) is a heterotrimeric serine/threonine phosphatase involved in essential cellu
190 tein phosphatase-2A (PP2A) is a multisubunit serine/threonine phosphatase involved in intracellular s
191 of protein phosphatase 2A, a family of major serine/threonine phosphatases involved in regulating cel
193 otein dephosphorylation catalyzed by protein serine/threonine phosphatases is necessary for proper fu
195 at protein phosphatase 1 (PP1), a ubiquitous serine/threonine phosphatase, is a novel potent positive
196 phatase 2A (PP2A) is an essential eukaryotic serine/threonine phosphatase known to play important rol
197 urface receptors such as CTLA-4 and CD28 and serine/threonine phosphatases may represent a novel mech
201 to be calcineurin because inhibitors of this serine/threonine phosphatase partially rescue the block
203 nd that PPM1A, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with
204 data suggest that the PPEF family of protein serine/threonine phosphatases plays a specific and conse
205 okine-induced activation of NF-kappaB, while serine-threonine phosphatases posttranscriptionally regu
210 (PKA)-activated inhibitor of type 1 protein serine/threonine phosphatase (PP1), in a yeast two-hybri
211 the factor that activates the type 1 protein serine/threonine phosphatase (PP1), which dephosphorylat
214 ed roles of highly expressed skeletal muscle serine/threonine phosphatases (PP1, PP2A, PP2B, and PP2C
216 ists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzy
218 previously unrecognized requirement for the serine-threonine phosphatase PP2A in the function of T(r
222 to be due to the combined activities of the serine/threonine phosphatase PP2A and the tyrosine phosp
225 cific phosphatase activity that contains the serine/threonine phosphatase PP2A, the tyrosine phosphat
228 c acid, an inhibitor of the major PPP family serine/threonine phosphatases PP2A and protein phosphata
230 suppressed by SCF through phosphorylation of serine/threonine phosphatase (PP2A) and correlated well
233 mised in a strain lacking functional type 2C serine/threonine phosphatases (PP2C), Ptc1 and Ptc3.
235 esent physiological evidence for the protein serine/threonine phosphatase, PP5, as an effector of Rac
237 Here we show that the oncogenic p53-induced serine/threonine phosphatase, PPM1D (or Wip1), dephospho
238 We now identify a potential role for the serine-threonine phosphatase PPM1G in translational regu
240 reen that identifies the PP2A heterotrimeric serine/threonine phosphatases PPP2R2A, PPP2R2D, PPP2R5A,
241 d after conserved regions within the protein-serine/threonine phosphatases (PPs) of the PP1/2A/2B sup
242 rential regulation of okadaic acid-sensitive serine/threonine phosphatases; presumably, these phospha
243 ated at the post-translational level, by the serine-threonine phosphatase protein phosphatase 2A (PP2
244 f oncogenes or the disruption of the general serine-threonine phosphatase protein phosphatase 2A (PP2
247 2Ralpha) and gamma chain and also endogenous serine/threonine phosphatase protein phosphates 1 and/or
248 Inhibition of tyrosine phosphatases and serine/threonine phosphatases protein phosphatase 1 (PP1
249 nomic approach, we have identified a protein serine/threonine phosphatase, protein phosphatase 2A (PP
250 e was also inactivated by treatment with the serine/threonine phosphatase, protein phosphatase 2A; ok
251 ases in Mycobacterium tuberculosis, only one serine/threonine phosphatase, PstP, has been identified.
252 ment of SH2-B with protein phosphatase 2A, a serine/threonine phosphatase, reduces the many forms to
254 A1AT, protein phosphatase 2A (PP2A), a major serine-threonine phosphatase, regulates similar biologic
255 Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase regulating many cellular pr
256 osphatase I (PP1) is an essential eukaryotic serine/threonine phosphatase required for many cellular
258 s appear to be mediated by the activation of serine-threonine phosphatase, since they are blocked by
259 d sodium molybdate) but not by inhibitors of serine/threonine phosphatases (sodium fluoride, okadaic
260 es), the precise role of the co-transcribing serine/threonine phosphatase (SP-STP) has remained enigm
261 ates an important property of eukaryote-type serine/threonine phosphatase (SP-STP) of group A Strepto
262 , how the presence or absence of the cognate serine/threonine phosphatase Stp1 affects Stk1 function
264 tly avoid the taste, is dependent on several serine/threonine phosphatase substrates and the PP1-bind
265 ed by inhibition of all known subfamilies of serine/threonine phosphatases, suggesting that multiple
266 lcineurin is a calcium-calmodulin-regulated, serine-threonine phosphatase that functions as a key ind
267 in (PP2B) is a calcium/calmodulin-activated, serine-threonine phosphatase that transmits signals to t
270 rotein phosphatase 2A (PP2A) is a multimeric serine/threonine phosphatase that carries out multiple f
272 Experiments were performed to identify the serine/threonine phosphatase that dephosphorylates FOXO1
273 d-type p53-induced phosphatase 1 (WIP1) is a serine/threonine phosphatase that dephosphorylates prote
276 ex that binds to and inhibits calcineurin, a serine/threonine phosphatase that is activated by TCR en
277 n phosphatase 2A (PP2A) is a multifunctional serine/threonine phosphatase that is critical to many ce
278 We have recently reported that a protein serine/threonine phosphatase that is designated PP5 and
280 hosphorylation of this site is mediated by a serine/threonine phosphatase that is inhibited by okadai
282 p53-induced phosphatase PPM1D (or Wip1) is a serine/threonine phosphatase that is transcriptionally u
283 stimulates protein phosphatase 2A (PP2A), a serine/threonine phosphatase that modulates essential si
284 rotein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many b
285 Protein phosphatase 2A (PP2A) is a major serine/threonine phosphatase that regulates a wide varie
286 neurin (Cn) is a Ca(2+)/calmodulin-dependent serine/threonine phosphatase that regulates differentiat
287 Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase that regulates many cellula
288 tresses inhibited activity of calcineurin, a serine/threonine phosphatase that regulates NFAT activat
289 osphatase 2A (PP2A) is a family of mammalian serine/threonine phosphatases that is involved in the co
290 e are conserved between different eukaryotic serine/threonine phosphatases, these results should appl
291 Addition of protein phosphatase 1 gamma, a serine/threonine phosphatase, to rat liver cytosol reduc
294 reductase active site has been identified in serine-threonine phosphatases using a descriptor built f
295 diated early events, the activity of protein serine/threonine phosphatases was markedly increased in
296 dentified cancer genes was PPP6C, encoding a serine/threonine phosphatase, which harbored mutations t
297 at PDP1 belongs to the PPM family of protein serine/threonine phosphatases, which, in spite of a low
298 Protein phosphatase-2A (PP2A) is an abundant serine/threonine phosphatase with anti-inflammatory acti
299 named PPX or PPP4) is a PP2A-related protein serine/threonine phosphatase with important roles in a v
300 e TGN contains a mutation in PTC1, a type 2c serine/threonine phosphatase with widespread influences.
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