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1 e structure-function studies of this protein serine/threonine phosphatase.
2 phatase 4 (PP4; also called PPX and PPP4), a serine/threonine phosphatase.
3 ciates with protein phosphatase 2A (PP2A), a serine/threonine phosphatase.
4 38 kDa catalytic subunit of a type 1 protein serine/threonine phosphatase.
5 but not the activity of PP2A, another major serine/threonine phosphatase.
6 ms, controls a serine/threonine kinase and a 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 (PP2A) is a highly conserved and ubiquitous serine/threonine phosphatase.
10 own about the expression and function of the serine-threonine phosphatases.
11 2A (PP2A), an abundantly expressed family of serine-threonine phosphatases.
12 gement during platelet aggregation activates serine/threonine phosphatases.
13 rity to members of the PP2C class of protein serine/threonine phosphatases.
14 e 2A (PP2A) is a member of the intracellular 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 lls, BAD was rapidly dephosphorylated by the serine-threonine phosphatase 1 alpha, and localized in t
18 orylation of mitotic FAK in vitro by protein serine/threonine phosphatase 1 restores the ability of F
21 protein that regulates functions of protein serine/threonine phosphatase-1 in cell proliferation and
22 ro and in vivo evidence to show that protein serine/threonine phosphatase-1 is a major phosphatase th
23 ctase active site is highly conserved in the serine/threonine phosphatase-1 subfamily, but not in the
24 CCC: PPP2R1A encodes a regulatory subunit of serine/threonine phosphatase 2, and ARID1A encodes adeni
25 toichiometric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in
26 at the protein HOX11 interacted with protein serine-threonine phosphatase 2A catalytic subunit (PP2AC
28 tro mixing experiments indicate that protein serine/threonine phosphatase 2A (PP2A) can dephosphoryla
29 vidence indicates that regulation of protein-serine/threonine phosphatase 2A (PP2A) involves its asso
33 many kinase cascades, heterotrimeric protein serine/threonine phosphatase 2A (PP2A), is composed of c
34 V was shown to stably associate with protein serine/threonine phosphatase 2A (PP2A), which was propos
37 downstream repressor COUP-TFII by inhibiting serine/threonine phosphatase 2A activity, and that decre
38 sein kinase 2 activity and increased protein serine/threonine phosphatase 2A activity, resulting in a
39 chanisms control the activity of the protein serine/threonine phosphatase 2A catalytic subunit (PP2Ac
44 wn that EGCG can negatively regulate protein serine/threonine phosphatase-2A (PP-2A) to positively re
47 lytic and regulatory subunits of the protein serine/threonine phosphatase 4 complex (PP4c/PP4R1).
50 , including purple acid phosphatase, protein serine/threonine phosphatases, 5'-nucleotidase, and DNA
51 noprecipitated c-Fos protein with the type 2 serine/threonine phosphatase A (PP2A) and immunoblotting
52 nd treatment with either protein tyrosine or serine/threonine phosphatases abolished its activity.
55 ediated by KCC2 is completely independent of serine-threonine phosphatase activity, suggesting that t
56 d FIN13 expressed in mammalian cells exhibit serine-threonine phosphatase activity, which requires Mn
57 nuclei-free cell lysates, we find increased serine/threonine phosphatase activity associated with Go
59 ubiquitination of proteins, we examined the serine/threonine phosphatase activity in our CAOV3 cells
60 y has been shown to have modest tyrosine and serine/threonine phosphatase activity, we find that it i
64 ts lacking PP1cgamma, a catalytic subunit of serine/threonine phosphatase, alpha(IIb)beta3 failed to
66 Interestingly, okadaic acid, an inhibitor of serine/threonine phosphatase, also strongly activated tr
68 h repeat protein phosphatase 1) is a protein-serine/threonine phosphatase and a negative regulator of
69 the protein phosphatase 2A (PP2A) family of serine-threonine phosphatases, and this interaction is r
70 ein kinase C (PKC) activation, inhibition of serine/threonine phosphatase, and an active protein tyro
71 in phosphatase-2A (PP2A), a widely expressed serine/threonine phosphatase, and the heterotrimeric G p
72 activating several tyrosine phosphatases and serine/threonine phosphatases, and it suppresses the cel
73 hod is applicable to other DUSPs and protein-serine/threonine phosphatases, and the substrate specifi
78 of the phosphoprotein phosphatase family of serine/threonine phosphatases are thought to exist in di
79 s (PLMs), potent and selective inhibitors of serine threonine phosphatases, are of interest for their
80 tein phosphatase-1 (PP1), a major eukaryotic serine/threonine phosphatase, are defined by the associa
82 thelial cells, we identify PP2A as the first serine/threonine phosphatase associated with the multipr
83 in phosphatase 4 (PP4), a novel PP2A-related serine/threonine phosphatase, at a 50% inhibitory concen
84 we examined the regulatory interactions of a serine/threonine phosphatase (BA-Stp1), serine/threonine
85 gly, has the sequence hallmarks of a phospho-serine/threonine phosphatase belonging to the PPP family
86 cancer cells, it was determined that PP2A, a serine/threonine phosphatase, binds and dephosphorylates
89 es a G(1) cell cycle arrest, implicating the serine/threonine phosphatase calcineurin as one Ca(2+)/C
90 (slc4a7) and the Ca(2+)/calmodulin-activated serine/threonine phosphatase calcineurin exist and play
92 ies have revealed that the calcium-dependent serine/threonine phosphatase calcineurin mediates the ef
93 g infection is modulated by Ca(2+)-dependent serine/threonine phosphatase calcineurin, an important t
94 order to explore the redox regulation of the serine/threonine phosphatase calcineurin, we have invest
101 uct was discovered to be an inhibitor of the serine/threonine phosphatase, calcineurin, and its signa
103 idues, and treatment of cRaf-1 with protein (serine/threonine) phosphatases can deactivate it, at lea
104 Treatment of CKIepsilon with any of several serine/threonine phosphatases causes a marked increase i
106 ase 2A (PP2A) is a family of multifunctional serine/threonine phosphatases consisting of a catalytic
107 tase 2A (PP2A) is an abundant heterotrimeric serine/threonine phosphatase containing highly conserved
108 a activation and PDZ-mediated formation of a serine/threonine phosphatase-containing complex by synde
109 esting in view of literature suggesting that serine/threonine phosphatases could be subject to redox
111 rotein phosphatases, including the family of serine/threonine phosphatases designated PP2A, is essent
113 ole for the dephosphorylation events via the serine/threonine phosphatases during the integrin outsid
115 A) is a ubiquitously expressed member of the serine-threonine phosphatase family that is involved in
116 otein kinases Cdk7 and Cdk9, whereas protein serine/threonine phosphatase FCP1 dephosphorylates CTD.
118 Surprisingly, this structure revealed a serine/threonine phosphatase fold that unexpectedly targ
119 is a homologue of the PPM family of protein-serine/threonine phosphatases found in all eukaryotes as
120 in phosphatase 2A (PP2A) is one of the major serine/threonine phosphatases found in eukaryotic cells.
121 tural gene for a putative PPP family protein-serine/threonine phosphatase from the microcystin-produc
122 frames (ORFs) encoding two potential protein-serine/threonine phosphatases from the cyanobacterium Sy
124 determinant for the targeting of the type 1 serine/threonine phosphatase (Glc7) to the bud neck.
125 protein phosphatase X (PPX)), a PP2A-related serine/threonine phosphatase, has been shown to be invol
130 otein phosphatase 2A (PP2A), one of the main serine-threonine phosphatases in mammalian cells, mainta
131 Protein phosphatase 2A (PP2A), the major serine/threonine phosphatase in eukaryotic cells, is a h
132 ion C (rdgC) gene encodes an unusual protein serine/threonine phosphatase in that it contains at leas
134 ence for the involvement of a type 1 protein serine/threonine phosphatase in the ultraviolet radiatio
136 h RNA interference (RNAi)-based screening of serine/threonine phosphatases in Drosophila S2 cells, we
137 impaired distribution and lower activity of serine/threonine phosphatases in the context of HIV infe
138 impaired distribution and lower activity of serine/threonine phosphatases in the context of HIV infe
139 ed activity of calcineurin, a Ca2+-dependent serine/threonine phosphatase, increases synaptic express
140 ons show that LTD expression is increased by serine/threonine phosphatase inhibition, and negatively
142 e required for iNOS transcription, while the serine-threonine phosphatase inhibitor (OA) had no effec
143 nadate [PV], phenylarsine oxide [PAO]) and a serine-threonine phosphatase inhibitor (okadaic acid [OA
144 inocytes, the tumor promoter okadaic acid, a serine-threonine phosphatase inhibitor, increased bindin
146 in, prostaglandin E(2), cAMP-raising agents, serine/threonine phosphatase inhibitor and activation of
148 ate, the Ca(2+) ionophore ionomycin, and the serine/threonine phosphatase inhibitor calyculin A incre
150 hibitors citrate and tartrate or the protein serine/threonine phosphatase inhibitor okadaic acid.
151 stimulated by treatment with calyculin A, a serine/threonine phosphatase inhibitor that elevates MLC
152 protein kinases A and C, and okadaic acid (a serine/threonine phosphatase inhibitor) decreased the cu
153 beta(3)-fibrinogen blocker) or okadaic acid (serine/threonine phosphatase inhibitor) dramatically enh
154 reatment of eosinophils with okadaic acid, a serine/threonine phosphatase inhibitor, at the concentra
155 nduction by nickel; however, okadaic acid, a serine/threonine phosphatase inhibitor, induced Cap43 to
156 When cells were lysed in the presence of serine/threonine phosphatase inhibitor, NaF, the PKA-enh
157 cells were treated with okadaic acid (OA), a serine/threonine phosphatase inhibitor, to induce tau ph
158 cose transport stimulated by okadaic acid, a serine/threonine phosphatase inhibitor, was also 45% low
160 nd ex vivo skin and esophagus cultures, with serine/threonine phosphatase inhibitors causes a dramati
161 nt cell cytosol, is resistant to the classic serine/threonine phosphatase inhibitors okadaic acid and
162 Treatment of cells with the cell-permeable serine/threonine phosphatase inhibitors okadaic acid or
164 , an inhibitor of type 1 and type 2A protein serine/threonine phosphatase, inhibits both receptor-ind
165 nd phosphatases modulate GPCR signaling, how serine/threonine phosphatases integrate with G protein s
166 vel cytoskeletal associated protein, proline serine threonine phosphatase interacting protein (PST PI
167 s resulted in the identification of proline, serine, threonine phosphatase interacting protein (PSTPI
168 quence similarity with the PST PIP (proline, serine, threonine phosphatase interacting protein)/CDC15
169 CD2BP1 and its murine ortholog, proline-serine-threonine phosphatase interacting protein (PSTPIP
170 c15 homology family protein PSTPIP2 (proline-serine-threonine phosphatase interacting protein 2), spo
171 ted an interaction between pyrin and proline serine threonine phosphatase-interacting protein 1 (PSTP
172 ression of the F-BAR domain protein, proline serine threonine phosphatase-interacting protein 2 (PSTP
175 f a cytoskeletal-associated protein, proline-serine-threonine phosphatase-interacting protein (PSTPIP
176 h dominant missense mutations in the proline-serine-threonine phosphatase-interacting protein 1 gene
178 d may be a curative option for other proline-serine-threonine phosphatase-interacting protein 1-assoc
179 ich carry a missense mutation in the proline-serine-threonine phosphatase-interacting protein 2 (Pstp
181 pressions of anti-inflammatory IL37, proline-serine-threonine phosphatase-interacting protein 2 (PSTP
183 The mouse Lupo (I282N) mutation in proline-serine-threonine phosphatase-interacting protein 2 (PSTP
184 in phosphatase 2A (PP2A) is a heterotrimeric serine/threonine phosphatase involved in essential cellu
185 tein phosphatase-2A (PP2A) is a multisubunit serine/threonine phosphatase involved in intracellular s
186 of protein phosphatase 2A, a family of major serine/threonine phosphatases involved in regulating cel
189 at protein phosphatase 1 (PP1), a ubiquitous serine/threonine phosphatase, is a novel potent positive
190 phatase 2A (PP2A) is an essential eukaryotic serine/threonine phosphatase known to play important rol
191 urface receptors such as CTLA-4 and CD28 and serine/threonine phosphatases may represent a novel mech
195 to be calcineurin because inhibitors of this serine/threonine phosphatase partially rescue the block
197 nd that PPM1A, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with
198 data suggest that the PPEF family of protein serine/threonine phosphatases plays a specific and conse
199 okine-induced activation of NF-kappaB, while serine-threonine phosphatases posttranscriptionally regu
204 (PKA)-activated inhibitor of type 1 protein serine/threonine phosphatase (PP1), in a yeast two-hybri
205 the factor that activates the type 1 protein serine/threonine phosphatase (PP1), which dephosphorylat
208 ed roles of highly expressed skeletal muscle serine/threonine phosphatases (PP1, PP2A, PP2B, and PP2C
210 ists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzy
213 previously unrecognized requirement for the serine-threonine phosphatase PP2A in the function of T(r
217 to be due to the combined activities of the serine/threonine phosphatase PP2A and the tyrosine phosp
220 cific phosphatase activity that contains the serine/threonine phosphatase PP2A, the tyrosine phosphat
223 c acid, an inhibitor of the major PPP family serine/threonine phosphatases PP2A and protein phosphata
225 suppressed by SCF through phosphorylation of serine/threonine phosphatase (PP2A) and correlated well
228 mised in a strain lacking functional type 2C serine/threonine phosphatases (PP2C), Ptc1 and Ptc3.
230 esent physiological evidence for the protein serine/threonine phosphatase, PP5, as an effector of Rac
232 Here we show that the oncogenic p53-induced serine/threonine phosphatase, PPM1D (or Wip1), dephospho
233 We now identify a potential role for the serine-threonine phosphatase PPM1G in translational regu
235 reen that identifies the PP2A heterotrimeric serine/threonine phosphatases PPP2R2A, PPP2R2D, PPP2R5A,
236 d after conserved regions within the protein-serine/threonine phosphatases (PPs) of the PP1/2A/2B sup
237 rential regulation of okadaic acid-sensitive serine/threonine phosphatases; presumably, these phospha
238 ated at the post-translational level, by the serine-threonine phosphatase protein phosphatase 2A (PP2
239 f oncogenes or the disruption of the general serine-threonine phosphatase protein phosphatase 2A (PP2
242 2Ralpha) and gamma chain and also endogenous serine/threonine phosphatase protein phosphates 1 and/or
243 Inhibition of tyrosine phosphatases and serine/threonine phosphatases protein phosphatase 1 (PP1
244 nomic approach, we have identified a protein serine/threonine phosphatase, protein phosphatase 2A (PP
245 Knockdown of Nqo1 enhanced activity of the serine/threonine phosphatase, protein phosphatase 2A, wh
246 e was also inactivated by treatment with the serine/threonine phosphatase, protein phosphatase 2A; ok
247 ases in Mycobacterium tuberculosis, only one serine/threonine phosphatase, PstP, has been identified.
248 ment of SH2-B with protein phosphatase 2A, a serine/threonine phosphatase, reduces the many forms to
250 A1AT, protein phosphatase 2A (PP2A), a major serine-threonine phosphatase, regulates similar biologic
251 Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase regulating many cellular pr
252 osphatase I (PP1) is an essential eukaryotic serine/threonine phosphatase required for many cellular
254 s appear to be mediated by the activation of serine-threonine phosphatase, since they are blocked by
255 d sodium molybdate) but not by inhibitors of serine/threonine phosphatases (sodium fluoride, okadaic
256 es), the precise role of the co-transcribing serine/threonine phosphatase (SP-STP) has remained enigm
257 ates an important property of eukaryote-type serine/threonine phosphatase (SP-STP) of group A Strepto
258 , how the presence or absence of the cognate serine/threonine phosphatase Stp1 affects Stk1 function
260 tly avoid the taste, is dependent on several serine/threonine phosphatase substrates and the PP1-bind
262 ed by inhibition of all known subfamilies of serine/threonine phosphatases, suggesting that multiple
263 lcineurin is a calcium-calmodulin-regulated, serine-threonine phosphatase that functions as a key ind
264 in (PP2B) is a calcium/calmodulin-activated, serine-threonine phosphatase that transmits signals to t
267 rotein phosphatase 2A (PP2A) is a multimeric serine/threonine phosphatase that carries out multiple f
269 Experiments were performed to identify the serine/threonine phosphatase that dephosphorylates FOXO1
270 d-type p53-induced phosphatase 1 (WIP1) is a serine/threonine phosphatase that dephosphorylates prote
273 ex that binds to and inhibits calcineurin, a serine/threonine phosphatase that is activated by TCR en
274 n phosphatase 2A (PP2A) is a multifunctional serine/threonine phosphatase that is critical to many ce
275 We have recently reported that a protein serine/threonine phosphatase that is designated PP5 and
277 hosphorylation of this site is mediated by a serine/threonine phosphatase that is inhibited by okadai
279 p53-induced phosphatase PPM1D (or Wip1) is a serine/threonine phosphatase that is transcriptionally u
280 stimulates protein phosphatase 2A (PP2A), a serine/threonine phosphatase that modulates essential si
281 rotein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many b
283 Protein phosphatase 2A (PP2A) is a major serine/threonine phosphatase that regulates a wide varie
284 neurin (Cn) is a Ca(2+)/calmodulin-dependent serine/threonine phosphatase that regulates differentiat
285 Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase that regulates many cellula
287 tresses inhibited activity of calcineurin, a serine/threonine phosphatase that regulates NFAT activat
288 osphatase 2A (PP2A) is a family of mammalian serine/threonine phosphatases that is involved in the co
289 e are conserved between different eukaryotic serine/threonine phosphatases, these results should appl
290 Addition of protein phosphatase 1 gamma, a serine/threonine phosphatase, to rat liver cytosol reduc
293 reductase active site has been identified in serine-threonine phosphatases using a descriptor built f
294 diated early events, the activity of protein serine/threonine phosphatases was markedly increased in
295 dentified cancer genes was PPP6C, encoding a serine/threonine phosphatase, which harbored mutations t
296 at PDP1 belongs to the PPM family of protein serine/threonine phosphatases, which, in spite of a low
297 uppressor protein phosphatase 2A (PP2A) is a serine/threonine phosphatase whose activity is inhibited
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.