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1 4 (PP4; also called PPX and PPP4), a serine/threonine phosphatase.
2 with protein phosphatase 2A (PP2A), a serine/threonine phosphatase.
3 catalytic subunit of a type 1 protein serine/threonine phosphatase.
4 t the activity of PP2A, another major serine/threonine phosphatase.
5 hosphatase and a protein phosphatase 2A-like threonine phosphatase.
6 trols a serine/threonine kinase and a serine/threonine phosphatase.
7 ovel PKC isozyme and a bFGF-dependent serine/threonine phosphatase.
8 losporin-sensitive, calcium-regulated serine/threonine phosphatase.
9 is a highly conserved and ubiquitous serine/threonine phosphatase.
10 ture-function studies of this protein serine/threonine phosphatase.
11 during platelet aggregation activates serine/threonine phosphatases.
12 members of the PP2C class of protein serine/threonine phosphatases.
13 ut the expression and function of the serine-threonine phosphatases.
14 te with members of the PP2A family of serine/threonine phosphatases.
15 th calyculin A, a potent inhibitor of serine/threonine phosphatases.
16 P2A) is a member of the intracellular serine/threonine phosphatases.
17 A), an abundantly expressed family of serine-threonine phosphatases.
18 D was rapidly dephosphorylated by the serine-threonine phosphatase 1 alpha, and localized in the mito
19 on of mitotic FAK in vitro by protein serine/threonine phosphatase 1 restores the ability of FAK to a
20 In the cortex, mRNAs for neuronal tyrosine/threonine phosphatase 1, and microtubule-associated tau
22 otably, genetic disruption of protein serine/threonine phosphatase-1 (PP1) and its regulator NIPP1 de
23 in vivo evidence to show that protein serine/threonine phosphatase-1 is a major phosphatase that dire
24 ctive site is highly conserved in the serine/threonine phosphatase-1 subfamily, but not in the serine
25 P2R1A encodes a regulatory subunit of serine/threonine phosphatase 2, and ARID1A encodes adenine-thym
28 ing experiments indicate that protein serine/threonine phosphatase 2A (PP2A) can dephosphorylate thes
29 indicates that regulation of protein-serine/threonine phosphatase 2A (PP2A) involves its association
33 metric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in which
34 nase cascades, heterotrimeric protein serine/threonine phosphatase 2A (PP2A), is composed of catalyti
35 hown to stably associate with protein serine/threonine phosphatase 2A (PP2A), which was proposed to p
38 eam repressor COUP-TFII by inhibiting serine/threonine phosphatase 2A activity, and that decreased CO
39 nase 2 activity and increased protein serine/threonine phosphatase 2A activity, resulting in an incre
40 protein HOX11 interacted with protein serine-threonine phosphatase 2A catalytic subunit (PP2AC), as w
41 s control the activity of the protein serine/threonine phosphatase 2A catalytic subunit (PP2Ac), incl
42 Casein kinase 2 catalyzed protein serine/threonine phosphatase 2A phosphorylation thereby inhibit
46 EGCG can negatively regulate protein serine/threonine phosphatase-2A (PP-2A) to positively regulate
52 ding purple acid phosphatase, protein serine/threonine phosphatases, 5'-nucleotidase, and DNA repair
53 pitated c-Fos protein with the type 2 serine/threonine phosphatase A (PP2A) and immunoblotting of c-F
56 e transactivation, tyrosine phosphatase, and threonine phosphatase activities in their function as pa
58 -free cell lysates, we find increased serine/threonine phosphatase activity associated with Golgi-enr
61 tination of proteins, we examined the serine/threonine phosphatase activity in our CAOV3 cells follow
63 of Eya1 to the nucleus, where Eya1 uses its threonine phosphatase activity to control Myc phosphoryl
64 by KCC2 is completely independent of serine-threonine phosphatase activity, suggesting that these tw
65 een shown to have modest tyrosine and serine/threonine phosphatase activity, we find that it is much
66 expressed in mammalian cells exhibit serine-threonine phosphatase activity, which requires Mn2+ and
70 ing PP1cgamma, a catalytic subunit of serine/threonine phosphatase, alpha(IIb)beta3 failed to dephosp
72 tingly, okadaic acid, an inhibitor of serine/threonine phosphatase, also strongly activated transcrip
73 t protein phosphatase 1) is a protein-serine/threonine phosphatase and a negative regulator of the PI
75 ase C (PKC) activation, inhibition of serine/threonine phosphatase, and an active protein tyrosine ph
76 phatase-2A (PP2A), a widely expressed serine/threonine phosphatase, and the heterotrimeric G protein
77 ing several tyrosine phosphatases and serine/threonine phosphatases, and it suppresses the cell growt
78 applicable to other DUSPs and protein-serine/threonine phosphatases, and the substrate specificity da
79 otein phosphatase 2A (PP2A) family of serine-threonine phosphatases, and this interaction is required
83 phosphoprotein phosphatase family of serine/threonine phosphatases are thought to exist in different
84 osphatase-1 (PP1), a major eukaryotic serine/threonine phosphatase, are defined by the association of
85 ), potent and selective inhibitors of serine threonine phosphatases, are of interest for their antitu
86 In this review, we present protein serine/threonine phosphatases as viable therapeutic targets, di
87 cells, we identify PP2A as the first serine/threonine phosphatase associated with the multiprotein T
88 phatase 4 (PP4), a novel PP2A-related serine/threonine phosphatase, at a 50% inhibitory concentration
89 ined the regulatory interactions of a serine/threonine phosphatase (BA-Stp1), serine/threonine kinase
91 cells, it was determined that PP2A, a serine/threonine phosphatase, binds and dephosphorylates Rb2/p1
94 1) cell cycle arrest, implicating the serine/threonine phosphatase calcineurin as one Ca(2+)/CaM-depe
95 ) and the Ca(2+)/calmodulin-activated serine/threonine phosphatase calcineurin exist and play a role
97 e revealed that the calcium-dependent serine/threonine phosphatase calcineurin mediates the effects o
98 tion is modulated by Ca(2+)-dependent serine/threonine phosphatase calcineurin, an important target o
99 o explore the redox regulation of the serine/threonine phosphatase calcineurin, we have investigated
106 discovered to be an inhibitor of the serine/threonine phosphatase, calcineurin, and its signaling pa
108 and treatment of cRaf-1 with protein (serine/threonine) phosphatases can deactivate it, at least part
109 ent of CKIepsilon with any of several serine/threonine phosphatases causes a marked increase in kinas
111 (PP2A) is a family of multifunctional serine/threonine phosphatases consisting of a catalytic C, a st
112 hatase-1, revealed that this class of serine/threonine phosphatases contain in their putative active
113 (PP2A) is an abundant heterotrimeric serine/threonine phosphatase containing highly conserved struct
114 ation and PDZ-mediated formation of a serine/threonine phosphatase-containing complex by syndecan-4 a
115 in view of literature suggesting that serine/threonine phosphatases could be subject to redox control
118 the dephosphorylation events via the serine/threonine phosphatases during the integrin outside-in si
119 nlike kinases, it remains unclear how serine/threonine phosphatases engage the signaling networks tha
121 ubiquitously expressed member of the serine-threonine phosphatase family that is involved in regulat
123 We have identified a novel type 2C serine-threonine phosphatase, FIN13, whose expression is induce
124 rprisingly, this structure revealed a serine/threonine phosphatase fold that unexpectedly targets tyr
125 omologue of the PPM family of protein-serine/threonine phosphatases found in all eukaryotes as well a
127 ene for a putative PPP family protein-serine/threonine phosphatase from the microcystin-producing cya
128 (ORFs) encoding two potential protein-serine/threonine phosphatases from the cyanobacterium Synechocy
131 phosphatase X (PPX)), a PP2A-related serine/threonine phosphatase, has been shown to be involved in
134 ere we provide evidence that ppm-1, a serine/threonine phosphatase homologous to human PP2Calpha(PPM1
136 haromyces cerevisiae, is an essential serine/threonine phosphatase implicated in the regulation of a
137 tein phosphatase 2A (PP2A), the major serine/threonine phosphatase in eukaryotic cells, is a heterotr
138 rdgC) gene encodes an unusual protein serine/threonine phosphatase in that it contains at least two E
140 r the involvement of a type 1 protein serine/threonine phosphatase in the ultraviolet radiation-induc
141 In this review, we concentrate on serine/threonine phosphatases in apicomplexan parasites, with t
142 nterference (RNAi)-based screening of serine/threonine phosphatases in Drosophila S2 cells, we identi
143 hosphatase 2A (PP2A), one of the main serine-threonine phosphatases in mammalian cells, maintains cel
144 vity of calcineurin, a Ca2+-dependent serine/threonine phosphatase, increases synaptic expression of
145 w that LTD expression is increased by serine/threonine phosphatase inhibition, and negatively regulat
147 red for iNOS transcription, while the serine-threonine phosphatase inhibitor (OA) had no effect on iN
148 [PV], phenylarsine oxide [PAO]) and a serine-threonine phosphatase inhibitor (okadaic acid [OA]).
149 staglandin E(2), cAMP-raising agents, serine/threonine phosphatase inhibitor and activation of protei
151 e Ca(2+) ionophore ionomycin, and the serine/threonine phosphatase inhibitor calyculin A increased Se
154 ated by treatment with calyculin A, a serine/threonine phosphatase inhibitor that elevates MLC phosph
155 kinases A and C, and okadaic acid (a serine/threonine phosphatase inhibitor) decreased the current c
156 -fibrinogen blocker) or okadaic acid (serine/threonine phosphatase inhibitor) dramatically enhanced E
157 t of eosinophils with okadaic acid, a serine/threonine phosphatase inhibitor, at the concentrations t
158 s, the tumor promoter okadaic acid, a serine-threonine phosphatase inhibitor, increased binding of ac
159 n by nickel; however, okadaic acid, a serine/threonine phosphatase inhibitor, induced Cap43 to a grea
160 n cells were lysed in the presence of serine/threonine phosphatase inhibitor, NaF, the PKA-enhancing
161 ere treated with okadaic acid (OA), a serine/threonine phosphatase inhibitor, to induce tau phosphory
162 ansport stimulated by okadaic acid, a serine/threonine phosphatase inhibitor, was also 45% lower with
165 ivo skin and esophagus cultures, with serine/threonine phosphatase inhibitors causes a dramatic incre
167 cytosol, is resistant to the classic serine/threonine phosphatase inhibitors okadaic acid and microc
168 ment of cells with the cell-permeable serine/threonine phosphatase inhibitors okadaic acid or calycul
169 Treatment of erythroid cells with serine and threonine phosphatase inhibitors stimulated the hyperpho
171 hibitor of type 1 and type 2A protein serine/threonine phosphatase, inhibits both receptor-induced ac
172 phatases modulate GPCR signaling, how serine/threonine phosphatases integrate with G protein signalin
173 oskeletal associated protein, proline serine threonine phosphatase interacting protein (PST PIP), via
174 ed in the identification of proline, serine, threonine phosphatase interacting protein (PSTPIP), a no
175 2BP1 and its murine ortholog, proline-serine-threonine phosphatase interacting protein (PSTPIP1), are
176 ology family protein PSTPIP2 (proline-serine-threonine phosphatase interacting protein 2), spontaneou
177 imilarity with the PST PIP (proline, serine, threonine phosphatase interacting protein)/CDC15 family
178 oskeletal-associated protein, proline-serine-threonine phosphatase-interacting protein (PSTPIP), whos
179 interaction between pyrin and proline serine threonine phosphatase-interacting protein 1 (PSTPIP1), t
180 ant missense mutations in the proline-serine-threonine phosphatase-interacting protein 1 gene (PSTPIP
181 Missense mutation in the proline-serine-threonine phosphatase-interacting protein 2 (Pstpip2) ge
182 Missense mutation (L98P) of proline-serine-threonine phosphatase-interacting protein 2 (Pstpip2) in
183 ouse Lupo (I282N) mutation in proline-serine-threonine phosphatase-interacting protein 2 (PSTPIP2) le
184 ns of anti-inflammatory IL37, proline-serine-threonine phosphatase-interacting protein 2 (PSTPIP2), a
185 of the F-BAR domain protein, proline serine threonine phosphatase-interacting protein 2 (PSTPIP2), l
187 utations in the gene encoding proline serine threonine phosphatase-interacting protein-1 (PSTPIP1) ha
188 phatase 2A (PP2A) is a heterotrimeric serine/threonine phosphatase involved in essential cellular fun
189 osphatase-2A (PP2A) is a multisubunit serine/threonine phosphatase involved in intracellular signalin
190 ein phosphatase 2A, a family of major serine/threonine phosphatases involved in regulating cell proli
191 The multifunctional activity of many serine/threonine phosphatases is achieved through their associa
192 ein phosphatase 1 (PP1), a ubiquitous serine/threonine phosphatase, is a novel potent positive physio
194 2A (PP2A) is an essential eukaryotic serine/threonine phosphatase known to play important roles in c
195 receptors such as CTLA-4 and CD28 and serine/threonine phosphatases may represent a novel mechanism f
196 ne-Threonine)-rich transactivation domain, a threonine phosphatase motif (TPM), and a tyrosine protei
198 Addition of the inhibitor-of-protein serine/threonine phosphatases, okadaic acid, blocks the ATRA-me
200 alcineurin because inhibitors of this serine/threonine phosphatase partially rescue the block to adip
203 PPM1A, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with and dep
204 ggest that the PPEF family of protein serine/threonine phosphatases plays a specific and conserved ro
205 nduced activation of NF-kappaB, while serine-threonine phosphatases posttranscriptionally regulate iN
210 activated inhibitor of type 1 protein serine/threonine phosphatase (PP1), in a yeast two-hybrid scree
211 tor that activates the type 1 protein serine/threonine phosphatase (PP1), which dephosphorylates eIF-
214 s of highly expressed skeletal muscle serine/threonine phosphatases (PP1, PP2A, PP2B, and PP2C) on AS
216 stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzymes tha
220 due to the combined activities of the serine/threonine phosphatase PP2A and the tyrosine phosphatase
222 usly unrecognized requirement for the serine-threonine phosphatase PP2A in the function of T(reg) cel
224 hosphatase activity that contains the serine/threonine phosphatase PP2A, the tyrosine phosphatase HeP
228 an inhibitor of the major PPP family serine/threonine phosphatases PP2A and protein phosphatase 1 (P
229 sed by SCF through phosphorylation of serine/threonine phosphatase (PP2A) and correlated well with fe
235 hysiological evidence for the protein serine/threonine phosphatase, PP5, as an effector of Rac GTPase
237 e show that the oncogenic p53-induced serine/threonine phosphatase, PPM1D (or Wip1), dephosphorylates
238 now identify a potential role for the serine-threonine phosphatase PPM1G in translational regulation
240 at identifies the PP2A heterotrimeric serine/threonine phosphatases PPP2R2A, PPP2R2D, PPP2R5A, and PP
241 conserved regions within the protein-serine/threonine phosphatases (PPs) of the PP1/2A/2B superfamil
242 regulation of okadaic acid-sensitive serine/threonine phosphatases; presumably, these phosphatases a
243 enes or the disruption of the general serine-threonine phosphatase protein phosphatase 2A (PP2A) can
245 the post-translational level, by the serine-threonine phosphatase protein phosphatase 2A (PP2A).
247 ) and gamma chain and also endogenous serine/threonine phosphatase protein phosphates 1 and/or 2A act
248 hibition of tyrosine phosphatases and serine/threonine phosphatases protein phosphatase 1 (PP1), PP2A
249 pproach, we have identified a protein serine/threonine phosphatase, protein phosphatase 2A (PP2A), as
250 lso inactivated by treatment with the serine/threonine phosphatase, protein phosphatase 2A; okadaic a
252 SH2-B with protein phosphatase 2A, a serine/threonine phosphatase, reduces the many forms to two.
254 rotein phosphatase 2A (PP2A), a major serine-threonine phosphatase, regulates similar biologic proces
255 n phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase regulating many cellular processes
256 se I (PP1) is an essential eukaryotic serine/threonine phosphatase required for many cellular process
258 r to be mediated by the activation of serine-threonine phosphatase, since they are blocked by low dos
259 m molybdate) but not by inhibitors of serine/threonine phosphatases (sodium fluoride, okadaic acid, a
260 e precise role of the co-transcribing serine/threonine phosphatase (SP-STP) has remained enigmatic.
261 important property of eukaryote-type serine/threonine phosphatase (SP-STP) of group A Streptococcus
262 he presence or absence of the cognate serine/threonine phosphatase Stp1 affects Stk1 function and GBS
264 id the taste, is dependent on several serine/threonine phosphatase substrates and the PP1-binding pro
265 nhibition of all known subfamilies of serine/threonine phosphatases, suggesting that multiple phospha
268 phosphatase 2A (PP2A) is a multimeric serine/threonine phosphatase that carries out multiple function
271 p53-induced phosphatase 1 (WIP1) is a serine/threonine phosphatase that dephosphorylates proteins in
272 in is a calcium-calmodulin-regulated, serine-threonine phosphatase that functions as a key inducer of
273 Calcineurin is a calcium-dependent, serine/threonine phosphatase that functions as a signaling inte
275 binds to and inhibits calcineurin, a serine/threonine phosphatase that is activated by TCR engagemen
276 hatase 2A (PP2A) is a multifunctional serine/threonine phosphatase that is critical to many cellular
277 have recently reported that a protein serine/threonine phosphatase that is designated PP5 and contain
279 ylation of this site is mediated by a serine/threonine phosphatase that is inhibited by okadaic acid
281 uced phosphatase PPM1D (or Wip1) is a serine/threonine phosphatase that is transcriptionally upregula
282 ates protein phosphatase 2A (PP2A), a serine/threonine phosphatase that modulates essential signaling
283 phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many biologic
284 tein phosphatase 2A (PP2A) is a major serine/threonine phosphatase that regulates a wide variety of c
285 (Cn) is a Ca(2+)/calmodulin-dependent serine/threonine phosphatase that regulates differentiation-spe
286 n phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase that regulates many cellular proce
287 inhibited activity of calcineurin, a serine/threonine phosphatase that regulates NFAT activation.
288 B) is a calcium/calmodulin-activated, serine-threonine phosphatase that transmits signals to the nucl
289 se 2A (PP2A) is a family of mammalian serine/threonine phosphatases that is involved in the control o
290 onserved between different eukaryotic serine/threonine phosphatases, these results should apply to al
291 ion of protein phosphatase 1 gamma, a serine/threonine phosphatase, to rat liver cytosol reduced acti
294 se active site has been identified in serine-threonine phosphatases using a descriptor built from the
295 early events, the activity of protein serine/threonine phosphatases was markedly increased in the cel
296 ed cancer genes was PPP6C, encoding a serine/threonine phosphatase, which harbored mutations that clu
297 belongs to the PPM family of protein serine/threonine phosphatases, which, in spite of a low level o
298 phosphatase-2A (PP2A) is an abundant serine/threonine phosphatase with anti-inflammatory activity.
299 PX or PPP4) is a PP2A-related protein serine/threonine phosphatase with important roles in a variety
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