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1 dly than controls, but not when treated with protein phosphatase.
2 in reduces ERK activity via recruitment of a protein phosphatase.
3 tiate signal transduction inhibiting type 2C protein phosphatases.
4 d analyze the development of drugs targeting protein phosphatases.
5 TPase activation by inhibiting PP2C.D family protein phosphatases.
6 trin homology domain and leucine-rich repeat protein phosphatase 1 (PHLPP1) as a regulatory phosphata
7 trin homology domain and leucine rich repeat protein phosphatase 1 (PHLPP1) is a member of the serine
8 disrupt protein-protein interactions between protein phosphatase 1 (PP1) and its regulator CPI-17, re
9 atase drives this reversal in budding yeast, protein phosphatase 1 (PP1) and protein phosphatase 2A (
15 Here we show in vitro and in Drosophila that Protein Phosphatase 1 (PP1) inactivates Mps1 by dephosph
17 regulatory subunit 1A (PPP1R1A) is a potent protein phosphatase 1 (PP1) inhibitor; however, its role
19 ly, pharmacological or genetic inhibition of protein phosphatase 1 (PP1) prevented HTTex1 aggregation
20 We show that PKA directly phosphorylates the protein phosphatase 1 (PP1) regulatory subunit myosin ph
21 IF2alpha phosphatases comprising a catalytic protein phosphatase 1 (PP1) subunit in complex with a PP
23 he mitotic chromosome periphery and recruits protein phosphatase 1 (PP1) to chromatin at anaphase ons
24 tes with the broadly acting serine/threonine protein phosphatase 1 (PP1) to dephosphorylate eIF2alpha
25 The Ska1 C-terminal domain (CTD) recruits protein phosphatase 1 (PP1) to kinetochores to promote t
27 kinase activity of the IGF-1R by activating protein phosphatase 1 (PP1) to promote dephosphorylation
28 We also demonstrated that functional CK2 and protein phosphatase 1 (PP1) were selectively tethered to
29 ew study, we investigated the interaction of protein phosphatase 1 (PP1) with the SR protein splicing
30 /2 as a positive regulator, whereas purified protein phosphatase 1 (PP1), dephosphorylated Thr-450 in
31 this study we show that Gwl associates with protein phosphatase 1 (PP1), particularly PP1gamma, whic
32 R cytoplasmic domain (cd) and the associated protein phosphatase 1 (PP1), requiring NMDARcd movement,
38 rate specificity of the catalytic subunit of protein phosphatase 1 (PP1c) is dictated by PP1c-interac
39 n MEL-28/ELYS docks the catalytic subunit of protein phosphatase 1 (PP1c) to direct kinetochore disas
42 oduct of which recruits the alpha-isoform of protein phosphatase 1 catalytic subunit (PP1alpha) and e
46 MBS85), paxillin and CPI-17 (PKC-potentiated protein phosphatase 1 inhibitor protein of 17 kDa) phosp
47 etermined the expression and localization of protein phosphatase 1 regulatory inhibitor subunit 11 (P
50 ction closest to the mapped region, PPP1R3B (protein phosphatase 1 regulatory subunit 3B), encodes a
51 nophilin (abbreviated spn; gene name Ppp1r9b protein phosphatase 1 regulatory subunit 9b) and the cla
54 se 5 (Cdk5), glycogen synthase kinase 3beta, protein phosphatase 1, or protein phosphatase 2A, but re
55 131, which affects the expression of ORMDL3, protein phosphatase 1, regulatory inhibitor subunit 1B (
56 between TIBC and a variant near the gene for protein phosphatase 1, regulatory subunit 3B (PPP1R3B; r
57 s dephosphorylation by kinetochore-localized protein phosphatase 1, which allows Cdc20 to activate th
58 neurons, NMDA receptor stimulation induces a protein phosphatase 1-dependent dephosphorylation of CDK
61 T840 dephosphorylation could be blocked by a protein phosphatase 1/2A (PP1/PP2A) inhibitor and was pa
62 brain slices of WKY rats pretreated with the protein phosphatase 1/2A, calcineurin, or casein kinase-
63 ion of the PH domain and leucine-rich repeat protein phosphatases 1 (PHLPP1), a phosphatase of Akt.
65 yrosine phosphatases or the serine/threonine protein phosphatases 1 and 2A decreased Ih at maximal ac
67 ttributed to the intracellular inhibition of protein phosphatases 1/2A due to lack of specific transm
68 sphorylation-dependent mechanism mediated by protein phosphatase-1 (PP1) and dual specificity phospha
69 s mediated at least in part by inhibition of protein phosphatase-1 (PP1c) via persulfidation at Cys-1
71 in phosphatase (MP) holoenzyme consisting of protein phosphatase-1 catalytic subunit (PP1c) and MP ta
75 at involves the phosphatases calcineurin and protein phosphatase-1, as well the serine/threonine kina
80 opsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr pr
82 how the potential of LB100, a small-molecule protein phosphatase 2 A (PP2A) inhibitor, as a monothera
84 2A (PP2A) regulatory subunit B family genes protein phosphatase 2, regulatory Subunit B', beta (PPP2
85 regulatory Subunit B', gamma (PPP2R5C); and protein phosphatase 2, regulatory Subunit B', delta (PPP
86 se 2, regulatory Subunit B', beta (PPP2R5B); protein phosphatase 2, regulatory Subunit B', gamma (PPP
87 BR1) interacted with the B'' subunit of rice protein phosphatase 2A (OsPP2A B'') and underwent revers
88 d sphingolipids are required to activate the protein phosphatase 2A (PP2A(Cdc55)) to attenuate Swe1 p
89 Somatic missense mutations in the Ser/Thr protein phosphatase 2A (PP2A) Aalpha scaffold subunit ge
90 dding yeast, protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) activities have each been
94 ells was associated with a lower activity of protein phosphatase 2A (PP2A) and augmented activity of
95 /ERK and its subsequent dephosphorylation by protein phosphatase 2A (PP2A) and inhibition of focal ad
97 dynamics of PIN proteins are affected by the protein phosphatase 2A (PP2A) and the PINOID kinase, whi
101 un with chromatin is positively regulated by protein phosphatase 2A (PP2A) complexes targeted to c-Ju
102 kinase 1 (RACK1) as the regulatory subunit, protein phosphatase 2A (PP2A) dephosphorylates threonine
104 ly conserved serine (Ser)/threonine-specific protein phosphatase 2A (PP2A) functions as a heterotrime
105 ivation chaperones control the biogenesis of protein phosphatase 2A (PP2A) holoenzymes that contain a
107 Here, we show that overexpression of the protein phosphatase 2A (PP2A) inhibitor protein PME-1 dr
116 de novo mutations revealed four mutations in protein phosphatase 2A (PP2A) regulatory subunit B famil
117 orylation and activation of serine/threonine protein phosphatase 2A (PP2A) regulatory subunit, B56bet
120 in 2 subunits of serine/threonine (Ser/Thr) protein phosphatase 2A (PP2A) were identified in 16 indi
121 ated that activation of the tumor suppressor protein phosphatase 2A (PP2A), a negative regulator of m
122 f key regulators of hepatic gluconeogenesis, protein phosphatase 2A (PP2A), AMP-activated protein kin
124 xes that appear to act through regulation of protein phosphatase 2A (PP2A), but their functions in ma
129 Binding of YAP to MT brings it together with protein phosphatase 2A (PP2A), leading to the dephosphor
130 Exposure of BL41-3 cells to an inhibitor of protein phosphatase 2A (PP2A), okadaic acid, resulted in
131 his study, we show that the tumor suppressor protein phosphatase 2A (PP2A), one of the major Ser/Thr
132 The phosphorylation of Tau is regulated by protein phosphatase 2A (PP2A), which in turn is modulate
136 d Bub1 kinase and the Sgo1-bound phosphatase protein phosphatase 2A (PP2A)-Rts1 underlie a tension-de
145 t, Cdr2-T166 phosphorylation is regulated by protein phosphatase 2A but not by the Sds23-PP6 pathway.
147 this is mediated by metabolic activation of protein phosphatase 2A in complex with the B55beta targe
149 have previously shown that the Dictyostelium protein phosphatase 2A regulatory subunit B56, encoded b
150 cts with protein phosphatase 2A and recruits protein phosphatase 2A with glycogen synthase kinase 3be
151 (armadillo/huntingtin, elongation factor 3, protein phosphatase 2A, and the yeast kinase TOR1) or BE
152 named after Huntingtin, elongation factor 3, protein phosphatase 2A, and yeast kinase TOR1) repeat.
153 hase kinase 3beta, protein phosphatase 1, or protein phosphatase 2A, but reduces p35 subunit of Cdk5.
154 ties of tau kinases and phosphatases such as protein phosphatase 2A, irrespective of fisetin treatmen
155 more, we show that a novel host cell factor, protein phosphatase 2A, is involved in NS2 dephosphoryla
156 f six (A-F) Huntingtin, elongation factor 3, protein phosphatase 2A, target of rapamycin (HEAT) repea
158 stead, both agents increased the activity of protein phosphatase 2A, which inactivates protein kinase
160 ase-mediated restriction of synthesis of the protein phosphatase 2A-A (PP2A-A), a key factor that fac
167 ion were reduced in TRAIL(-/-) mice, whereas protein phosphatase 2Ac levels were increased compared w
168 to and deactivates the catalytic subunit of protein phosphatase 2Ac, resulting in increased nuclear
169 kinase A (PKA), protein kinase C (PKC), and protein phosphatase 2B (calcineurin) to modulate second
170 in the non-miR-185 targets serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform,
171 ibitors of NMDA-type glutamate receptors and protein phosphatase 2B prevented depolarization-induced
173 itory and RelA phosphatase activities of the protein phosphatase 2C (PP2C) phosphatase family member,
174 , together with a plant-specific subclade of protein phosphatase 2C (PP2C), form functional holorecep
176 and Brassica napus gene paralogues encoding protein phosphatase 2C (PP2C, group A), which is known t
178 ors, which alleviates negative regulation by protein phosphatases 2C (PP2Cs) of the protein kinase OP
179 eventing its inhibitory dephosphorylation by protein phosphatase-2C rather than inducing de novo kina
181 e the cellular phosphatase catalytic subunit protein phosphatase 4C (PP4C) in the regulation of this
185 al differentially expressed proteins, namely protein phosphatase 5 (PP5), formyl peptide receptor 2,
186 y, when paired with the deactivation of a GR-protein phosphatase 5 pathway, resulted in sustained GR
188 etion of protein phosphatase 2A (PP2A) or of protein phosphatase 6 (PP6) protects cells from the redu
189 -A, DNA-PK catalytic subunit (DNA-PKcs), and protein phosphatase 6 (PP6), which interacts with DNA-PK
193 Two of them belong to clade A of type 2C protein phosphatases: ABA-HYPERSENSITIVE GERMINATION 1 (
194 hree Clade E Growth-Regulating (EGR) Type 2C protein phosphatases act as negative growth regulators t
195 N function in ICL repair is dependent on its protein phosphatase activity and ability to be SUMOylate
196 of phosphate and tensin homolog through its protein phosphatase activity and that the increase in IN
197 Here we report inherited dysregulation of protein phosphatase activity as a cause of intellectual
198 d concomitant with a significant increase in protein phosphatase activity for two colon cancer cell l
199 iety of PTEN mutant constructs, we show that protein phosphatase activity of PTEN targets PTK6, with
200 A Deltacdc55 mutation affecting Cdc55-PP2A protein phosphatase activity prevented Orm dephosphoryla
201 of 709 genes, among which genes involved in protein phosphatase activity were overrepresented, sugge
204 ence that DOG1 can interact with the type 2C protein phosphatases AHG1 and AHG3 and that this represe
205 d erbB4 and decreased receptor-type tyrosine-protein phosphatase-alpha (RPTPalpha) and dysbindin-1, e
206 n inducible model of loss of function of the protein phosphatase and tensin homologue (PTEN), a phosp
207 lated Pah1 was a substrate for the Nem1-Spo7 protein phosphatase and was degraded by the 20S proteaso
208 annels, membrane receptors, protein kinases, protein phosphatases and proteins of unknown function.
210 ely, suppressor of cytokine signaling (SOCS) proteins, phosphatases, and protein inhibitor of activat
211 nvolvement of specific calcineurin isoforms, protein phosphatase at 14D (Pp2B-14D)/calcineurin A at 1
213 strongly associated with proteolysis of the protein phosphatase calcineurin (CN) and the elevated ex
214 gically blocked by antagonists of either the protein phosphatase calcineurin or neurotensin receptors
215 av activates the Ca(2+)/calmodulin-dependent protein phosphatase calcineurin, which is essential for
218 Application of AID to the calcium-regulated protein phosphatase, calcineurin, revealed functions in
219 genetics to show that the calcium-regulated protein phosphatase, calcinuerin, regulates invasion in
220 nhibition of activities of PP2A or PP2A-like protein phosphatases can increase transcript levels of s
221 kinases phosphorylate client proteins, while protein phosphatases catalyze their dephosphorylation an
223 ) or control of RPA phosphorylation (the PP4 protein phosphatase complex) are not recruited to the ge
225 ted this specificity and found that distinct protein phosphatases counteract Ssp1 activity toward its
227 PRR complexes are under tight control by protein phosphatases, E3 ligases, and other regulatory p
229 on of Gadd34 (Ppp1r15A),which targets type 1 protein phosphatase for dephosphorylation of eIF2alpha-P
230 rypanosoma brucei, as the translocation of a protein phosphatase from the cytosol forms part of a cru
231 horylated ABI5 may prevent PP2A or PP2A-like protein phosphatases from removing the phosphate from AB
232 rstanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of kno
233 e characterize a mitochondrial IMS-localized protein phosphatase identified in photosynthetic eukaryo
234 us on comprehensively identifying and naming protein phosphatases in available apicomplexan genomes,
236 vity by interacting with casein kinase-2 and protein phosphatases in the hypothalamus and that imbala
238 presence of micromolar concentrations of the protein phosphatase inhibitor okadaic acid, implicating
242 nd PP6, are multifunctional serine/threonine protein phosphatases involved in many cellular processes
244 persensitive germination3 (AHG3), encoding a protein phosphatase, is specifically transcribed in the
245 kt and PHLPP1 (PH domain leucine-rich repeat protein phosphatase isoform 1), a Ser473-specific Akt ph
246 ent kinase (Cdk) 1 while activities of major protein phosphatases, like PP1 and PP2A, appear directly
250 endent engagement of specific members of the protein phosphatase metallo-dependent (PPM/PP2C) family
251 ne carboxyl methyltransferase 1 (LCMT-1) and protein phosphatase methylesterase 1 (PME-1) and regulat
252 ce that overexpress the PP2A methylesterase, protein phosphatase methylesterase-1 (PME-1), or the PP2
254 he phosphatase PH domain leucine-rich repeat protein phosphatase (PHLPP) downstream of PTEN is highly
255 eckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP) suppresses receptor tyrosine
256 onstrated that PH domain leucine-rich repeat protein phosphatase (PHLPP), a novel family of Ser/Thr p
258 eins via hyperactivation of the Mn-dependent protein phosphatase PhpP, a key enzyme involved in the r
261 osphatase (PHLPP), a novel family of Ser/Thr protein phosphatases, plays an important role in regulat
262 copy (MS) analysis, which identified several protein phosphatases (PP), including PP2A A and C subuni
263 hat balances the activities of SRPK1 and the protein phosphatase PP1, thereby regulating the phosphor
265 its positive functional influence on type I protein phosphatase (PP1), likely resulting in negative
269 ced obesity via a mechanism involving type 2 protein phosphatase (PP2A) dephosphorylation of endothel
270 caffolding A subunit of the serine/threonine protein phosphatase, PP2A, and that phosphorylation of A
271 tor of certain forms of the serine/threonine protein phosphatase, PP2A, when phosphorylated by the ki
272 ys were used to assess the expression of the protein phosphatase PP5 in endobronchial biopsies and AS
276 kinome have been reported, the roles of most protein phosphatases (PPs) during Plasmodium development
277 ca mutant plants, revealing that active PP2C protein phosphatases protect and stabilize RopGEF1 from
280 pathways and disease pathologies, targeting protein phosphatases remains an underexplored opportunit
281 EMENT In the present study, we show that the protein phosphatase Shp2 is an important mediator of oli
282 GULATORY COMPONENT OF ABA RECEPTORS, TYPE 2C PROTEIN PHOSPHATASE Sucrose non-fermenting1-related prot
283 ed in photosynthetic eukaryotes as well as a protein phosphatase target of the highly conserved eukar
285 sphorylation by inhibiting the activity of a protein phosphatase that constitutively dephosphorylates
286 dc55) is a highly conserved serine-threonine protein phosphatase that is involved in diverse cellular
287 hosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondria
288 pyruvate dehydrogenase kinase, and a type 2C protein phosphatase that may catalyze the dephosphorylat
289 m- and calmodulin-dependent serine/threonine protein phosphatase that plays a role in a wide range of
290 ly conserved transcriptional coactivator and protein phosphatase that plays vital roles in multiple d
291 y establish a functional precedent for CDC25 protein phosphatases that lies outside of their canonica
292 ancy pathways converge at clade A of type 2C protein phosphatases.The DOG1 protein is a major regulat
293 tly reported that EYA1 functions as a unique protein phosphatase to dephosphorylate Myc at pT58 to re
296 ecipitation experiments demonstrated loss of protein phosphatases type 1 and type 2 from the RyR comp
298 ations is suppressed by inactivation of PhpP protein phosphatase, which concomitantly restores protei
299 enously phosphorylated Pah1 by the Nem1-Spo7 protein phosphatase, which is highly specific for the si
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