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1 PP1 also associates with NCX1; however, the molecular ba
2 PP1 binds multiple motifs of DNA-PKcs, regulates DNA-PKc
3 PP1 dephosphorylates an Spt5 carboxy-terminal repeat (CT
4 PP1 dephosphorylates key CDC7 and CDK2 kinase substrates
5 PP1 first reactivates PP2A-B55; this enables PP2A-B55 in
6 PP1 inhibition involves metal center oxidation rather th
7 PP1 is delivered by the evolutionarily conserved tail of
8 PP1 pharmacological inhibitors would thus not be able to
9 PP1 plays critical roles in many essential physiological
10 PP1 recruitment to human, mitotic PP2A-B56 holoenzymes a
11 PP1 therefore facilitates the metaphase-to-anaphase tran
12 PP1-mediated dephosphorylation of Mps1 occurs at kinetoc
13 ow are underpinned by protein phosphatase 1 (PP1) activity, the inhibition of which extends readthrou
14 interactions between protein phosphatase 1 (PP1) and its regulator CPI-17, resulted in a reversible
15 vidence suggests that protein phosphatase 1 (PP1) and other protein phosphatases modulate NCC phospho
16 sal in budding yeast, protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) activities have e
18 F1 mutants that block Protein Phosphatase 1 (PP1) binding activated telomeric origins but did not elo
20 The serine-threonine protein phosphatase 1 (PP1) deactivates this pathway whereas prolonging eIF2alp
22 nd in Drosophila that Protein Phosphatase 1 (PP1) inactivates Mps1 by dephosphorylating its T-loop.
23 tment of GCs with the protein phosphatase 1 (PP1) inhibitor tautomycin increased phosphorylation of Y
24 (PPP1R1A) is a potent protein phosphatase 1 (PP1) inhibitor; however, its role in tumor development i
27 genetic inhibition of protein phosphatase 1 (PP1) prevented HTTex1 aggregation in both human cells an
28 ly phosphorylates the protein phosphatase 1 (PP1) regulatory subunit myosin phosphatase targeting sub
29 omprising a catalytic protein phosphatase 1 (PP1) subunit in complex with a PPP1R15-type regulatory s
32 eriphery and recruits protein phosphatase 1 (PP1) to chromatin at anaphase onset, in a similar manner
33 cally, Dok3 recruited protein phosphatase 1 (PP1) to dephosphorylate Card9, an essential player in in
35 domain (CTD) recruits protein phosphatase 1 (PP1) to kinetochores to promote timely anaphase onset [1
36 ature localization of protein phosphatase 1 (PP1) to kinetochores, which antagonizes Ipl1-mediated ph
38 IGF-1R by activating protein phosphatase 1 (PP1) to promote dephosphorylation of inhibitory Ser/Thr
39 ed the interaction of protein phosphatase 1 (PP1) with the SR protein splicing factor (SRSF1) to unde
41 t Gwl associates with protein phosphatase 1 (PP1), particularly PP1gamma, which mediates the dephosph
42 d) and the associated protein phosphatase 1 (PP1), requiring NMDARcd movement, and persistently reduc
43 The metalloenzyme protein phosphatase 1 (PP1), which is responsible for >=50% of all dephosphoryl
44 are both regulated by protein phosphatase 1 (PP1), which silences the SAC and stabilizes kinetochore-
49 is sufficient to bind protein phosphatase 1 (PP1)alpha, a ubiquitously expressed phosphatase in the p
52 leasable version of a protein phosphatase-1 (PP1)-disrupting peptide (PDP-Nal) that triggers protein
53 Serine/threonine protein phosphatase type-1 (PP1), a major phosphatase in the heart, consists of a ca
55 yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine (1NA-PP1) and 1-(tert-butyl)-3-(2-methylbenzyl)-1H-pyrazolo[3
58 highly specific pharmacologic inhibitor (1NM-PP1) of Ret also caused a substantial reduction in pulpa
59 ld be blocked by a protein phosphatase 1/2A (PP1/PP2A) inhibitor and was partly blocked by a NMDA rec
60 yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine (2MB-PP1) but not by other 4-amino-5-(4-methylphenyl)-7-(t-bu
64 nase activity by administration of 1NMPP1, a PP1 derivative, and 2) smooth muscle-specific BDNF knock
66 st that I-2, despite its assumed action as a PP1 inhibitor, is a positive regulator of PP1 function i
69 th a metabolic labeling method, we defined a PP1/2A-sensitive phosphorylation site at Thr-48 in human
70 ctivation of PP2A-B56 by dephosphorylating a PP1-docking site in PP2A-B56, thereby promoting the recr
73 he waning of stress responses and requires a PP1 catalytic subunit and a regulatory subunit, PPP1R15A
75 4) is induced downstream of ATF4, binds to a PP1-targeting subunit GADD34 at the endoplasmic reticulu
76 reases upon PP1 depletion, consistent with a PP1 function in termination first uncovered in yeast.
77 cal, yet novel mechanism, interacting with a PP1 pocket that is engaged only by these two PP1 regulat
78 C phosphorylation, but little is known about PP1's role and the mechanism regulating its function in
81 we demonstrate that Rif1 is a high-affinity PP1 adaptor, able to out-compete the well-established PP
83 ed regulation between CaMKII (activator) and PP1 (inhibitor) and then the model performance was valid
85 ugh the interactions of Ng, CaM, CaMKII, and PP1, providing a mechanism to precisely control the sens
88 between kinetochore localization of Ipl1 and PP1, a balance that is essential for accurate meiotic ch
89 ernary complex comprised of SHOC2, MRAS, and PP1 (SHOC2 complex) functions as a RAF S259 holophosphat
90 in-of-function mutations in SHOC2, MRAS, and PP1 that promote complex formation are found in Noonan s
91 uggest that PKA-mediated phosphorylation and PP1/PP2A-dependent dephosphorylation of the alpha2 subun
100 lve the crystal structure of the human ASPP2/PP1 complex and show that ASPP2 recruits PP1 using both
101 ubR1-associated PP2A, unlike KNL1-associated PP1, plays a significant role in end-on conversion.
106 he ASPP2 SH3 domain can discriminate between PP1 isoforms using an acidic specificity pocket in the n
107 data also reveal that Ki-67 and RepoMan bind PP1 using an identical, yet novel mechanism, interacting
108 NA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allo
115 n of HTTex1 single phosphorylation events by PP1 could constitute an efficient and direct molecular t
116 ibutor to suppression of memory formation by PP1 may provide a novel therapeutic target for memory-re
117 enzymes and the sequences of these conserved PP1-docking motifs suggest that PP1 regulates PP2A-B55 a
118 regulated by CDK1-cyclin B and counteracting PP1 and PP2A family phosphatases through modulation of b
123 The PNUTS W401A mutation, which disrupts PP1 binding, causes genome-wide acceleration of transcri
124 g PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzym
128 hat in anaphase, when the spindle elongates, PP1/Repo-Man promotes the accumulation of NuMA at the co
134 M1 metal loading and loss are essential for PP1 regulation in cells, which has broad implications fo
135 n in cells, which has broad implications for PP1 maturation, activity, and holoenzyme subunit exchang
137 a adaptation pathway by inhibition of Gadd34-PP1 phosphatase with guanabenz protects oligodendrocytes
138 o signalling triggers assembly of the GADD34/PP1 complex in a negative feedback loop to inhibit Yap a
139 tion of the eIF2alpha holophosphatase GADD34:PP1, increases the phosphorylation of eIF2alpha in Schwa
141 2, HR37, and HR46) that in addition to HR40 (PP1) from our previous study, have been determined to ha
145 in PP1c-R-subunit interactions, which impair PP1 targeting to proteins involved in electrical and Ca(
148 that the major effect of RSK-2 is to inhibit PP1 rather than to directly phosphorylate YB-1 on Ser(10
149 rupting Dok3-Card9 interaction or inhibiting PP1 activity represents therapeutic opportunities to dev
150 erived from the promiscuous kinase inhibitor PP1 to search for analogs that could potentially target
152 4 at the endoplasmic reticulum, and inhibits PP1 activity to increase eIF2alpha phosphorylation and A
153 (low dose inhibits PP2A; high dose inhibits PP1) delayed AS160 Ser(588) (both doses) and Thr(642) (h
155 ied by a second metal (M1) being loaded into PP1, as free metal cannot dissociate the complex and M1-
156 estruction of cyclin B and was resolved into PP1-dependent categories with unique sequence motifs.
158 tivities of major protein phosphatases, like PP1 and PP2A, appear directly or indirectly repressed by
160 ortex at mid anaphase, kinetochore-localized PP1-Sds22 helps to break cortical symmetry by inducing t
166 at Drosophila ASPP is part of a multiprotein PP1 complex and that PP1 association is necessary for se
168 ther show that platelets activate RhoA-MYPT1-PP1-mediated YAP1 dephosphorylation and promote its nucl
169 pothesized that a direct and functional NCX1-PP1 interaction is a prerequisite for pSer-68-PLM dephos
172 cells by the ATP-competitive inhibitor 1-NM-PP1 reproduced the splicing defects and proved that it i
173 d eosinophil migration, additively with 1-NM-PP1, indicating a role for matrix metalloproteases in Tr
174 Furthermore, knockdown of PP1-alpha but not PP1-beta or PP1-gamma1 by small interfering RNA caused g
178 itions even when the levels or activities of PP1 and PP2A are strongly inhibited at kinetochores.
179 Phactr1 mutant that disrupts the binding of PP1 but not that of actin fails to alter Slack currents.
181 2 selectively binds a unique conformation of PP1 that contains a single metal (M2) at its active site
182 Here, we investigate the contribution of PP1, docked on its conserved kinetochore receptor Spc105
183 abilised by spatially-restricted delivery of PP1 near the C-terminus of Ndc80, a core kinetochore-mic
185 e, p37 negatively regulates this function of PP1, resulting in lower cortical NuMA levels and correct
189 to test whether a DCT-enriched inhibitor of PP1, protein phosphatase 1 inhibitor-1 (I1), mediates cA
191 study, we aimed to analyze the mechanisms of PP1 targeting to the NCX1-pSer-68-PLM complex and hypoth
193 EFb) catalyzes inhibitory phosphorylation of PP1 and PP4 complexes that localize to 3' and 5' ends of
195 tions lead us to propose that recruitment of PP1 to Spc105/Knl1 is carefully regulated to ensure that
197 igned to impede MYPT1-mediated regulation of PP1, also decreased TEER in a reversible and non-toxic m
200 subunit (PNUTS), an inhibitory regulator of PP1, is also recruited to DNA damage sites to promote NH
206 , knockdown of PP1-alpha but not PP1-beta or PP1-gamma1 by small interfering RNA caused greater AS160
207 t switches comprising Cdk9 and either PP4 or PP1 govern pause release and the elongation-termination
211 intimate contacts with the composite Phactr1/PP1 surface, which are required for efficient dephosphor
212 tified mouse fibroblast and neuronal Phactr1/PP1 substrates, which include cytoskeletal components an
213 rmined high-resolution structures of Phactr1/PP1 bound to the dephosphorylated forms of its substrate
214 Sequence specificity explains why Phactr1/PP1 exhibits orders-of-magnitude enhanced reactivity tow
216 ivities of SRPK1 and the protein phosphatase PP1, thereby regulating the phosphoryl content of the RS
217 of the serine/threonine-protein phosphatase PP1-alpha catalytic subunit or protein kinase A activati
219 ols cortical NuMA levels via the phosphatase PP1 and its regulatory subunit Repo-Man, but it acts ind
220 ional molecule that recruits the phosphatase PP1 to promote the dephosphorylation of pAKT to give AKT
222 nal influence on type I protein phosphatase (PP1), likely resulting in negative regulation of cAMP/ca
224 ition of the CDK1-counteracting phosphatases PP1 and PP2A-B55, allowing wide-spread dephosphorylation
225 eletal muscle serine/threonine phosphatases (PP1, PP2A, PP2B, and PP2C) on AS160 dephosphorylation.
226 heckpoint involves two protein phosphatases, PP1 and PP2A-B56, that are thought to extinguish checkpo
227 site-dependent deceleration caused by PNUTS-PP1 and Spt5 dephosphorylation is required to convert Po
229 quire poly(A) site recognition and the PNUTS-PP1 complex, which is in turn necessary for transcriptio
235 eutic value of inhibition of the PKA/PPP1R1A/PP1 pathway in the treatment of primary and metastatic E
237 red a novel PP1-regulatory subunit (PPP1R3A [PP1 regulatory subunit type 3A]) in the RyR2 macromolecu
238 MAP) is an endothelial cell (EC)-predominant PP1 regulatory subunit and a member of the myosin phosph
239 A first generation photoproximity probe, PP1, responds to 365 nm light to simultaneously cleave a
240 osome movement, may instead serve to promote PP1 recruitment to kinetochores fully attached to spindl
241 henyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP1) analogs tested, whereas WT PKCdelta was insensitive
242 ditionally show that artificially recruiting PP1 to Spc105/Knl1 before, but not after, chromosome bio
243 form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms
244 PP2/PP1 complex and show that ASPP2 recruits PP1 using both its canonical RVxF motif, which binds the
245 complex, specifically the Ska1 CTD, recruits PP1 to kinetochores to oppose spindle checkpoint signali
246 by the Aurora-B kinase and RepoMan (recruits PP1 onto mitotic chromatin at anaphase)-associated phosp
248 sable for error correction; in fact, reduced PP1 docking on Spc105 improved chromosome segregation an
250 nalysis showed that Phactr1 binding remodels PP1's hydrophobic groove, creating a new composite surfa
253 m different systems have suggested that Rif1-PP1 interaction is conserved and has important biologica
255 Recombinant inhibitor-2 protein (a selective PP1 inhibitor) delayed AS160 dephosphorylation on both p
258 PKA phosphorylation at Thr35, and subsequent PP1 binding and inhibition, was required for PPP1R1A-med
262 lude that female mice lacking the C-terminal PP1-binding domain of PPP1R15A show reduced dietary inta
264 part of a multiprotein PP1 complex and that PP1 association is necessary for several in vivo functio
267 f this study was to test the hypothesis that PP1 is dysregulated in paroxysmal atrial fibrillation (P
269 tructure of the PP1:TTN complex reveals that PP1 selectivity is defined by a covalent bond between TT
270 ariety of molecular techniques, we show that PP1 catalytic subunit (PP1c) co-localized, co-fractionat
273 se conserved PP1-docking motifs suggest that PP1 regulates PP2A-B55 and PP2A-B56 activities in a vari
274 , PP1 dephosphorylated NCC in vitro, and the PP1 inhibitor calyculin A increased NCC phosphorylation.
275 characterized AGC-family kinase Ypk3 and the PP1 phosphatase Glc7, whereas TORC2 regulates phosphoryl
276 th its canonical RVxF motif, which binds the PP1 catalytic domain, and its SH3 domain, which engages
280 and a targeted oxidative inactivation of the PP1 metal center, that sustains eIF2alpha phosphorylatio
281 mage-inducible protein 34), a subunit of the PP1 phosphatase complex that promotes the dephosphorylat
282 in vitro affecting neither stability of the PP1-PPP1R15A complex nor substrate-specific dephosphoryl
285 MYC on the kinase NUAK1, which acts through PP1 and PNUTS to ensure that splicing keeps up with MYC-
288 o a PP1-binding peptide or fused directly to PP1 rescues mitotic defects caused by Ska1 depletion.
290 enhance gene expression in other cell types, PP1 activation to relieve IRS1 inhibition may be a more
291 yadenylation signal (CPS) and increases upon PP1 depletion, consistent with a PP1 function in termina
293 which binds NHERF1 through a conserved VxF/W PP1 motif, dephosphorylates Ser(290) Mutating (257)VPF(2
295 escribe a mitotic phosphatase relay in which PP1 reactivation is required for the reactivation of bot
296 bined allosteric/torpedo mechanism, in which PP1-dependent slowing down of polymerases over terminati
297 ting protein of p53) proteins associate with PP1 catalytic subunits and are implicated in multiple fu
298 otic activation of Gwl, its association with PP1 is disrupted in mitotic cells and egg extracts.
300 , we demonstrate the association of DAT with PP1 and PP2A in the mouse brain and heterologous cell sy