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1 Ch and PMA was blocked by Ro-31-8425 or beta-pseudosubstrate.
2 on and dephosphorylation requires an exposed pseudosubstrate.
3 n cAMP-dependent protein kinase upon binding pseudosubstrate.
4 not by the alpha, delta, or alpha beta gamma pseudosubstrate.
5 d-type aPKC, but not a construct lacking the pseudosubstrate.
6 ylation, as it was inhibited by the PKC-zeta pseudosubstrate.
7 rate but not by the alpha, delta, or epsilon pseudosubstrate.
8 plex bound to a peptide sequence acting as a pseudosubstrate.
9 dies suggest that PIP3 binds directly to the pseudosubstrate.
10 tophosphorylated C-termini act as inhibitory pseudosubstrates.
11 hows desulfation activity toward arylsulfate pseudosubstrates.
12 Fs) by treating C2C12 myotubes with PKCtheta pseudosubstrates.
14 activity by myristoylated PKC (zeta/lambda) pseudosubstrate, a specific inhibitor of PKCzeta, and Go
16 peptide, myristoylated protein kinase C-zeta pseudosubstrate, also significantly decreased the entero
17 interaction activates aPKC by displacing the pseudosubstrate, although full activity requires the Par
18 atory module of aPKCiota, comprising the PB1 pseudosubstrate and C1 domains, forms a cooperative and
21 atalysis; and exposure of the amino-terminal pseudosubstrate and masking of the carboxyl terminus acc
24 nzyme activity in vitro by both the PKC-zeta pseudosubstrate and RO 31-8220 correlated well with inhi
25 gulatory region of PKCepsilon containing the pseudosubstrate and zinc finger-like sequences was found
27 tanol, cell-permeable myristoylated PKC-zeta pseudosubstrate, and expression of kinase-inactive RAF,
28 y many viral antagonists, including poxvirus pseudosubstrate antagonists that mimic the natural subst
35 th kinase was mapped to what appears to be a pseudosubstrate autoinhibitory domain at the extreme car
36 lly falls into two categories: regulation by pseudosubstrate autoinhibitory domains, and remodeling o
39 in, that demonstrate the molecular basis for pseudosubstrate binding to the active state with phospho
42 Both RO 31-8220 and myristoylated PKC-zeta pseudosubstrate blocked insulin-induced activation and a
43 mtide-2-related inhibitory peptide (AIPm), a pseudosubstrate blocker of CaMKII, whereas axotomized ne
44 tion of ESO cells was reduced by the epsilon pseudosubstrate but not by the alpha, delta, or alpha be
45 ES cells was reduced by the alpha beta gamma pseudosubstrate but not by the alpha, delta, or epsilon
46 gene, drumstick (drm), which functions as a pseudosubstrate by displacing Bowl from the Hyd-Lin comp
48 he complex formation of C1s with its natural pseudosubstrate, C1 inhibitor (C1 inh), and promotion of
49 (C1a, C1b, and C2) appears to strengthen the pseudosubstrate-catalytic domain interaction in a nucleo
50 ing to PKCgamma was initially prevented by a pseudosubstrate clamp, which kept the diacylglycerol-bin
51 ion or exposure for 1 hour to myristoylated, pseudosubstrate-derived peptide inhibitors against PKCal
53 ticity and memory have relied on the PKCzeta pseudosubstrate-derived zeta-inhibitory peptide (ZIP).
54 h RVPO (>12 fold), and phosphorylated in the pseudosubstrate domain at the Ser-411, Thr-421, and Ser-
55 g of the active PKA catalytic subunit to its pseudosubstrate domain inhibitor (PKI) fused with glutat
58 ated a knock-in mouse with a mutation in the pseudosubstrate domain of PKCy, which keeps PKCy in the
59 e corresponding to the unique PKCiota/lambda pseudosubstrate domain was introduced into an in vitro a
61 egulatory elements, including the inhibitory pseudosubstrate domain, consequently rendering the kinas
62 elated to SCA14 with a point mutation in the pseudosubstrate domain, PKCy-A24E, known to induce a con
63 horylation sites at Thr(141) adjacent to the pseudosubstrate domain, Thr(218) in the C1A-C1B interdom
64 ain bears a striking resemblance to the SOCS pseudosubstrate domain, we examined whether Jak-2 associ
69 (EPSP) synthase has been examined using the pseudosubstrates, (E)- and (Z)-3-fluorophosphoenolpyruva
72 itory associations between caspase-1 and its pseudosubstrate, Flightless I (FliI), while RNF34 ubiqui
73 HF), the product tetrahydrofolate (THF), the pseudosubstrate folate, reduced and oxidized NADPH cofac
74 toylated peptide based on the autoinhibitory pseudosubstrate fragment of the atypical PKCzeta, zeta i
75 KI), an inhibitor of a novel PKC (an nPKCeta pseudosubstrate fragment), and an antioxidant (melatonin
79 or substrates of AMPK, inhibit the kinase as pseudosubstrates in a Rapamycin-regulated fashion in vit
82 Inhibition of PKC-theta and PKC-zeta using pseudosubstrates inhibited IL-1beta-stimulated activatio
83 PC/C inhibitors have been reported to act as pseudosubstrates, inhibiting the APC/C by preventing sub
86 Our results reveal a simple, elegant mode of pseudosubstrate inhibition that combines high-affinity a
87 the PKR kinase domain can drastically impact pseudosubstrate inhibition while leaving substrate phosp
90 ow APC/C activity is suppressed by the small pseudosubstrate inhibitor Acm1 from budding yeast (Sacch
92 P specifically associated with the caspase-1 pseudosubstrate inhibitor Flightless-1 and its binding p
93 erminal portion of the BPS region binds as a pseudosubstrate inhibitor in the substrate peptide bindi
94 ir ability to escape inhibition by the model pseudosubstrate inhibitor K3, encoded by the vaccinia vi
95 ential and that soluble BubR1 functions as a pseudosubstrate inhibitor of APC/C(Cdc20) during interph
98 because it was not inhibited by the specific pseudosubstrate inhibitor of PKC, PKC(19-31), and it was
102 r, in the presence of an N-myristoylated PKC pseudosubstrate inhibitor peptide (MyrPsiPKC-I(19-27)),
103 vation of Kv3.3 currents, and a specific PKC pseudosubstrate inhibitor peptide prevented the effects
105 In permeabilized 3T3-L1 cells, addition of pseudosubstrate inhibitor peptides of casein kinase II (
106 he atypical PKCzeta by myristoylated PKCzeta pseudosubstrate inhibitor significantly decreased the A(
107 PhK13 has been proposed to function as a pseudosubstrate inhibitor with Cys-308 occupying the sit
108 ither bisindolylmaleimide-I or a peptide PKC pseudosubstrate inhibitor, and COX-2 mRNA and protein we
109 y been shown to inhibit Cdc20 by acting as a pseudosubstrate inhibitor, but in this paper, we show th
114 -alkylating agents (e.g., temozolomide) with pseudosubstrate inhibitors (such as O(6)-benzylguanine)
116 h untreated and ionophore-treated cells, but pseudosubstrate inhibitors only bound to TF-factor VIIa
118 tantial differences in the concentrations of pseudosubstrate inhibitors which rescued cells from SOD1
120 activity, as intrathecal delivery of a zeta-pseudosubstrate inhibitory peptide (PKCzeta-PS) 35 min f
121 and PIP3 current activation is blocked by a pseudosubstrate inhibitory peptide of atypical PKC but n
124 f the PKA catalytic subunit (PKA-C) from the pseudosubstrate inhibitory sequence, drive RIalpha conde
125 and for residues 102-115, which include the pseudosubstrate inhibitory site, support the prediction
126 the idea that residues conserved between the pseudosubstrate K3L protein and the authentic substrate
127 nsulin, but not PIP(3), activated truncated, pseudosubstrate-lacking forms of PKC-zeta and PKC-lambda
129 Moreover, treatment with PKClambda/zeta pseudosubstrate lead to significant reduction of FGF2-me
131 tate) and the inhibitors (high magnesium and pseudosubstrate) locking it into discrete minima (dynami
132 1+ by ran1+ and suggest that mei3+ employs a pseudosubstrate mechanism for its inhibitory function.
133 ructure of the Grp1 Sec7-PH tandem reveals a pseudosubstrate mechanism of autoinhibition in which the
134 E2, and these results are consistent with a pseudosubstrate mechanism of inhibition of eIF2alpha kin
135 emonstrate that instead of acting through a "pseudosubstrate" mechanism as previously hypothesized, E
137 re regulated by an N-terminal autoinhibitory pseudosubstrate motif centered on a critical proline res
139 a peptide (uPEP2) containing the typical PKC pseudosubstrate motif present in all PKCs that autoinhib
140 htly bound securin protein, which contains a pseudosubstrate motif that blocks the separase active si
141 within its NH(2)-terminal regulatory half, a pseudosubstrate motif that occupies the kinase active si
144 DK1-cyclin B1 inhibits separase by deploying pseudosubstrate motifs from intrinsically disordered loo
145 In both complexes, separase is inhibited by pseudosubstrate motifs that block substrate binding at t
146 bitor Acm1, which incorporates D and KEN box pseudosubstrate motifs, we describe the molecular basis
148 ave previously shown that the autoinhibitory pseudosubstrate must be removed from the active site in
149 udosubstrate motifs by APC/C inhibitors, and pseudosubstrates must bind their cognate activators tigh
151 ic surface, resulting in displacement of the pseudosubstrate of aPKC and re-engagement in the substra
152 These data support a model in which the pseudosubstrate of aPKCs is tethered to the acidic surfa
153 Cancer-associated hotspot mutations in the pseudosubstrate of PKCbeta that impair autoinhibition re
154 TR internalization by more than 50%, whereas pseudosubstrates of cyclic AMP-dependent kinase A, prote
156 rotein kinase C-zeta (PKC-zeta) inhibitor (a pseudosubstrate oligopeptide), but not a PKC-alphabeta i
157 protein kinase C zeta (PKC zeta) inhibitors (pseudosubstrate or small interfering RNA silencing).
158 hat purified recombinant PelA hydrolyzed the pseudosubstrate p-nitrophenyl acetate in vitro, and site
160 Strikingly, the enzyme is inhibited by the pseudosubstrate peptide Ala-Cys(-S-GlcNAc)-Ala, and has
162 Use of PKC agonists and isozyme-specific pseudosubstrate peptide antagonists suggested a role for
163 nanopore sensor for Pim kinases that bears a pseudosubstrate peptide attached by an enhanced engineer
164 rat kidney cells incubated with Rab2 and the pseudosubstrate peptide displayed abundant swollen or di
167 This depression was partially blocked by a pseudosubstrate peptide inhibitor of cGMP-dependent prot
168 ation by DAG was specifically inhibited by a pseudosubstrate peptide inhibitor of cPKCs (PKC alpha(22
169 inase activates the subunit for binding to a pseudosubstrate peptide inhibitor of protein kinase A.
175 ion of protein kinase C activity utilizing a pseudosubstrate peptide sequence blocked IRES activity d
176 CTD can be inhibited specifically by a CDK7 pseudosubstrate peptide that also inhibits transcription
179 Marinobufagenin, dihydroouabain, and zeta-pseudosubstrate peptide were used to determine if PKMzet
183 orylation, or by intracellular delivery of a pseudosubstrate peptide, also disrupts sarcomeric organi
184 d 8, stimulated phosphorylation of the alpha-pseudosubstrate peptide, and in primary mouse keratinocy
185 cells in the presence of a protein kinase C pseudosubstrate peptide, but not a control peptide, inhi
190 g unsuitable for phosphotransfer, as well as pseudosubstrate peptides of various lengths, we identify
191 Pharmacologic agents, isoform-selective pseudosubstrate peptides, and antisense oligonucleotides
192 ine phospholipase C (PC-PLC), PKC (including pseudosubstrate peptides, chelerythrine, and the alpha/b
193 KC-alpha activation by classical inhibitors, pseudosubstrate peptides, or the overexpression of domin
195 P and was therefore used to assess whether a pseudosubstrate perturbed the rate of holoenzyme dissoci
196 he region within PKR that interacts with the pseudosubstrate, pK3, is the same region that interacts
199 tion by a Src kinase inhibitor and a PKCzeta-pseudosubstrate prevented eritoran-induced apoptosis.
201 KA inhibitor (PKI) containing a specific PKA pseudosubstrate, R-R-N-A, was subcloned into a pTREX vec
203 f RSK1 competed with PKAc for binding to the pseudosubstrate region (amino acids 93-99) of PKARIalpha
205 ased on the endogenous zeta protein kinase C pseudosubstrate region block agonist-induced adhesion to
207 e PKAc, which requires Arg-95 and -96 in the pseudosubstrate region of PKARIalpha for their interacti
209 hat contains a sequence corresponding to the pseudosubstrate region of PKC-alpha (P1) partially rever
210 says, but PKC alpha constructs that lack the pseudosubstrate region or constructs of the whole cataly
211 We also find that PAK6 is regulated by the pseudosubstrate region, indicating a common type II PAK
212 as measured by phosphorylating the PKC-delta pseudosubstrate region-derived substrate was also reduce
214 itutively autoinhibited, but mutation of the pseudosubstrate releases this inhibition and causes incr
215 ell polarity, and that addition of a PKCzeta pseudosubstrate restores osteoclastogenesis and bone res
216 I to the cell-free reactions containing CKII pseudosubstrates reversed the endocytosis block, suggest
218 terminal regulatory domain, which includes a pseudosubstrate segment that plugs the active site.
220 ubstrate suggests that basic residues in the pseudosubstrate sequence are required for maintaining aP
221 We propose that in the absence of AMP this pseudosubstrate sequence binds to the active site groove
222 ially associated with the C subunit with the pseudosubstrate sequence docked in the active site cleft
223 ormational change in which an autoinhibitory pseudosubstrate sequence is released from the active sit
224 kinase C adopts a conformation in which its pseudosubstrate sequence is removed from the active site
225 kinase C adopts a conformation in which its pseudosubstrate sequence is removed from the active site
226 l five (or certain) arginine residues in the pseudosubstrate sequence of PKC-iota by site-directed mu
227 a myristoylated peptide corresponding to the pseudosubstrate sequence of protein kinase inhibitor (my
229 active site is blocked by binding either the pseudosubstrate sequence or a heterologous substrate.
231 d in the central region of Acm1 constitute a pseudosubstrate sequence required for APC(Cdh1) inhibiti
232 hibitory peptide (ZIP) based on the PKC-zeta pseudosubstrate sequence reverses established LTP in vit
234 PRKs are regulated by N-terminal domains, a pseudosubstrate sequence, Rho-binding domains, and a C2
239 N-Myristoylated peptides derived from the pseudosubstrate sequences of PKC isozymes were used to i
240 plays a high degree of conservation with the pseudosubstrate sequences of the protein kinase C (PKC)
241 and -eta were very similar to the endogenous pseudosubstrate sequences of these PKC isozymes, indicat
243 ugh PhK13-1 does not appear to function as a pseudosubstrate, several specificity determinants employ
244 The italicized amino acids form a putative pseudosubstrate site (Ser is replaced with Ala), which t
245 es that are juxtaposed to the autoinhibitory pseudosubstrate site in cGMP-dependent protein kinase ty
246 te that a conserved serine juxtaposed to the pseudosubstrate site in type I PKGs contributes importan
247 the pseudosubstrate site, but Arg-75 in the pseudosubstrate site is critical for autoinhibition.
248 h active kinases, kinase-dead PKC eta with a pseudosubstrate site mutation designed to give an active
250 from SLE T cells, one located adjacent to a pseudosubstrate site of the RI alpha subunit and the oth
252 lation site of Ibeta cGK is well outside the pseudosubstrate site, but Arg-75 in the pseudosubstrate
253 cGK enhances proteolysis within and near the pseudosubstrate site; treatment of dimeric cGK with thre
255 s as a conformational switch to position the pseudosubstrate so that it blocks the active site, a con
257 nitiated by the addition of Mg(2+) ions or a pseudosubstrate strand to the ribozyme, and the ensuing
258 ract the inhibitory effects of the exogenous pseudosubstrate suggests that basic residues in the pseu
259 e (FMP) on SERCA, producing a phosphorylated pseudosubstrate tethered to the nucleotide-binding site
261 in Roq1 binds the ubiquitin ligase Ubr1 as a pseudosubstrate, thereby modulating the degradation of s
262 essenger binding unleashes an autoinhibitory pseudosubstrate to allow substrate phosphorylation.
263 ddition of the exogenous arginine-containing pseudosubstrate tridecapeptide to inhibit this constitut
265 paradoxical effects of the PKR mutations on pseudosubstrate vs. substrate interactions reflect diffe
266 sponsiveness to PIP3 was seen when exogenous pseudosubstrate was used to inhibit mouse liver PKC-lamb
267 ibits eIF-2alpha kinases by functioning as a pseudosubstrate, we observed that K3L directly interacte
268 is reversibly regulated by an autoinhibitory pseudosubstrate, which blocks the active site of the enz
269 A was also observed in the reaction with the pseudosubstrate, (Z)-3-fluorophosphoenolpyruvate, strong