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1 , IKKbeta, and protein kinase, CK2 (formerly casein kinase II).
2 ion of Puf6p mediated by protein kinase CK2 (casein kinase II).
3 1 includes a potential phosphorylation site (casein kinase II).
4 l sites that are recognized by CK2 (formerly casein kinase II).
5 estin2 at Thr-383 is shown to be mediated by casein kinase II.
6 for phosphorylation by protein kinase C and casein kinase II.
7 s constitutive phosphorylation by the enzyme casein kinase II.
8 KBP46 can be phosphorylated by human and Sf9 casein kinase II.
9 , which in turn increases enzyme activity of casein kinase II.
10 by U(S)3 and U(L)13 and nucleotidylylated by casein kinase II.
11 and inactivated by purified GSK-3 beta plus casein kinase II.
12 have established that CDK1 can phosphorylate casein kinase II.
13 stimulated by in vitro phosphorylation with casein kinase II.
14 tivity and its subsequent phosphorylation by casein kinase II.
15 ivity) is inactivated via phosphorylation by casein kinase II.
16 P<0.0001) through a mechanism that includes casein kinase II.
17 ein kinase C (PKC) and to a lesser extent by casein kinase II.
18 ognition motifs for other kinases as well as casein kinase II.
19 e result of trace contamination (<0.1%) with casein kinase II.
20 ting it and stabilizes mature, but unstable, casein kinase II.
21 sphorylating recombinant NRF-1 with purified casein kinase II.
22 lation of the enzyme's cytoplasmic domain by casein kinase II.
23 ncodes a nonessential specificity subunit of casein kinase II.
24 EENV, was an efficient in vitro substrate of casein kinase II.
25 into a homomultimer upon phosphorylation by casein kinase II.
26 were phosphorylated with [gamma-32P]ATP and casein kinase II.
27 , Ser-101 and Thr-117 were phosphorylated by casein kinase II.
28 protein that is phosphorylated at Ser(14) by casein kinase II.
29 ain binding to Asf1-T(270) phosphorylated by casein kinase II.
30 estored by treatment with the serine kinase, casein kinase II.
31 omain that contains several target sites for casein kinase II.
32 lpha and is constitutively phosphorylated by casein kinase II.
33 s the disruption of the catalytic subunit of casein kinase II.
34 showed that Opi1p was also phosphorylated by casein kinase II.
35 sphorylation of DMP1 by a nuclear isoform of casein kinase II.
36 he acidotrophic kinases, casein kinase I and casein kinase II.
37 lated from murine kidney were incubated with casein kinase II.
38 o potential phosphorylation sites motifs for casein kinase II ((335)SFQE) and protein kinase C (PKC)
40 ng 1 (YY1) in vitro and in vivo by CK2alpha (casein kinase II), a multifunctional serine/threonine pr
42 he predicted sequence of the beta subunit of casein kinase II, a highly conserved serine/threonine ki
44 altose-binding protein-Opi1p as a substrate, casein kinase II activity was dose-and time-dependent an
46 Also copurifying with the holoenzyme are casein kinase II and a histone acetyltransferase activit
47 damage in a manner dependent on TCOF1 and on casein kinase II and ATM, which are known to modify TCOF
48 , and additional sites for protein kinase C, casein kinase II and cAMP-/cGMP-dependent protein kinase
49 hese kinases, however, were not identical to casein kinase II and displayed a pharmacologic profile d
50 appears to be mediated, at least in part, by casein kinase II and p38 kinase as inhibitors of these k
51 member of this set, is nucleotidylylated by casein kinase II and phosphorylated by viral protein kin
53 this repression by directly interacting with Casein Kinase II and preventing it from activating HDAC3
54 ational modification were present including: casein kinase II and protein kinase C phosphorylation si
56 through a mechanism involving p38 kinase and casein kinase II and that phosphorylation is necessary f
57 phosphorylated by protein kinase C (PKC) and casein kinase II and that PKC mediates phosphorylation o
58 orylation of the C-terminal PEST sequence by casein kinase II and/or by the interaction of NF-kappaB
59 protein kinase A but not protein kinase C or casein kinase II, and aquaporin-5 was phosphorylated in
60 best) by PKC, cGMP-dependent protein kinase, casein kinase II, and casein kinase I and not at all pho
62 se A/calcium calmodulin-dependent kinase II, casein kinase II, and proline-directed kinase, indicatin
63 er(363) is an in vivo phosphorylated site by casein kinase II, and this specific phosphorylation lead
64 and signaling pathways, including CaMK, PKA, Casein kinase-II, and the Raf-MEK-ERK and PI-3K-Akt path
65 tes that both the alpha and beta subunits of casein kinase II are retained by the column from rat bra
66 ein kinases JNK, ERK, p38, and CK2 (formerly casein kinase II) are involved in the regulation of NFAT
69 his report we identify CK2 (formerly termed "casein kinase II") as the kinase responsible for phospho
70 roduct, eukaryotic initiation factor 5A, and casein kinase II, as well as many previously uncharacter
71 Thr1704-sites of phosphorylation by PKA and casein kinase II at the interface between the proximal a
73 ng tyrosine-, di-leucine-, or acidic cluster/casein kinase II-based internalization signals were over
74 RNA designed to knock down expression of the casein kinase II beta-subunit gene family lengthens peri
77 rane trafficking proteins are substrates for casein kinase II, calcium/calmodulin-dependent protein k
78 We also show that casein kinase I, but not casein kinase II, can phosphorylate and activate cdk5 in
79 2, whereas PKC, p90 ribosomal S6 kinase, and casein kinase II, can phosphorylate serine 71, threonine
80 t sites by at minimum two different kinases, casein kinase II (CK II) and tousled-like kinase (tlk).
82 hosphorylation by protein kinase C (PK C) or casein kinase II (CK II) within or near the nonhelical t
86 ar substrates of human protein kinases (e.g. casein kinase II (CK2) and Akt), that implicated several
87 ant for phosphorylation by recombinant human Casein Kinase II (CK2) and by a CK2-like kinase in Arabi
89 e regulatory subunit of the serine-threonine casein kinase II (CK2) as a binding partner of LOV-1 and
90 s presented here identify the protein kinase casein kinase II (CK2) as a BMP receptor type Ia (BRIa)
91 Here, using a genetic screen, we identify casein kinase II (CK2) as a factor required for piRNA pa
103 an interactive association between CHOP and casein kinase II (CK2) results in the phosphorylation of
105 that the conserved serine/threonine kinase, casein kinase II (CK2), promotes miRISC function in Caen
106 y, Brd4 association with p53 is modulated by casein kinase II (CK2)-mediated phosphorylation of a con
108 t the Xenopus homolog of the beta subunit of casein kinase II (CKII beta) binds to and regulates Mos.
110 is HFR1 can be phosphorylated by recombinant casein kinase II (CKII) and plant extract in vitro and t
115 The N-terminal phosphorylation by cellular casein kinase II (CKII) at S21, T32, and S43, and other
116 ion of pseudosubstrate inhibitor peptides of casein kinase II (CKII) blocked TR internalization by mo
117 tion of PU.1 at serine 148, located within a casein kinase II (CKII) consensus motif, increases the t
121 roaches, we have identified a novel role for casein kinase II (CKII) in the modification of the polym
131 es the amino acid composition in a consensus casein kinase II (CKII) phosphorylation site at Ser-254.
133 Phosphorylation of its cytosolic domain by casein kinase II (CKII) promotes the localization of fur
136 protein kinase C (PKC) site, Ser378, or the casein kinase II (CKII) site, Ser392, or bis-phosphoryla
138 d characterization of the first cell surface casein kinase II (CKII) substrate (Tc-1) of Trypanosoma
140 Csx/Nkx2.5 kinase is a catalytic subunit of casein kinase II (CKII) that phosphorylates the serine r
141 cidotropic kinases casein kinase I (CKI) and casein kinase II (CKII) to phosphorylate bacterial fusio
142 showed that protein kinase A (PKA), PKC, and casein kinase II (CKII) were able to differentially phos
143 e for this kinase activity was identified as casein kinase II (CKII), a cellular serine-threonine pro
144 hat lipin 1beta is a bona fide substrate for casein kinase II (CKII), a protein kinase that is essent
145 ains two consensus recognition sequences for casein kinase II (CKII), a serine and threonine kinase t
146 ssociated kinase (BAK) suggest identity with casein kinase II (CKII), an enzyme known to mediate basa
147 , including ubiquitin-conjugating enzyme E2, casein kinase II (CKII), and the multifunctional protein
148 nown that caldesmon (CaD) is a substrate for casein kinase II (CKII), and the phosphorylation of CaD
164 s work, we show that Pah1 is a substrate for casein kinase II (CKII); its phosphorylation was time- a
167 protein kinase A (PKA), and beta subunit of casein kinase II (CKIIbeta) as well as by kinases presen
168 located in these acidic stretches lie within casein kinase II consensus motifs, and Nopp52 is an exce
170 trospray mass spectrometry demonstrated that casein kinase II could introduce up to five phosphates i
171 n calmodulin on serine/threonine residues by casein kinase II decreased its affinity for Ca(2+)-ATPas
172 s from ovariectomized mice exhibit increased casein kinase II-dependent phosphorylation of the nuclea
173 , PKCbetaII, PKCgamma, and PKCdelta (but not casein kinase II) directly phosphorylated Ser(24) in vit
176 to be phosphorylated by p34(cdc2) kinase and casein kinase II exclusively on serines implicates these
181 ylation of native and deglycosylated BSPs by casein kinase II identified seven phosphorylation sites
182 nd that recombinant AP180 is a substrate for casein kinase II in vitro and that its phosphorylation w
186 We report here that HP1 is phosphorylated by casein kinase II in vivo at three serine residues locate
187 ned the role of protein kinase CK2 (formerly casein kinase II) in increased N-methyl-d-aspartate rece
188 quired an agonist but was not blocked by the casein kinase II inhibitor apigenin, the protein kinase
190 rrays showed that protein kinase A, MEK, and casein kinase II inhibitors blocked induction of DBH and
191 f the RNA-stimulated hyperphosphorylation to casein kinase II inhibitors, and the distinct glycerol g
192 e lysate and in cultured K562 cells and that casein kinase II is capable of quantitatively phosphoryl
201 fat facets, and a number of kinases, such as casein kinase II, MARK (microtubule affinity regulating
202 ated transcription complexes is inhibited by casein kinase II-mediated phosphorylation of La serine 3
203 d an antibody that specifically recognizes a casein kinase II-mediated phosphorylation on serine-14 o
204 conformational state that is inaccessible to casein kinase II-mediated phosphorylation, demonstrating
205 pase-3-mediated cleavage can be regulated by casein kinase II-mediated phosphorylation, suggesting th
208 yperphosphorylation coincided with increased casein kinase II mRNA and protein levels, suggesting a r
209 wild type in all of the E7 mutants, only the casein kinase II mutant had the ability to maintain high
210 an AP-1 inhibitor; but not by inhibitors of casein kinase II, NFkappaB, PLA(2), phospholipase D (PLD
211 d that VIPR-RP is phosphorylated in vitro by casein kinase II on Ser-69/71 and Thr-110, and by cAMP-d
212 dition, our data indicate that inhibition of casein kinase II or GSK3beta significantly reduced hnRNP
213 ylated by protein kinase C (PKC), but not by casein kinase II or p90 ribosomal S6 kinase, also activa
214 ctivity of eIF2B, whereas phosphorylation by casein kinase II or protein kinase C was without effect.
217 n kinase G, rhodopsin kinase, CaM kinase II, casein kinase II, or cyclin-dependent kinase 5, at conce
218 not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic ev
224 These data supported the conclusion that casein kinase II phosphorylation at Ser10 played a role
225 uniquely possess lysine residues following a casein kinase II phosphorylation motif which is critical
227 he nuclei of infected cells, indicating that casein kinase II phosphorylation of S186 occurs in the n
228 ltered the cluster of acidic residues with a casein kinase II phosphorylation site at the extreme car
230 interest because its partner, gE, contains a casein kinase II phosphorylation site in its endodomain;
231 ation mutant, two Rb-binding site mutants, a casein kinase II phosphorylation site mutant, and a tran
233 d in which three serine residues that form a casein kinase II phosphorylation site were changed to al
234 rate that the constitutive carboxyl-terminal casein kinase II phosphorylation sites are necessary for
236 two peptides showed that, among 9 potential casein kinase II phosphorylation sites, 2 serines were p
237 g domain of many proteins, several potential casein kinase II phosphorylation sites, a helix-turn-hel
238 tants of IkappaBbeta1 lacking the C-terminal casein kinase II phosphorylation sites, which form a sta
248 arin-sensitive kinase was not the ubiquitous casein kinase II present in a variety of cell types.
249 ication of Elf1 suggests an association with casein kinase II, previously implicated in roles in tran
252 veral potential sites for phosphorylation by casein kinase II, protein kinase C, tyrosine kinases, gl
253 opy; these peptides contain target sites for casein kinase II, protein tyrosine kinase, and PIM-1 kin
255 serine 72 and pharmacological inhibition of casein kinase II reduced GTPCH-1 phosphorylation and blu
258 clude that nucleotidylylation of proteins by casein kinase II requires the presence of the signaling
260 Ser184 of Geminin could be phosphorylated by Casein kinase II, resulting in the enhanced binding to H
263 c for CKI, whereas the others were shared by casein kinase II (Ser-705), Cdc28-cyclin B (Ser-602), Ph
264 trated that Ser(10) can be phosphorylated by casein kinase II, Ser(21) can be phosphorylated by prote
265 the major sorting determinant is a conserved casein kinase II site followed by a dileucine motif (157
267 We found that phosphorylation at predicted casein kinase II sites in the transposase N-terminus inh
268 genesis, we show that phosphorylation of the casein kinase II sites potentiates VIPR-RP transcription
269 ype c-myb or c-myb mutated at the N-terminal casein kinase II sites was only weakly oncogenic at 10 w
271 rine residues, comprising putative consensus casein kinase II sites, that modulate the rate of PRV tr
273 ll three members of the protein kinase C and casein kinase II substrate in neurons (PACSIN) family an
274 ously reported that the protein kinase C and casein kinase II substrate in neurons (PACSIN) forms a c
275 inhibitors of protein kinase CK2 (formerly, casein kinase II), such as emodin and DRB, were able to
278 er types of serine kinases tested, including casein kinase II, the alpha and zeta isoforms of protein
279 ere that when Ser(363) was phosphorylated by casein kinase II, the cleavage of Cx45.6 catalyzed by ca
280 , mutations eliminating two target sites for casein kinase II, the glutamate-rich C terminus, or the
281 ate for purified casein kinase I but not for casein kinase II; the endogenous connexin49 protein kina
286 glycosylates glycogen synthase kinase-3 and casein kinase II, two enzymes critical in the regulation
287 sequence motifs that were phosphorylated by casein kinase II type(s), whereas the remaining four pep
288 hnRNP protein in nuclear extracts reflects a casein kinase II-type activity, its RNA-dependent hyperp
289 phosphorylation sites via protein kinase C, casein kinase II, tyrosine kinase, and cAMP- and cGMP-de
290 (Y) and phosphorylated HMG-I, as modified by casein kinase II, using far Western and protein-protein
292 alt extracts from isolated axonemes, whereas casein kinase II was excluded from the flagellar compart
294 and [gamma-32P]GTP indicated that endogenous casein kinase II was phosphorylating monomeric gE, while
295 in vitro by the insulin receptor kinase and casein kinase II were resolved by two-dimensional phosph
296 hosphorylation is enhanced by stimulation of casein kinase II, which is known to be present in coated
297 indicates that this kinase is distinct from casein kinase II, which is known to co-purify with GRP94
298 osphorylation sites for protein kinase C and casein kinase II, which were observed in I kappa B alpha
299 that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a