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1 he pleiotropic protein kinase, CK2 (formerly casein kinase 2).
2 mulation by phosphorylation by CK2 (formerly casein kinase 2).
3 s identified as protein kinase CK2 (formerly casein kinase 2).
4 modulated CSNK2B (the regulatory subunit of casein kinase 2).
5 n synthase kinase-3beta, whereas stimulating casein kinase 2.
6 ing that this phosphorylation is mediated by casein kinase 2.
7 ved sites (Ser712/713) are phosphorylated by casein kinase 2.
8 iated vimentin kinases and identified one as casein kinase 2.
9 ites in the acidic domain of WRN targeted by Casein Kinase 2.
10 t we identified as substrates for Erk1/2 and casein kinase 2.
11 I, whereas Ca(V)1.1-T1579 is a substrate for casein kinase 2.
12 c but not the cardiac CCRK with cyclin H and casein kinase 2.
13 iated by the alpha prime (alpha') subunit of casein kinase 2.
14 es with thapsigargin (10 mum), inhibition of casein kinase 2 (4,5,6,7-tetrabromobenzotriazole; 10 mum
15 overed that murine Arl13b is a substrate for casein kinase 2, a contaminant in our preparation from h
19 of either Galpha(q) or Galpha(o) stimulates casein kinase 2 activation and Lef/Tcf-sensitive gene ex
20 ha(q) or Galpha(o) blocks Wnt stimulation of casein kinase 2 activation, as does suppression of the p
21 ied extracellular regulated kinase 2 blocked casein kinase 2 activity and increased protein serine/th
23 minal kinase; (ii) inhibition of calpain and casein kinase 2 activity; and (iii) induction of fibrobl
27 of which contains a large number of putative casein kinase 2 and protein kinase C phosphorylation sit
28 lation through a dynamic interaction between casein kinase 2 and protein serine/threonine phosphatase
30 molecular events of this modulation involved casein kinase 2 and the synaptic vesicle rapid endocytos
31 s NMDA receptor activity by interacting with casein kinase-2 and protein phosphatases in the hypothal
33 has been shown recently to potently inhibit casein kinase 2 as well as PI3K, we hypothesize that cas
35 ; allograft inflammatory factor 1 (AIF1) and casein kinase 2, beta polypeptide (CSNK2B), all found in
36 levels of [Ca2+]i KHC was phosphorylated by casein kinase 2, but KHC was rapidly dephosphorylated by
38 posttranslationally regulated by TNF-induced casein kinase 2 catalytic subunit (CK2alpha') phosphoryl
40 anine nucleotide exchange factor (eIF-2B) by casein kinase 2 (CK-2) was previously shown to stimulate
41 ific inhibitors of casein kinase 1 (CK1) and casein kinase 2 (CK2) (10 muM D4476, 100 muM CK2-inhibit
42 rapeutic potential against TNBC by targeting Casein Kinase 2 (CK2) (PDB ID: 3H30) and ULK2 (Unc-51-li
46 ZEBRA, Ser167 and Ser173, are substrates for casein kinase 2 (CK2) and are constitutively phosphoryla
48 to directly associate with and modulate both casein kinase 2 (CK2) and protein kinase A (PKA), which
49 glycerolipid biosynthesis, is stimulated by casein kinase 2 (CK2) and that a phosphorylated protein
51 ified the regulatory (beta) subunit of human casein kinase 2 (CK2) as a CDC34-interacting protein and
56 ave identified polo-like kinase 1 (Plk1) and casein kinase 2 (CK2) as two kinases of CLIP-170 and map
57 lear condensate; and that phosphorylation by casein kinase 2 (CK2) at ~80 serines targets Nopp140 to
60 e that phosphorylated CD45 was identified as casein kinase 2 (CK2) by use of an in-gel kinase assay i
61 sing Ciona eggs and found that inhibition of casein kinase 2 (CK2) caused a shift from meiotic to mit
62 ormally long circadian periods, we show that casein kinase 2 (CK2) has a role in determining period l
64 d for robust in vitro phosphorylation by the casein kinase 2 (CK2) holoenzyme, a cytoplasmic kinase s
66 Our previous results highlighted a role for casein kinase 2 (CK2) in the modulation of dopamine D1 r
67 We demonstrate a role for protein kinase casein kinase 2 (CK2) in the phosphorylation and regulat
68 iated stimulation, PTEN is phosphorylated by casein kinase 2 (CK2) in the Ser380-Thr382-Thr383 cluste
70 A, S167 and S173, that are phosphorylated by casein kinase 2 (CK2) in vitro are also phosphorylated i
71 7 -: tetrabromobenzotriazole (TBB), a potent casein kinase 2 (CK2) inhibitor, as a strong suppressor
72 enhanced by LXR ligands and reduced both by casein kinase 2 (CK2) inhibitors and by activation of it
73 rylation by either protein kinase C (PKC) or casein kinase 2 (CK2) inhibits the assembly of myosin-II
74 beta subunit of the serine/threonine kinase casein kinase 2 (CK2) interacts specifically with the cy
84 Previous in vitro studies indicated that casein kinase 2 (CK2) mediated the phosphorylation of NS
86 We demonstrated that increased activity of casein kinase 2 (CK2) observed in HPC and in MDSC could
87 w that murine caspase-9 is phosphorylated by casein kinase 2 (CK2) on a serine near the site of caspa
89 ay is a key regulator of RUNX2 stability, as Casein kinase 2 (CK2) phosphorylates RUNX2, recruiting t
91 ith SUMOylated RNF111, which is regulated by casein kinase 2 (CK2) phosphorylation of ARKL1 at a seri
92 The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequ
93 The Foxc2 amino terminus has a consensus casein kinase 2 (CK2) phosphorylation site at serine 124
98 and overexpression experiments, we show that casein kinase 2 (CK2) promotes stress granule dynamics.
99 that phosphorylation of recombinant TFIIF by casein kinase 2 (CK2) reduces or eliminates some of the
102 serine residues 16 and 18, which are within casein kinase 2 (CK2) sites, and serine residue 114, whi
103 inases with enriched substrates detects that casein kinase 2 (CK2) subunits negatively regulate lifes
104 ctivated through pharmacologic inhibition of casein kinase 2 (CK2) to eradicate disease in high-risk
105 sh1 is phosphorylated by the Cka2 subunit of casein kinase 2 (CK2) to promote its E3 activity for Cse
108 he major site of in vitro phosphorylation by casein kinase 2 (CK2) was the conserved Ser(232) in the
109 D025 potently inhibits catalytic subunits of casein kinase 2 (CK2), a constitutively active serine/th
110 ntly shown that the serine/threonine kinase, casein kinase 2 (CK2), a major regulator of cell growth
113 ere, we report that Brg1 is also a target of casein kinase 2 (CK2), a serine/threonine kinase, in pro
114 wn previously to require the Cka2 subunit of casein kinase 2 (CK2), a ubiquitous enzyme with multiple
117 eral kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated pro
118 nsists of Daz interacting protein 1 (Dzip1), casein kinase 2 (CK2), and B56 containing protein phosph
119 dentify the heterotetrameric protein kinase, casein kinase 2 (CK2), as a new KSR1-binding partner.
121 on was dependent on XRCC1 phosphorylation by casein kinase 2 (CK2), enhancing XRCC1's interaction wit
122 on events catalyzed first by MEK and then by casein kinase 2 (CK2), followed by interaction with impo
123 s of ATR could be counteracted by inhibiting casein kinase 2 (CK2), the kinase responsible for phosph
124 e, and this phosphorylation was catalyzed by casein kinase 2 (CK2), the levels of which were dramatic
126 -LDH associates with NDPK-A, AMPK alpha1 and casein kinase 2 (CK2), whereas H-LDH associates with loc
127 a striking resemblance to that of eukaryotic casein kinase 2 (CK2), which also exhibits dual nucleoti
128 perone complex and IKK through activation of casein kinase 2 (CK2), which in turn activates NF-kappaB
129 d51 phosphorylation at threonine 13 (T13) by casein kinase 2 (CK2), which in turn triggers direct bin
130 ed up-regulation of the SK channel modulator casein kinase 2 (CK2), which we corroborated by immunohi
131 ulator of Poll III (MAF1), via a synergistic casein kinase 2 (CK2)- and mammalian target of rapamycin
132 es astrocytic protein synthesis and, through casein kinase 2 (CK2)-dependent mechanisms, disrupts the
134 their spontaneous intrinsic pacemaking via a casein kinase 2 (CK2)-dependent signaling pathway, which
149 nts indicate that phosphorylation of TLE1 by casein kinase-2 (CK2) at Ser-239 and Ser-253 is necessar
152 hibition of one of the catalytic subunits of casein kinase 2, CK2A1, but not CK2A2, improved cell via
153 how that the catalytic subunit of Drosophila casein kinase 2 (CK2alpha) is expressed predominantly in
154 ynthase promoter activity were controlled by casein kinase 2 complexed with protein serine/threonine
155 to mutation to alanine or disruption of the casein kinase 2 consensus sequence directing phosphoryla
156 uired Rab11-dependent trafficking and FAM20C/casein kinase 2-dependent C-terminal phosphorylation of
157 required for insulin induction of Sort1 in a casein kinase 2-dependent manner and that inhibition of
158 B by markedly enhancing GTPCH-1 activity via casein kinase 2-dependent phosphorylation on serine 81.
161 an influence in Wnt signaling is not clear; casein kinase 2 has been reported to be constitutively a
163 other kinases; only c-src (IC50, 15 microM), casein kinase 2 (IC50, 20 microM), erk 1 (IC50, 20 micro
166 These findings illustrate a new function of casein kinase 2 in the endothelium and provide insight i
167 inase 2 as well as PI3K, we hypothesize that casein kinase 2 inhibition is responsible for the enhanc
168 in-1, and parkin, whereas treatment with the casein kinase 2 inhibitor 5,6-dichloro-1-beta-d-ribofura
169 on spontaneous release was reproduced by the casein kinase 2 inhibitor 5,6-dichlorobenzimidazole ribo
170 tric-oxide synthase transcription, we used a casein kinase 2 inhibitor coupled with immunoprecipitati
172 r localization of Atx3 was not affected by a casein kinase-2 inhibitor or by mutating a predicted nuc
174 osphoprotein Dishevelled, demonstrating that casein kinase 2 is downstream of heterotrimeric G protei
175 dues including two serines phosphorylated by casein kinase 2 is required for the localization of VMAT
182 hin TMVs through a process that requires the casein kinase 2-mediated phosphorylation of RanGAP1.
189 900 (Ser900) as a unique site of reversible casein kinase 2 phosphorylation in the cytoplasmic domai
193 ylation of calmodulin by protein kinase CK2 (casein kinase 2) rapidly and reversibly modulated KCNQ2
194 a physical interaction between S6KII and the casein kinase 2 regulatory subunit (CK2beta), suggesting
195 We now show that TFIIF phosphorylated by casein kinase 2 remains competent to support PIC assembl
196 ation of ErbB2 or loss of the betasubunit of casein kinase 2, shifted the whole population toward a f
197 ly, in vitro phosphorylation assays with the casein kinase 2 show that the presence of the basic-leuc
209 n FCP1 kinase from HeLa cells and identified casein kinase 2, which, surprisingly, displayed a negati