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1 fied protein, RACK-1 (receptor for activated C kinase).
2 collectively RACKs (receptors for activated C-kinase).
3 teins, STICKs (substrates that interact with C-kinase).
4 zyme-specific RACKs (receptors for activated C-kinase).
5 tively called RACKs (Receptors for Activated C-Kinases).
6 h Hesperadin, a potent inhibitor of Aurora B/C kinases.
10 ) domain-containing protein interacting with C kinase 1 (PICK1), because MF-PYR synapses in young PIC
11 protein (GRIP) and protein interacting with C kinase 1 (PICK1)-regulate the availability of AMPARs f
14 Caenorhabditis elegans Receptor of Activated C Kinase 1 (RACK-1) is required for cytokinesis, germlin
15 f these proteins, the receptor for activated C kinase 1 (RACK1) and the dynein intermediate chain, co
16 p-regulated levels of receptor for activated C kinase 1 (RACK1) and the intermediate filament protein
20 ere, we show that the receptor for activated C kinase 1 (RACK1) is a novel pVHL-interacting protein.
21 demonstrate that the receptor for activated C kinase 1 (RACK1) serves as an adaptor for PKC-mediated
22 re we report that the receptor for activated C kinase 1 (RACK1), a novel binding protein of heterotri
24 agamma interacts with Receptor for Activated C Kinase 1 (RACK1), a protein that not only binds activa
25 -3 interacts with the receptor for activated-C kinase 1 (RACK1), a scaffold protein that folds into a
26 us interacts with the receptor for activated C kinase 1 (RACK1), a scaffolding/anchoring protein impl
28 ytosis, viz., receptor for activated protein C kinase 1 (RACK1), muscle integrin binding protein (MIB
29 r/scaffolding protein receptor for activated C kinase 1 (RACK1), which was previously reported to int
33 ding protein PICK1 (protein interacting with C kinase 1) contains an N-terminal PSD-95/Discs large/ZO
34 suppressor, PICK1 (Protein interacting with C kinase 1), is a transport protein that regulates the t
36 : Increases in c-src, receptor for activated C kinase 1, calreticulin, and caspase 3 and decreases in
37 rectly binds to the protein interacting with C-kinase 1 (PICK1) and forms a complex with alpha-amino-
39 Here we show that protein interacting with C-kinase 1 (PICK1) is a downstream effector of GTP-bound
41 nteraction with the protein interacting with C-kinase 1 (PICK1) to regulate NMDA receptor (NMDAR)-ind
42 rasynaptic sites by protein interacting with C-kinase 1 (PICK1), because disrupting GluR2/PICK1 inter
43 Here, we show that receptor for activated C-kinase 1 (Rack1) can bind with c-Jun and ubiquitin lig
44 e scaffold protein RACK1 (receptor activated C-kinase 1, GNB2L1) as a novel ATG5 interactor and an au
46 lated in neurons by protein interacting with C kinase-1 (PICK1) and protein kinase C (PKC), and show
50 es implicate PICK1 (protein interacting with C kinase-1) in activity-dependent internalization of Glu
51 th respect to RACK-1 (receptor for activated C kinase-1), an adaptor protein that has been proposed t
53 protein or ABP) and protein interacting with C-kinase-1 (PICK) regulate subunit trafficking and plast
54 n (GRIP)/(ABP), and protein interacting with C-kinase-1 (PICK1) that interact with the GluR2 subunit
56 raction of TRPC3 with receptor for activated C-kinase-1 (RACK1) not only determines plasma membrane l
58 we show that PICK1 (protein interacting with C kinase), a PDZ domain-containing protein, interacts wi
59 , we created a genetically encoded reporter (C kinase activity reporter (CKAR)) to visualize the rate
60 gy transfer-based reporter for PKC activity, C kinase activity reporter (CKAR), to the plasma membran
62 t of protein kinase B/Akt and protein kinase C kinase activity, but dependent on calcium/calmodulin s
63 ishmania homologue of receptor for activated C kinase) Ag has been shown to be more durable than vacc
65 oshin-2 from chromosome arms by the Aurora B/C kinase, an event crucial for the efficient resolution
66 e identified RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins
67 shmania homologue of receptors for activated C kinase) and an intradermal murine infection model empl
68 actions with PICK1 (protein interacting with C-kinase) and by dephosphorylating protein kinase C alph
69 SRBC (sdr-related gene product that binds to c-kinase) and two other family members [PTRF (Pol I and
70 protein epsilonRACK (receptor for activated C-kinase), and PKC isozyme-selective inhibitors and acti
71 on) bound to RACK1, a receptor for activated C kinase, and RACK1 bound to the human Na(+)/H(+) exchan
72 eishmania homolog of receptors for activated C kinase) antigen is of interest as a vaccine candidate
74 large lobe, and the protein kinase A, G, and C kinase C-tail greatly impaired receptor phosphorylatio
75 on agonist psiepsilon receptor for activated C kinase caused mitoK(ATP)-dependent inhibition of MPT o
77 otein kinase/protein kinase G/protein kinase C) kinases, controls the processing phosphorylation of c
78 a biallelic splice-site mutation in protein C kinase delta (PRKCD), causing the absence of the corre
79 2-N), (b) kinase-like domain (CD16/Jak2-B), (c) kinase domain (CD16/Jak2-C), or (d) amino-terminal an
80 horing protein RACK1 (receptor for activated C kinase) eliminated the 5-HT(2) modulation of GABA(A) c
81 (for RING-finger protein that interacts with C kinase) from a yeast two-hybrid screen using the amino
83 nRACK (tat-psiepsilon-receptor for activated C kinase), increased the rate of oxygen consumption in t
84 reated cells does not act in the presence of C-kinase inhibitors or cycloheximide, suggesting that si
87 ishmania homologue of activated receptor for c-kinase (LACK), as is the case when these mice are immu
88 its interaction with receptor for activated C kinase, or by suppressing the expression of PKCepsilon
89 e antagonistic (RACK; receptor for activated C kinase) peptide significantly inhibited GPVI and PAR-i
91 Z domain-containing Protein interacting with C kinase (PICK1) and N-ethylmaleimide sensitive fusion p
93 otein (ABP), and protein that interacts with C-kinase (PICK1), but not the PDZ domain protein PSD-95,
94 I regulatory light chain phosphorylation and C-kinase-potentiated protein phosphatase inhibitor phosp
95 agonist, psi epsilon receptor for activated c kinase (psiepsilonRACK) can be prevented, but not reve
96 tapeptide, psiepsilon receptor for activated C-kinase (psiepsilonRACK), derived from an epsilonPKC se
97 ding proteins such as receptor for activated C kinase (RACK) 1 are involved in the targeting of signa
98 In mammalian cells the receptor of activated C kinase (RACK1) is an important scaffolding protein for
99 R, but does bind to a receptor for activated C kinase (RACK1), a 37-kDa scaffold protein, and that RA
100 1.5, K(v)beta1.3, the receptor for activated C kinase (RACK1), PKCbetaI, PKCbetaII, and PKCtheta in H
101 omal subunit protein, receptor for activated C kinase (RACK1), that are not phosphorylated in uninfec
102 olog of the mammalian receptor for activated c kinase (RACK1), that is important for parasite thermot
104 Here we report that a receptor for activated C kinase, RACK1, is a component of messenger ribonucleop
105 of PKCepsilon and its receptor for activated C kinase, RACK2, illustrated a peroxynitrite-dependent i
106 ng proteins, such as receptors for activated C kinase (RACKs), play an important role in regulating t
108 -anchoring proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection
110 crophage-enriched myristoylated alanine-rich C kinase substrate (MacMARCKS), a membrane-associated PK
111 crophage-enriched myristoylated alanine-rice C kinase substrate (MacMARCKS), a membrane-associated PK
112 ne binding of the myristoylated alanine-rich C kinase substrate (MARCKS) [10], but to our knowledge i
115 to phosphorylate myristoylated alanine-rich C kinase substrate (MARCKS) and release phosphatidylinos
116 C at Thr(514) and myristoylated alanine-rich C kinase substrate (MARCKS) and these effects were aboli
117 Here, we identify myristoylated alanine-rich C kinase substrate (MARCKS) as novel PSA binding partner
118 ffector domain of myristoylated alanine-rich C kinase substrate (MARCKS) binds strongly to membranes
120 provided that the myristoylated alanine-rich C kinase substrate (MARCKS) is a central regulatory mole
127 proteins such as myristoylated alanine-rich C kinase substrate (MARCKS) may have a role in regulatin
128 monstrated that a myristoylated alanine-rich C kinase substrate (MARCKS) peptide comprising the phosp
129 responding to the myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation site domain
130 tudy reveals that myristoylated alanine-rich C kinase substrate (MARCKS) protein coordinates activati
131 hosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein in these cells.
132 ne binding of the myristoylated alanine-rich C kinase substrate (MARCKS) requires both its myristate
133 tor region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane
134 ing domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivat
135 or domain (ED) of myristoylated alanine-rich C kinase substrate (MARCKS) which interacts with PSA wit
136 viously found the myristoylated alanine-rich C kinase substrate (MARCKS), a key protein kinase C (PKC
137 entrations of the myristoylated alanine-rich C kinase substrate (MARCKS), a major cellular substrate
138 ffector domain of myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C su
140 tor domain of the myristoylated alanine-rich C kinase substrate (MARCKS), or a peptide corresponding
141 g a COOH-terminal myristoylated alanine-rich C kinase substrate (MARCKS)-related domain that caps and
142 KS (also known as myristoylated alanine-rich C kinase substrate (MARCKS)-related protein) is a member
143 derived from the myristoylated alanine-rich C kinase substrate (MARCKS-PSD, Calbiochem) for use in c
144 hosphorylation of myristoylated alanine-rich C kinase substrate (phospho-MARCKS) at the phosphorylati
146 ein 12 (AKAP12; also known as src-suppressed C kinase substrate (SSeCKS) and Gravin) is a multivalent
148 of phosphorylated myristoylated alanine-rich C kinase substrate and its subsequent diffusion and deph
149 ng domains of the myristoylated alanine-rich C kinase substrate and neuromodulin were previously foun
150 hosphorylation of myristoylated alanine-rich C kinase substrate by membrane-localized PKC constitutes
151 lipid ligand MED (myristoylated alanine-rich C kinase substrate effector domain) or elevated concentr
152 PKC-dependent myristoylated alanine-rich C kinase substrate phosphorylation in epsilonPKC knock-o
154 se anchor protein-myristoylated alanine-rich C kinase substrate protein that may facilitate localized
155 on of eGFP-tagged myristoylated alanine-rich C kinase substrate protein) required oscillatory DAG pro
156 horylation of the myristoylated alanine-rich C kinase substrate protein, a PKC substrate, in phorbol
158 hosphorylation of myristoylated alanine-rich C kinase substrate was decreased, and mRNA levels of nuc
159 peripheral (e.g., myristoylated alanine-rich C kinase substrate) and integral (e.g., the epidermal gr
160 substrate MARCKS (myristoylated alanine-rich C kinase substrate) as a potential target molecule for k
161 e MARCKS protein (myristoylated alanine-rich C kinase substrate) is an actin- and calmodulin-binding
167 on site domain of myristoylated alanine-rich C kinase substrate, a conserved catalytic domain, and fo
171 rate that Lck and myristoylated alanine-rich C kinase substrate, two main myristoylated kinases in T
175 hosphorylation of Myristoylated alanine-rich C-kinase substrate (MARCKS) and LAMC2 protein level were
176 n-binding protein myristoylated alanine-rich C-kinase substrate (MARCKS) as a key mediator of the H(2
177 in of the protein myristoylated alanine-rich C-kinase substrate (MARCKS) bind to phosphatidylserine e
179 phosphorylate the myristoylated alanine-rich C-kinase substrate (MARCKS) motif of DGKzeta, we tested
181 rized MK protein, myristoylated alanine-rich C-kinase substrate (MARCKS), which was upregulated 3.4-
184 ffector domain of myristoylated alanine-rich C-kinase substrate (MARCKS-ED) has been demonstrated to
185 tor domain of the myristoylated alanine-rich C-kinase substrate (MARCKS-ED) is a highly basic, unstru
187 in mice that the myristoylated alanine-rich C-kinase substrate protein (MARCKS), a prominent cellula
188 role of MARCKS (myristoylated, alanine-rich C-kinase substrate) in dendrites of 3-week-old hippocamp
190 ylated (inactive) myristoylated alanine-rich C-kinase substrate, a PKC target that promotes arborizat
191 njury molecule 1, annexin A3, src-suppressed C-kinase substrate, and CD44) and showed a higher prolif
192 Mice lacking the myristoylated alanine-rich C-kinase substrate, or MARCKS protein, exhibit abnormali
194 tor (sdr)-related gene product that binds to c-kinase] was isolated in a yeast two-hybrid screening,
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