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1 s the activities of PKC, IP(3) receptor, and phospholipase C beta.
2 iting G alpha(q) stimulation of the effector phospholipase C beta.
3 alpha protein responsible for activation of phospholipase C beta.
4 rotein signaling pathways such as Galpha and phospholipase C-beta.
5 pha) from activating its downstream effector phospholipase C-beta.
6 aused a decrement in its ability to activate phospholipase C-beta.
7 mer had no effect on its ability to activate phospholipase C-beta.
8 y protein kinase C, possibly at the level of phospholipase C-beta.
9 om Galpha(q) to the nucleus independently of phospholipase C-beta.
10 hatidylinositol (4,5)-bisphosphate (PIP2) by phospholipase C beta 1 (PLC beta 1) and PLC beta 2 in mi
19 q alpha and the single Cys mutants activated phospholipase C-beta 1 normally, while the double Cys mu
20 er, the ETA receptor and downstream effector phospholipase C-beta 1 were co-localized within T-tubule
21 ailed to alter interactions of Gq alpha with phospholipase C-beta 1, the G protein beta gamma subunit
22 yte contractility by activating ETA receptor-phospholipase C-beta 1-PKC-epsilon signaling complexes p
23 es of purified phosphatidylinositol-specific phospholipases C-beta 1 and C-beta 2 to membranes of var
24 ng affinity of phosphatidylinositol-specific phospholipases C-beta 1, even though alpha 11 is a poten
26 role of phosphatidic acid (PA) in regulating phospholipase C-beta(1) (PLC-beta(1)) activity was deter
27 ivity of mammalian phosphoinositide-specific phospholipase C beta 2 (PLC-beta 2) is regulated by the
28 din 1, delta-like 4, BclII modifying factor, phospholipase C, beta 2, adrenergic receptor, beta 1, ac
29 association of phosphatidylinositol-specific phospholipases C-beta 2 even though these subunits stron
30 ype and mutant Gbetagamma subunits activated phospholipase C beta(2) with similar potencies; however,
31 d protein chimeras in which the PH domain of phospholipase C-beta(2) (PLC-beta(2)), which is regulate
32 hmerle (she) encodes a zebrafish ortholog of Phospholipase C, beta 3 (Plcbeta3) required in cranial n
35 ing-10; G-protein coupled receptor kinase-2; phospholipase C beta-3; arrestin) is predicted and valid
36 a(q) and regulation of G alpha(q)-stimulated phospholipase C beta activity when introduced into full-
38 R activated NF-kappaB without an increase in phospholipase C-beta activity, and the response was only
39 activation was paralleled by an increase in phospholipase C-beta activity, and was blocked by pharma
40 the NHERF2 PTH1R complex markedly activates phospholipase C beta and inhibits adenylyl cyclase throu
41 ma(2) were 10-fold less potent in activating phospholipase C-beta and adenylyl cyclase than beta(1)ga
42 ptors couple preferentially to activation of phospholipase C-beta and in some cells to stimulation of
43 timulates CREB transcriptional activity in a phospholipase C-beta and protein kinase C (PKC)-dependen
45 nity and was unable to mediate activation of phospholipase C-beta and the p42/44 mitogen-activated pr
46 s well established that adenylyl cyclase and phospholipase C-beta are two proximal signal effectors f
47 uroactive substances increased the amount of phospholipase C-beta associated with membranes, G(alphaq
50 y inhibited Galpha(q)-mediated activation of phospholipase C-beta both in vitro and in cells, possibl
51 more, these RGS proteins block activation of phospholipase C beta by guanosine 5'-(3-O-thio) triphosp
52 lated HUVEC migration and proliferation in a phospholipase C beta-dependent fashion and decreased Gal
53 hototransduction pathway, which requires the phospholipase C-beta encoded by norpA (no receptor poten
54 examined in three assays: activation of pure phospholipase C-beta in lipid vesicles; activation of re
55 A kinase defective protein kinase D and a phospholipase C beta inhibitor blocked receptor-induced
57 xamined for their ability to stimulate three phospholipase C-beta isozymes and type II adenylyl cycla
58 effect of NAC on Galphaq palmitoylation and phospholipase C beta-mediated signaling in endothelial c
59 Here, we show that TRP forms a complex with phospholipase C-beta (NORPA), rhodopsin (RH1), calmoduli
60 eved either by agonist-induced activation of phospholipase C beta or with a rapamycin-inducible syste
61 , there were no differences in the levels of phospholipase C-beta or protein kinase C-alpha in the tw
63 annels that are not only activated by the Gq-phospholipase C beta pathway (receptor-activated Ca entr
64 + entry in response to stimulation of the Gq-phospholipase C beta pathway, which is similar to that m
66 of forskolin-stimulated adenylyl cyclase and phospholipase C beta (PLC beta) activation was measured
67 n through G alpha(q) involves stimulation of phospholipase C beta (PLC beta) that results in increase
69 t protein kinases inhibit agonist-stimulated phospholipase C-beta (PLC-beta) activity and inositol 1,
73 e have demonstrated that G-protein-activated phospholipase C-beta (PLC-beta) interacts with cell pola
74 ignaling from G protein-coupled receptors to phospholipase C-beta (PLC-beta) is regulated by coordina
77 gamma subunits, and some Rho family GTPases, phospholipase C-beta (PLC-beta) isoforms hydrolyze phosp
78 G proteins to activation of an unidentified phospholipase C-beta (PLC-beta) isozyme and inhibition o
80 the cells with ACh and an m2 antagonist, the phospholipase C-beta (PLC-beta) response to CCK-8 and SP
81 trate that US28/1-314 exhibits a more potent phospholipase C-beta (PLC-beta) signal than does wild-ty
82 nhibition or activation of Ca2+ channels and phospholipase C-beta (PLC-beta), the enzyme responsible
83 uction which include the essential effector, phospholipase C-beta (PLC-beta), which is also known as
86 ported the coupling of dopamine signaling to phospholipase C beta (PLCbeta) both in vitro and in vivo
87 and one of its downstream signal transducer phospholipase C beta (PLCbeta) can differentially affect
88 with the specific inhibitors of Gbetagamma, phospholipase C-beta (PLCbeta), or PKC, but not of prote
89 eptor antagonist, chemical disruptors of the phospholipase C-beta, protein kinase A, c-Src and epider
90 he presence of phosphatidylinositol-specific phospholipases C-beta s' major physiological substrate,
91 MCMV is an activator of CREB, NF-kappaB, and phospholipase C-beta signaling pathways and has been imp
92 ) is more potent and effective in activating phospholipase C-beta than either the beta1 gamma1 (farne
95 CC3 domain inhibited PAR1 signaling to G(q)-phospholipase C-beta through coiled-coil interactions wi
97 om the plasma membrane through the action of phospholipase C-beta, triggering translocation of tubby
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