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1 ty stimulatable by the inhibitory subunit of cGMP phosphodiesterase.
2 sites on G alpha t with the effector enzyme cGMP phosphodiesterase.
3 degeneration caused by a defective opsin or cGMP phosphodiesterase.
4 protein transducin, which in turn stimulates cGMP phosphodiesterase.
5 or the gene encoding the beta-subunit of the cGMP phosphodiesterase.
6 pigment, rhodopsin, and the effector enzyme, cGMP phosphodiesterase.
7 sing it to bind GTP and stimulate the enzyme cGMP phosphodiesterase.
8 ntly after transducin binds to its effector, cGMP phosphodiesterase.
9 es the phosphorylation profile of a putative cGMP-phosphodiesterase.
10 D sulindac that has been reported to inhibit cGMP phosphodiesterases.
12 P as bait we identified the delta subunit of cGMP phosphodiesterase 6 (PDE6delta) as a novel hIP-inte
13 ed rhodopsin or more efficient activation of cGMP phosphodiesterase 6 by G alpha(t)G2A; alternatively
18 ation, rhodopsin-transducin (G(t)) coupling, cGMP phosphodiesterase activity, and slower formation of
20 tly bind the bilin phycocyanobilin via their cGMP phosphodiesterase/adenyl cyclase/FhlA (GAF) domains
23 , and molecular modeling of the Te-PixJ GAF (cGMP phosphodiesterase/adenyl cyclase/FhlA) domain assem
24 bring together the PAS (Per-ARNT-Sim), GAF (cGMP phosphodiesterase/adenyl cyclase/FhlA), and PHY (ph
25 olution structure of the chromophore-binding cGMP phosphodiesterase/adenylcyclase/FhlA (GAF) domain f
26 ines and a hairpin protrusion connecting the cGMP phosphodiesterase/adenylyl cyclase/FhlA (GAF) and p
27 ture of photoconversion for the photosensing cGMP phosphodiesterase/adenylyl cyclase/FhlA (GAF) domai
28 ytochromobilin chromophore buried within the cGMP phosphodiesterase/adenylyl cyclase/FhlA (GAF) domai
29 states following studies of the 23-kDa GAF (cGMP phosphodiesterase/adenylyl cyclase/FhlA) domain fra
30 -cGMP or by MY-5445 (a specific inhibitor of cGMP phosphodiesterase) alone suggest that NO increases
31 action between the gamma subunit (Pgamma) of cGMP phosphodiesterase and the alpha subunit (Talpha) of
32 ptosyn) and certain derivatives that inhibit cGMP-phosphodiesterases and thereby increase cellular le
33 function, its poor ability to activate PDE6 (cGMP phosphodiesterase) and decreased GTPase activity, a
34 on of G alpha(transducin) with its effector, cGMP phosphodiesterase, and inhibits transducin-mediated
35 ks the lipid modifications found on G(t) and cGMP phosphodiesterase, and the mechanism for membrane a
38 ly demonstrated that 350 bp of the human rod cGMP phosphodiesterase beta-subunit (beta-PDE) gene prom
39 utations in the genes encoding rhodopsin and cGMP phosphodiesterase beta-subunit (PDE-beta) respectiv
40 rod-specific genes, including rhodopsin and cGMP phosphodiesterase beta-subunit, in synergy with oth
42 e OSI-461, both of which inhibit cyclic GMP (cGMP)-phosphodiesterases but lack COX-2 inhibitory activ
43 cin mediates signaling between rhodopsin and cGMP phosphodiesterase by transiently binding its gamma
45 rate photoreceptors leads to activation of a cGMP-phosphodiesterase effector and the generation of a
47 M in rod photoreceptors, it is possible that cGMP phosphodiesterase functions to increase cytoplasami
48 tion of GAP activity by an effector subunit, cGMP phosphodiesterase gamma and in protein folding and
53 ansducin is a key step for the regulation of cGMP phosphodiesterase in retinal rod outer segments.
54 ted rhodopsin (R*) with the effector enzyme, cGMP phosphodiesterase in vertebrate photoreceptor cells
55 ucin the G-protein that couples rhodopsin to cGMP-phosphodiesterase in the phototransduction cascade.
56 optosis by a mechanism involving cyclic GMP (cGMP) phosphodiesterase inhibition, sustained elevation
60 with cell permeable cGMP derivatives, or the cGMP phosphodiesterase inhibitor sulindac sulfone (exisu
63 We have used this natural mutation, and the cGMP phosphodiesterase inhibitor zaprinast, in wild-type
64 gradation with sildenafil, a specific type 5 cGMP phosphodiesterase inhibitor, on flow-mediated dilat
65 tion or environmental acidification, while a cGMP-phosphodiesterase inhibitor circumvents egress repr
67 transducin (G(t alpha)), interacts with the cGMP phosphodiesterase inhibitory gamma-subunit (Pgamma)
69 otransduction partners transducin (G(t)) and cGMP phosphodiesterase, it is a peripheral protein of th
71 The mammalian multisubunit photoreceptor cGMP phosphodiesterase PDE alpha beta gamma 2 (PDE6 fami
72 of the gamma-subunit of its effector enzyme, cGMP phosphodiesterase (PDE gamma), and another yet unid
73 -displayed arrestin fragments against RP and cGMP phosphodiesterase (PDE) activity inhibition using s
74 PDEdelta was originally copurified with rod cGMP phosphodiesterase (PDE) and shown to interact with
75 it of transducin (Galphat-GTP) activates the cGMP phosphodiesterase (PDE) by binding the inhibitory g
78 y, there was a reduction in the level of rod cGMP phosphodiesterase (PDE) proportional to the decreas
79 se is generated by spontaneous activation of cGMP phosphodiesterase (PDE) through a process that does
81 ontrols inactivation of the effector enzyme, cGMP phosphodiesterase (PDE), during turnoff of the visu
82 hown that P gamma, the regulatory subunit of cGMP phosphodiesterase (PDE), is ADP-ribosylated by endo
83 tolerance would be increased activity of the cGMP phosphodiesterase (PDE), which decreases cGMP level
84 monitored rhodopsin-dependent activation of cGMP phosphodiesterase (PDE), wild type arrestin quenche
89 etinal cyclic guanosine 3',5'-monophosphate (cGMP) phosphodiesterase (PDE) is a key regulator of phot
90 cells contain guanosine 3',5'-monophosphate (cGMP) phosphodiesterase (PDE) isoforms of the PDE5 and P
93 The catalytic core of photoreceptor-specific cGMP-phosphodiesterase (PDE) consists of two subunits, P
97 ation channel-3 [CNG3], blue-cone opsin, and cGMP phosphodiesterase [PDE]); were evaluated during dif
98 ccompanied by a rapid phosphorylation of the cGMP phosphodiesterase PDE5, an enzyme whose activity is
100 ein transducin (G(t)) on the effector enzyme cGMP phosphodiesterase (PDE6) at the surface of disk mem
101 the inhibitory gamma subunit (Pgamma) of rod cGMP phosphodiesterase (PDE6) has been reported to turn
108 The unique feature of rod photoreceptor cGMP phosphodiesterase (PDE6) is the presence of inhibit
110 was originally identified as a putative rod cGMP phosphodiesterase (PDE6) subunit in the retina, whe
111 ue to the massive reduction in levels of rod cGMP phosphodiesterase (PDE6) subunits (alpha, beta, and
112 transduction in retinal rod photoreceptors, cGMP phosphodiesterase (PDE6), is a catalytic heterodime
113 l enzyme of the visual transduction cascade, cGMP phosphodiesterase (PDE6), is regulated by its gamma
118 otoreceptor G protein, transducin, activates cGMP-phosphodiesterase (PDE6) by displacing the inhibito
119 o studies, showing that the delta subunit of cGMP phosphodiesterase (PDEdelta), which possesses a hyd
125 GMP but modestly inhibited by rolipram and a cGMP phosphodiesterase peak that was sensitive to inhibi
127 cally with transducin bound to its effector, cGMP phosphodiesterase, rather than with transducin alon
128 due to a mutation of the rod-specific enzyme cGMP phosphodiesterase, resulting in permanently opened
129 alysis of the Galpha(t)G38D interaction with cGMP phosphodiesterase revealed marked impairment of the
130 gene PDE6B encoding the beta subunit of rod cGMP-phosphodiesterase shows that the cGMP-binding and c
131 analog) or MY-5445 (a specific inhibitor of cGMP phosphodiesterase) suggests that NO induces GFAP vi
132 er inhibitory activity for trypsin-activated cGMP phosphodiesterase than nonphosphorylated P gamma, i
133 t synergistically with a downstream effector cGMP phosphodiesterase to stimulate the GTPase activity
134 joins rhodopsin and the beta subunit of rod cGMP-phosphodiesterase to become the third component of
136 nd the factors controlling expression of the cGMP phosphodiesterase type 6 (PDE6) genes, we have char
138 d with the alphabeta subunit (Palphabeta) of cGMP phosphodiesterase, was specifically radiolabeled by
139 on of RGS9-1.Gbeta5L by the effector enzyme, cGMP phosphodiesterase, which is based entirely on the e
140 (dB-cGMP), and of the selective inhibitor of cGMP-phosphodiesterase zaprinast (ZAP), caused an inhibi
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