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