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1 n of mevalonate, the metabolic precursor for geranylgeranyl.
4 ds, we show that PDEdelta specifically binds geranylgeranyl and farnesyl moieties with a Kd of 19.06
5 the isoprenoid of gamma(1) from farnesyl to geranylgeranyl and of gamma(2) from geranylgeranyl to fa
7 LCK: myristoyl, palmitoyl, palmitoyl), RhoA (geranylgeranyl), and K-Ras (farnesyl) proteins in differ
10 94 of the RhoGDIalpha are located within the geranylgeranyl binding pocket, suggesting that halothane
12 st that halothane binds to a site within the geranylgeranyl chain binding pocket of RhoGDIalpha, wher
13 located in the vicinity of, but outside, the geranylgeranyl chain binding pocket, suggesting that the
14 uble bonds and branched methyl groups of the geranylgeranyl chain significantly restrict the number o
19 (geranylgeranyl) and the beta1 gamma11-S73L (geranylgeranyl) dimers were more active than the native
21 complex cyclization-rearrangement of (E,E,E)-geranylgeranyl diphosphate (8, GGPP) to a mixture of abi
23 r for protein geranylgeranylation reactions, geranylgeranyl diphosphate (GGDP), is the product of the
24 ilic substitution reaction between the C(20) geranylgeranyl diphosphate (GGPP) and a protein-derived
25 of approximately 55 carbons in length using geranylgeranyl diphosphate (GGPP) and isopentenyl diphos
27 diphosphates farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP) are intermediates in t
28 In plants, farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP) are precursors to many
29 hypothesis, the current study identifies C20 geranylgeranyl diphosphate (GGPP) as a precursor for lyc
30 alized) metabolism via cycloisomerization of geranylgeranyl diphosphate (GGPP) by diterpene synthases
31 (MpGPS.SSU) on production of monoterpene and geranylgeranyl diphosphate (GGPP) diversities, and plant
32 LSU produced GPP, farnesyl diphosphate, and geranylgeranyl diphosphate (GGPP) from dimethylallyl dip
33 PS2) of specialized metabolism that converts geranylgeranyl diphosphate (GGPP) into labda-7,13E-dieny
35 logues suggests that the C-10 locus of bound geranylgeranyl diphosphate (GGPP) is in close proximity
36 es a bifunctional farnesyl diphosphate (FPP)/geranylgeranyl diphosphate (GGPP) synthase (TgFPPS) that
37 uced elsewhere in the plant cell derive from geranylgeranyl diphosphate (GGPP) synthesized by GGPP sy
38 clization of the linear isoprenoid substrate geranylgeranyl diphosphate (GGPP) to form taxa-4(5),11(1
39 talyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene di
40 lation of (S)-glyceryl phosphate [(S)-GP] by geranylgeranyl diphosphate (GGPP) to produce (S)-geranyl
41 ynthase catalyzes the cyclization of (E,E,E)-geranylgeranyl diphosphate (GGPP) to taxa-4(5),11(12)-di
42 bon farnesyl diphosphate (FPP), or 20-carbon geranylgeranyl diphosphate (GGPP) via a dioxygenase- or
44 ynthase catalyzes the synthesis of all-trans-geranylgeranyl diphosphate (GGPP), an isoprenoid used fo
45 te synthase (CPS), whose substrate, (E,E,E,)-geranylgeranyl diphosphate (GGPP), is also a direct prec
46 nthesis, is composed of a chlorin ring and a geranylgeranyl diphosphate (GGPP)-derived isoprenoid, wh
48 ne synthase-catalyzed cyclization of (E,E,E)-geranylgeranyl diphosphate (GGPP, 7) to taxadiene (5) is
49 etic evaluation of abietadiene synthase with geranylgeranyl diphosphate and (+)-copalyl diphosphate p
50 l, mechanistically distinct cyclizations, of geranylgeranyl diphosphate and of copalyl diphosphate, i
51 sidues deleted from the preprotein converted geranylgeranyl diphosphate and the intermediate (+)-copa
53 nant Escherichia coli-expressed protein used geranylgeranyl diphosphate as substrate and catalyzed th
55 for renal function, identifying dysregulated geranylgeranyl diphosphate biosynthesis as a potential d
57 iphosphate, which is made from the all-trans geranylgeranyl diphosphate by copal-8-ol diphosphate syn
58 ps from the universal diterpenoid progenitor geranylgeranyl diphosphate derived by the plastidial met
59 tional class I diTPS PxaTPS8, which converts geranylgeranyl diphosphate into a previously unknown 5,7
60 In M. tuberculosis, however, omega,E,E,E-geranylgeranyl diphosphate is not utilized for the synth
61 decaprenyl diphosphate, and the omega,E,E,E-geranylgeranyl diphosphate is utilized by a membrane-ass
62 fold), and in planta geranyl diphosphate and geranylgeranyl diphosphate levels (4- to 8-fold) were si
64 hosphate synthase, shown here to produce the geranylgeranyl diphosphate precursor, providing a critic
65 hesis and forces reevaluation of the role of geranylgeranyl diphosphate reductase in tocopherol biosy
66 of modifying the chain length specificity of geranylgeranyl diphosphate synthase (but not, apparently
67 rotein that could be identified as the mouse geranylgeranyl diphosphate synthase (GGPP synthase) base
68 h-rescue" and enzyme-inhibition experiments, geranylgeranyl diphosphate synthase (GGPPS) is shown to
69 large subunit, which may be either an active geranylgeranyl diphosphate synthase (GGPPS) or an inacti
70 of farnesyl diphosphate synthase (FPPS) and geranylgeranyl diphosphate synthase (GGPPS), the two enz
71 report the inhibition of a human recombinant geranylgeranyl diphosphate synthase (GGPPSase) by 23 bis
72 way by generating combinatorial mutations in geranylgeranyl diphosphate synthase and levopimaradiene
73 tional spruce IDS, a geranyl diphosphate and geranylgeranyl diphosphate synthase in white spruce (Pic
74 acts with a catalytic large subunit, such as geranylgeranyl diphosphate synthase, and determines its
75 e known to serve as inhibitors of the enzyme geranylgeranyl diphosphate synthase, and their activity
76 In contrast, a strain of E. coli carrying geranylgeranyl diphosphate synthase, phytoene desaturase
77 including farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase, that catalyzes the
78 Unlike farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase, which are homodimer
81 -erythritol-4-phosphate (MEP) pathway genes, geranylgeranyl diphosphate synthases 3 (GGPPS3) and GGPP
82 ll subunit with the phylogenetically distant geranylgeranyl diphosphate synthases from Taxus canadens
83 f amino acid sequence identity (56-75%) with geranylgeranyl diphosphate synthases of plant origin.
84 eam pathways for isopentenyl diphosphate and geranylgeranyl diphosphate synthesis and the downstream
85 tive sites, the first for the cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate an
86 se residues in catalyzing the cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate.
87 y distinct cyclizations in the conversion of geranylgeranyl diphosphate to a mixture of abietadiene d
88 g diterpene cyclases that together transform geranylgeranyl diphosphate to ent-kaurene, the olefin pr
89 converts the universal diterpenoid precursor geranylgeranyl diphosphate to syn-CPP catalyzes the comm
90 ynthesis of Taxol involve the cyclization of geranylgeranyl diphosphate to taxa-4(5),11(12)-diene fol
91 atalyzes the transfer of a prenyl group from geranylgeranyl diphosphate to the carboxy-terminal cyste
92 oth the protonation-initiated cyclization of geranylgeranyl diphosphate to the intermediate (+)-copal
93 hase) for conversion of the acyclic, achiral geranylgeranyl diphosphate to the polycyclic, chiral abi
94 , converts the universal diterpene precursor geranylgeranyl diphosphate to the stable bicyclic interm
97 ate from the universal diterpenoid precursor geranylgeranyl diphosphate was also mapped to this same
98 hway-intermediates, farnesyl diphosphate and geranylgeranyl diphosphate, also reduced endometrial cel
99 ays use [(3)H]farnesyl diphosphate and [(3)H]geranylgeranyl diphosphate, electrophoretic mobility shi
100 ich is produced from the substrate all-trans geranylgeranyl diphosphate, represents a so far unidenti
101 f lipid groups from farnesyl diphosphate and geranylgeranyl diphosphate, respectively, to a cysteine
102 This study suggests that, in osteoclasts, geranylgeranyl diphosphate, the substrate for prenylatio
103 ranyl diphosphate, farnesyl diphosphate, and geranylgeranyl diphosphate, to the parent structures of
104 ega,E,Z-farnesyl diphosphate, or omega,E,E,E-geranylgeranyl diphosphate, with Km values for the allyl
105 or 5',6' bond positions of lycopene but not geranylgeranyl diphosphate, zeta-carotene, or phytoene.
106 oding isoprenoid isopentenyl diphosphate and geranylgeranyl diphosphate-producing enzymes, DXS3, DXR,
112 the first bifunctional farnesyl-diphosphate/geranylgeranyl-diphosphate synthase identified in eukary
113 o enzymes, farnesyl-diphosphate synthase and geranylgeranyl-diphosphate synthase, required for the pr
115 e inhibitor of the 20S proteasome, prevented geranylgeranyl-enhanced degradation of Rho proteins.
117 1)gamma(2) complex required insertion of the geranylgeranyl group into the prenyl pocket in order to
119 p) and the beta1gamma2 dimer (containing the geranylgeranyl group) were purified from baculovirus-inf
124 n either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid covalently attached to cystein
125 n either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid covalently attached via a thio
127 ase-catalyzed addition of either farnesyl or geranylgeranyl isoprenoid lipids, Rce1-catalyzed endopro
129 In this study, we focused on the role of geranylgeranyl isoprenoids GGPP and geranylgeraniol (GGO
134 ting in the addition of either a farnesyl or geranylgeranyl isoprenyl lipid moiety to the cysteine re
135 ith either a 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenyl lipid, proteolysis of the C-ter
136 These data demonstrate that inhibition of geranylgeranyl isoprenylation of CaaX proteins in the aq
141 th adenosine plus homocysteine or N-acetyl-S-geranylgeranyl-l-cysteine decreased RhoA carboxyl methyl
144 e I (GGTase I) catalyzes the attachment of a geranylgeranyl lipid group near the carboxyl terminus of
145 ns are posttranslationally modified with two geranylgeranyl lipid moieties that enable their stable a
146 I) catalyze the attachment of a farnesyl or geranylgeranyl lipid, respectively, near the C-terminus
147 he modification of proteins with farnesyl or geranylgeranyl lipids, a process called protein prenylat
149 aining chimeric Ggamma chains with identical geranylgeranyl modification displayed rhodopsin affiniti
150 ince these molecules require modification by geranylgeranyl moieties for their cellular localization
151 es not have a preference for the farnesyl or geranylgeranyl moieties in the model substrates N-acetyl
152 y to use farnesol to label both farnesyl and geranylgeranyl moieties on proteins, differentiation spe
156 polybasic domain"), directly preceding their geranylgeranyl moiety, and it has been suggested that th
159 enzymatic conversion of [(3)H]GG-OH to [(3)H]geranylgeranyl monophosphate and [(3)H]geranylgeranyl py
160 taining hydrophobic modifications other than geranylgeranyl or farnesyl do not bind with significant
161 ine nucleotides and their prenylation with a geranylgeranyl or farnesyl isoprenoid moiety and subsequ
163 Switching prenyl groups from farnesyl to geranylgeranyl or vice versa had little effect on bindin
164 h either the gamma(2) subunit (modified with geranylgeranyl) or the gamma(2-L71S) subunit (gamma(2) w
165 dolichyl-P-P, dolichyl-P, farnesyl-P-P, and geranylgeranyl-P-P but also suggest that yeast contain o
167 The retention times for farnesyl-peptide and geranylgeranyl-peptide are 8.4 and 16.9 min, respectivel
168 ults demonstrate that specific inhibition of geranylgeranyl prenylation causes a potent and selective
169 The findings indicate that inhibition of geranylgeranyl prenylation should be further studied as
170 going alternative prenylation by the related geranylgeranyl protein transferase I (GGPTase-I) in huma
171 Farnesyl protein transferase (FTase) or geranylgeranyl protein transferase I (GGTase I) were use
172 recombinant farnesyl protein transferase or geranylgeranyl protein transferase I are performed to co
173 tivity against farnesyl protein transferase, geranylgeranyl protein transferase I, FPP synthase, or G
174 racterized potent and specific inhibitors of geranylgeranyl-protein transferase type I (GGPTase I), a
175 ng little inhibitory activity against either geranylgeranyl-protein transferase type I (GGTase I) (K(
176 dification by the related prenyltransferase, geranylgeranyl:protein transferase type I (GGPTase-I).
177 uvastatin were reversed by mevalonic acid or geranylgeranyl pyrophosphatase, and mimicked by geranylg
180 [(3)H]geranylgeranyl monophosphate and [(3)H]geranylgeranyl pyrophosphate ([(3)H]GG-P-P) in CTP-depen
181 isoprenoids farnesyl pyrophosphate (FPP) and geranylgeranyl pyrophosphate (GGPP) are synthetic precur
182 he isoprenyl precursors, mevalonic acid, and geranylgeranyl pyrophosphate (GGpp) attenuated the stati
183 fer with a lower efficiency than FPP whereas geranylgeranyl pyrophosphate (GGPP) does not transfer at
184 trations of farnesyl pyrophosphate (FPP) and geranylgeranyl pyrophosphate (GGPP) in cultured cells.
185 nce that the FPP-derived, 20-carbon molecule geranylgeranyl pyrophosphate (GGPP) is a potent endogeno
186 cessing and prevents RhoB upregulation while geranylgeranyl pyrophosphate (GGPP) restores Rap1a proce
187 ferase domain-containing protein-1) utilizes geranylgeranyl pyrophosphate (GGpp) to synthesize vitami
189 d by farnesyl pyrophosphate (FPP) but not by geranylgeranyl pyrophosphate (GGPP), implicating perturb
190 trong anion dependence were competitive with geranylgeranyl pyrophosphate (GGPP), rather than with th
191 metabolites farnesyl pyrophosphate (FPP) and geranylgeranyl pyrophosphate (GGPP), which are used for
192 in this article that downstream depletion of geranylgeranyl pyrophosphate (GGPP), which is required f
198 ation and was employed for detection of both geranylgeranyl pyrophosphate and a secondary oxysterol s
199 ibitor lovastatin depletes cellular pools of geranylgeranyl pyrophosphate and farnesol pyrophosphate
200 rations of isoprenoid intermediates, such as geranylgeranyl pyrophosphate and farnesyl pyrophosphate.
201 cretion and mRNA levels, effects reversed by geranylgeranyl pyrophosphate and mimicked by inhibiting
203 revented by mevalonate and by the isoprenoid geranylgeranyl pyrophosphate but not by cholesterol.
204 to simvastatin were blocked by mevalonate or geranylgeranyl pyrophosphate but not by farnesyl pyropho
205 nthesis pathway intermediates mevalonate and geranylgeranyl pyrophosphate but not squalene, indicatin
206 f simvastatin was reversed by mevalonate and geranylgeranyl pyrophosphate but not squalene, indicatin
209 oli, to esterify bacteriochlorophyllide with geranylgeranyl pyrophosphate in vitro, thereby generatin
211 Pases with isoprenoid molecules derived from geranylgeranyl pyrophosphate or farnesyl pyrophosphate i
216 of transcription 1), a downstream target of geranylgeranyl pyrophosphate signaling, was enhanced.
217 ere we report the crystal structure of human geranylgeranyl pyrophosphate synthase, the first mammali
222 or farnesyl pyrophosphate and its derivative geranylgeranyl pyrophosphate were also increased in the
223 ects were absent in slices co-incubated with geranylgeranyl pyrophosphate, a mevalonate product that
225 This inhibitory effect was reversed with geranylgeranyl pyrophosphate, an isoprenoid intermediate
226 are completely reversed by mevalonate and by geranylgeranyl pyrophosphate, implicating geranylgeranyl
227 t Hmg2 degradation is the 20-carbon isoprene geranylgeranyl pyrophosphate, rather than a sterol.
228 or the inhibition of tube formation, whereas geranylgeranyl pyrophosphate, the substrate for the gera
229 ication by regulating the cellular levels of geranylgeranyl pyrophosphate, we demonstrate that the im
234 the presence or absence of mevalonate (MVA), geranylgeranyl-pyrophosphate (GGPP) and farnesyl-pyropho
236 nprecedented evidence that-like immune cells-geranylgeranyl-pyrophosphate depletion and thus inhibiti
237 imvastatin was blocked after incubation with geranylgeranyl-pyrophosphate to circumvent loss of isopr
238 n of isoprenoids (farnesyl-pyrophosphate and geranylgeranyl-pyrophosphate) rather than cholesterol in
239 ersed by cotreatment with mevalonolactone or geranylgeranyl-pyrophosphate, but not by farnesyl-pyroph
242 Initially, LIL3 was shown to interact with geranylgeranyl reductase (CHLP), an enzyme of terpene bi
243 t due to the decreasing transcript levels of geranylgeranyl reductase (GGDR) which restricts the isop
245 thesis and signaling and on AZI1 Arabidopsis geranylgeranyl reductase1 mutants with reduced monoterpe
249 lls, implying that a dependence on 20-carbon geranylgeranyl signals may be a common conserved feature
250 -specific inhibitor), however, abolished the geranylgeranyl-supplementation-induced recovery from the
251 geranyl (GSPP), (S)-farnesyl (FSPP), and (S)-geranylgeranyl thiodiphosphate (GGSPP) were prepared fro
252 nesyl to geranylgeranyl and of gamma(2) from geranylgeranyl to farnesyl had no impact on the affiniti
255 ein farnesyl transferase (FTase) and protein geranylgeranyl transferase (GGTase) inhibitors as cancer
257 onstrated that coexpression of homogentisate geranylgeranyl transferase (HGGT), stacked with caroteno
260 cceptor site within the alpha-subunit of Rab geranylgeranyl transferase (Rabggta), an enzyme that att
262 FPPS (IC50 > 600 microM), but inhibited Rab geranylgeranyl transferase (RGGT) (IC50 = 16-35 microM)
263 bone affinity than 2 and weakly inhibits Rab geranylgeranyl transferase (RGGT), selectively preventin
264 of farnesyl transferase (such as Ras) and of geranylgeranyl transferase (such as RAP-1) were inhibite
266 change factor, GTPase activating protein, or geranylgeranyl transferase activity in vitro but promote
268 hibitors of protein farnesyl transferase and geranylgeranyl transferase enzymes and in mutant mice hy
272 but not binucleation, was also caused by the geranylgeranyl transferase I inhibitor, GGTI-298, which
274 A reductase, or with an inhibitor of protein geranylgeranyl transferase I, each of which induced the
275 b GTPases by the cytosolic heterodimeric Rab geranylgeranyl transferase II complex (RabGG transferase
277 otein prenylation by farnesyl transferase or geranylgeranyl transferase in vitro, in cultured cells a
278 ein prenylation and blocking the activity of geranylgeranyl transferase induces a venous angiogenesis
280 vastatin was reproduced by incubation with a geranylgeranyl transferase inhibitor and blocked by coex
281 nesyl transferase (FT) inhibitor FTI-276 and geranylgeranyl transferase inhibitor GGTI-298, and preny
282 ted by simvastatin, we demonstrated that the geranylgeranyl transferase inhibitor replicated the effe
283 tion of FBXL2 localization with GGTi-2418, a geranylgeranyl transferase inhibitor, sensitizes xenotra
284 by inhibitors of geranylgeranyl-transferase (geranylgeranyl transferase inhibitor-298) and downstream
286 the development of farnesyl transferase and geranylgeranyl transferase inhibitors (FTIs and GGTIs) a
287 geranylgeranylation either directly through geranylgeranyl transferase inhibitors or indirectly thro
288 rophosphate prevented, whereas inhibition of geranylgeranyl transferase mimicked, the effects of lova
289 treatment of Caco-2 cells with inhibitors of geranylgeranyl transferase or the Rho proteins significa
290 in geranylgeranylation, embryos deficient in geranylgeranyl transferase type I show germ cell migrati
293 hibition of isoprenylation via reductions in geranylgeranyl transferase-1 activity as well as increas
298 of lovastatin were mimicked by inhibitors of geranylgeranyl-transferase (geranylgeranyl transferase i
299 s of the alternative prenylation of K-Ras by geranylgeranyl-transferase I (when FTase is inhibited) i
300 hydrophobic prenyl group (either farnesyl or geranylgeranyl), which localises the GTPase to cell memb
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