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   1  was carried out in 9 steps from trans,trans-farnesyl acetate using a palladium catalyzed decarboxyla
     2 epoxylinalool, (Z)-jasmone, 2-acetylpyrrole, farnesyl acetone, geranyl acetone, cadinol, cubenol and 
     3 imination of hydrogen diphosphate from (E,E)-farnesyl and dimethylallyl diphosphate (FDP and DMADP) t
     4 ed for the DCS-catalyzed turnover of (2Z,6E)-farnesyl and neryl diphosphates, suggested the intermedi
  
     6  in the active state, with membrane-anchored farnesyl and unrestrained HVR, the catalytic domain fluc
     7 ent of Ras-PDEdelta inhibitors targeting the farnesyl binding pocket of PDEdelta with nanomolar affin
  
  
  
  
    12 ofuran analogues were prepared from triepoxy farnesyl bromides by a zinc-initiated reduction-eliminat
    13  on possible polycyclization pathways of the farnesyl cation leading to the complex sesquiterpene pen
  
    15 erate possible carbocations derived from the farnesyl cation, the first reactive intermediate of the 
  
  
    18 , and phosphorylated once more to generate a farnesyl-CoA amphiphile that self-assembles into spheric
    19 cally transferring the farnesyl group of the farnesyl-CoA micelle onto a peptide via phosphopantethei
  
    21  C-terminal membrane anchor that comprises a farnesyl-cysteine-methyl-ester and a polybasic domain.  
    22  and other cis-prenyl transferases (e.g. cis-farnesyl, decaprenyl, undecaprenyl diphosphate synthases
  
    24 ion of the recombinant protein, SAV_76, with farnesyl diphosphate (1, FPP) in the presence of Mg(2+) 
    25 erea, catalyzes the multistep cyclization of farnesyl diphosphate (2) to the tricyclic sesquiterpene 
    26 color catalyzes the multistep cyclization of farnesyl diphosphate (2, FPP) to the tricyclic sesquiter
  
  
  
  
    31 gh either geranyl diphosphate (C10) or trans-farnesyl diphosphate (C15), to yield monoterpenes and se
    32  enzyme GGDP synthase (GGDPS) that condenses farnesyl diphosphate (FDP) and isopentenyl pyrophosphate
    33 10-geranyl diphosphate (GDP) and only 4% C15-farnesyl diphosphate (FDP) in the presence of Co(2+) or 
    34 in order of increasing potency at inhibiting farnesyl diphosphate (FDP) synthase (their intracellular
    35 zes the metal-dependent cyclization of (E,E)-farnesyl diphosphate (FDP) to the cadinane sesquiterpene
    36 idago canadensis catalyzes the conversion of farnesyl diphosphate (FDP) to the plant sesquiterpene (+
  
  
  
    40 trates for modification with the isoprenoids farnesyl diphosphate (FPP) and anilinogeranyl diphosphat
  
  
    43 ly synthesizes the "regular" sesquiterpenoid farnesyl diphosphate (FPP) by coupling isopentenyl dipho
  
    45 tep in its biosynthesis, condensation of two farnesyl diphosphate (FPP) molecules to dehydrosqualene,
    46  transfer of a 15-carbon farnesyl group from farnesyl diphosphate (FPP) to a conserved cysteine in th
    47  an initial condensation of two molecules of farnesyl diphosphate (FPP) to form presqualene diphospha
    48 yzes the ionization-dependent cyclization of farnesyl diphosphate (FPP) to form the bicyclic eremophi
    49 talyzes the condensation of two molecules of farnesyl diphosphate (FPP) to give presqualene diphospha
  
  
    52 -carbon geranyl diphosphate (GPP), 15-carbon farnesyl diphosphate (FPP), or 20-carbon geranylgeranyl 
  
  
  
  
    57   Toxoplasma gondii possesses a bifunctional farnesyl diphosphate (FPP)/geranylgeranyl diphosphate (G
  
    59 beetle protein extracts, but only when (Z,E)-farnesyl diphosphate [(Z,E)-FPP] was offered as a substr
    60 yme active site, we conclude that folding of farnesyl diphosphate alone does not always dictate the s
    61  Here, the synthesis of a benzophenone-based farnesyl diphosphate analogue containing a stable phosph
  
  
  
    65 isoprenoid mevalonate pathway-intermediates, farnesyl diphosphate and geranylgeranyl diphosphate, als
    66 functional, catalyzing the formation of both farnesyl diphosphate and geranylgeranyl diphosphate.    
  
  
  
    70  picture of the conformation of enzyme-bound farnesyl diphosphate at the active site of presilphiperf
    71 o be involved in isopentenyl diphosphate and farnesyl diphosphate biosynthesis leading to AN were not
    72 essarily reflect the original orientation of farnesyl diphosphate bound in the corresponding enzyme a
  
    74 ation of isopentenyl diphosphate (IPP), with farnesyl diphosphate catalysed by a cis-isoprenyltransfe
  
  
    77 ed with the SNP rs2645424 on chromosome 8 in farnesyl diphosphate farnesyl transferase 1 (FDFT1) (P =
    78 emethylase (CYP51A1), and squalene synthase (farnesyl diphosphate farnesyl transferase 1)) via novel 
    79 te synthase (FPS) catalyzes the synthesis of farnesyl diphosphate from isopentenyl diphosphate and di
    80 n adds a further seven isoprene units to E,Z-farnesyl diphosphate in a processive manner to generate 
    81 ne cyclase that catalyzes the cyclization of farnesyl diphosphate in the first committed step of the 
    82 ta-caryophyllene and alpha-humulene from E,E-farnesyl diphosphate in trichomes of leaf but not of ste
    83 f the tomato sesquiterpene synthases use z,z-farnesyl diphosphate in vitro as well, or more efficient
    84  TCs from Dictyostelium discoideum converted farnesyl diphosphate into (2S,3R,6S,9S)-(-)-protoillud-7
    85 hese results established that cyclization of farnesyl diphosphate involves displacement of the diphos
    86  may be significantly more selective for the farnesyl diphosphate substrate than the active site bind
  
    88 eactions, chimeric proteins constructed from farnesyl diphosphate synthase (chain elongation) and chr
  
    90 stimulate Vgamma2Vdelta2 cells by inhibiting farnesyl diphosphate synthase (FDPS) in the mevalonate p
  
    92 nts of the first two enzymes in the pathway, farnesyl diphosphate synthase (FDS) and carotenoid synth
  
  
    95 r therapeutic agents involving inhibition of farnesyl diphosphate synthase (FPPS) and geranylgeranyl 
  
  
  
    99  related Z-prenyl diphosphate synthases, E,Z-farnesyl diphosphate synthase (Rv1086) and decaprenyl di
  
   101  neryl diphosphate synthase1 (NDPS1) and Z,Z-farnesyl diphosphate synthase (zFPS), which are encoded 
   102 y by the targeted overexpression of an avian farnesyl diphosphate synthase along with two versions of
  
   104     We screened 26 bisphosphonates against a farnesyl diphosphate synthase from Plasmodium vivax, fin
   105 ncer cells to pitavastatin is potentiated by farnesyl diphosphate synthase inhibitors or geranylgeran
   106 re excellent competitive inhibitors of avian farnesyl diphosphate synthase with KI = 1.0 +/- 0.12 muM
   107 res of one sulfonium bisphosphonate bound to farnesyl diphosphate synthase, finding that it binds exc
   108  3-hydroxy-3-methylglutaryl-CoA reductase or farnesyl diphosphate synthase, reduced endometrial organ
   109 ar to the isoprenoid chain elongation enzyme farnesyl diphosphate synthase, which also contains two a
   110  similar in some respects to that of dimeric farnesyl diphosphate synthase, which is not a cyclase.  
  
  
  
   114 zes the conversion of two molecules of (E,E)-farnesyl diphosphate to squalene via the cyclopropylcarb
   115 e synthase that catalyzes the cyclization of farnesyl diphosphate to the novel tricyclic hydrocarbon,
   116 step in HA biosynthesis is the conversion of farnesyl diphosphate to trichodiene (TD), a volatile org
  
   118 ations of isotopically pure [2-(2)H(1)](E,E)-farnesyl diphosphate with recombinant patchoulol synthas
  
  
   121 diphosphate and dimethylallyl diphosphate to farnesyl diphosphate, a crucial metabolic intermediate i
   122 e synthase (FPPS) catalyzes the synthesis of farnesyl diphosphate, an important precursor of sterols,
   123  was inactive, whereas the LSU produced GPP, farnesyl diphosphate, and geranylgeranyl diphosphate (GG
   124 l cation, the product of 11,1-cyclization of farnesyl diphosphate, is the product of the first commit
   125 ion that following the initial ionization of farnesyl diphosphate, minimal enzymatic intervention may
   126 noterpene synthases and three that preferred farnesyl diphosphate, the substrate for sesquiterpene sy
   127 on of the universal sesquiterpene precursor, farnesyl diphosphate, to form the bicyclic hydrocarbon a
   128 scherichia coli, and demonstrated to cyclize farnesyl diphosphate, yielding beta-selinene as the domi
   129 fuels and the rapid engineering of microbial farnesyl diphosphate-overproducing platforms for the pro
  
  
  
  
  
  
  
   137 squiterpene synthases, exclusively using Z-Z-farnesyl-diphosphate (zFPP) in plastids, probably arisen
   138 ll interfering RNA showed that inhibition of farnesyl-diphosphate farnesyl transferase (squalene synt
  
  
   141 In summary, we report the first bifunctional farnesyl-diphosphate/geranylgeranyl-diphosphate synthase
  
   143 the opposite preference of tH palmitoyls and farnesyl for ordered and disordered membrane domains, cl
   144    To determine whether protein prenylation (farnesyl/geranylgeranylation) regulates matrix metallopr
   145 reaction requires farnesyldiphosphate as the farnesyl group donor and is catalyzed by the farnesyltra
   146 se (FTase) catalyzes transfer of a 15-carbon farnesyl group from farnesyl diphosphate (FPP) to a cons
  
   148 on of geranyl diphosphate (GPP) with the cis-farnesyl group in phosphoglycolipid 5 to form the (C25) 
  
   150 cs simulations collectively suggest that the farnesyl group is sequestered within a hydrophobic regio
   151 Farnesylation, the attachment of a 15-carbon farnesyl group near the C-terminus of protein substrates
   152 s achieved by enzymatically transferring the farnesyl group of the farnesyl-CoA micelle onto a peptid
  
  
  
  
  
  
   159 s protein is permanently modified by a lipid farnesyl group, and acts as a dominant negative, disrupt
  
  
   162 hat the GDP/GTP exchange, HVR sequestration, farnesyl insertion, and orientation/localization of the 
  
  
   165 ur results suggest that the binding of PDE6A farnesyl is essential to normal function of AIPL1 and it
   166 d their prenylation with a geranylgeranyl or farnesyl isoprenoid moiety and subsequent trafficking to
  
  
  
  
   171  inhibitor (FTI), suggesting that progerin's farnesyl lipid is important for disease pathogenesis and
   172     Whether RD is caused by the retention of farnesyl lipid on prelamin A, or by the retention of the
   173 se (FTase) catalyzes transfer of a 15 carbon farnesyl lipid to cysteine in the C-terminal Ca1a2X sequ
  
  
   176  Ras isoforms, K-Ras4B HVR contains a single farnesyl modification and positively charged polylysine 
   177 as4B is targeted to the plasma membrane by a farnesyl modification that operates in conjunction with 
   178 trifluoromethoxy-AGPP gave both analogue and farnesyl modified dansyl-GCVIM but only farnesylated dan
   179      Lipid anchors composed of palmitoyl and farnesyl moieties in H-, N-, and K-Ras are widely suspec
   180 rminus of Rnd3 consisting of both the Cys241-farnesyl moiety and a Rho-associated coiled coil contain
  
   182  subunit through direct interaction with the farnesyl moiety, mutations compromising the integrity of
   183 witch by modulating the accessibility of its farnesyl moiety, which does not require any supportive p
  
  
  
   187  direct the attachment of either a 15-carbon farnesyl or a 20-carbon geranylgeranyl moiety in vitro. 
  
   189 enyltransferase-catalyzed addition of either farnesyl or geranylgeranyl isoprenoid lipids, Rce1-catal
   190 oteins resulting in the addition of either a farnesyl or geranylgeranyl isoprenyl lipid moiety to the
  
   192 enerated in a three-step sequence in which a farnesyl-pantetheine conjugate is phosphorylated, adenyl
  
  
  
  
  
   198 dings indicate that progerin and full-length farnesyl-prelamin A are toxic to neurons of the enteric 
  
   200 cally modified mice that express full-length farnesyl-prelamin A in neurons (Zmpste24-deficient mice 
  
  
  
  
   205 vitro screen for resistance to lonafarnib, a farnesyl protein transferase inhibitor that blocks preny
   206 on of imatinib and lonafarnib, we identified farnesyl protein transferase mutations in residues ident
   207 we demonstrate that an inhibitor of p21(ras) farnesyl protein transferase suppressed the expression o
  
  
   210 urs) in the absence (control) or presence of farnesyl pyrophosphate (10 muM) or geranylgeranyl pyroph
   211 he synthesis of the wound-healing inhibitors farnesyl pyrophosphate (FPP) and cortisol, ligands for t
   212  by depleting mevalonate pathway metabolites farnesyl pyrophosphate (FPP) and geranylgeranyl pyrophos
   213 hese events were significantly attenuated by farnesyl pyrophosphate (FPP) but not by geranylgeranyl p
   214 of the 15-carbon sterol pathway intermediate farnesyl pyrophosphate (FPP) cause increased Hmg2p ubiqu
   215 ructure of inhibitor 1a co-crystallized with farnesyl pyrophosphate (FPP) in the active site of rat F
  
   217 roposed for the carbocationic cyclization of farnesyl pyrophosphate (FPP) to (+)-aristolochene cataly
   218 ules of isopentenyl pyrophosphate (IPP) with farnesyl pyrophosphate (FPP) to generate the C(55) undec
  
   220 MEV, squalene and ergosterol, as well as the farnesyl pyrophosphate (FPP)-derived side products farne
  
   222 e inhibitor GGTI-298, and prenyl substrates (farnesyl pyrophosphate [FPP] and geranylgeranyl pyrophos
   223 tidic acid receptor with weaker responses to farnesyl pyrophosphate and geranylgeranyl diphosphate.  
   224 gly, the levels of the cholesterol precursor farnesyl pyrophosphate and its derivative geranylgeranyl
   225 ived from dimethylorsellinic acid (DMOA) and farnesyl pyrophosphate have attracted much biosynthetic 
   226  from 3,5-dimethylorsellinic acid (DMOA) and farnesyl pyrophosphate have not been reported despite he
   227 derived from geranylgeranyl pyrophosphate or farnesyl pyrophosphate is an essential requisite for cel
  
   229 that decreases bone resorption by inhibiting farnesyl pyrophosphate synthase (FPPS) in osteoclasts, p
   230 he 5 alpha-halo-analogues potently inhibited farnesyl pyrophosphate synthase (FPPS) with IC50 values 
  
  
  
  
  
   236 nthesis are catalyzed by the related enzymes farnesyl pyrophosphate synthase and geranylgeranyl pyrop
   237 nomenon strongly augmented by zoledronate, a farnesyl pyrophosphate synthase inhibitor that increases
   238 ntaining bisphosphonate zoledronate inhibits farnesyl pyrophosphate synthase, a key enzyme of the mev
   239 droxy-3-methylglutaryl coenzyme A reductase, farnesyl pyrophosphate synthase, and cytochrome P-450-51
  
  
   242 carboxamide ribotide (ZMP), GDP-mannose, and farnesyl pyrophosphate were found to be rapidly altered 
  
   244 y hydroxymethylglutaryl-CoA, mevalonate, and farnesyl pyrophosphate, but not cholesterol and ubiquino
   245 e isoprenoid biosynthetic pathway leading to farnesyl pyrophosphate, the immediate molecular precurso
  
  
  
   249 VA), geranylgeranyl-pyrophosphate (GGPP) and farnesyl-pyrophosphate (FPP), all intermediates in the c
   250 odel of MS are via depletion of isoprenoids (farnesyl-pyrophosphate and geranylgeranyl-pyrophosphate)
  
   252  or geranylgeranyl-pyrophosphate, but not by farnesyl-pyrophosphate or cholesterol, suggesting that d
  
   254 ing a palladium catalyzed decarboxylative pi-farnesyl rearrangement of a diketo-dioxinone ester, arom
  
   256 ) ions and the unreactive substrate analogue farnesyl-S-thiolodiphosphate (FSPP), showing that the su
   257  Among numerous approaches, nitration of a 3-farnesyl-substituted unprotected pyrrole using AcONO2 ga
   258 ing both the porphyrin ring and the hydroxyl farnesyl tail, accompanied by protein movements in nearb
   259 lta exhibit a hydrophobic binding pocket for farnesyl, they have different effects on membrane bindin
   260 ipid compounds (farnesyl thiosalicylic acid, farnesyl thioacetic acid, 15-deoxy-Delta(12,14)-prostagl
  
   262 drophobic pocket previously reported to bind farnesyl thiodiphosphate (FsPP), as well as biphenyl pho
  
   264 ion conditions; this results in detection of farnesyl thiophosphate (FSP) in the structure of the bin
  
   266 ant, we show that the mechanism of action of farnesyl thiosalicylic acid differs from that of the rea
   267 ith a potentially novel mechanism of action, farnesyl thiosalicylic acid may be useful in the study o
   268 activity, including several lipid compounds (farnesyl thiosalicylic acid, farnesyl thioacetic acid, 1
   269 ggest that while Cys181-palmitate and Cys186-farnesyl together provide sufficient hydrophobic force f
   270 , interleukin-1beta (IL-1beta), statins, the farnesyl transferase (FT) inhibitor FTI-276 and geranylg
   271 used on the development of selective protein farnesyl transferase (FTase) and protein geranylgeranyl 
  
  
   274 rovision of structure-specific inhibitors of farnesyl transferase (FTase; e.g., FTI-277 or FTI-2628) 
   275 f both geranylgeranyl transferase (GGTI) and farnesyl transferase (FTI) inhibited the activation of N
  
   277 owed that inhibition of farnesyl-diphosphate farnesyl transferase (squalene synthase), but not 3-hydr
  
   279  and squalene synthase (farnesyl diphosphate farnesyl transferase 1)) via novel negative LXR DNA resp
  
   281 ploying cell-permeable inhibitors of protein farnesyl transferase and geranylgeranyl transferase enzy
   282 rest in their biology and the development of farnesyl transferase and geranylgeranyl transferase inhi
  
   284 m oncogenic transformation by (i) augmenting farnesyl transferase inhibition and (ii) suppressing the
  
   286 le the ortho-substituted isomer was a potent farnesyl transferase inhibitor (FTI) with an inhibition 
   287 oll onto a single-arm, open-label trial of a farnesyl transferase inhibitor for patients with HRAS mu
   288 he mechanism of mTOR activation, we used the farnesyl transferase inhibitor FTI-277, which partially 
  
  
  
   292 the presence of a mutant allele of the Cox10 farnesyl transferase involved in heme a biosynthesis or 
   293 measure the degree of protein prenylation by farnesyl transferase or geranylgeranyl transferase in vi
   294 inose synthase, trehalose synthase, amylase, farnesyl transferase, catalase, methyl transferase, lina
  
   296 ihydrochloride)]} but not by an inhibitor of farnesyl-transferase (farnesyl transferase inhibitor-277
   297 naling by small interfering RNA (siRNA) or a farnesyl-transferase inhibitor decreases KLF6 SV1 and su
  
  
   300 le in regulation of nuclear receptors [e.g., farnesyl X receptor (FXR)], leading to enhanced or suppr
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