ライフサイエンスコーパス: acetyl-CoA carboxylase

1 ol regulatory element binding protein-1c and acetyl CoA carboxylase.

2 he biotin carboxyl carrier protein (BCCP) of acetyl CoA carboxylase.

3 no significant change in phosphorylation of acetyl CoA carboxylase.

4 and increased phosphorylated (p-)AMPK and p-acetyl CoA carboxylase.

5 ted protein kinase and its primary substrate acetyl-CoA carboxylase.

6 ression of phosphorylation of AMP kinase and acetyl-CoA carboxylase.

7 AMP-activated protein kinase and its target acetyl-CoA carboxylase.

8 id not alter the phosphorylation of AMPK and acetyl-CoA carboxylase.

9 de content, and increased phosphorylation of acetyl-CoA carboxylase.

10 , and mRNA levels of fatty-acid synthase and acetyl-CoA carboxylase.

11 increased hepatic expression of SREBP-1c and acetyl-CoA carboxylase.

12 iotinylation of the biotin-dependent enzyme, acetyl-CoA carboxylase.

13 enes including fatty acid synthase (FAS) and acetyl-CoA carboxylase.

14 18:1 to erucate was produced by homodimeric acetyl-CoA carboxylase.

15 suggesting that mitochondria do not possess acetyl-CoA carboxylase.

16 hat catalyzes the second partial reaction of acetyl-CoA carboxylase.

17 acetyl-CoA to form malonyl-CoA, catalyzed by acetyl-CoA carboxylase.

18 le including Acc1p, the rate-limiting enzyme acetyl-CoA carboxylase.

19 iotin to AccB, a subunit of acetyl coenzyme (acetyl-CoA) carboxylase.

20 n carboxylase subunits of acetyl coenzyme A (acetyl-CoA) carboxylases.

21 ssion measurements of key lipogenic enzymes [acetyl CoA carboxylase 1 (ACC1), fatty acid synthase (FA

22 n chronic infection, a specific inhibitor of acetyl CoA carboxylase 1, 5-(tetradecyloxy)-2-furoic aci

23 etion and early pharmaceutical inhibition of acetyl CoA carboxylase 1, the rate limiting step of FAS,

24 mes, including fatty-acid synthase (FAS) and acetyl-CoA carboxylase 1 (ACC-1).

25 Acetyl-CoA carboxylase 1 (ACC1) currently is being inves

26 Recent studies suggest that acetyl-CoA carboxylase 1 (ACC1), an enzyme with crucial

27 By contrast, biotinylation of the acetyl-CoA carboxylase 1 and 2 (ACC1 and ACC2) fragments

28 esis of a novel series of dual inhibitors of acetyl-CoA carboxylase 1 and 2 (ACC1 and ACC2).

29 malonyl-CoA in the cytoplasm by the enzymes acetyl-CoA carboxylase 1 and fatty acid synthase.

30 t genes, such as liver-type pyruvate kinase, acetyl-CoA carboxylase 1, and fatty acid synthase.

31 nvolved in lipogenesis: fatty acid synthase, acetyl-CoA carboxylase 1, and glycerol-3-phosphate acylt

32 Malonyl-CoA, generated by acetyl-CoA carboxylases 1 and 2 (Acc1 and Acc2), is a ke

33 ranscription factor SREBP-1c and its targets acetyl-CoA carboxylase-1 and fatty acid synthase (FAS).

34 factor SREBP-1c and its associated enzymes, acetyl-CoA carboxylase-1 and fatty acid synthase, in the

35 he major phosphorylation site (Ser79) on rat acetyl-CoA carboxylase-1/alpha (ACC1) as a GST fusion.

36 Because malonyl CoA production via acetyl CoA carboxylase 2 (ACC2) inhibits the entry of lo

37 Acetyl-CoA carboxylase 2 (ACC)2 is a key regulator of mi

38 We have shown previously that acetyl-CoA carboxylase 2 (Acc2(-/-)) mutant mice, when f

39 To investigate the role of acetyl-CoA carboxylase 2 (ACC2) in the regulation of ene

40 cDNA encoding the 280-kDa acetyl-CoA carboxylase 2 (ACC2) isoform was isolated fro

41 e to nutrient abundance via hydroxylation of acetyl-coA carboxylase 2 (ACC2).

42 tein content of adipose triglyceride lipase, acetyl-CoA carboxylase 2 and AMP-activated protein kinas

43 ation/inactivation and reduced expression of acetyl-CoA carboxylase 2, causing a reduction of the mal

44 and Acacb (which encodes acetyl coenzyme A [acetyl-CoA] carboxylase 2 [ACC2], a critical regulator o

45 Deletion of acetyl CoA carboxylase-2 (Acc2) reportedly causes leanne

46 Moreover, phosphorylation of acetyl CoA carboxylase-2, a downstream target of AMPK, w

47 sphorylation of AMPK on Thr172 and decreased acetyl-CoA carboxylase-2 activity.

48 a downstream effect on the phospho-status of acetyl CoA carboxylase, a key regulator of cellular fat

49 boxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that c

50 s accompanied by decreased protein levels of acetyl-CoA carboxylase, a key regulator of both lipid ox

51 for membrane lipid synthesis is catalyzed by acetyl-CoA carboxylase, a large complex composed of four

52 ith a concomitant increase in phosphorylated acetyl-CoA-carboxylase, a direct target of AMPK, the pho

53 a rapid and sensitive homogeneous assay for acetyl CoA carboxylase (ACC) in a scintillation proximit

54 Within 3 h of FSH treatment, phospho-acetyl CoA carboxylase (ACC) levels were increased in ge

55 age-matched wild-type (+/+) control islets, acetyl CoA carboxylase (ACC) mRNA was fivefold and sixfo

56 phosphorylation of both AMPK on Thr-172 and acetyl CoA carboxylase (ACC) on Ser-79.

57 Recent data strongly implicate the AMPK-acetyl CoA carboxylase (ACC)-malonyl CoA pathway in the

58 K activity and a decrease in the activity of acetyl CoA carboxylase (ACC).

59 t cells and that required phosphorylation of acetyl-CoA carboxylase (ACC) 1 and/or ACC2 at the AMPK s

60 Deletion of fatty acid synthase or acetyl-CoA carboxylase (ACC) 1 in mice resulted in embry

61 activates AMPK in hepatocytes; as a result, acetyl-CoA carboxylase (ACC) activity is reduced, fatty

62 timulates fatty acid oxidation by regulating acetyl-CoA carboxylase (ACC) activity.

63 The rat acetyl-CoA carboxylase (ACC) alpha gene is transcribed f

64 bolism mediated by the SREBP-SCD pathway, an acetyl-CoA carboxylase (ACC) and certain nuclear hormone

65 gulation of two key liver lipogenic enzymes, acetyl-CoA carboxylase (ACC) and fatty acid synthase (FA

66 y acid and triglyceride synthesis, including acetyl-CoA carboxylase (ACC) and fatty acid synthase (FA

67 oA through a series of reactions mediated by acetyl-CoA carboxylase (ACC) and fatty acid synthase (FA

68 the carboxyl-transfer reaction of bacterial acetyl-CoA carboxylase (ACC) and thereby inhibits fatty

69 s been correlated with the inhibition of its acetyl-CoA carboxylase (ACC) by these compounds.

70 Acetyl-CoA carboxylase (ACC) catalyzes the first committ

71 Acetyl-CoA carboxylase (ACC) catalyzes the first step of

72 Acetyl-CoA carboxylase (ACC) catalyzes the formation of

73 Acetyl-CoA carboxylase (ACC) catalyzes the rate-determin

74 ing SREBP-1c, fatty acid synthase (FAS), and acetyl-CoA carboxylase (ACC) gene expression.

75 Cis-acting regulatory elements of the wheat acetyl-CoA carboxylase (ACC) gene family were identified

76 enesis in mice by liver-specific knockout of acetyl-CoA carboxylase (ACC) genes and treat the mice wi

77 Acetyl-CoA carboxylase (ACC) has crucial roles in fatty

78 e either a biochemical or a genetic block at acetyl-CoA carboxylase (ACC) in S. aureus, confirming th

79 A structurally novel acetyl-CoA carboxylase (ACC) inhibitor is identified fro

80 Conversely, lowering malonyl-CoA with an acetyl-CoA carboxylase (ACC) inhibitor or by the ectopic

81 The development of acetyl-CoA carboxylase (ACC) inhibitors for the treatmen

82 Synthesis of oxo-dihydrospiroindazole-based acetyl-CoA carboxylase (ACC) inhibitors is reported.

83 Acetyl-CoA carboxylase (ACC) inhibitors offer significan

84 Acetyl-coA carboxylase (ACC) is a central metabolic enzy

85 Acetyl-CoA carboxylase (ACC) is a key enzyme of fatty ac

86 Acetyl-CoA carboxylase (ACC) is a target of interest for

87 Escherichia coli acetyl-CoA carboxylase (ACC) is composed of four differe

88 henoxypropionates, inhibitors of the plastid acetyl-CoA carboxylase (ACC) of grasses, also inhibit To

89 treatment, including glucose metabolism and acetyl-CoA carboxylase (ACC) phosphorylation.

90 spite nutrient excess, induced both AMPK and acetyl-CoA carboxylase (ACC) phosphorylation.

91 sta4 null 129/sv mice, the expression of the acetyl-CoA carboxylase (ACC) transcript is enhanced seve

92 dent increase in phosphorylation of AMPK and acetyl-CoA carboxylase (ACC), a direct substrate.

93 ss is controlled by the rate-limiting enzyme acetyl-CoA carboxylase (ACC), an attractive but traditio

94 ted to the phosphorylation and inhibition of acetyl-CoA carboxylase (ACC), and secondary to this, a d

95 The effects of ethanol on AMPK, acetyl-CoA carboxylase (ACC), and SREBP-1 were assessed

96 orylation of AMPK and its downstream target, acetyl-CoA carboxylase (ACC), and they increased activit

97 tformin on AMPK and its downstream effector, acetyl-CoA carboxylase (ACC), as well as on lipid conten

98 nthesis enzymes [fatty acid synthase (FASN), acetyl-CoA carboxylase (ACC), ATP citrate lyase (ACLY)].

99 onsisting of a 9-amino-acid peptide from rat acetyl-CoA carboxylase (ACC), CREB peptide, and the addi

100 dation, AMP-activated protein kinase (AMPK), acetyl-CoA carboxylase (ACC), malonyl-CoA decarboxylase,

101 transferase-1 (CPT-1) and inhibiting that of acetyl-CoA carboxylase (ACC), pace-setting enzymes for f

102 Acetyl-CoA carboxylase (ACC), the first committed enzyme

103 iting AMP-activated kinase (AMPK), activates acetyl-CoA carboxylase (ACC), the key regulatory enzyme

104 en related to alterations in the activity of acetyl-CoA carboxylase (ACC), the rate-limiting enzyme i

105 se (AMPK), which phosphorylates and inhibits acetyl-CoA carboxylase (ACC), the rate-limiting enzyme i

106 physiologic consequence of AMPK activation, acetyl-CoA carboxylase (ACC), the rate-limiting enzyme o

107 c mice, AMPKalpha and its downstream target, acetyl-CoA carboxylase (ACC), were hyperphosphorylated,

108 AMPK phosphorylates and inhibits acetyl-CoA carboxylase (ACC), which catalyzes carboxylat

109 A novel target is the multifunctional enzyme acetyl-CoA carboxylase (ACC), which catalyzes the first

110 Inhibition of acetyl-CoA carboxylase (ACC), with its resultant inhibit

111 -Src, PDK1, AMPK, and its downstream target, acetyl-CoA carboxylase (ACC), without affecting cellular

112 n-enhanced phosphorylation of AMPK-Thr(172), acetyl-CoA carboxylase (ACC)-Ser(79), and LKB1-Ser(428).

113 yloxy)-2-furoic acid (TOFA), an inhibitor of acetyl-CoA carboxylase (ACC).

114 nzymes such as fatty acid synthase (FAS) and acetyl-CoA carboxylase (ACC).

115 step in fatty acid synthesis is catalyzed by acetyl-CoA carboxylase (ACC).

116 increased levels of phosphorylated AMPK and acetyl-CoA carboxylase (ACC).

117 nase (alpha2AMPK) and its downstream target, acetyl-CoA carboxylase (ACC).

118 peractivity of fatty acid synthase (FAS) and acetyl-CoA carboxylase (ACC).

119 CoA, which is synthesized from acetyl-CoA by Acetyl-CoA carboxylase (ACC).

120 rotonyl-CoA carboxylase (MCC) and eukaryotic acetyl-CoA carboxylase (ACC).

121 phosphorylation of both AMPK (Thr(172)) and acetyl-CoA carboxylase (ACC; Ser(79)).

122 between decreased phosphorylation, decreased acetyl-CoA carboxylase Acc1 phosphorylation, and sterol

123 The inhibition of the acetyl-CoA carboxylases ACC1 and ACC2 by AMPK maintains

124 Malonyl-CoA, generated by acetyl-CoA carboxylases ACC1 and ACC2, is a key metaboli

125 lonyl-coenzyme A (malonyl-CoA), generated by acetyl-CoA carboxylases ACC1 and ACC2, is a key metaboli

126 receptor element binding protein (SREBP)-1c, acetyl-CoA carboxylase (ACC1) and lipid uptake genes, su

127 rsus C18 FAs is regulated by the activity of acetyl-CoA carboxylase (Acc1), the first and rate-limiti

128 mRNA levels of fatty acid synthase (Fas) and acetyl-CoA carboxylase (Acc1).

129 Acetyl-CoA carboxylases (ACC1 and ACC2) catalyze the car

130 To elucidate the essential functions of acetyl-CoA carboxylase (ACC1FAS3) in Saccharomyces cerev

131 The phosphorylations of AMPKalpha and acetyl-CoA carboxylase (ACC2; a downstream AMPK target)

132 last using a single set of enzymes, of which acetyl CoA carboxylase (ACCase) is key in regulating fat

133 nuclear genes encoding multi-domain plastid acetyl-CoA carboxylase (ACCase) and plastid 3-phosphogly

134 tty acids, which together pinpoint plastidic acetyl-CoA carboxylase (ACCase) as the enzymatic target

135 Acetyl-CoA carboxylase (ACCase) catalyzes the committed

136 ransferase domain of the multidomain plastid acetyl-CoA carboxylase (ACCase) from herbicide-resistant

137 ast GAL10 promoter, yeast ACC1 leader, wheat acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) cDNA, and ye

138 In the plastids of most plants, acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) is a multisu

139 ents of two genes encoding plastid-localized acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) of wheat (Tr

140 Acetyl-CoA carboxylases (ACCs) are crucial for the metab

141 Acetyl-CoA carboxylases (ACCs) are crucial metabolic enz

142 Acetyl-CoA carboxylases (ACCs) are crucial metabolic enz

143 Inhibition of acetyl-CoA carboxylases (ACCs), a crucial enzyme for fat

144 Leptin decreased acetyl-CoA carboxylase activity 40% in muscle from chow-

145 In vivo bypass of acetyl-CoA carboxylase activity by expression of a malon

146 ant showed a reduced growth rate and reduced acetyl-CoA carboxylase activity compared with the wild-t

147 In muscle from DIO mice, acetyl-CoA carboxylase activity was basally low, and lep

148 ylase-expressing seeds indicated the in vivo acetyl-CoA carboxylase activity was reduced to approxima

149 , increased saturated fatty acids, decreased acetyl-CoA carboxylase activity, and decreased malonyl-C

150 atty acid hydroxylase alleviated the reduced acetyl-CoA carboxylase activity, restored the rate of fa

151 ivity and LKB1 phosphorylation and decreases acetyl-coA carboxylase activity; it also down-regulates

152 ysis identified that AKR1B10 associates with acetyl-CoA carboxylase-alpha (ACCA), a rate-limiting enz

153 es a 7-fold increase in transcription of the acetyl-CoA carboxylase-alpha (ACCalpha) gene in chick em

154 -triiodothyronine response element (T3RE) in acetyl-CoA carboxylase-alpha (ACCalpha) promoter 2 that

155 r, knockdown of two enzymes upstream of FAS, acetyl-CoA carboxylase-alpha and ATP-citrate lyase, fail

156 The mammalian gene (ACACA) encoding acetyl-CoA carboxylase-alpha, a key regulatory enzyme of

157 iates the ubiquitin-dependent degradation of acetyl-CoA carboxylase-alpha.

158 e and enhanced the Ser-79 phosphorylation of acetyl CoA carboxylase, an enzyme downstream of AMP kina

159 d with the accumulation pattern of cytosolic acetyl-CoA carboxylase, an enzyme using cytosolic acetyl

160 orrelate closely with the phosphorylation of acetyl-CoA carboxylase, an established target of AMP kin

161 Conversely, inhibitors of acetyl CoA carboxylase and fatty acid synthase mimicked

162 tream targets and regulators of lipogenesis, acetyl CoA carboxylase and fatty acid synthase.

163 K to phosphorylate its endogenous substrates acetyl CoA carboxylase and Raptor, and provokes mitochon

164 n carboxyl carrier protein (BCCP) subunit of acetyl CoA carboxylase and this post-translational modif

165 kinase (AMPK), increased phosphorylation of acetyl-CoA carboxylase and a decrease in the tissue cont

166 inistration is associated with activation of acetyl-CoA carboxylase and changes in the expression pro

167 nt of BCCP (apoBCCP87) from Escherichia coli acetyl-CoA carboxylase and compared this structure with

168 reduced the enzymatic activity of cytosolic acetyl-CoA carboxylase and concomitantly inhibited the d

169 ed protein kinase, MB inactivates downstream acetyl-CoA carboxylase and decreases cyclin expression.

170 which depends on the relative activities of acetyl-CoA carboxylase and FAS, is an indicator of energ

171 the 13C NMR findings, activities of hepatic acetyl-CoA carboxylase and fatty acid synthase were sign

172 dditionally, the steady-state mRNA levels of acetyl-CoA carboxylase and fatty acid synthase, required

173 e two major enzymes of fatty acid synthesis, acetyl-CoA carboxylase and fatty acid synthase, whose tr

174 gh-throughput screening is demonstrated with acetyl-CoA carboxylase and fatty acid synthase.

175 t-binding protein-1c and two of its targets, acetyl-CoA carboxylase and fatty acid synthase.

176 atic steatosis, as well as the expression of acetyl-CoA carboxylase and fatty acid synthase.

177 sult, expression of the mSREBP1 target genes acetyl-CoA carboxylase and fatty-acid synthase was suppr

178 n augmenting AMPK-induced phosphorylation of acetyl-CoA carboxylase and in activating the PI3K/AKT pa

179 des the beta-carboxyl transferase subunit of acetyl-CoA carboxylase and is present in the plastids of

180 er in mammalian cells, and the activities of acetyl-CoA carboxylase and malonyl-CoA decarboxylase are

181 nergy-sensing enzyme AMPK, and inhibition of acetyl-CoA carboxylase and mammalian target of rapamycin

182 The V(max) activities of acetyl-CoA carboxylase and of malonyl-CoA decarboxylase

183 reasing the activity of the anabolic factors acetyl-CoA carboxylase and ribosomal protein S6 and inhi

184 ding the enzymes regulating fatty acid, i.e. acetyl-CoA carboxylase and sterol synthesis, i.e. HMG-Co

185 We analyzed Acc-1 (plastid acetyl-CoA carboxylase) and Pgk-1 (plastid 3-phosphoglyc

186 phorylation of the endogenous AMPK substrate acetyl CoA carboxylase, and also interfered with activat

187 in greatly reducing hepatic lipogenic genes, acetyl CoA carboxylase, and fatty acid synthase and incr

188 ion, triggered the phosphorylations of AMPK, acetyl CoA carboxylase, and glycogen synthase kinase-3,

189 -gene encoding the biotinyl domain of E.coli acetyl-CoA carboxylase, and by a series of mutations con

190 ion, increased phosphorylation of raptor and acetyl-CoA carboxylase, and decreased phosphorylation of

191 hrough gastric gavage showed increased AMPK, acetyl-CoA carboxylase, and endothelial NO synthase phos

192 atory element-binding protein 1c (SREBP-1c), acetyl-CoA carboxylase, and fatty-acid synthase, three k

193 egulatory element-binding proteins 1c and 2, acetyl-CoA carboxylase, and HMG-CoA reductase mRNAs/prot

194 phorylation of AMP-activated protein kinase, acetyl-CoA carboxylase, and mitogen-activated protein ki

195 epatic lipogenic genes, fatty acid synthase, acetyl-CoA carboxylase, and stearoyl-CoA desaturase-1, w

196 involved in fatty acid synthesis, including acetyl-CoA carboxylase, and three out of five putative t

197 like fungi, which have an intramitochondrial acetyl-CoA carboxylase, animals require an alternative s

198 The bacterial and chloroplast multisubunit acetyl-CoA carboxylases are unusual in that the highly s

199 am effects of AMPK on the phosphorylation of acetyl-CoA carboxylase, are largely inhibited by the Ca(

200 adiponectin failed to phosphorylate cardiac acetyl-CoA carboxylase as it did in WT mouse heart.

201 -activated protein kinase (AMPK) at Thr 172, acetyl-CoA carboxylase at Ser 79, tuberous sclerosis 2 a

202 The phosphorylation of acetyl-CoA carboxylase at Ser-79 and of endothelial NO s

203 e activation of AMPK, the phosphorylation of acetyl-CoA carboxylase at Ser-79 was increased and enzym

204 ls of SREBP1-c, SREBP2, fatty-acid synthase, acetyl-CoA carboxylase, ATP citrate lyase, and Glut-1 we

205 effect on pyruvate carboxylase as opposed to acetyl CoA carboxylase, because the incorporation of glu

206 this occurs, the activity and properties of acetyl-CoA carboxylase beta (ACC-beta), the skeletal mus

207 yloxy)-2-furoic acid (TOFA), an inhibitor of acetyl-CoA carboxylase, both cause a significant reducti

208 he biotin carboxyl carrier protein (BCCP) of acetyl-CoA carboxylase, but lacks an extension that has

209 Because mammalian mitochondria lack an acetyl-CoA carboxylase capable of generating malonyl-CoA

210 Acetyl-CoA carboxylase catalyzes the committed step in f

211 Acetyl-CoA Carboxylase catalyzes the first committed ste

212 Acetyl-CoA carboxylase catalyzes the first committed ste

213 Acetyl-CoA carboxylase catalyzes the first committed ste

214 Acetyl-CoA carboxylase catalyzes the first committed ste

215 Acetyl-CoA carboxylase catalyzes the first committed ste

216 Acetyl-CoA carboxylase catalyzes the first committed ste

217 ly isolated from the other components of the acetyl-CoA carboxylase complex such that enzymatic activ

218 ese results, we propose that this M. xanthus acetyl-CoA carboxylase consists of two subunits, which a

219 Lower phosphorylated acetyl-CoA carboxylase content and higher gene expressio

220 and 1.4-fold, respectively, whereas mRNA for acetyl-CoA carboxylase decreased by 50%.

221 g preference for citrate cycling rather than acetyl-CoA carboxylase-dependent fatty acid synthesis.

222 s, including humans, express two isoforms of acetyl-CoA carboxylase (EC ), ACC1 (M(r) = 265 kDa) and

223 tion of AMPK and its downstream target, ACC (acetyl-CoA carboxylase), elevation in expression of FAS

224 by measuring a ligand-stimulated decrease in acetyl-CoA carboxylase expression.

225 o increased activities of HMG-CoA reductase, acetyl-CoA carboxylase, fatty acid synthase and serine p

226 sterol regulatory element binding protein-1, acetyl-CoA carboxylase, fatty acid synthase) in the grou

227 several fatty acid synthesis genes, namely, acetyl-CoA carboxylase, fatty acid synthase, SREBP1c, ch

228 epatic mRNA levels of key lipogenic enzymes, acetyl-CoA carboxylase, fatty-acid synthase, and stearoy

229 he overexpression of genes encoding PEX7 and acetyl-CoA carboxylase further improved fatty alcohol pr

230 We used the dexamethasone system to silence acetyl-CoA carboxylase gene and observed prolific root g

231 ugh glucose activation of promoter II of the acetyl-CoA carboxylase gene.

232 ated kinase 1/2, but phosphorylation of beta-acetyl-CoA carboxylase, glycogen synthase, and protein k

233 Eleven spontaneous mutations of acetyl-CoA carboxylase have been identified in many herb

234 g p21 waf1/cip1, p15 INK4B, CYP11A, mdr1 and acetyl-CoA carboxylase, have been mapped to GC-rich prom

235 Acetyl-CoA carboxylase I (ACCI) is a key lipogenic enzym

236 ransferase-1 mRNA in fat, down-regulation of acetyl CoA carboxylase in liver, and up-regulation of PP

237 tissue and increased UCP-3 and inhibition of acetyl-CoA carboxylase in skeletal muscle, findings cons

238 position between prokaryotic and eukaryotic acetyl-CoA carboxylases in terms of evolution.

239 xpression of S14 and a key lipogenic enzyme (acetyl-CoA carboxylase) in a panel of primary breast can

240 acid CoA transferase (decreased by 67%), and acetyl-CoA carboxylase (increased by 4-fold), resulting

241 TOFA, an inhibitor of acetyl-CoA carboxylase, increases ATP levels, but does n

242 Moreover, prior i.c.v. administration of an acetyl-CoA carboxylase inhibitor, 5-(tetradecyloxy)-2-fu

243 or cells, and this increase was abrogated by acetyl-CoA carboxylase inhibitor.

244 5'-pyrazolo[3,4-c]pyridin]-7'(2'H)-one-based acetyl-CoA carboxylase inhibitors is reported.

245 to serious metabolic diseases in humans, and acetyl-CoA carboxylase is a target for drug discovery in

246 Escherichia coli acetyl-CoA carboxylase is composed of biotin carboxylase

247 In yeast Saccharomyces cerevisiae, acetyl-CoA carboxylase is encoded by the ACC1 gene.

248 are exposed to high glucose concentrations, acetyl-CoA carboxylase is induced through glucose activa

249 vivo hydroxymethylglutaryl-CoA reductase and acetyl-CoA carboxylase (key regulatory enzymes of sterol

250 ts support recent studies that indicate that acetyl-CoA carboxylase may be a suitable target for an a

251 id synthase mRNA levels were not altered but acetyl CoA carboxylase mRNA levels were significantly de

252 increased levels of Fatty Acid Synthase and Acetyl CoA Carboxylase mRNAs, enzymes responsible for li

253 induction of fatty acid synthase, S(14), and acetyl-CoA carboxylase mRNAs to 20% (fatty acid synthase

254 (fatty acid synthase), 10% (S(14)), and 5% (acetyl-CoA carboxylase) of the induction seen by high gl

255 ls of the mRNA of fatty acid synthesis genes acetyl CoA carboxylase or fatty acid synthase.

256 e biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase or a second BirA monomer.

257 more, activation of AMPK also phosphorylates acetyl-CoA carboxylase or ACC, the pivotal enzyme of fat

258 Furthermore, inhibition of either acetyl-CoA carboxylase or acyl-CoA synthetase reduced mi

259 and fatty acid oxidation, activated the AMPK-acetyl-CoA carboxylase pathway, and promoted inefficient

260 centration of malonyl CoA was increased, and acetyl CoA carboxylase phosphorylation at serine 79 was

261 ent increased AMPK activation and downstream acetyl-CoA carboxylase phosphorylation and glucose uptak

262 activity, alphaThr-172 phosphorylation, and acetyl-CoA carboxylase phosphorylation are substantially

263 is completed, oligomycin-induced increase of acetyl-CoA carboxylase phosphorylation at Ser(79) is sti

264 P imbalance, AMPK activation, AMPK substrate acetyl-CoA carboxylase phosphorylation at Ser(79), and c

265 K phosphorylation and activity and increased acetyl-CoA carboxylase phosphorylation in leptin-deficie

266 Acetyl-CoA carboxylase phosphorylation was increased in

267 Thus its overexpression increased AMPK and acetyl-CoA carboxylase phosphorylation, and conversely,

268 K was associated with a dramatic increase in acetyl-CoA carboxylase phosphorylation.

269 and MIG12 leads to heterodimers and reduced acetyl-CoA carboxylase polymerization and activity.

270 in the lipopenic actions of hyperleptinemia, acetyl CoA carboxylase protein was reduced in the liver

271 epends on its rate of synthesis catalyzed by acetyl-CoA carboxylase relative to its rate of utilizati

272 lglutaryl-coenzyme A (HMG-CoA) reductase and acetyl-CoA carboxylase, respectively, were therefore stu

273 osphorylation of AMPKalpha and its substrate acetyl-CoA carboxylase, respectively.

274 lipid abundance in DCs with an inhibitor of acetyl-CoA carboxylase restored the functional activity

275 ociated with increased expression of FAS and acetyl CoA carboxylase, resulting in increased TG conten

276 opanoic acid, which inhibits the homodimeric acetyl-CoA carboxylase, severely inhibited the synthesis

277 lipogenic enzymes (i.e. fatty-acid synthase, acetyl-CoA carboxylase, stearoyl-CoA desaturase, squalen

278 this article, we show that the chloroplastic acetyl-CoA carboxylase subunit (accD) gene that is prese

279 s well as a protease subunit (clpP)-like and acetyl-CoA carboxylase subunit D (accD)-like open readin

280 regulated by overproduction of AccC, another acetyl-CoA carboxylase subunit known to form a complex w

281 in length factor, an acyl transferase, three acetyl-CoA carboxylase subunits, two cyclases, two oxyge

282 e of the mRNAs for the plastidic heteromeric acetyl-CoA carboxylase subunits.

283 P-1(32-36)amide activated AMPK and inhibited acetyl-CoA carboxylase, suggesting activation of fat met

284 id is a nanomolar inhibitor of the bacterial acetyl-CoA carboxylase that catalyses the first committe

285 is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committe

286 is one component of the multienzyme complex acetyl-CoA carboxylase that catalyzes the first committe

287 all biotinylated subunit of Escherichia coli acetyl-CoA carboxylase, the enzyme that catalyzes the fi

288 inducing the polymerization and activity of acetyl-CoA carboxylase, the first committed enzymatic re

289 oA generating system provided by a cytosolic acetyl-CoA carboxylase, the mitochondrial AAE13 protein

290 ion of both AMP-activated protein kinase and acetyl-CoA carboxylase, thereby increasing CPT activity

291 ffect of six mutations on the sensitivity of acetyl-CoA carboxylase to nine herbicides representing t

292 and its primary downstream targeting enzyme, acetyl-CoA carboxylase, up-regulated gene expression of

293 The mRNAs for fatty acid synthase and acetyl CoA carboxylase were elevated 9- and 16-fold in l

294 he plastid and cytosolic forms of the enzyme acetyl-CoA carboxylase, were analyzed with a view to und

295 nase causing phosphorylation/inactivation of acetyl-CoA carboxylase, whereas glucose has the inverse

296 SNF1 phosphorylates and inhibits acetyl-CoA carboxylase, which catalyzes the carboxylatio

297 is one component of the multienzyme complex acetyl-CoA carboxylase, which catalyzes the committed st

298 Acetyl-CoA carboxylase, which has a molecular mass of 26

299 ation is the phosphorylation/inactivation of acetyl-CoA carboxylase, which leads to reduced malonyl-C

300 tin carboxylase carrier protein from E. coli acetyl-CoA carboxylase, which reveal significant biotin-

301 Introduction of new herbicides targeting acetyl-CoA carboxylase will depend on their ability to o