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 no significant change in phosphorylation of acetyl CoA carboxylase.

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

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

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

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

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

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

9 d state of AMPK and of its downstream target acetyl-CoA carboxylase.

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

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

12 le including Acc1p, the rate-limiting 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 AMP-activated protein kinase and its target 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 iotin to AccB, a subunit of acetyl coenzyme (acetyl-CoA) carboxylase.

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

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

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

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

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

24 Acetyl-CoA carboxylase 1 (Acc1) connects central energy

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 -limiting enzyme of fatty acid biosynthesis, acetyl-CoA carboxylase 1 (ACC1), is O-GlcNAcylated and n

28 cell culture and mice via the inhibition of acetyl-CoA carboxylase 1 (ACC1), resulting in neuroprote

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

45 nted by increasing FAO via deletion of ACC2 (acetyl-CoA-carboxylase 2) in phenylephrine-stimulated ca

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

84 Preclinical and clinical data suggest that acetyl-CoA carboxylase (ACC) inhibitors have the potenti

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

86 Acetyl-CoA carboxylase (ACC) inhibitors offer significan

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

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

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

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

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

92 phloem-mobile systemic insecticide targeting acetyl-CoA carboxylase (ACC) of pest insects and mites u

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

112 induced autophagy and the phosphorylation of acetyl-CoA carboxylase (ACC), whereas alone it could blo

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

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

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

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

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

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

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

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

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

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

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

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

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

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

127 regulatory element-binding protein [SREBP], acetyl-CoA carboxylase [ACC], peroxisome proliferator-ac

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

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

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

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

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

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

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

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

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

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

138 ) protein levels in chicken liver, activated acetyl-CoA carboxylase (ACCalpha), and increased FASN, A

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

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

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

142 Acetyl-CoA carboxylase (ACCase) catalyzes the committed

143 Acetyl-CoA carboxylase (ACCase) catalyzes the first comm

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

145 cid synthesis (FAS) is partially mediated by acetyl-CoA carboxylase (ACCase), the first committed ste

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

189 roptosis to AMPK-mediated phosphorylation of acetyl-CoA carboxylase and polyunsaturated fatty acid bi

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

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

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

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

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

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

196 bserved long-term irreversible inhibition of ACETYL-COA CARBOXYLASE, and consequently FA synthesis.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

215 Acetyl-CoA carboxylase catalyzes the committed step in f

216 Acetyl-CoA Carboxylase catalyzes the first committed ste

217 Acetyl-CoA carboxylase catalyzes the first committed ste

218 Acetyl-CoA carboxylase catalyzes the first committed ste

219 Acetyl-CoA carboxylase catalyzes the first committed ste

220 Acetyl-CoA carboxylase catalyzes the first committed ste

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

236 nts, expresses a multicomponent, heteromeric acetyl-CoA carboxylase (htACCase), which catalyzes the g

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

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

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

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

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

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

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

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

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

246 5'-pyrazolo[3,4-c]pyridin]-7'(2'H)-one-based acetyl-CoA carboxylase inhibitors is reported.

247 The expression of fatty acid synthase and acetyl-CoA carboxylase involved in de novo biosynthesis

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

267 Acetyl-CoA carboxylase phosphorylation was increased in

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

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

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

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

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

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 esponded to AMP-activated protein kinase and acetyl-CoA carboxylase signaling.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 of accD (the plastid-encoded subunit of the acetyl-CoA carboxylase, which catalyzes the first and ra

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

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