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1 As, and we have named it long-chain acyl-CoA carboxylase.
2 cant change in phosphorylation of acetyl CoA carboxylase.
3 es the second partial reaction of acetyl-CoA carboxylase.
4 sed phosphorylated (p-)AMPK and p-acetyl CoA carboxylase.
5 to form malonyl-CoA, catalyzed by acetyl-CoA carboxylase.
6 e reduced activity of crotonyl-CoA reductase/carboxylase.
7 g Acc1p, the rate-limiting enzyme acetyl-CoA carboxylase.
8 the chloroplast genome, ribulose diphosphate carboxylase.
9 ted protein kinase and its target acetyl-CoA carboxylase.
10 accumulate chloroplastic phosphoenolpyruvate carboxylase.
11 erent from those of related biotin-dependent carboxylases.
12 anslational biotinylation of acyl coenzyme A carboxylases.
13 rent from that of the other biotin-dependent carboxylases.
14 zymes collectively known as biotin-dependent carboxylases.
15 xation reactions by supplying bicarbonate to carboxylases.
16 or multiple metabolic reactions catalyzed by carboxylases.
17 inimal biotin acceptor BCCP fragments of the carboxylases.
18 icity in dictating biotin distribution among carboxylases.
19 otein (BCCP) domain of five biotin-dependent carboxylases.
20  mechanism and evolution of biotin-dependent carboxylases.
21 carbonate, the required substrate of various carboxylases.
22  cell-specific deletion of acetyl coenzyme A carboxylase 1 (ACC1), an enzyme that catalyzes conversio
23 rements of key lipogenic enzymes [acetyl CoA carboxylase 1 (ACC1), fatty acid synthase (FASN), and st
24 By contrast, biotinylation of the acetyl-CoA carboxylase 1 and 2 (ACC1 and ACC2) fragments, both of w
25 ovel series of dual inhibitors of acetyl-CoA carboxylase 1 and 2 (ACC1 and ACC2).
26 nfection, a specific inhibitor of acetyl CoA carboxylase 1, 5-(tetradecyloxy)-2-furoic acid, was admi
27 lipogenesis: fatty acid synthase, acetyl-CoA carboxylase 1, and glycerol-3-phosphate acyltransferase.
28 arly pharmaceutical inhibition of acetyl CoA carboxylase 1, the rate limiting step of FAS, inhibit ge
29     We have shown previously that acetyl-CoA carboxylase 2 (Acc2(-/-)) mutant mice, when fed a high-f
30 ecause malonyl CoA production via acetyl CoA carboxylase 2 (ACC2) inhibits the entry of long chain fa
31 nt abundance via hydroxylation of acetyl-coA carboxylase 2 (ACC2).
32 t of adipose triglyceride lipase, acetyl-CoA carboxylase 2 and AMP-activated protein kinase (AMPK)gam
33 r 1c, fatty acid synthase, acetyl coenzyme A carboxylase 2, and carnitine palmitoyltransferase 1 alph
34 NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC), an atypical member of the disulfid
35 nservation with the related biotin-dependent carboxylases 3-methylcrotonyl-CoA carboxylase (MCC) and
36 ed by decreased protein levels of acetyl-CoA carboxylase, a key regulator of both lipid oxidation and
37 e lipid synthesis is catalyzed by acetyl-CoA carboxylase, a large complex composed of four subunits.
38 ased abundances of mRNA encoding Acetyl Co-A carboxylase (Acc) (up 25%) and Hsp70 (up 32%) in experim
39  that required phosphorylation of acetyl-CoA carboxylase (ACC) 1 and/or ACC2 at the AMPK sites.
40 ated by the SREBP-SCD pathway, an acetyl-CoA carboxylase (ACC) and certain nuclear hormone receptors
41                                   Acetyl-CoA carboxylase (ACC) catalyzes the rate-determining step in
42 c, fatty acid synthase (FAS), and acetyl-CoA carboxylase (ACC) gene expression.
43 ice by liver-specific knockout of acetyl-CoA carboxylase (ACC) genes and treat the mice with the hepa
44                                   Acetyl-CoA carboxylase (ACC) has crucial roles in fatty acid metabo
45  could be used to identify acetyl coenzyme A carboxylase (ACC) in Pseudomonas aeruginosa and human ce
46 biochemical or a genetic block at acetyl-CoA carboxylase (ACC) in S. aureus, confirming that regulati
47                The development of acetyl-CoA carboxylase (ACC) inhibitors for the treatment of metabo
48 of oxo-dihydrospiroindazole-based acetyl-CoA carboxylase (ACC) inhibitors is reported.
49                                   Acetyl-CoA carboxylase (ACC) inhibitors offer significant potential
50                                   Acetyl-CoA carboxylase (ACC) is a target of interest for the treatm
51 ent excess, induced both AMPK and acetyl-CoA carboxylase (ACC) phosphorylation.
52 utical inhibition of acetyl-coenzyme A (CoA) carboxylase (ACC), a key fatty acid biosynthetic enzyme,
53 olled by the rate-limiting enzyme acetyl-CoA carboxylase (ACC), an attractive but traditionally intra
54 ymes [fatty acid synthase (FASN), acetyl-CoA carboxylase (ACC), ATP citrate lyase (ACLY)].
55                RNAi silencing of Acetyl Co-A carboxylase (ACC), highly expressed in JGM-treated BPH,
56 olecule inhibitor of acetyl coenzyme A (CoA) carboxylase (ACC), the enzyme that controls the first ra
57 Kalpha and its downstream target, acetyl-CoA carboxylase (ACC), were hyperphosphorylated, indicative
58  AMPK phosphorylates and inhibits acetyl-CoA carboxylase (ACC), which catalyzes carboxylation of acet
59 get is the multifunctional enzyme acetyl-CoA carboxylase (ACC), which catalyzes the first committed s
60 levels of phosphorylated AMPK and acetyl-CoA carboxylase (ACC).
61 lation and inactivation of acetyl coenzyme A carboxylase (ACC).
62  downstream target phospho-acetyl-coenzyme A carboxylase (ACC).
63 2AMPK) and its downstream target, acetyl-CoA carboxylase (ACC).
64  of fatty acid synthase (FAS) and acetyl-CoA carboxylase (ACC).
65 an allosteric inhibitor of acetyl-coenzyme A carboxylases (ACC) ACC1 and ACC2, reduces hepatic de nov
66 reased phosphorylation, decreased acetyl-CoA carboxylase Acc1 phosphorylation, and sterol response el
67             The inhibition of the acetyl-CoA carboxylases ACC1 and ACC2 by AMPK maintains NADPH level
68 ement binding protein (SREBP)-1c, acetyl-CoA carboxylase (ACC1) and lipid uptake genes, such as PPARg
69 s is regulated by the activity of acetyl-CoA carboxylase (Acc1), the first and rate-limiting enzyme o
70  of fatty acid synthase (Fas) and acetyl-CoA carboxylase (Acc1).
71 which together pinpoint plastidic acetyl-CoA carboxylase (ACCase) as the enzymatic target of feedback
72                                   Acetyl-CoA carboxylase (ACCase) catalyzes the committed step of de
73 C2) that targets homomeric acetyl-coenzyme A carboxylase (ACCase) to plastids.
74                                      Acetone carboxylases (ACs) catalyze the conversion of substrates
75 s of pyruvate kinase and phosphoenolpyruvate carboxylase activities indicate that pyruvate is supplie
76 olysis, hepatic acetyl CoA content, pyruvate carboxylase activity and hepatic glucose production.
77  evolution, despite its competition with the carboxylase activity necessary for carbon fixation, yet
78                             They enhance the carboxylase activity of RuBisCO by increasing the local
79 entrating pathway that helps to maximize the carboxylase activity of the enzyme while suppressing its
80                    Ribulose-1,5-bisphosphate carboxylase activity was confirmed in H2/bicarbonate-gro
81 ssing seeds indicated the in vivo acetyl-CoA carboxylase activity was reduced to approximately half t
82 ydroxylase alleviated the reduced acetyl-CoA carboxylase activity, restored the rate of fatty acid sy
83 ate the expression of crotonyl-CoA reductase/carboxylase, an enzyme of the ethylmalonyl-CoA pathway i
84 hosphate synthetase 1 (urea cycle), pyruvate carboxylase (anaplerosis, gluconeogenesis), propionyl-Co
85 ynthesis and consists of two enzymes: biotin carboxylase and carboxyltransferase.
86 biotin acceptor protein of acetyl-coenzyme A carboxylase and catalyzes posttranslational biotinylatio
87  is associated with activation of acetyl-CoA carboxylase and changes in the expression profiles of re
88 kinase, MB inactivates downstream acetyl-CoA carboxylase and decreases cyclin expression.
89 ts and regulators of lipogenesis, acetyl CoA carboxylase and fatty acid synthase.
90 sis, as well as the expression of acetyl-CoA carboxylase and fatty acid synthase.
91 ssion of the mSREBP1 target genes acetyl-CoA carboxylase and fatty-acid synthase was suppressed, alon
92 RNAs for simultaneous repression of pyruvate carboxylase and glutaminase by selecting all seed matche
93 g AMPK-induced phosphorylation of acetyl-CoA carboxylase and in activating the PI3K/AKT pathway throu
94  stimulated flux through phosphoenolpyruvate carboxylase and malic enzyme, altered the balance betwee
95 ng enzyme AMPK, and inhibition of acetyl-CoA carboxylase and mammalian target of rapamycin signaling
96 nslational regulation of phosphoenolpyruvate carboxylase and nitrate reductase.
97 orylate its endogenous substrates acetyl CoA carboxylase and Raptor, and provokes mitochondrial bioge
98 xidation partially occurred through pyruvate carboxylase and rendered NNT knockdown cells more sensit
99  activity of the anabolic factors acetyl-CoA carboxylase and ribosomal protein S6 and inhibiting aero
100 vitro activities of both phosphoenolpyruvate carboxylase and Rubisco were increased.
101 abolic pathway from NaAD using unprecedented carboxylase and sulfur transferase reactions to form the
102 keto acid dehydrogenase E1 component, biotin carboxylase and superoxide dismutase were related to ene
103 a conserved component among biotin-dependent carboxylases and catalyzes the MgATP-dependent carboxyla
104  these proteins likely function as guanidine carboxylases and guanidine transporters, respectively.
105 the expression of proteins annotated as urea carboxylases and multidrug efflux pumps.
106 anaplerosis, gluconeogenesis), propionyl-CoA carboxylase, and 3-methylcrotonyl-CoA carboxylase (branc
107 sed phosphorylation of raptor and acetyl-CoA carboxylase, and decreased phosphorylation of ULK1 (Ser-
108 malic acid inhibition of phosphoenolpyruvate carboxylase, and enzyme kinetics) was simulated.
109 nt-binding protein 1c (SREBP-1c), acetyl-CoA carboxylase, and fatty-acid synthase, three key function
110 enolpyruvate carboxykinase (PEPCK), pyruvate carboxylase, and glucose-6-phosphatase, and the neonate'
111 red the phosphorylations of AMPK, acetyl CoA carboxylase, and glycogen synthase kinase-3, decreased g
112 lement-binding proteins 1c and 2, acetyl-CoA carboxylase, and HMG-CoA reductase mRNAs/proteins and in
113 -CoA content, a potent activator of pyruvate carboxylase, and increased glycerol conversion to glucos
114 oxylases propionyl-CoA carboxylase, pyruvate carboxylase, and methylcrotonoyl-CoA carboxylase is fast
115 strates, including Raptor, acetyl coenzyme A carboxylase, and PGC-1alpha, is attenuated in IRE1alpha-
116 n fatty acid synthesis, including acetyl-CoA carboxylase, and three out of five putative type II digl
117                             Biotin-dependent carboxylases are widely distributed in nature and have i
118                      Interestingly, pyruvate carboxylase ASO also reduced adiposity, plasma lipid con
119                                     Pyruvate carboxylase ASO did not alter de novo fatty acid synthes
120                                     Pyruvate carboxylase ASO had similar effects in Zucker Diabetic F
121                                     Pyruvate carboxylase ASO reduced plasma glucose concentrations an
122 1-c, SREBP2, fatty-acid synthase, acetyl-CoA carboxylase, ATP citrate lyase, and Glut-1 were signific
123 LmPC), a biotin-dependent enzyme with biotin carboxylase (BC) and carboxyltransferase (CT) activities
124                          ACC contains biotin carboxylase (BC) and carboxyltransferase (CT) activities
125 catalyzed by the holo-ACC components, biotin carboxylase (BC) and carboxyltransferase (CT), were simu
126                                       Biotin carboxylase (BC) is a conserved component among biotin-d
127                           PC contains biotin carboxylase (BC), carboxyltransferase (CT) and biotin ca
128  moiety to a specific lysine residue of each carboxylase BCCP domain.
129 h was predicted to inhibit acetyl coenzyme A carboxylase beta, a key fatty acid oxidation enzyme that
130 yl-CoA carboxylase, and 3-methylcrotonyl-CoA carboxylase (branched chain amino acids catabolism).
131 gulation of the model C4 phosphoenolpyruvate carboxylase (C4-Pepc) promoter in maize (Zea mays).
132 x ), the maximum rate of phosphoenolpyruvate carboxylase carboxylation (Vpmax ), and foliar dark resp
133             In human cells, biotin-dependent carboxylases catalyze key reactions in gluconeogenesis,
134 ncoding a plastid-targeted acetyl-coenzyme A carboxylase, cause hypersensitivity to spectinomycin.
135 ioesters catalysed by crotonyl-CoA reductase/carboxylase (CCRC) homologues.
136 e AMPK substrates, p53 and acetyl-coenzyme A carboxylase, changes that correlated with increased miR-
137 on hypotheses by feeding leaves with the PEP carboxylase competitive inhibitors malate and diethyl ox
138 ient and specific interactions with the urea carboxylase component of urea amidolyase.
139 34H encodes a 3-octaprenyl-4-hydroxybenzoate carboxylase (CpsUbiX, UniProtKB code: Q489U8) that is in
140 ulation of plastid-encoded acetyl Coenzyme A carboxylase D proteins accounting for the generation of
141 cle defects, organic acidurias, and pyruvate carboxylase deficiency as a treatable condition in the d
142 host was supported by experiments with a PEP carboxylase-deficient mutant strain in blood and cerebro
143 e for citrate cycling rather than acetyl-CoA carboxylase-dependent fatty acid synthesis.
144 c group must first gain access to the biotin carboxylase domain and become carboxylated and then tran
145 al conformation in the absence of the biotin carboxylase domain and that the carboxyltransferase doma
146  version, consisting of little more than the carboxylase domain of the plastidic accD gene fused to a
147 onments, where heteromeric acetyl-coenzyme A carboxylase encoded in part by the chloroplast genome ca
148                           Microorganisms use carboxylase enzymes to form new carbon-carbon bonds by i
149    We confirmed that BPL-1 biotinylates four carboxylase enzymes, and we demonstrate that BPL-1 is re
150 g a ligand-stimulated decrease in acetyl-CoA carboxylase expression.
151 tty acid synthesis genes, namely, acetyl-CoA carboxylase, fatty acid synthase, SREBP1c, chREBP, gluco
152 al citrate synthase flux (V CS) and pyruvate carboxylase flux (V PC) in vivo.
153 ssue (WAT) leading to reductions in pyruvate carboxylase flux.
154 acetyl-CoA allosteric activation of pyruvate carboxylase flux.
155 uvate dehydrogenase and anaplerotic pyruvate carboxylase fluxes.
156 one, the latter required by the enzyme gamma-carboxylase for gamma-carboxylation of all vitamin K-dep
157 ession of genes encoding PEX7 and acetyl-CoA carboxylase further improved fatty alcohol production by
158                                  Geranyl-CoA carboxylase (GCC) is essential for the growth of Pseudom
159               First, the phosphoenolpyruvate carboxylase gene (ppc) from Klebsiella pneumoniae was ov
160 e dexamethasone system to silence acetyl-CoA carboxylase gene and observed prolific root growth when
161 trix, OCN is gamma-carboxylated by the gamma-carboxylase (GGCX) on three glutamic acid residues, a ce
162  associated with mutations in gamma-glutamyl carboxylase (GGCX) that often has fatal outcomes.
163 tem for studying mutations in gamma-glutamyl carboxylase (GGCX), the enzyme responsible for convertin
164   Eleven spontaneous mutations of acetyl-CoA carboxylase have been identified in many herbicide-resis
165 c (CE) assay for measuring acetyl coenzyme A carboxylase holoenzyme (holo-ACC) activity and inhibitio
166 crystal structure of the long-chain acyl-CoA carboxylase holoenzyme from Mycobacterium avium subspeci
167  and BCCP domains and other biotin-dependent carboxylase holoenzymes are known, there is currently no
168 ain (120 kDa), multi-domain biotin-dependent carboxylase in bacteria.
169 on catalyzed by phosphoribosylaminoimidazole carboxylase in purine metabolism.
170             We assessed the role of pyruvate carboxylase in regulating glucose and lipid metabolism i
171 increased UCP-3 and inhibition of acetyl-CoA carboxylase in skeletal muscle, findings consistent with
172   Carbonic anhydrase and phosphoenolpyruvate carboxylase in vitro activity varied significantly despi
173 [3,4-c]pyridin]-7'(2'H)-one-based acetyl-CoA carboxylase inhibitors is reported.
174       Tissue-specific inhibition of pyruvate carboxylase is a potential therapeutic approach for nona
175 metabolic diseases in humans, and acetyl-CoA carboxylase is a target for drug discovery in the treatm
176 n yeast Saccharomyces cerevisiae, acetyl-CoA carboxylase is encoded by the ACC1 gene.
177  In particular, we demonstrate that pyruvate carboxylase is essential to re-supply the depleted pool
178 yruvate carboxylase, and methylcrotonoyl-CoA carboxylase is fast and limited by the bimolecular assoc
179 ed protein kinase called phosphoenolpyruvate carboxylase kinase (PPCK).
180 ria monocytogenes by inhibiting its pyruvate carboxylase (LmPC), a biotin-dependent enzyme with bioti
181 luding the central metabolic enzyme pyruvate carboxylase (LmPC).
182 -dependent carboxylases 3-methylcrotonyl-CoA carboxylase (MCC) and propionyl-CoA carboxylase (PCC).
183                         3-methylcrotonyl CoA carboxylase (MCCase) is a nuclear-encoded, mitochondrial
184 rucial in bicarbonate provision for pyruvate carboxylase-mediated oxaloacetate synthesis.
185 levels of Fatty Acid Synthase and Acetyl CoA Carboxylase mRNAs, enzymes responsible for lipid synthes
186 inus resembles aminoimidazole ribonucleotide carboxylase/mutase, LarC binds Ni and could act in Ni de
187 stinct lineages of biotin-dependent acyl-CoA carboxylases, one carboxylating the alpha carbon of a sa
188 result of enhanced activity of cytosolic PEP carboxylase or by limited supply of energetic and reduct
189 ding form I ribulose-1,5-bisphosphate (RuBP) carboxylase oxygenase (RubisCO) along with a divergently
190                    Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco) concentrations were quan
191 educed affinity of ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCO) to CO2 under conditions
192 lvin Cycle enzyme, Ribulose 1,5 bisphosphate carboxylase oxygenase (Rubisco).
193 tosynthesis (e.g., ribulose-1,5-bisphosphate carboxylase oxygenase genes rbcS and rbcL), imply large-
194                     Ribulose-1,5-biphosphate-carboxylase-oxygenase (RuBisCO) has a crucial role in ca
195 hybrid type II/III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) that couples adenosine m
196 100 genes encoding ribulose-1,5 bisphosphate carboxylase-oxygenase subunit proteins of the Calvin cyc
197 ies of the enzymes ribulose 1,5-bisphosphate carboxylase/ oxygenase and carbonic anhydrase to facilit
198                        Ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase uses the energy
199 boxysomal enzymes, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase (
200 n by concentrating ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and its substrate CO2 wi
201  of carbon, ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes primary carbon
202         The enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes two competing
203 hibitors from dead-end ribulose-bisphosphate carboxylase/oxygenase (Rubisco) complexes requires the a
204 rbon-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) in a paracrystalline lat
205                    Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) is a critical yet severe
206                    Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in c
207  CO2-fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) is inhibited by nonprodu
208                    Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involv
209 hetic organisms, D-ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major enzyme assi
210                     Ribulose-1,5-biphosphate carboxylase/oxygenase (Rubisco) is the most abundant enz
211  CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) often limit plant produc
212                    Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) plays a critical role in
213 ntalize the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) with carbonic anhydrase.
214 om the reaction of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) with O2 instead of CO2 ,
215 ion at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), simultaneously enhancin
216                    Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the carboxylating enzym
217 ge subunit (LS) of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme catalyzing t
218 alog-bound form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco).
219 imary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco).
220 on fixing enzyme, ribulose-1,5-bis-phosphate carboxylase/oxygenase (Rubisco).
221  CO2 fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco).
222 e carboxylating enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO).
223 hs by sequestering ribulose-1,5-bisphosphate carboxylase/oxygenase and carbonic anhydrase in the micr
224 sulate the enzymes ribulose 1,5-bisphosphate carboxylase/oxygenase and carbonic anhydrase.
225 e small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and its reverse peptide with a ser
226 and, by extension, ribulose-1,5-bisphosphate carboxylase/oxygenase and the carbonic anhydrase CcaA, w
227 e dual activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and the resulting loss of CO(2) by
228 refolding of bacterial ribulose-bisphosphate carboxylase/oxygenase but gained this ability when CrCpn
229  Mg(2+) within the ribulose-1,5-bisphosphate carboxylase/oxygenase family of enzymes.
230 imple kinetic model of ribulose bisphosphate carboxylase/oxygenase function.
231 enitrification and ribulose 1,5-bisphosphate carboxylase/oxygenase gene clusters, underscoring its ab
232           Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyses the key reaction in the
233  small subunit of ribulose-1,5-bis-phosphate carboxylase/oxygenase, and ferredoxin, we exposed these
234 ss II aldolase, or ribulose 1,5-bisphosphate carboxylase/oxygenase, large subunit (RuBisCO) superfami
235 ontribution of the ribulose-1,5-bisphosphate carboxylase/oxygenase-bypass to seed storage metabolism
236                  d-Ribulose 1,5-bisphosphate carboxylase/oxygenases (RuBisCOs) are promiscuous, catal
237 cid oxidation, activated the AMPK-acetyl-CoA carboxylase pathway, and promoted inefficient metabolism
238 rent correlation with gluconeogenic pyruvate carboxylase (PC) activity in hepatocytes.
239 mine, which require the activity of pyruvate carboxylase (PC) and glutaminase 1 (GLS1), respectively.
240                                     Pyruvate carboxylase (PC) has important roles in metabolism and i
241  in the structure of the tetrameric pyruvate carboxylase (PC) holoenzyme.
242                                     Pyruvate carboxylase (PC), a multifunctional biotin-dependent enz
243 ression of the mitochondrial enzyme pyruvate carboxylase (PC), resulting in diminished production of
244  the carboxyl transferase domain of pyruvate carboxylase (PC).
245 onyl-CoA carboxylase (MCC) and propionyl-CoA carboxylase (PCC).
246  The activities of phosphoenolpyruvate (PEP) carboxylase (PEPC) and the PEP-regenerating enzyme, pyru
247 tant functions for phosphoenolpyruvate (PEP) carboxylase (PEPC) in inorganic phosphate (Pi)-starved p
248                          Phosphoenolpyruvate carboxylase (PEPC) is a crucial enzyme that catalyzes an
249                          Phosphoenolpyruvate carboxylase (PEPC) is a tightly controlled cytosolic enz
250 ymatic rates of Rubisco, phosphoenolpyruvate carboxylase (PEPc), and carbonic anhydrase (CA).
251 e for C4 photosynthesis, Phosphoenolpyruvate Carboxylase (PEPC), evolved from nonphotosynthetic PEPC
252 tion after inhibition of phosphoenolpyruvate carboxylases (PEPCs), and increases in PEPC transcript a
253 le via a stage-dependent phosphoenolpyruvate carboxylase/phosphoenolpyruvate carboxykinase process th
254 ed AMPK activation and downstream acetyl-CoA carboxylase phosphorylation and glucose uptake in isolat
255 vels, and diminished acetyl coenzyme A (CoA) carboxylase phosphorylation than in the wild-type livers
256                                   Acetyl-CoA carboxylase phosphorylation was increased in gastrocnemi
257 K activity, particularly phosphoenolpyruvate carboxylase (PPC) and PPDK in rNAD-ME1.
258 production of the enzyme phosphoenolpyruvate carboxylase (PPC) and that adventitious overexpression o
259                          Phosphoenolpyruvate carboxylase (PPC; EC 4.1.1.31) catalyzes primary nocturn
260 osphate synthase (PpsAB) and phenylphosphate carboxylase (PpcABCD) and syntrophic terephthalate-degra
261 n of the BCCP fragments of the mitochondrial carboxylases propionyl-CoA carboxylase, pyruvate carboxy
262 EPC is phosphorylated by Phosphoenolpyruvate Carboxylase Protein Kinase (PPCK).
263 ecimens and found that only hepatic pyruvate carboxylase protein levels related strongly with glycemi
264 umulated a chloroplastic phosphoenolpyruvate carboxylase protein, albeit at reduced amounts relative
265 or biotin auxotrophs and identified pyruvate carboxylase (Pyc) as required for biotin biosynthesis.
266  low CO2 , including both PEPCs and pyruvate carboxylase (PYC), whereas ME abundance did not change a
267 s in the acetyl-CoA binding site of pyruvate carboxylase (PycA) rescued cefuroxime resistance and res
268 the mitochondrial carboxylases propionyl-CoA carboxylase, pyruvate carboxylase, and methylcrotonoyl-C
269     Maize genes encoding phosphoenolpyruvate carboxylase, pyruvate, orthophosphate dikinase, and the
270 tate exclusively via the phosphoenolpyruvate carboxylase reaction.
271 taacuI::kan mutant phenotype by crotonyl-CoA carboxylase/reductase from R. sphaeroides was attributed
272 a mutation in the gene encoding crotonyl-CoA carboxylase/reductase, demonstrating that acetate produc
273               Many bicarbonate-incorporating carboxylases rely on the organic cofactor biotin for the
274 artment in which algae sequester the primary carboxylase, ribulose-1,5-bisphosphate carboxylase/oxyge
275 d an archaeal-type ribulose-1,5-bisphosphate carboxylase (RubisCO) involved in AMP recycling.
276 lvin cycle enzyme, ribulose 1,5-bisphosphate carboxylase (RubisCO), prevents photoheterotrophic growt
277 ptation is that of ribulose-1,5-bisphosphate carboxylase (RubisCO), the enzyme responsible for fixati
278 of biotinylation suggests that mitochondrial carboxylase sequences evolved to produce fast associatio
279 e, we show that the chloroplastic acetyl-CoA carboxylase subunit (accD) gene that is present in the p
280  in steady-state behavioural assays, acetone carboxylase subunit (acxC) mutant behaviour was altered.
281  protease subunit (clpP)-like and acetyl-CoA carboxylase subunit D (accD)-like open reading frames.
282  translation of the plastid-encoded ACC beta-carboxylase subunit.
283 mide activated AMPK and inhibited acetyl-CoA carboxylase, suggesting activation of fat metabolism in
284 at the otherwise integrative enzyme pyruvate carboxylase (TgPyC) is dispensable not only in glycolysi
285 pic polypeptide (GIP) receptor, and pyruvate carboxylase) that are important regulators of beta-cell
286 ng system provided by a cytosolic acetyl-CoA carboxylase, the mitochondrial AAE13 protein is essentia
287 x mutations on the sensitivity of acetyl-CoA carboxylase to nine herbicides representing the three ch
288 version of lactate to pyruvate, via pyruvate carboxylase to oxaloacetate, and via PCK2 to phosphoenol
289  pathways with varying flux ratio of RubisCO carboxylase to oxygenase may contribute to the adaptive
290 ene that targets homomeric acetyl-coenzyme A carboxylase to plastids, where the multidomain protein c
291 mary downstream targeting enzyme, acetyl-CoA carboxylase, up-regulated gene expression of carnitine p
292                     The activity of pyruvate carboxylase was low in muscle, and no PEP carboxykinase
293 tivity in HCS-catalyzed biotinylation to the carboxylases was investigated in single turnover stopped
294  canola endogenous reference gene (acety-CoA-carboxylase) was constructed and used for duplex real-ti
295 os of PEPC and PPDK to ribulose bisphosphate carboxylase were substantially lower than 1, even at low
296  SNF1 phosphorylates and inhibits acetyl-CoA carboxylase, which catalyzes the carboxylation of acetyl
297                                     Pyruvate carboxylase, which catalyzes the first step of gluconeog
298 ction of new herbicides targeting acetyl-CoA carboxylase will depend on their ability to overcome the
299 e may be fixed via the ribulose bisphosphate carboxylase, Wood-Ljungdahl pathway or reductive TCA cyc
300  of the unusual beta-subunit of the acyl-CoA carboxylase (YCC) responsible for this reaction, alone a

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