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1 fatty acid oxidation (acetylCoA carboxylase; carnitine-palmitoyltransferase).
2 ng enzyme activities for arylsulfatase A and carnitine palmitoyltransferase.
3 Both residues are replaced by glycine in carnitine palmitoyltransferases.
4 complex I was associated with a decrease in carnitine palmitoyltransferase 1 (cPT1) and cPT2 levels.
7 ated with changes in ACSL1 (R(2) = 0.39) and carnitine palmitoyltransferase 1 (R(2) = 0.30) expressio
8 nthase, acetyl coenzyme A carboxylase 2, and carnitine palmitoyltransferase 1 alpha) in both WT and A
9 tty acid oxidation through the inhibition of carnitine palmitoyltransferase 1 by its product malonyl-
11 of the lipogenic pool but diminution of the carnitine palmitoyltransferase 1 inhibitory pool under c
13 ated receptor alpha and induction of hepatic carnitine palmitoyltransferase 1, suggesting increased e
14 unction through its allosteric inhibition of carnitine palmitoyltransferase 1, the enzyme that normal
16 cid oxidation by stimulating the activity of carnitine palmitoyltransferase-1 (CPT-1) and inhibiting
18 atty acids (LCFAs) into the mitochondria via carnitine palmitoyltransferase-1 (CPT-1) is inhibited by
20 l downstream effects including inhibition of carnitine palmitoyltransferase-1 (CPT-1) with resultant
21 ns, C75 inhibits FAS activity and stimulates carnitine palmitoyltransferase-1 (CPT-1), consistent wit
24 Malonyl-CoA is an established inhibitor of carnitine palmitoyltransferase-1 (CPT1), an outer mitoch
25 o this end, we targeted the liver isoform of carnitine palmitoyltransferase-1 (encoded by the CPT1A g
26 r-activated receptor alpha protein and liver-carnitine palmitoyltransferase-1 (l-CPT-1) mRNA increase
27 lipogenesis and decrease in the activity of carnitine palmitoyltransferase-1 and total energy expend
28 quent treatment of mice for 4 weeks with the carnitine palmitoyltransferase-1 inhibitor, oxfenicine (
29 omir) consumed diets containing 0.01% of the carnitine palmitoyltransferase-1 inhibitor, R-etomoxir,
32 genes of fatty acid oxidation such as Cpt-1 (carnitine palmitoyltransferase-1) as well as Pgc-1alpha
34 l-CoA is a potent inhibitor of mitochondrial carnitine palmitoyltransferase-1, a key enzyme involved
35 reflect a metabolic bottleneck downstream of carnitine palmitoyltransferase-1, a mitochondrial enzyme
36 lcohol-induced liver injury due to increased carnitine palmitoyltransferase-1, phosphorylated 5'AMP-a
38 , cg01082498, and cg09737197) in intron 1 of carnitine palmitoyltransferase 1A (CPT1A) were strongly
39 onent of mitochondrial fatty acid transport, carnitine palmitoyltransferase 1A (CPT1A), as a direct H
40 e in malonyl-CoA levels and desinhibition of carnitine palmitoyltransferase 1A (CPT1A), which increas
41 cy of NOX4 resulted in reduced expression of carnitine palmitoyltransferase 1A (CPT1A), which is a ke
43 rile (PCN) down-regulated the mRNA levels of carnitine palmitoyltransferase 1A (in beta-oxidation) an
44 ation of transmembrane domain 2 (TM2) of rat carnitine palmitoyltransferase 1A (rCPT1A), to elucidate
45 metabolism genes acyl coenzyme A oxidase and carnitine palmitoyltransferase 1A in livers of alcohol-f
48 n, including carnitine O-octaniltransferase, carnitine palmitoyltransferase 1A, hydroxyacyl-CoA-dehyd
50 oactivator 1alpha, uncoupling protein 1, and carnitine palmitoyltransferase 1alpha, were increased by
51 malonyl-CoA with simultaneous inhibition of carnitine palmitoyltransferase 1b and 2) catalyze the pa
53 These effects, coupled with an increased carnitine palmitoyltransferase 1b, led to increased fatt
54 imiting for glucose oxidation and suppresses carnitine palmitoyltransferase-1B (CPT-1B), a key enzyme
57 of the constituents of the AMPAR complex is carnitine palmitoyltransferase 1C (CPT1C), a brain-speci
58 tochondrial long-chain fatty acid oxidation, carnitine palmitoyltransferase 2 (CPT2), on muscle and h
59 52 to alanine resulted in 50 and 93% loss in carnitine palmitoyltransferase activity, respectively.
60 whereas, in obese Zucker rat hearts, muscle carnitine palmitoyltransferase and medium-chain acyl-CoA
61 al membranes express two active but distinct carnitine palmitoyltransferases: carnitine palmitoyltran
62 oefficients for mitochondrial outer-membrane carnitine palmitoyltransferase (CPT I) over hepatic keto
65 ng-chain fatty acids in the early 1960s, the carnitine palmitoyltransferase (CPT) system has since co
67 set out to determine if the cDNA encoding a carnitine palmitoyltransferase (CPT)-like protein recent
68 idea that malonyl-coenzyme A (CoA)-sensitive carnitine palmitoyltransferase (CPT-I) is localized on t
69 ated with increased expression of the muscle carnitine palmitoyltransferase (CPT-I) isoform as measur
70 nction and altered lipid metabolism and that carnitine palmitoyltransferases (CPT) have a major role
71 the metabolic channeling of acyl-CoA through carnitine palmitoyltransferases (CPT-1/2) and attenuated
72 tradiol inhibited hypothalamic expression of carnitine palmitoyltransferase (CPT1a and CPT1c) and pyr
75 s were transduced with adenoviruses encoding carnitine palmitoyltransferase I (CPT I) isoforms or bet
76 nd an inhibitor of the two known isoforms of carnitine palmitoyltransferase I (CPT I), which control
81 oxidase], and mitochondrial differentiation [carnitine palmitoyltransferase I (CPT-I) isoforms] were
82 d by the outer mitochondrial membrane enzyme carnitine palmitoyltransferase I (CPTI) and inhibited by
84 ut distinct carnitine palmitoyltransferases: carnitine palmitoyltransferase I (CPTI), which is malony
86 N-terminal amino acid residues of rat liver carnitine palmitoyltransferase I (L-CPTI) are essential
87 N-terminal amino acid residues of rat liver carnitine palmitoyltransferase I (L-CPTI) on malonyl-CoA
88 n catalytic activity in the liver isoform of carnitine palmitoyltransferase I (L-CPTI), we separately
89 xidative flux, the expression of muscle-type carnitine palmitoyltransferase I (M-CPT I) was character
90 n the expression of the gene encoding muscle carnitine palmitoyltransferase I (M-CPT I), an enzyme in
91 induced accumulation of mRNA encoding muscle carnitine palmitoyltransferase I (M-CPT I), an enzyme th
93 t in the heart, but the liver isoform (liver carnitine palmitoyltransferase I [L-CPT1]) is elevated i
94 lated to the role of ACC-beta in controlling carnitine palmitoyltransferase I activity and fatty acid
96 uscle suppress the activity of mitochondrial carnitine palmitoyltransferase I and thus fatty acid oxi
100 chain free fatty acids into mitochondria via carnitine palmitoyltransferase I relative to overall oxi
101 tricarboxylic acid cycle rates, flux through carnitine palmitoyltransferase I was 23% lower in hypert
103 ndrial (medium-chain acyl-CoA dehydrogenase, carnitine palmitoyltransferase I) and extramitochondrial
105 tty acid oxidation through the inhibition of carnitine palmitoyltransferase I, a mitochondrial compon
106 oncentration of malonyl-CoA, an inhibitor of carnitine palmitoyltransferase I, have been linked to th
108 activated receptor alpha target, muscle-type carnitine palmitoyltransferase I, providing a second mec
109 me for fatty acid oxidation in mitochondria, carnitine palmitoyltransferase I; and by reduction of su
111 FAO by pretreatment of fasting rats with the carnitine palmitoyltransferase-I (CPT-I) inhibitor reduc
112 ent, endogenous, and allosteric inhibitor of carnitine palmitoyltransferase-I (CPT-I), a key enzyme f
113 sequence coverage for the membrane proteins carnitine palmitoyltransferase-I (CPT-I), long-chain acy
115 idative responses to fasting are maintained; carnitine palmitoyltransferase-I induction and glucose l
116 tic expression of enzymes of fat catabolism (carnitine palmitoyltransferase-I, acyl-CoA oxidase, and
118 analysis of the 5'-flanking sequence of the carnitine palmitoyltransferase Ibeta (CPT-Ibeta) gene de
119 onyl coA-sensitive and detergent-labile; and carnitine palmitoyltransferase II (CPTII), which is malo
120 is presentation closely resembles adult-type carnitine palmitoyltransferase II deficiency except that
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