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1 (+) or without (-) etomoxir (an inhibitor of carnitine palmitoyltransferase I).
2 tty acid oxidation through the inhibition of carnitine palmitoyltransferase I, a mitochondrial compon
3 lated to the role of ACC-beta in controlling carnitine palmitoyltransferase I activity and fatty acid
4 tic expression of enzymes of fat catabolism (carnitine palmitoyltransferase-I, acyl-CoA oxidase, and
6 uscle suppress the activity of mitochondrial carnitine palmitoyltransferase I and thus fatty acid oxi
7 ndrial (medium-chain acyl-CoA dehydrogenase, carnitine palmitoyltransferase I) and extramitochondrial
8 me for fatty acid oxidation in mitochondria, carnitine palmitoyltransferase I; and by reduction of su
9 etabolic enzymes, pyruvate dehydrogenase and carnitine palmitoyltransferase I by modulating the level
11 s were transduced with adenoviruses encoding carnitine palmitoyltransferase I (CPT I) isoforms or bet
12 nd an inhibitor of the two known isoforms of carnitine palmitoyltransferase I (CPT I), which control
17 oxidase], and mitochondrial differentiation [carnitine palmitoyltransferase I (CPT-I) isoforms] were
19 FAO by pretreatment of fasting rats with the carnitine palmitoyltransferase-I (CPT-I) inhibitor reduc
20 ent, endogenous, and allosteric inhibitor of carnitine palmitoyltransferase-I (CPT-I), a key enzyme f
21 sequence coverage for the membrane proteins carnitine palmitoyltransferase-I (CPT-I), long-chain acy
22 ons in intramuscular pH (acidosis) attenuate carnitine palmitoyltransferase-I (CPT-I)-supported bioen
24 ptake of fatty acids and their expression of carnitine palmitoyltransferase I (CPT1A), a critical enz
25 d by the outer mitochondrial membrane enzyme carnitine palmitoyltransferase I (CPTI) and inhibited by
27 ut distinct carnitine palmitoyltransferases: carnitine palmitoyltransferase I (CPTI), which is malony
28 oncentration of malonyl-CoA, an inhibitor of carnitine palmitoyltransferase I, have been linked to th
29 idative responses to fasting are maintained; carnitine palmitoyltransferase-I induction and glucose l
33 N-terminal amino acid residues of rat liver carnitine palmitoyltransferase I (L-CPTI) are essential
34 N-terminal amino acid residues of rat liver carnitine palmitoyltransferase I (L-CPTI) on malonyl-CoA
35 n catalytic activity in the liver isoform of carnitine palmitoyltransferase I (L-CPTI), we separately
36 t in the heart, but the liver isoform (liver carnitine palmitoyltransferase I [L-CPT1]) is elevated i
37 xidative flux, the expression of muscle-type carnitine palmitoyltransferase I (M-CPT I) was character
38 n the expression of the gene encoding muscle carnitine palmitoyltransferase I (M-CPT I), an enzyme in
39 induced accumulation of mRNA encoding muscle carnitine palmitoyltransferase I (M-CPT I), an enzyme th
42 activated receptor alpha target, muscle-type carnitine palmitoyltransferase I, providing a second mec
43 chain free fatty acids into mitochondria via carnitine palmitoyltransferase I relative to overall oxi
44 tricarboxylic acid cycle rates, flux through carnitine palmitoyltransferase I was 23% lower in hypert