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1 hesized as a probe of the active site in the medium chain acyl-CoA dehydrogenase.
2 in modulating thioester polarization in the medium chain acyl-CoA dehydrogenase.
3 s to the glutamate which acts as the base in medium chain acyl-CoA dehydrogenase.
4 ay which does not require involvement of the medium-chain acyl-CoA dehydrogenase.
5 on of fatty acid oxidation enzyme integrity, medium-chain acyl-CoA dehydrogenase activity and fat oxi
6 promotes TAMs differentiation by attenuating medium-chain acyl-CoA dehydrogenase activity and that in
7 of PPARalpha and PPARalpha-regulated genes (medium chain acyl-CoA dehydrogenase and pyruvate dehydro
8 ed its ability to receive electrons from the medium chain acyl-CoA dehydrogenase and the glutaryl-CoA
10 ity on short- or medium-chain acyl CoAs, and medium-chain acyl-CoA dehydrogenase and short-chain acyl
11 f cytotoxic fatty acids by the mitochondrial medium-chain acyl-CoA dehydrogenase and the peroxisomal
12 atriuretic peptide, beta myosin heavy chain, medium chain acyl-CoA dehydrogenase, and adrenomedullin
13 y did not change the basal acyl-CoA oxidase, medium chain acyl-CoA dehydrogenase, and malic enzyme mR
14 ase II from rat liver is compared to that of medium chain acyl-CoA dehydrogenase, and the structural
15 fatty acid oxidation, such as cytochrome c, medium-chain acyl-CoA dehydrogenase, and adipocyte prote
16 a, muscle carnitine palmitoyl transferase-1, medium-chain acyl-CoA dehydrogenase, and uncoupling prot
17 reductive half-reaction of ETF with porcine medium chain acyl-CoA dehydrogenase are unaltered when a
20 the rates of inactivation of short chain and medium chain acyl-CoA dehydrogenases by this inhibitor a
21 pha target genes encoding key mitochondrial (medium-chain acyl-CoA dehydrogenase, carnitine palmitoyl
23 responsive element (NRRE-1) derived from the medium chain acyl-CoA dehydrogenase gene promoter and nu
24 of the electron-transfer properties of human medium-chain acyl-CoA dehydrogenase (hwtMCADH) has been
25 Oxidation of thioester substrates in the medium-chain acyl-CoA dehydrogenase involves alpha-proto
27 oA dehydrogenase is very similar to those of medium chain acyl-CoA dehydrogenase, isovaleryl-CoA dehy
28 ed the binding of octenoyl-CoA to pig kidney medium chain acyl-CoA dehydrogenase (MCAD) by isothermal
29 expression of fatty acid synthase (FASN) and medium chain acyl-CoA dehydrogenase (MCAD) protein withi
30 376, via Glu-376 --> Asp (E376D) mutation in medium chain acyl-CoA dehydrogenase (MCAD), creates a co
31 c glutamate, identified as Glu376 in porcine medium chain acyl-CoA dehydrogenase (MCAD), Glu254 in hu
32 roduct), and octynoyl-CoA (inactivator) with medium chain acyl-CoA dehydrogenase (MCAD), were essenti
34 lations have been performed on the wild-type medium-chain acyl-CoA dehydrogenase (MCAD) and two of it
36 igate the redox and ionization properties of medium-chain acyl-CoA dehydrogenase (MCAD) from pig kidn
38 d previously in regulating the gene encoding medium-chain acyl-CoA dehydrogenase (MCAD), which cataly
39 nctional role in the recombinant human liver medium-chain acyl-CoA dehydrogenase (MCAD)-catalyzed rea
45 e promoter region of the gene encoding human medium-chain acyl-CoA dehydrogenase (MCAD, which catalyz
46 Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double
47 regulated genes were reduced (long chain and medium chain acyl-CoA dehydrogenases) or failed to be in
48 pression of apolipoprotein AI, AII, or CIII; medium chain acyl-CoA dehydrogenase; or stearoyl-CoA des
49 yanion hole in the reaction catalyzed by pig medium-chain acyl-CoA dehydrogenase (pMCAD) has been inv
50 d type, E99G, and E376Q mutants of the human medium chain acyl-CoA dehydrogenase showed that these tw
52 s folding of the fatty acid oxidation enzyme medium-chain acyl-CoA dehydrogenase, we tested whether a
53 s, muscle carnitine palmitoyltransferase and medium-chain acyl-CoA dehydrogenase were unaltered with
54 f-reaction of ETF catalyzed by sarcosine and medium chain acyl-CoA dehydrogenases which reduce the fl
55 ast, the activity and steady-state levels of medium-chain acyl-CoA dehydrogenase, which catalyzes a r
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