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1  deficiency of mitochondrial medium- or very long-chain acyl-CoA dehydrogenase.
2 -CoA dehydrogenase family except for IVD and long-chain acyl-CoA dehydrogenase.
3  mice decreased acetylation of mitochondrial long-chain acyl-CoA dehydrogenase, a known SIRT3 deacety
4 iltration analysis indicated that, like very-long-chain acyl-CoA dehydrogenase, ACAD-9 is a dimer, in
5 of 3-mercaptopropionic acid, an inhibitor of long chain acyl-CoA dehydrogenase, and partially inhibit
6 olic enzymes, such as acetyl-CoA synthetase, long-chain acyl-CoA dehydrogenase, and 3-hydroxy-3-methy
7  specificity, it appears that ACAD9 and very-long-chain acyl-CoA dehydrogenase are unable to compensa
8                  In three patients with very-long-chain acyl-CoA dehydrogenase deficiency, this treat
9 ce carrying the targeted inactivation of the long chain acyl CoA dehydrogenase gene (Acadl) are also
10 bution and gene regulation of ACAD9 and very-long-chain acyl-CoA dehydrogenase identify the presence
11 e, very long chain acyl-CoA synthetase, very long chain acyl-CoA dehydrogenase) in livers of the etha
12 CoA dehydrogenase (IVD), and Glu261 in human long chain acyl-CoA dehydrogenase (LCAD), has been sugge
13                  Crystal structures of human long-chain acyl-CoA dehydrogenase (LCAD) and the catalyt
14                           A kinetic study of long-chain acyl-CoA dehydrogenase (LCAD) and very long-c
15                                              Long-chain acyl-CoA dehydrogenase (LCAD) catalyzes the i
16 ) deficiency, none have been documented with long-chain acyl-CoA dehydrogenase (LCAD) deficiency.
17                                              Long-chain acyl-CoA dehydrogenase (LCAD) is a key mitoch
18                                              Long-chain acyl-CoA dehydrogenase (LCAD) is a mitochondr
19 stance, we studied mice with a deficiency of long-chain acyl-CoA dehydrogenase (LCAD), a key enzyme i
20 nother mitochondrial C(12) oxidation enzyme, long-chain acyl-CoA dehydrogenase (LCAD), also developed
21 mice lacking the fatty acid oxidation enzyme long-chain acyl-CoA dehydrogenase (LCAD).
22 base-arrangement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr
23                Moreover, the FAO enzyme very-long-chain acyl-CoA dehydrogenase physically interacted
24                        With the exception of long-chain acyl-CoA dehydrogenase protein level, which w
25 chain acyl-CoA dehydrogenase (LCAD) and very long-chain acyl-CoA dehydrogenase revealed that 5-trans-
26 er between the two human genes encoding very long chain acyl-CoA dehydrogenase (VLCAD) and postsynapt
27                                         Very long chain acyl-CoA dehydrogenase (VLCAD; ACADVL) was fo
28                                         Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the
29                                         Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is
30                                         Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is
31 h many patients have been found to have very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency, no
32 ifically exhibit down-regulation of the very-long-chain acyl-CoA dehydrogenase (VLCAD) enzyme, which
33                                         Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a major enz
34                                         Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a member of
35                                         Very long-chain acyl-CoA dehydrogenase (VLCAD) is an inner mi
36 tion that is highly homologous to human very-long-chain acyl-CoA dehydrogenase was identified by larg
37 urated acyl-CoAs are poor substrates of very long-chain acyl-CoA dehydrogenase when compared with myr