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1 cted based on the structure of a four-domain acyl-CoA oxidase.
2 enhanced expression of a known target gene, acyl-CoA oxidase.
3 n acyl-CoA dehydrogenase and the peroxisomal acyl-CoA oxidase.
4 ability to package catalase, luciferase and acyl-CoA oxidase.
5 rate-limiting enzyme of this cycle is fatty acyl-CoA oxidase.
6 e, we determine the crystal structure of the acyl-CoA oxidase 1 (ACOX-1) homodimer and the ACOX-2 hom
7 ered the expression of 28 transcripts [e.g., acyl-CoA oxidase 1 (ACOX1) and FAT atypical cadherin 1 (
8 oss-of-function mutations in the peroxisomal acyl-CoA oxidase 1 (ACOX1) gene cause neurodegeneration
12 out of the peroxisomal beta-oxidation enzyme acyl-CoA oxidase 1 (Acox1-AKO) was not sufficient to aff
15 In tissues expressing the "a" isoform of acyl-CoA oxidase-1 (ACOX1), a key peroxisomal fatty acid
19 CoA Oxidase 2 (ACOX2) encodes branched-chain acyl-CoA oxidase, a peroxisomal enzyme believed to be in
22 ssion of the canonical PPARalpha-target gene acyl-CoA-oxidase (ACO) in a PPARalpha-dependent manner i
24 the 5'-flanking region of H202-producing rat acyl-CoA oxidase (ACOX) gene and in other genes inducibl
25 stem, which consists of three enzymes: fatty acyl-CoA oxidase (ACOX), enoyl-CoA hydratase/3-hydroxyac
26 yltransferase (CAT) fusion construct for rat acyl-CoA oxidase (ACOX), the rate-limiting enzyme in the
27 on of fatty acids is catalyzed by the enzyme acyl-CoA oxidase (ACOX), which oxidizes a fatty acyl-CoA
29 ween ibr3 and acx3, which is defective in an acyl-CoA oxidase acting in fatty acid beta-oxidation, ha
30 cluded induction of acetylcholinesterase and acyl CoA oxidase activities and oxidative impairment, wh
32 ated animals showed significant induction of acyl-CoA oxidase activity, probably caused by PPARalpha
38 henotype results from loss of function of an acyl-CoA oxidase (ACX1A) that catalyzes the first step i
39 0.0001) and increased peroxisomal activity (acyl CoA oxidase and catalase activity) compared to the
41 fied by peptide sequence analysis, including acyl-CoA oxidase and a trifunctional enzyme of the perox
44 rate that peroxisomal beta-oxidation enzymes acyl-CoA oxidase and D-bifunctional protein are essentia
46 basis for the substrate specificities of the acyl-CoA oxidases and reveal why some of these enzymes h
47 e deficient in PPAR alpha, peroxisomal fatty acyl-CoA oxidase, and some of the other enzymes of the t
48 atabolism (carnitine palmitoyltransferase-I, acyl-CoA oxidase, and uncoupling protein-2) and their co
49 m to long-chain (ACX1) and long-chain (ACX2) acyl-CoA oxidases, and show that the corresponding endog
50 PARalpha (PPARalpha(-/-)), peroxisomal fatty acyl-CoA oxidase (AOX(-/-)), and in both PPARalpha and A
51 ng the PPARalpha-dependent regulation of the acyl-CoA oxidase (AOX) promoter, the rate-limiting step
53 The first step of this system, catalyzed by acyl-CoA oxidase (AOX), converts fatty acyl-CoA to 2-tra
55 dation pathway in mice at the level of fatty acyl-CoA oxidase (AOX), the first and rate-limiting enzy
56 We previously generated mice lacking fatty acyl-CoA oxidase (AOX), the first enzyme of the L-hydrox
57 e proliferators, whereas those lacking fatty acyl-CoA oxidase (AOX-/-), the first enzyme of the perox
59 xpression of mRNAs for the peroxisomal fatty acyl-CoA oxidase, bifunctional enzyme, or thiolase, whic
60 sappeared; there was increased expression of acyl CoA oxidase, carnitine palmitoyl transferase 1, and
63 ected with H2O2-generating peroxisomal fatty acyl-CoA oxidase cDNA, which encodes the first and rate-
65 al beta-oxidation pathway--disorders such as acyl CoA oxidase deficiency and bifunctional protein def
68 utant, which disrupts a putative peroxisomal acyl-CoA oxidase/dehydrogenase, ibr1 and ibr10 display n
69 bidopsis mutant defective in two peroxisomal acyl-CoA oxidases does not metabolize ascr#18 and does n
71 amely acyl-CoA synthetase (acs-1 and acs-2), acyl-CoA oxidase (F08A8.1 and F08A8.2), and stearoyl-CoA
73 anoyl-CoA alpha hydroxylase (PAHX) and fatty acyl-CoA oxidase (FACO) mRNA levels during differentiati
79 lone or in pairs and purified, the resulting acyl-CoA oxidase homo- and heterodimers displayed differ
80 In addition, the structure of peroxisomal acyl-CoA oxidase II from rat liver is compared to that o
82 alpha and of the classical peroxisomal fatty acyl-CoA oxidase in energy metabolism, and in the develo
83 to be made for the roles of uncharacterized acyl-CoA oxidases in C. elegans and in other nematode sp
84 uences share significant homology with known acyl-CoA oxidases, including the conserved CGGHGY motif,
85 catalyzing straight-chain acyl-CoAs by fatty acyl-CoA oxidase, L-bifunctional protein, and thiolase,
86 CoA dehydrogenases) or failed to be induced (acyl-CoA oxidase, liver carnitine palmitoyl-CoA transfer
87 RXRalpha deficiency did not change the basal acyl-CoA oxidase, medium chain acyl-CoA dehydrogenase, a
88 substrate specificities suggest that the two acyl-CoA oxidases might play a general house-keeping rol
89 lpha-mediated responses such as induction of acyl-CoA oxidase mRNA by PPs are present in the MuSHalph
91 ls from patients with deficiencies of either acyl-CoA oxidase or D-bifunctional protein, the first tw
92 f the genes encoding the peroxisomal enzymes acyl-CoA oxidase (POX1) and medium-chain acyl-CoA synthe
93 l-branched fatty acyl-CoAs by branched-chain acyl-CoA oxidase (pristanoyl-CoA oxidase/trihydroxycopro
94 AtACX2 are members of a family that includes acyl-CoA oxidases specific for shorter-chain acyl-CoAs.
95 arkably, we show that most of the C. elegans acyl-CoA oxidases that participate in ascaroside biosynt
96 ans-double bond by acyl-CoA dehydrogenase or acyl-CoA oxidase, the resultant 2,5, 7-decatrienoyl-CoA
100 Full-length cDNAs coding for two distinct acyl-CoA oxidases were isolated by screening an Arabidop
101 result demonstrated that CrACX2 is a genuine acyl-CoA oxidase, which is responsible for the first ste