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1 een mapped onto the structure of short chain acyl-CoA dehydrogenase.
2 of mitochondrial medium- or very long-chain acyl-CoA dehydrogenase.
3 probe of the active site in the medium chain acyl-CoA dehydrogenase.
4 not require involvement of the medium-chain acyl-CoA dehydrogenase.
5 g thioester polarization in the medium chain acyl-CoA dehydrogenase.
6 such an intermediate in the biogenesis of an acyl-CoA dehydrogenase.
7 ogenase family except for IVD and long-chain acyl-CoA dehydrogenase.
8 The enzyme is a homologue of acyl-CoA dehydrogenase.
9 amate which acts as the base in medium chain acyl-CoA dehydrogenase.
10 not as favorable as that observed with other acyl-CoA dehydrogenases.
11 oxylation reaction which is unique among the acyl-CoA dehydrogenases.
12 and has high levels of homology with various acyl-CoA dehydrogenases.
13 The same mechanism may regulate other acyl-CoA dehydrogenases.
14 e dehydrogenase (PDH), citrate synthase, and acyl-CoA dehydrogenases.
15 ng induces a large enzyme potential shift in acyl-CoA dehydrogenases.
16 FkbI has a similar fold to acyl-CoA dehydrogenases.
17 ehyde dehydrogenase 2 (ALDH2), ATP synthase, acyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, and man
21 ased acetylation of mitochondrial long-chain acyl-CoA dehydrogenase, a known SIRT3 deacetylation targ
24 rally distinct subfamily of acyl coenzyme A (acyl-CoA) dehydrogenase (ACAD) enzymes that are alpha2be
25 nalysis indicated that, like very-long-chain acyl-CoA dehydrogenase, ACAD-9 is a dimer, in contrast t
30 (MCD) belongs to the family of FAD-dependent acyl-CoA dehydrogenase (ACD) and is a key enzyme of the
31 nserved Caenorhabditis elegans gene acdh-11 (acyl-CoA dehydrogenase [ACDH]) facilitates heat adaptati
33 of the enzymes discussed in this review [the acyl-CoA dehydrogenases (ACDs), CDP-6-deoxy-l-threo-d-gl
36 nthesis of the substrates used for measuring acyl-CoA dehydrogenase activities; however, the yields a
37 cid oxidation enzyme integrity, medium-chain acyl-CoA dehydrogenase activity and fat oxidation are el
38 differentiation by attenuating medium-chain acyl-CoA dehydrogenase activity and that inhibition of t
39 confirmed that conversion is performed by an acyl-CoA dehydrogenase and a subsequent hydratase yieldi
41 he powerful epoxyketone residue involving an acyl-CoA dehydrogenase and an unconventional free-standi
42 and PPARalpha-regulated genes (medium chain acyl-CoA dehydrogenase and pyruvate dehydrogenase kinase
43 or medium-chain acyl CoAs, and medium-chain acyl-CoA dehydrogenase and short-chain acyl-CoA dehydrog
44 y to receive electrons from the medium chain acyl-CoA dehydrogenase and the glutaryl-CoA dehydrogenas
45 atty acids by the mitochondrial medium-chain acyl-CoA dehydrogenase and the peroxisomal acyl-CoA oxid
47 a tetrameric enzyme that shares a fold with acyl-CoA dehydrogenases and class D flavin-containing mo
48 is similar to those of previously determined acyl-CoA dehydrogenases and consists of an NH2-terminal
49 7 and Phe-320, which are conserved among all acyl-CoA dehydrogenases and coordinate the enzyme-bound
50 base in medium-chain (MCAD) and short-chain acyl-CoA dehydrogenases and is conserved in all members
51 f these ORFs, two had sequence similarity to acyl-CoA dehydrogenases and polyketide synthases, respec
52 lism (eg, pyruvate dehydrogenase complex and Acyl-CoA dehydrogenase) and enzymes involved in electron
53 s, such as acetyl-CoA synthetase, long-chain acyl-CoA dehydrogenase, and 3-hydroxy-3-methylglutaryl-C
55 ptide, beta myosin heavy chain, medium chain acyl-CoA dehydrogenase, and adrenomedullin correlate equ
56 nge the basal acyl-CoA oxidase, medium chain acyl-CoA dehydrogenase, and malic enzyme mRNA levels.
57 topropionic acid, an inhibitor of long chain acyl-CoA dehydrogenase, and partially inhibited by 2-tet
58 at liver is compared to that of medium chain acyl-CoA dehydrogenase, and the structural basis for the
59 nitine palmitoyl transferase-1, medium-chain acyl-CoA dehydrogenase, and uncoupling protein 3), calci
60 chain acyl-CoA dehydrogenase and short-chain acyl-CoA dehydrogenase are unable to catalyze oxidation
61 y, it appears that ACAD9 and very-long-chain acyl-CoA dehydrogenase are unable to compensate for each
62 lf-reaction of ETF with porcine medium chain acyl-CoA dehydrogenase are unaltered when alphaT244M ETF
67 t is generally held that the active sites of acyl-CoA dehydrogenases are desolvated when substrate bi
69 eview examines the structure of medium chain acyl-CoA dehydrogenase, as a representative of the dehyd
70 ious work demonstrated that the medium-chain acyl-CoA dehydrogenase both bioactivates and is inhibite
71 inactivation of short chain and medium chain acyl-CoA dehydrogenases by this inhibitor and related 2-
72 miting step in the inactivation of the other acyl-CoA dehydrogenases can involve the abstraction of a
73 nes encoding key mitochondrial (medium-chain acyl-CoA dehydrogenase, carnitine palmitoyltransferase I
75 The crystal structure of rat short chain acyl-CoA dehydrogenase complexed with the inhibitor acet
76 Children with medium-chain acyl-coenzyme A (acyl-CoA) dehydrogenase defects can metabolize fatty aci
78 tine are effective in some cases of multiple acyl-CoA dehydrogenase deficiency and primary carnitine
79 ciencies in ETF or ETF-QO result in multiple acyl-CoA dehydrogenase deficiency, a human metabolic dis
81 on transferring flavoprotein and short chain acyl-CoA dehydrogenase-electron transferring flavoprotei
82 sly expressed and purified FadE28-FadE29, an acyl-CoA dehydrogenase encoded by the igr operon, cataly
84 beta-oxidation gene (medium and short chain acyl-CoA dehydrogenase) expression levels remain unchang
85 nases and is conserved in all members of the acyl-CoA dehydrogenase family except for IVD and long-ch
86 atalytically essential glutamate base in the acyl-CoA dehydrogenase family is found either on the loo
90 -CoA dehydrogenase is the only member of the acyl-CoA dehydrogenase family with a cationic residue, A
91 ch is a tyrosine in all other members of the acyl-CoA dehydrogenase family, is important for conferri
92 n example of convergent evolution within the acyl-CoA dehydrogenase family, leading to the independen
95 ely high oxidase activity of the short chain acyl-CoA dehydrogenase from the obligate anaerobe Megasp
96 the targeted inactivation of the long chain acyl CoA dehydrogenase gene (Acadl) are also sensitive t
97 ement (NRRE-1) derived from the medium chain acyl-CoA dehydrogenase gene promoter and nuclear protein
98 susceptibility variations in the short-chain acyl-CoA dehydrogenase gene, and guidelines for the bioc
101 otein complex decreased, indicating that the acyl-CoA dehydrogenases have the ability to compete with
104 on-transfer properties of human medium-chain acyl-CoA dehydrogenase (hwtMCADH) has been studied using
105 gene regulation of ACAD9 and very-long-chain acyl-CoA dehydrogenase identify the presence of two inde
107 ydrogenase is also differentiated from other acyl-CoA dehydrogenases in that the catalytic base must
108 g chain acyl-CoA synthetase, very long chain acyl-CoA dehydrogenase) in livers of the ethanol-fed ani
109 of thioester substrates in the medium-chain acyl-CoA dehydrogenase involves alpha-proton abstraction
114 efines a side of the binding cavity in other acyl-CoA dehydrogenases is replaced by a leucine (Leu-37
115 ase is very similar to those of medium chain acyl-CoA dehydrogenase, isovaleryl-CoA dehydrogenase, an
121 studied mice with a deficiency of long-chain acyl-CoA dehydrogenase (LCAD), a key enzyme in mitochond
122 genase (IVD), and Glu261 in human long chain acyl-CoA dehydrogenase (LCAD), has been suggested to aff
124 ement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr255Glu, hav
125 nheme FeII-dependent halogenase KtzD and the acyl-CoA dehydrogenase-like flavoprotein KtzA, proposed
126 been performed on the wild-type medium-chain acyl-CoA dehydrogenase (MCAD) and two of its mutant form
127 g of octenoyl-CoA to pig kidney medium chain acyl-CoA dehydrogenase (MCAD) by isothermal titration mi
130 ctive site residue, Glu-376, of medium-chain acyl-CoA dehydrogenase (MCAD) has been known to abstract
131 fatty acid synthase (FASN) and medium chain acyl-CoA dehydrogenase (MCAD) protein within the same ce
132 376 --> Asp (E376D) mutation in medium chain acyl-CoA dehydrogenase (MCAD), creates a complementary c
133 identified as Glu376 in porcine medium chain acyl-CoA dehydrogenase (MCAD), Glu254 in human isovalery
134 octynoyl-CoA (inactivator) with medium chain acyl-CoA dehydrogenase (MCAD), were essentially identica
135 in regulating the gene encoding medium-chain acyl-CoA dehydrogenase (MCAD), which catalyzes the initi
137 in the recombinant human liver medium-chain acyl-CoA dehydrogenase (MCAD)-catalyzed reaction, we bec
143 gion of the gene encoding human medium-chain acyl-CoA dehydrogenase (MCAD, which catalyzes a rate-lim
144 ructures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in wh
146 ter introduction of a 2-trans-double bond by acyl-CoA dehydrogenase or acyl-CoA oxidase, the resultan
147 es were reduced (long chain and medium chain acyl-CoA dehydrogenases) or failed to be induced (acyl-C
148 polipoprotein AI, AII, or CIII; medium chain acyl-CoA dehydrogenase; or stearoyl-CoA desaturase mRNAs
149 trate-binding cavity relative to short-chain acyl-CoA dehydrogenase, permitting the optimal binding o
150 synthases (pltB, pltC), an acyl coenzyme A (acyl-CoA) dehydrogenase (pltE), an acyl-CoA synthetase (
151 n the reaction catalyzed by pig medium-chain acyl-CoA dehydrogenase (pMCAD) has been investigated usi
155 CoA dehydrogenase (LCAD) and very long-chain acyl-CoA dehydrogenase revealed that 5-trans-tetradeceno
159 f liver-specific expression of a short-chain acyl-CoA dehydrogenase (SCAD) transgene in the SCAD-defi
161 and E376Q mutants of the human medium chain acyl-CoA dehydrogenase showed that these two active site
162 te of FkbI reveal key differences from other acyl-CoA dehydrogenases, suggesting that FkbI may recogn
163 , which bears superficial resemblance to the acyl-CoA dehydrogenase superfamily of flavoproteins.
168 regulatory circuit involving a heat-induced acyl-CoA dehydrogenase that controls the lipid saturatio
169 drogenase 9 (ACAD9) is a recently identified acyl-CoA dehydrogenase that demonstrates maximum activit
170 longs to an important flavoprotein family of acyl-CoA dehydrogenases that catalyze the alpha,beta-deh
171 detectable semiquinone; however, like other acyl-CoA dehydrogenases, the human enzyme stabilizes an
174 ydrogenase kinase, medium-chain length fatty acyl-CoA dehydrogenase, ubiquinone-cytochrome c reductas
175 the two human genes encoding very long chain acyl-CoA dehydrogenase (VLCAD) and postsynaptic density
179 ents have been found to have very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency, none have bee
182 s highly homologous to human very-long-chain acyl-CoA dehydrogenase was identified by large-scale ran
183 hydrogenase family member, human short chain acyl-CoA dehydrogenase, was incubated with dimethylglyci
184 With the known structure of medium chain acyl-CoA dehydrogenase, we hypothesize a possible struct
185 the fatty acid oxidation enzyme medium-chain acyl-CoA dehydrogenase, we tested whether acetylation-de
186 nitine palmitoyltransferase and medium-chain acyl-CoA dehydrogenase were unaltered with fasting.
187 -CoAs are poor substrates of very long-chain acyl-CoA dehydrogenase when compared with myristoyl-CoA.
188 ETF catalyzed by sarcosine and medium chain acyl-CoA dehydrogenases which reduce the flavin to the s
189 near Acads, a gene encoding the short chain acyl CoA dehydrogenase, which is mutated in BALB/cByJ mi
190 vity and steady-state levels of medium-chain acyl-CoA dehydrogenase, which catalyzes a rate-limiting
191 loning revealed that IBR3 encodes a putative acyl-CoA dehydrogenase with a consensus peroxisomal targ
192 CoA dehydrogenase, and bacterial short chain acyl-CoA dehydrogenase with a three-domain structure com
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