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1 The product is a novel 2-oxo acid.
2 tionally regulated by redox mechanisms and 2-oxo acids.
3 that is activated by redox mechanisms and 2-oxo acids.
4 dues, CysI and CysII, are both involved in 2-oxo acid activation, with AOX1A activity being more incr
6 H2(18)O, we established synthesis of the C8-oxo acid and C12 aldehyde with the retention of the hydr
7 anion formed during decarboxylation of the 2-oxo acid and E1beta His128 to provide the proton require
8 acid substrate, (b) decarboxylation of the 2-oxo acid and reductive acetylation of the tethered lipoy
9 e is an acetylene analogue of a variety of 2-oxo acids and as such may have general utility as an inh
10 , Leu and Ile as well as the corresponding 2-oxo acids but also transaminates Met and its cognate ket
11 ich lack the ketolytic enzyme succinyl-CoA:3-oxo-acid CoA-transferase (SCOT), to demonstrate that ket
14 fference in skeletal muscle branched-chain 2-oxo acid dehydrogenase (BCOADH) activity between groups.
15 irulence was not associated with a loss of 2-oxo acid dehydrogenase activity, as the wild-type pneumo
16 rogenase complex (PDC), the branched chain 2-oxo acid dehydrogenase complex (BCOADC), and the 2-oxogl
17 ngly, the E2 subunit of the branched chain 2-oxo acid dehydrogenase complex also remained intact in t
18 plex, the E2 subunit of the branched chain 2-oxo acid dehydrogenase complex, the E2 subunit of the ox
20 dihydrolipoyl acyltransferase component of 2-oxo acid dehydrogenase complexes and will assist in furt
21 he two major classes of the superfamily of 2-oxo acid dehydrogenase complexes with different assembly
23 to the linker regions in the E2 chains of 2-oxo acid dehydrogenase complexes, and it is likely this
24 ) hetero-tetrameric E1 components of other 2-oxo acid dehydrogenase complexes, except that in E1o, th
25 en identified as subunits of the following 2-oxo acid dehydrogenase complexes: the pyruvate dehydroge
26 their pendant lipoyl groups in the parent 2-oxo acid dehydrogenase complexes; an important aspect of
29 sferase components (E2) from the family of 2-oxo acid dehydrogenase multienzyme complexes form large
32 ate dehydrogenase (PDC-E2), branched-chain 2-oxo-acid dehydrogenase (BCOADC-E2), and 2-oxo-glutarate
33 enase complex (PDC-E2), the branched-chain 2-oxo-acid dehydrogenase complex (BCOADC-E2), and the 2-ox
34 9 (45%), against PDC-E2 and branched-chain 2-oxo-acid dehydrogenase complex E2 (BCOADC-E2) in 4 of 49
35 19 patients (78.9%), to the branched-chain 2-oxo-acid dehydrogenase complex E2 (BCOADC-E2) in 6 of 19
36 re-absorption of the IgA using recombinant 2-oxo-acid dehydrogenase complex significantly diminished
38 utoantigens belong to E2 components of the 2-oxo-acid dehydrogenase family of mitochondrially located
39 equenced, and identified as members of the 2-oxo-acid dehydrogenase pathway, including the E2 subunit
40 of pyruvate dehydrogenase, branched chain 2-oxo-acid dehydrogenase, and 2-oxo-glutarate dehydrogenas
41 ainst PDC-E2, E2 subunit of branched chain 2-oxo-acid dehydrogenase, and E2 subunit of 2-oxoglutarate
42 octanoyl-ACP) to the lipoyl domains of the 2-oxo acid dehydrogenases and the H subunit of glycine cle
44 also catalyze the slow decarboxylation of 2-oxo acids) enabled the observation of the substrate-thia
47 herefore, we propose a mechanism whereby the oxo acids generated after oxidation of the cysteine thio
48 he direct decarboxylative arylation of alpha-oxo acids has been achieved by synergistic visible-light
49 Importantly, we detected the signature 2-oxo-acid N-terminal peptide in tryptic digests of bronch
50 alkyl ketone architectures from simple alpha-oxo acid precursors via an acyl radical intermediate.
51 o small amounts of additional amino acid and oxo acid products through partitions of the main reactio
52 known to be involved in regulation by the 2-oxo acids pyruvate and glyoxylate) and propose that this
53 residues are involved in: (a) binding the 2-oxo acid substrate, (b) decarboxylation of the 2-oxo aci
55 y involved in the three-step conversion of 2-oxo acids to their respective acyl-CoA derivatives, but
56 us epidermidis reduces a broad spectrum of 2-oxo acids, which are difficult substrates for transition
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