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1 lding domain of a large multienzyme complex, 2-oxoglutarate dehydrogenase.
2 complete in many other anaerobes (absence of 2-oxoglutarate dehydrogenase activity), isotopic labelin
4 acid as a cofactor (pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and glycine decarboxylase).
5 e to succinate and thus functionally replace 2-oxoglutarate dehydrogenase and succinyl-CoA synthetase
6 arboxylic acid (TCA) cycle because they lack 2-oxoglutarate dehydrogenase and thus cannot convert 2-o
10 -dependent E1o component (EC 1.2.4.2) of the 2-oxoglutarate dehydrogenase complex catalyses a rate-li
12 -E2) in 6 of 19 patients (31.6%), and to the 2-oxoglutarate dehydrogenase complex E2 (OGDC-E2) in 1 o
13 2 (BCOADC-E2) in 4 of 49 (8%), to PDC-E2 and 2-oxoglutarate dehydrogenase complex E2 (OGDC-E2) in 9 o
14 t of the gene encoding the E1 subunit of the 2-oxoglutarate dehydrogenase complex in the antisense or
16 cle enzymes, pyruvate dehydrogenase complex, 2-oxoglutarate dehydrogenase complex, NAD-malic enzyme,
23 ith engineered variants of the E2 subunit of 2-oxoglutarate dehydrogenase indicate that binding sites
25 are reported unique properties of the human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc)
26 bunit binding domain from Escherichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed
27 e succinyltransferase (E2o) component of the 2-oxoglutarate dehydrogenase multienzyme complex is comp
28 succinyltransferase polypeptide chain of the 2-oxoglutarate dehydrogenase multienzyme complex of Esch
30 se (E2p, E2o) components of the pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes are s
33 amine diphosphate-dependent Escherichia coli 2-oxoglutarate dehydrogenase, which is a key component o
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