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1 bunit of the pyruvate dehydrogenase complex, dihydrolipoamide acetyltransferase.
2 lowed by reductive acetyl transfer to lipoyl-dihydrolipoamide acetyltransferase.
3 nding affinity for the PDH-binding domain of dihydrolipoamide acetyltransferase as measured by surfac
4 e peripheral subunit-binding domain from the dihydrolipoamide acetyltransferase component of the Baci
5 , as well as in reductive acetylation of the dihydrolipoamide acetyltransferase component.
6 ocytes resulted in deregulated expression of dihydrolipoamide acetyltransferase (Dlat), a gene encodi
7 ion of Th17 cells was dependent on bacterial dihydrolipoamide acetyltransferase (DlaT), a major prote
8 nding protein associated with the 60-subunit dihydrolipoamide acetyltransferase (E(2)) core provides
9 antigen pyruvate dehydrogenase complex (PDC) dihydrolipoamide acetyltransferase (E2) bind to the plas
10 d in 1 M NaCl and 0.1 M glycine into a large dihydrolipoamide acetyltransferase (E2) complex and smal
11 dehydrogenase-binding protein (E3BP) and the dihydrolipoamide acetyltransferase (E2) component enzyme
12 e peripheral subunit-binding domain from the dihydrolipoamide acetyltransferase (E2) component of the
13 pyruvate decarboxylase (E1alpha and E1beta), dihydrolipoamide acetyltransferase (E2), and dihydrolipo
14 ach of the 12 pentagonal faces of the 60-mer dihydrolipoamide acetyltransferase (E2).
15 lytic domain from the Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2pCD).
16 py of the Saccharomyces cerevisiae truncated dihydrolipoamide acetyltransferase (tE(2)) component of
17  the structures of the truncated 60-mer core dihydrolipoamide acetyltransferase (tE2) of the Saccharo
18          Here we present evidence that Lat1 (dihydrolipoamide acetyltransferase), the E2 component of
19                                              Dihydrolipoamide acetyltransferase, the E2 component of
20                                              Dihydrolipoamide acetyltransferase, the E2 of the PDC, h
21                    The maximum activation by dihydrolipoamide acetyltransferase was demonstrated by P
22  acetylation state of the lipoyl moieties of dihydrolipoamide acetyltransferase with the maximum stim

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