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1 nding to the inner lipoyl domain (L2) of the dihydrolipoyl acetyltransferase.
2 ylation of the lipoyl domain (E2plip) of the dihydrolipoyl acetyltransferase component of the pyruvat
4 kinase 2 (PDK2) activity is enhanced by the dihydrolipoyl acetyltransferase core (E2 60mer) that bin
5 the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase E2 component are identic
8 n procedure is applied to image pairs of the dihydrolipoyl acetyltransferase (E2) catalytic core of t
9 tylation of the lipoyl group attached to the dihydrolipoyl acetyltransferase (E2) component involves
12 r+ peripheral subunit-binding domain) of the dihydrolipoyl acetyltransferase (E2) component of the py
13 etylated forms of the lipoyl moieties of the dihydrolipoyl acetyltransferase (E2) component through u
14 (E1p) component and the lipoyl domain of the dihydrolipoyl acetyltransferase (E2) component was inves
19 subcomplex comprising the 60-mer icosahedral dihydrolipoyl acetyltransferase (E2) decorated with 60 c
21 ted how binding to the lipoyl domains of the dihydrolipoyl acetyltransferase (E2) produces the predom
22 h is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to
23 ase fused to the inner lipoyl domain (L2) of dihydrolipoyl acetyltransferase (E2)) dimers was enhance
24 t (PDP1c) to the L2 (inner lipoyl) domain of dihydrolipoyl acetyltransferase (E2), which is also inte
26 structural core formed of multiple copies of dihydrolipoyl acetyltransferase (E2p), which exhibits th
27 peripheral subunit-binding domain (PSBD) of dihydrolipoyl acetyltransferase in the pyruvate dehydrog
29 nsertion into the gene for the plastidic E2 (dihydrolipoyl acetyltransferase) subunit, plE2, of the c
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