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1 is was attributed to inhibition of the alpha-ketoglutarate dehydrogenase complex.
2 sferase, alanine aminotransferase, and alpha-ketoglutarate dehydrogenase complex.
3 ration by reversible inhibition of the alpha-ketoglutarate dehydrogenase complex.
4 A to the reduction of NAD(+) using the alpha-ketoglutarate dehydrogenase complex.
5 f central metabolism, the pyruvate and alpha-ketoglutarate dehydrogenase complexes.
6 ored full activity to the pyruvate and alpha-ketoglutarate dehydrogenase complexes.
7 nent of the pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase complexes.
9 target DLST-the E2 subcomponent of the alpha-ketoglutarate dehydrogenase complex, a rate-controlling
10 ipoamide dehydrogenase subunits of the alpha-ketoglutarate dehydrogenase complex (alphaKGDH), a key r
12 mide dehydrogenase, a component of the alpha-ketoglutarate dehydrogenase complex and two other mitoch
13 e to supply alpha-ketoglutarate to the alpha-ketoglutarate dehydrogenase complex and would, in part,
15 , we demonstrate that the pyruvate and alpha-ketoglutarate dehydrogenase complexes directly catalyze
16 hyl transferase, and components of the alpha-ketoglutarate dehydrogenase complex in conjunction with
17 absolute content of complex I, as well as a-ketoglutarate dehydrogenase complex, in any preparation.
18 ase complex (OGHDC) (also known as the alpha-ketoglutarate dehydrogenase complex) is a rate-limiting
20 24 h, resulted in a pronounced loss of alpha-ketoglutarate dehydrogenase complex (KGDHC) activity in
23 ain metabolism and the activity of the alpha-ketoglutarate dehydrogenase complex (KGDHC), a mitochond
26 ity of a key mitochondrial enzyme, the alpha-ketoglutarate dehydrogenase complex (KGDHC), declines in
29 nslational lipoylation of pyruvate and alpha-ketoglutarate dehydrogenase complexes, resulting in dimi
31 ThPP levels causes dysfunction of the alpha-ketoglutarate dehydrogenase complex, which explains the