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1 an unbiased proteomic search, we identified mitochondrial aldehyde dehydrogenase 2 (ALDH2) as an enz
2 nce through pharmacological re-activation of mitochondrial aldehyde dehydrogenase 2 (ALDH2) using Ald
5 estored I/R-induced suppressed activities of mitochondrial aldehyde dehydrogenase, 3-ketoacyl-CoA thi
13 % of the Oriental population have less liver mitochondrial aldehyde dehydrogenase (ALDH2) activity th
15 replacement using the crystal structure of a mitochondrial aldehyde dehydrogenase (ALDH2) as a model.
17 2 gene encoding the inactive variant form of mitochondrial aldehyde dehydrogenase (ALDH2) protects ne
18 caused the rate-limiting step of human liver mitochondrial aldehyde dehydrogenase (ALDH2) to change f
19 ine nucleophilic attack on propanal in human mitochondrial aldehyde dehydrogenase (ALDH2) yielded an
21 mbinant human cytosolic (ALDH1, high Km) and mitochondrial aldehyde dehydrogenase (ALDH2, low Km) in
22 mutation in the gene encoding for the liver mitochondrial aldehyde dehydrogenase (ALDH2-2), present
23 essing factors include overexpression of the mitochondrial aldehyde dehydrogenase gene ALD5 or disrup
24 wo structures of a Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase in binary complexes
25 enzymes, cytosolic alcohol dehydrogenase and mitochondrial aldehyde dehydrogenase, in part determine
30 The low-activity Oriental variant of human mitochondrial aldehyde dehydrogenase possesses a lysine
31 with the effect of Mg2+ ions on human liver mitochondrial aldehyde dehydrogenase revealed that the b