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1 easurements for the analogous enzyme system, dopamine beta-monooxygenase.
2 e PHM structures can be directly extended to dopamine beta-monooxygenase.
3 lycine alpha-hydroxylating monooxygenase and dopamine beta-monooxygenase.
4 the role of the noncoupled nature of PHM and dopamine beta-monooxygenase active sites, as compared to
5  in the H-abstraction reactions catalyzed by dopamine beta-monooxygenase and peptidylglycine alpha-hy
6 rison with the homologous mammalian enzymes, dopamine beta-monooxygenase and peptidylglycine alpha-hy
7 er copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomim
8                The activation of dioxygen by dopamine beta-monooxygenase (DbetaM) and peptidylglycine
9  alpha-hydroxylating monooxygenase (PHM) and dopamine beta-monooxygenase (DbetaM) are copper-dependen
10  alpha-hydroxylating monooxygenase (PHM) and dopamine beta-monooxygenase (DbetaM) are homologous copp
11 trix to provide reducing equivalents for the dopamine beta-monooxygenase (DbetaM) reaction.
12          The interactions of reductants with dopamine beta-monooxygenase (DbetaM) were examined using
13 PTT) is a potent tight-binding inhibitor for dopamine beta-monooxygenase (DbetaM) with a dissociation
14 ously proposed for the copper monooxygenase, dopamine beta-monooxygenase (DbetaM), involve the accumu
15 The electronic and steric constraints of the dopamine beta-monooxygenase (DbetaM; E.C. 1.14.17.1) act
16         Previous studies have shown that the dopamine beta-monooxygenase (DbetaM; E.C. 1.14.17.1)/1-(
17 viously characterized as potent irreversible dopamine-beta-monooxygenase (DbetaM) and monoamine oxida
18 he nature of coupling between the uptake and dopamine-beta-monooxygenase (DbetaM) catalyzed hydroxyla
19 he copper monooxygenase family that includes dopamine beta-monooxygenase (DBM) and peptidylglycine al
20                                              Dopamine beta-monooxygenase (DBM) and peptidylglycine al
21                                Expression of dopamine beta-monooxygenase (DBM), the enzyme that conve
22 to a well-characterized suicide inhibitor of dopamine beta-monooxygenase (EC 1.14.17.1) where the pro
23 ate-dependent copper monooxygenases, PAM and dopamine-beta-monooxygenase, established that these comp
24 ooxygenase (TbetaM), the insect homologue of dopamine beta-monooxygenase, is a neuroregulatory enzyme
25 , reflecting deficiency of the copper enzyme dopamine beta-monooxygenase, is arguably the most import
26 nce for the reactive superoxo species in the dopamine beta-monooxygenase/peptidylglycine alpha-hydrox
27 ycine max) cytochrome b561 associated with a dopamine beta-monooxygenase redox domain (CYBDOM), which
28 lycine alpha-hydroxylating monooxygenase and dopamine beta-monooxygenase with substrates of comparabl

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