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1 s jannaschii, Bacillus cereus ATCC 10987 and Methylococcus capsulatus.
2 eiphilum (a betaproteobacterium, 4 Mbp), and Methylococcus capsulatus (a gammaproteobacterium, 3.3 Mb
3 rane-bound methane monooxygenase (pMMO) from Methylococcus capsulatus and ammonia monooxygenase (AMO)
5 particulate methane monooxygenase (pMMO) in Methylococcus capsulatus Bath was assessed by analysis o
6 associated methane monooxygenase (pMMO) from Methylococcus capsulatus Bath was isolated by ion-exchan
13 Soluble methane mono-oxygenase (sMMO) of Methylococcus capsulatus (Bath) catalyses the O2-depende
14 he soluble methane monooxygenase system from Methylococcus capsulatus (Bath) catalyzes the oxidation
15 Soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) catalyzes the selective
16 determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibr
17 dical clock substrate, catalyzed by MMO from Methylococcus capsulatus (Bath) gave only cubylmethanol
18 lated proteins have been identified, and the Methylococcus capsulatus (Bath) genome has been sequence
19 ins from Methylosinus trichosporium OB3b and Methylococcus capsulatus (Bath) have a similar secondary
20 ponent of soluble methane monooxygenase from Methylococcus capsulatus (Bath) have been thoroughly inv
21 ethane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) in frozen 4:1 buffer/gly
22 report here crystal structures of MMOH from Methylococcus capsulatus (Bath) in the diiron(II), diiro
23 The soluble methane monooxygenase system of Methylococcus capsulatus (Bath) includes three protein c
24 he soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a multicomponent enzy
25 Soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a three-component enz
26 O; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enz
28 activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibit
31 the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 A
33 e methane monooxygenase (sMMO) isolated from Methylococcus capsulatus (Bath) utilizes a carboxylate-b
34 Several strains of methanotrophs, including Methylococcus capsulatus (Bath), express a membrane-boun
35 s, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (
36 s, soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (
42 nthetic pathway were in the proteobacterium, Methylococcus capsulatus, in which sterol biosynthesis i
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