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1 lpha,17alpha-[(R)-(1'-alpha-furylmethylidene)dioxy]-19-norpreg n-4-ene-3,20-dione ((18)F-FFNP), as we
2 arbonyl)amino-5-bromo-2,3-(dimethylmethylene)dioxy -4-hydroxymethylcyclopentane, was synthesized star
4 st 1-(4-amino-phenyl)-4-methyl-7,8-methylene-dioxy-5H-2, 3-benzodiazepine (GYKI 52466), but only mode
6 igand mutations thus destabilize the ferrous-dioxy complex and uncouple the reduction of O2 from oxid
9 lexes to O2 does not give detectable ferrous-dioxy complexes and leads to the uncoupled reduction of
12 dihydrobiopterin-containing iNOSoxy, ferrous-dioxy decay was much slower and was not associated with
13 kinetic and quantitative links among ferrous-dioxy disappearance, H(4)B oxidation, and Arg hydroxylat
14 synthesis and establish that (1) the ferrous-dioxy enzyme reacts quantitatively with NOHA but not wit
15 NOS, the beginning ferrous enzyme, a ferrous-dioxy (Fe(II)O(2)) intermediate, Fe(III)NO, and an endin
17 Optical spectra of the ferric, ferrous, heme-dioxy, ferrous-NO, ferric-NO, and ferrous-CO forms of ea
18 nitric-oxide synthesis, we followed ferrous-dioxy heme (Fe(II)O(2)) formation and disappearance, H(4
19 coupled to disappearance of an initial heme-dioxy intermediate and to Arg hydroxylation in a single
27 y H(4)B transfers an electron to the ferrous-dioxy intermediate to enable the formation of a heme-bas
28 hat H4B first provides an electron to a heme-dioxy intermediate, and then the H4B radical receives an
29 on transfer between H(4)B and an enzyme heme-dioxy intermediate, and this in turn alters the kinetics
32 hase of a hemicarcerand with four butane-1,4-dioxy linker groups (5) in C(6)D(5)CD(3) at 77 K yields
34 the biosynthetic reaction, implicate ferrous-dioxy nNOS as a critical reactant in that step, and elim
37 conclude the following: (1) The rate of heme-dioxy reduction is linked to pterin radical formation an
38 methyl-3,3'-di-tert-butyl-1,1'-biphenyl-2,2'-dioxy [(S)-BIPHEN] as a chiral auxiliary and screened in
39 o ferrous eNOS generated a transient ferrous dioxy species (Soret peak at 427 nm) whose formation and
40 ly with the disappearance of the enzyme heme-dioxy species and with the formation of a tetrahydrobiop
42 ctivity toward substrate, but decreases heme-dioxy stability and lowers the driving force for heme re
43 ctivities from 20:1 to 82:1 favoring the 1,3-dioxy-substituted products have been achieved using Me2S
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