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1 activity is activated by either arsenite or antimonite.
2 nsport of trivalent metalloids, arsenite and antimonite.
3 but not arsR2, are inducible by arsenite and antimonite.
4 teraction between A1 and A2 brought about by antimonite.
5 sAB pump provides resistance to arsenite and antimonite.
6 ying out unisite catalysis in the absence of antimonite.
7 , is allosterically activated by arsenite or antimonite.
8 n A2 both in the absence and the presence of antimonite.
14 litate uptake of the metalloids arsenite and antimonite, and the Escherichia coli homolog, GlpF, faci
18 peciation was dominated by antimonate, while antimonite concentrations were low, further supporting o
19 ime for efficient reduction of antimonate to antimonite currently hinders higher Sb removal in the st
22 um sp. strain NRC-1 contains an arsenite and antimonite extrusion system with significant differences
24 ace complex as observed for arsenic(III) and antimonite(III) might be due to the relatively small siz
25 FSBA together mimicked the effect of ATP and antimonite, implying that this fully protected conformat
27 uman epidermal keratinocytes to arsenite and antimonite in contrast to comparisons of arsenite with o
28 l was more effective than either arsenite or antimonite in dissociating the repressor-promoter comple
29 or genes responsible for the accumulation of antimonite in Escherichia coli, TnphoA was used to creat
32 le A2 is recruited in multisite catalysis by antimonite in the presence of a functional A1 domain.
33 parallels between responses to arsenite and antimonite indicate the skin carcinogenic risk of exposu
34 is known about the transport of arsenite and antimonite into microbes, but the identities of mammalia
35 nity ATP site, whereas the allosteric ligand antimonite is required to allow ATP binding to A2, resul
44 spiration, resulting in the precipitation of antimonite [Sb(III)] as microcrystals of antimony trioxi
45 LmAQP1, is responsible for the transport of antimonite [Sb(III)], an activated form of Pentostam or
46 P1) adventitiously facilitates the uptake of antimonite [Sb(III)], an active form of Pentostam(R) or
49 nd acr3-2 are required for maximal AsIII and antimonite (SbIII) resistance, but acr3-1 (negatively re
50 ied as involved in induction by arsenite and antimonite, suggesting coordination between As(III) and
52 e regulatory protein, ArsR, for arsenite and antimonite to produce the reporter protein, which in thi
56 t inorganic arsenic (arsenite) and antimony (antimonite), we hypothesized that common intracellular t
57 ries out unisite catalysis in the absence of antimonite, while A2 is recruited in multisite catalysis