ライフサイエンスコーパス: antimonite

コーパス検索結果 (１語後でソート)

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1 but not arsR2, are inducible by arsenite and antimonite.

2 teraction between A1 and A2 brought about by antimonite.

3 sAB pump provides resistance to arsenite and antimonite.

4 ying out unisite catalysis in the absence of antimonite.

5 , is allosterically activated by arsenite or antimonite.

6 n A2 both in the absence and the presence of antimonite.

7 activity is activated by either arsenite or antimonite.

8 nsport of trivalent metalloids, arsenite and antimonite.

9 ss of vectorial translocation of arsenite or antimonite across the membrane.

10 Arsenite or antimonite allosterically activates the ArsA ATPase acti

11 However, upon incubation with ATP and antimonite, almost complete protection from trypsin was

12 cedents are for such sites to sense arsenite/antimonite (alpha3) and zinc (alpha5).

13 litate uptake of the metalloids arsenite and antimonite, and the Escherichia coli homolog, GlpF, faci

14 Thus antimonite binding may act as a switch in regulating ATP

15 ted in increased sensitivity to arsenite and antimonite but not arsenate.

16 exhibits increased tolerance to arsenite and antimonite compared to a wild-type strain.

17 ), which was related to an increase in Vmax; antimonite did not stimulate activity.

18 Antimonite elicits its effects by sequestering ArsA in t

19 um sp. strain NRC-1 contains an arsenite and antimonite extrusion system with significant differences

20 finity and it requires the allosteric ligand antimonite for binding ATP.

21 ace complex as observed for arsenic(III) and antimonite(III) might be due to the relatively small siz

22 FSBA together mimicked the effect of ATP and antimonite, implying that this fully protected conformat

23 m useful in the detection of arsenite and/or antimonite in a variety of samples.

24 l was more effective than either arsenite or antimonite in dissociating the repressor-promoter comple

25 or genes responsible for the accumulation of antimonite in Escherichia coli, TnphoA was used to creat

26 TP-dependent extrusion pump for arsenite and antimonite in Escherichia coli.

27 ective as or more effective than arsenite or antimonite in induction in vivo.

28 le A2 is recruited in multisite catalysis by antimonite in the presence of a functional A1 domain.

29 is known about the transport of arsenite and antimonite into microbes, but the identities of mammalia

30 nity ATP site, whereas the allosteric ligand antimonite is required to allow ATP binding to A2, resul

31 s (MRP1 substrates) as well as the metalloid antimonite (K(i) 2.8 microM).

32 This study shows that on addition of antimonite, much more adduct is formed.

33 On addition of antimonite, multisite catalysis involving both A1 and A2

34 ce of alternative electron acceptors such as antimonite, nitrate, selenate, and sulfate.

35 The arsenite and antimonite resistance elements were shown to be regulate

36 f random insertional mutants, from which one antimonite-resistant mutant was isolated.

37 As(III) and antimonite (Sb(III)) resistance and accumulation studies

38 spiration, resulting in the precipitation of antimonite [Sb(III)] as microcrystals of antimony trioxi

39 LmAQP1, is responsible for the transport of antimonite [Sb(III)], an activated form of Pentostam or

40 P1) adventitiously facilitates the uptake of antimonite [Sb(III)], an active form of Pentostam(R) or

41 In this study, antimony species such as antimonite [Sb(III)], antimonate [Sb(V)] and trimethyl a

42 trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)].

43 nd acr3-2 are required for maximal AsIII and antimonite (SbIII) resistance, but acr3-1 (negatively re

44 ied as involved in induction by arsenite and antimonite, suggesting coordination between As(III) and

45 sense the model target analytes arsenite and antimonite, the target analytes in this study.

46 e regulatory protein, ArsR, for arsenite and antimonite to produce the reporter protein, which in thi

47 ries out unisite catalysis in the absence of antimonite, while A2 is recruited in multisite catalysis

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