ライフサイエンスコーパス: fluoroaluminate

コーパス検索結果 (１語後でソート)

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1 Supporting data were obtained using MgIDP-fluoroaluminate.

2 -) (FPBA = tris(2,2',2' '-nonafluorobiphenyl)fluoroaluminate) (4), [rac-Et(Indenyl)(2)ZrMe](+)[FPBA](

3 Together, GDP and fluoroaluminate (AlF4-) form a transition state analog o

4 In the presence of fluoroaluminate and Ca(2+), ADP (or AMP-PCP) favors form

5 ization was measured using phosphate analogs fluoroaluminate and fluoroscandium.

6 and Lys(684) participate in stabilization of fluoroaluminate and Mg(2+) at the phosphorylation site.

7 tion state formation by measurement of MgADP-fluoroaluminate binding.

8 , phosphate accelerated formation of the ADP-fluoroaluminate complex 3-fold.

9 Sulfite accelerated formation of the ADP-fluoroaluminate complex 9-fold when 200 microM ADP plus

10 n the MF(1) crystal structure with the MgADP-fluoroaluminate complex bound to two catalytic sites, th

11 ADP-fluoroaluminate complex formation is restricted to a sin

12 ng MgADP in a single catalytic site, the ADP-fluoroaluminate complex formed at least 10-fold more slo

13 The rate of formation of the ADP-fluoroaluminate complex in (alpha Y300C)3 beta 3 gamma i

14 The results indicate that the MgADP-fluoroaluminate complex is a transition state analog and

15 auses slow, complete inactivation as the ADP-fluoroaluminate complex is formed.

16 drolyzable GTP analog, and the GDP.magnesium fluoroaluminate complex provide evidence that the Mg(2+)

17 at the enhanced rate of formation of the ADP-fluoroaluminate complex reflects augmented cooperativity

18 a subcomplex does not form an inhibitory ADP-fluoroaluminate complex under any of the conditions exam

19 F-, phosphate inhibits formation of the ADP-fluoroaluminate complex.

20 wild-type are similar, the mutant forms ADP-fluoroaluminate complexes 7 times faster than wild-type

21 ter incubation with excess ADP and Mg2+, ADP-fluoroaluminate complexes are formed in three catalytic

22 Al3+, F-, Mg2+, and excess ADP occurs as ADP-fluoroaluminate complexes form in two catalytic sites.

23 r hydrolyzing ATP and forming inhibitory ADP-fluoroaluminate complexes in catalytic sites.

24 nce spectrum observed after entrapping MgADP-fluoroaluminate complexes in two catalytic sites of the

25 vely, abolishes cooperative formation of ADP-fluoroaluminate complexes in two catalytic sites.

26 rimental observations of fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase (be

27 wever, protein refolding reactions using ADP-fluoroaluminate complexes, or single-ring GroEL and GroE

28 Fluoroaluminate forms a complex at the catalytic site yi

29 Fluoroaluminate induced a very large increase in MgADP b

30 rmal transition state formation as judged by fluoroaluminate-induced MgADP binding affinity changes,

31 beta-Glu-181 to Gln abolished the effects of fluoroaluminate on MgADP binding.

32 ed by 1300-fold and was not inhibited by ADP-fluoroaluminate or ADP-fluoroscandium.

33 ATPase of mutants was not inhibited by MgADP-fluoroaluminate or MgADP-fluoroscandium, showing the Arg

34 was slightly inhibited by MgADP-azide, MgADP-fluoroaluminate, or MgADP-fluoroscandium, in contrast to

35 m mutant betaY331W was potently inhibited by fluoroaluminate plus MgADP but not by MgADP alone.

36 f [125I]IAAP binding to vanadate-trapped (or fluoroaluminate-trapped) Pgp without any further nucleot

37 ADP-fluoroaluminate was more inhibitory than in wild-type, b

38 omplex of G alpha(i1) with GDP and magnesium fluoroaluminate, whereas the K180P mutation destabilizes

39 nd G(i) family G proteins in the presence of fluoroaluminate, which mimics the presence of the termin

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