ライフサイエンスコーパス: adenylyl imidodiphosphate

1 ve supercoils with a nonhydrolyzable analog, adenylyl imidodiphosphate.

2 orted by the nonhydrolyzable ATP analogue 5'-adenylyl imidodiphosphate.

3 tylase (L2) determined with or without bound adenylyl imidodiphosphate.

4 to a closed conformation upon the binding of adenylyl-imidodiphosphate.

5 e of substrate analogs beryllium fluoride or adenylyl-imidodiphosphate.

6 Saturation of the ATP binding site with adenylyl imidodiphosphate afforded protection against ph

7 angstrom) and in complex with verapamil and adenylyl imidodiphosphate (AMP-PNP) (3.2 angstrom).

8 The inhibitor adenylyl imidodiphosphate (AMP-PNP) induces stochastic p

9 t AMP, ADP and the non-hydrolysable analogue adenylyl imidodiphosphate (AMP-PNP) partially substitute

10 rylation, since the nonhydrolyzable analogue adenylyl imidodiphosphate (AMP-PNP) protects equally wel

11 itions, ATP is two times more effective than adenylyl imidodiphosphate (AMP-PNP), a hydrolysis-resist

12 Delay of closing in wild type by adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable

13 ee Ca(2+)) as did replacing pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable

14 egment homogenates with ATP or its analogue, adenylyl imidodiphosphate (AMP-PNP), is required for the

15 f the minus-end vesicle motor followed by 5'-adenylyl imidodiphosphate (AMP-PNP)-induced microtubule

16 NA, we demonstrate here that nonhydrolyzable adenylyl-imidodiphosphate (AMP-PNP) can be used to prelo

17 In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable A

18 by intracellular ATP, as well as GTP and 5'-adenylyl-imidodiphosphate (AMP-PNP), were accompanied by

19 sine 5'-O-(thiotriphosphate) (ATPgammaS) and adenylyl-imidodiphosphate (AMP-PNP).

20 monophosphate (AMP), and of an ATP analogue, adenylyl imidodiphosphate (AMPPNP), bound to Escherichia

21 e conformation of enzyme-bound AdoMet and 5'-adenylyl imidodiphosphate (AMPPNP).

22 resence of the nonhydrolyzable ATP analogues adenylyl-imidodiphosphate and adenosine 5'-O-thiotriphos

23 n on the strong binding of S-1.MgAMP-PNP (5'-adenylyl imidodiphosphate) and on the weak binding of S-

24 with 1 mM of the kinesin inhibitor AMP-PNP (adenylyl-imidodiphosphate) and by anti-kinesin antibody

25 While ATP or AMP-PNP (adenylyl-imidodiphosphate) binding to wild-type myosin s

26 ase was confirmed by the presence of four 5'-adenylyl-imidodiphosphate-binding sites (K(D) = 4.1 x 10

27 nting analysis of the intact SGS revealed an adenylyl imidodiphosphate-dependent change in protection

28 for myosin II ATP-Mg(2+) = ATP = AMP-PNP (5'-adenylyl imidodiphosphate) > pyrophosphate = tripolyphos

29 n occurred even in the presence of Ca(2+) or adenylyl-imidodiphosphate, indicating that the mechanism

30 NeqAB in complex with nucleotides, ADP, and adenylyl-imidodiphosphate (non-hydrolysable analog of AT

31 ubstituting the nonhydrolyzable ATP analog 5-adenylyl-imidodiphosphate or UTP for ATP in the pipette.

32 analogs 5'-adenylyl methylenediphosphate, 5'-adenylyl imidodiphosphate, or 5'-adenylyl-O-(3-thiotriph

33 d by changing CFTR activity with vanadate or adenylyl-imidodiphosphate, or by introducing the Walker

34 Subsequent introduction of adenylyl imidodiphosphate precipitated a burst of large-

35 lographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP sta

36 esence of the ATP phosphorylation antagonist adenylyl-imidodiphosphate, with an ED50 of approximately