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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 e of substrate analogs beryllium fluoride or adenylyl-imidodiphosphate.
7 t AMP, ADP and the non-hydrolysable analogue adenylyl imidodiphosphate (AMP-PNP) partially substitute
8 rylation, since the nonhydrolyzable analogue adenylyl imidodiphosphate (AMP-PNP) protects equally wel
9 itions, ATP is two times more effective than adenylyl imidodiphosphate (AMP-PNP), a hydrolysis-resist
11 ee Ca(2+)) as did replacing pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable
12 egment homogenates with ATP or its analogue, adenylyl imidodiphosphate (AMP-PNP), is required for the
13 f the minus-end vesicle motor followed by 5'-adenylyl imidodiphosphate (AMP-PNP)-induced microtubule
15 by intracellular ATP, as well as GTP and 5'-adenylyl-imidodiphosphate (AMP-PNP), were accompanied by
17 monophosphate (AMP), and of an ATP analogue, adenylyl imidodiphosphate (AMPPNP), bound to Escherichia
19 resence of the nonhydrolyzable ATP analogues adenylyl-imidodiphosphate and adenosine 5'-O-thiotriphos
20 n on the strong binding of S-1.MgAMP-PNP (5'-adenylyl imidodiphosphate) and on the weak binding of S-
21 with 1 mM of the kinesin inhibitor AMP-PNP (adenylyl-imidodiphosphate) and by anti-kinesin antibody
23 ase was confirmed by the presence of four 5'-adenylyl-imidodiphosphate-binding sites (K(D) = 4.1 x 10
24 nting analysis of the intact SGS revealed an adenylyl imidodiphosphate-dependent change in protection
25 for myosin II ATP-Mg(2+) = ATP = AMP-PNP (5'-adenylyl imidodiphosphate) > pyrophosphate = tripolyphos
26 n occurred even in the presence of Ca(2+) or adenylyl-imidodiphosphate, indicating that the mechanism
27 NeqAB in complex with nucleotides, ADP, and adenylyl-imidodiphosphate (non-hydrolysable analog of AT
28 ubstituting the nonhydrolyzable ATP analog 5-adenylyl-imidodiphosphate or UTP for ATP in the pipette.
29 analogs 5'-adenylyl methylenediphosphate, 5'-adenylyl imidodiphosphate, or 5'-adenylyl-O-(3-thiotriph
30 d by changing CFTR activity with vanadate or adenylyl-imidodiphosphate, or by introducing the Walker
32 lographic structures; it is closed in the 5'-adenylyl-imidodiphosphate state, but open in the ADP sta
33 esence of the ATP phosphorylation antagonist adenylyl-imidodiphosphate, with an ED50 of approximately
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