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1  the P3 -1-(2-nitrophenyl) ester of ATP (NPE-caged ATP).
2 m infrared spectroscopy and UV photolysis of caged ATP.
3 ude similar to those following photolysis of caged ATP.
4 tension transients elicited by photolysis of caged ATP.
5 n in a femtoliter volume by rapid release of caged ATP.
6 traction is initiated by a sudden release of caged ATP.
7 75 mg/ml was incubated with dimethoxybenzoin-caged ATP.
8 estored or stimulated by flash photolysis of caged ATP.
9 tivity was not influenced by the addition of caged-ATP.
10 3)-1-(2 nitrophenyl) ethyl ester of ATP (NPE-caged ATP), and time-resolved phosphate (P(i)) release w
11 re determined with laser flash photolysis of caged ATP (cATP) in alpha-toxin-permeabilized tonic, rab
12                      Following photolysis of caged ATP, cells without calponin that contained a nonph
13                         On photolysis of NPE-caged ATP in the absence of Ca2+ the ATPase activity was
14                         On photolysis of NPE-caged ATP in the presence of Ca2+ at 20 degrees C, the f
15 s were activated from rigor by photolysis of caged ATP in the presence of Ca2+.
16 ith transients elicited by the photolysis of caged ATP in the presence of saturating Ca2+ greatly pre
17  P3-1-(2-nitrophenyl)ethyl ester of ATP (NPE-caged ATP) in the presence and absence of Ca2+.
18 ons) in muscle following flash photolysis of caged ATP, in both the presence and absence of Ca.
19  ADP formation following release of ATP from caged ATP is similar whether or not twitchin is phosphor
20               Following photolysis of either caged ATP or caged ADP, probes promptly reoriented towar
21 ss-bridge detachment following photolysis of caged ATP, suggesting that the observed structural chang
22 n conjunction with laser flash photolysis of caged ATP, to resolve millisecond rotational transitions
23 These rates are comparable to those when NPE-caged ATP was used.
24                   The MDCC-PBP assay and NPE-caged ATP were used to measure the ATPase rate in single
25             Caged nucleotides (caged-ADP and caged-ATP) were used to initiate nucleotide binding to P
26 and glibenclamide and by the photorelease of caged ATP within neurones.

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