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Molecular modeling studies of these compounds complexed with FTase and farnesyl pyrophosphate are also described.
We found that all compounds complexed with plasmid DNA, but only the molecule containing 8 tat-peptide chains shows significant transfection capabilities.
The crystal structures for two of the identified compounds complexed with the N-terminal ATP binding domain of human Hsp90α were determined.
The X-ray crystal structures of some of these compounds complexed with TF·FVIIa were determined and results were applied to design the next round of inhibitors.
We found that all these compounds complexed with plasmid DNA and showed significant transfection capabilities in a variety of mammalian cell lines, but acrylyl-tat or tat alone showed no significant transfection capability.
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In previous studies we reported a novel series of organometallic compounds, RuII complexed with clotrimazole, displaying potent trypanosomatid activity with unnoticeable toxicity toward normal mammalian cells.
This compound, which complexed with the sodium cation, was the first compound known to display such activity and became known as dibenzo-18-crown-6, an 18-atom heterocycle containing 6 oxygen atoms.
The binding mode of compound 23 complexed with VEGFR-2 was predicted using FlexX algorithm.
Here we report the X-ray crystal structure of Compound 6 complexed with HDAC8 to 1.98 Å resolution.
In contrast, based on our work, less than 400 mg of naringenin are required if the compound is complexed with HPβCD.
To assist our design of selective cIAP inhibitors, we modeled the binding modes of compound 1 complexed with XIAP BIR3 and cIAP1 BIR3 proteins.
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