Balanol analogues probe specificity determinants and the conformational malleability of the cyclic 3',5'-adenosine monophosphate-dependent protein kinase catalytic subunit.

@article{Akamine2004BalanolAP,
  title={Balanol analogues probe specificity determinants and the conformational malleability of the cyclic 3',5'-adenosine monophosphate-dependent protein kinase catalytic subunit.},
  author={Pearl Akamine and Madhusudan and Laurence L. Brunton and Horng D. Ou and Jaume M. Canaves and Nguyen-huu Xuong and Susan S. Taylor},
  journal={Biochemistry},
  year={2004},
  volume={43 1},
  pages={
          85-96
        }
}
The protein kinase family is a prime target for therapeutic agents, since unregulated protein kinase activities are linked to myriad diseases. Balanol, a fungal metabolite consisting of four rings, potently inhibits Ser/Thr protein kinases and can be modified to yield potent inhibitors that are selective-characteristics of a desirable pharmaceutical compound. Here, we characterize three balanol analogues that inhibit cyclic 3',5'-adenosine monophosphate-dependent protein kinase (PKA) more… CONTINUE READING