@article{pittir19978,
          volume = {3},
          number = {11},
           month = {June},
          author = {P Wipf and RJ Halter},
           title = {Chemistry and biology of wortmannin},
         journal = {Organic and Biomolecular Chemistry},
           pages = {2053 -- 2061},
            year = {2005},
             url = {http://d-scholarship-dev.library.pitt.edu/19978/},
        abstract = {Recent synthetic and biological studies of the viridin class of steroidal furans have revealed multiple opportunities for fundamental discoveries as well as advanced drug design. Wortmannin is a potent enzyme inhibitor that binds to the ATP site of important regulatory kinases such as PI-3 kinase and Polo-like kinase. The natural product shares a unique mechanism-based biological activation pathway with other viridins. Furthermore, while there have been several encouraging approaches toward the total synthesis of these compounds, there is still ample room for improvements in synthetic strategies and tactics, and the development of structurally simplified analogs that exert more specific biological effects and are devoid of toxicity issues that have thwarted the clinical development of the parent compounds. {\copyright} The Royal Society of Chemistry 2005.}
}