Natural products reveal cancer cell dependence on oxysterol-binding proteins

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Natural products reveal cancer cell dependence on oxysterol-binding proteins

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Title: Natural products reveal cancer cell dependence on oxysterol-binding proteins
Author: Burgett, Anthony W G; Poulsen, Thomas B; Wangkanont, Kittikhun; Anderson, D Ryan; Kikuchi, Chikako; Shimada, Kousei; Okubo, Shuichi; Fortner, Kevin C; Mimaki, Yoshihiro; Kuroda, Minpei; Murphy, Jason P; Schwalb, David J; Petrella, Eugene C; Cornella-Taracido, Ivan; Schirle, Markus; Tallarico, John A; Shair, Matthew David

Note: Order does not necessarily reflect citation order of authors.

Citation: Burgett, Anthony W G, Thomas B Poulsen, Kittikhun Wangkanont, D Ryan Anderson, Chikako Kikuchi, Kousei Shimada, Shuichi Okubo, et al. 2011. “Natural Products Reveal Cancer Cell Dependence on Oxysterol-Binding Proteins.” Nature Chemical Biology 7 (9) (August 7): 639–647. doi:10.1038/nchembio.625.
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Abstract: Cephalostatin 1, OSW-1, ritterazine B and schweinfurthin A are natural products that potently, and in some cases selectively, inhibit the growth of cultured human cancer cell lines. The cellular targets of these small molecules have yet to be identified. We have discovered that these molecules target oxysterol binding protein (OSBP) and its closest paralog, OSBP-related protein 4L (ORP4L)—proteins not known to be involved in cancer cell survival. OSBP and the ORPs constitute an evolutionarily conserved protein superfamily, members of which have been implicated in signal transduction, lipid transport and lipid metabolism. The functions of OSBP and the ORPs, however, remain largely enigmatic. Based on our findings, we have named the aforementioned natural products ORPphilins. Here we used ORPphilins to reveal new cellular activities of OSBP. The ORPphilins are powerful probes of OSBP and ORP4L that will be useful in uncovering their cellular functions and their roles in human diseases.
Published Version: doi:10.1038/nchembio.625
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Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:33464237
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