This is a great paper that provides a mechanism to explain the dose-limiting cardiotoxicity of the chemotherapeutic drug doxorubicin. Contrary to much current thought, toxicity does not involve iron-dependent redox cycling of the small molecule itself.
Clear explanation by Jason Locasale of a complicated metabolic pathway highly relevant to cancer cell survival in Nature Reviews Cancer.
Interesting new method & results from the Lindquist lab that exploits the interaction between chaperones and client proteins to monitor drug interactions in cells. Small molecules stabilize target protein conformation, leading to reduced chaperone binding which in turn can be detected be reduced target-chaperone co-IP.
Nice review of the role of BCL2 family proteins in cancer in Nature Reviews Cancer. I also like this earlier review from the Letai lab on the same subject. Clinically useful small molecule inhibitors are at hand, but lethal mechanisms still remain murky.
The Horvitz lab reports on an interesting model of hypoxia-reoxygenation in C. elegans. During the reoxygenation period worms thrash about at a high rate and this effect is suppressed by mutations in worm HIF-1. Thrashing is restored by a gof mutation in a cytochrome P450 gene and seems to involve the production of specific lipid mediators from worm PUFA stores. Interesting model and result.
Another paper challenging the model proposed in the 2007 Kohanski Cell paper that iron-catalyzed ROS production can explain the lethal mechanism of action of various bactericidal antibiotics.
http://www.sciencemag.org/content/340/6140/1583.abstract
Explains the effects on aminoglycosides, but what about the iron-dependent effects for other lethal antibiotics?