Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c.

@article{Shimizu2000ElectrophysiologicalSO,
  title={Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c.},
  author={Shigeomi Shimizu and Tomohiro Ide and Toshio Yanagida and Yoshihide Tsujimoto},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 16},
  pages={12321-5}
}
The Bcl-2 family of proteins, consisting of anti-apoptotic and pro-apoptotic members, regulates cell death by controlling mitochondrial membrane permeability that is crucial for apoptotic signal transduction. We have recently shown that some of these proteins, such as Bcl-x(L), Bax, and Bak, directly modulate the mitochondrial voltage-dependent anion channel (VDAC) and thus regulate apoptogenic cytochrome c release and potential loss. To elucidate the molecular mechanisms of VDAC regulation by… CONTINUE READING
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