Inhibition of Bax channel-forming activity by Bcl-2.

@article{Antonsson1997InhibitionOB,
  title={Inhibition of Bax channel-forming activity by Bcl-2.},
  author={Bruno Antonsson and Franco Conti and A Ciavatta and Sylvie Montessuit and Sialyl Lewis and I. Martinou and Luca Bernasconi and Alain Bernard and J J Mermod and Gonzalo Mazzei and Kinsey Maundrell and Franco Gambale and R{\'e}my Sadoul and J C Martinou},
  journal={Science},
  year={1997},
  volume={277 5324},
  pages={370-2}
}
Proteins of the Bcl-2 family are intracellular membrane-associated proteins that regulate programmed cell death (apoptosis) either positively or negatively by as yet unknown mechanisms. Bax, a pro-apoptotic member of the Bcl-2 family, was shown to form channels in lipid membranes. Bax triggered the release of liposome-encapsulated carboxyfluorescein at both neutral and acidic pH. At physiological pH, release could be blocked by Bcl-2. Bcl-2, in contrast, triggered carboxyfluorescein release at… CONTINUE READING
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