Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL.

@article{Inohara1998MtdAN,
  title={Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL.},
  author={Naohiro Inohara and Daryoush Ekhterae and Itxaso Garc{\'i}a and R Carri{\'o} and Jes{\'u}s Merino and A Merry and Sheng-hong Chen and Gabriel N{\'u}{\~n}ez},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 15},
  pages={8705-10}
}
We have identified and characterized Mtd, a novel regulator of apoptosis. Sequence analysis revealed that Mtd is a member of the Bcl-2 family of proteins containing conserved BH1, BH2, BH3, and BH4 regions and a carboxyl-terminal hydrophobic domain. In adult tissues, Mtd mRNA was predominantly detected in the brain, liver, and lymphoid tissues, while in the… CONTINUE READING