Endoproteolytic processing and stabilization of wild-type and mutant presenilin.

@article{Ratovitski1997EndoproteolyticPA,
  title={Endoproteolytic processing and stabilization of wild-type and mutant presenilin.},
  author={Tamara Ratovitski and Hilda H. Slunt and Gopal Thinakaran and Donald L. Price and Sangram S. Sisodia and David R Borchelt},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 39},
  pages={24536-41}
}
Presenilin 1 (PS1), mutated in pedigrees of early-onset familial Alzheimer's disease, is a polytopic integral membrane protein that is endoproteolytically cleaved into 27-kDa N-terminal and 17-kDa C-terminal fragments. Although these fragments are the principal PS1 species found in normal mammalian brain, the role of endoproteolysis in the maturation of PS1 has been unclear. The present study, which uses stably transfected mouse neuroblastoma N2a cells, demonstrates that full-length… CONTINUE READING
51 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 51 extracted citations

Similar Papers

Loading similar papers…